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ATP + 20S proteasome
ADP + phosphorylated S20 proteasome
-
phosphorylation by Plk1 enhances the proteolytic activity
-
-
?
ATP + 3F3/2 kinase
ADP + phosphorylated 3F3/2 kinase
ATP + 53BP1
ADP + phosphorylated 53BP1
ATP + 5FAM-RALMEASFADQAR-NH2
ADP + phosphorylated 5FAM-RALMEASFADQAR-NH2
substrate peptide, based on human Cdc25C, used in biochemical activity assay
-
-
?
ATP + 85kDa microtubule-associated protein
ADP + phosphorylated 85kDa microtubule-associated protein
ATP + a protein
ADP + a phosphoprotein
ATP + abnormal spindle pole protein
ADP + phosphorylated abnormal spindle pole protein
ATP + alpha-casein
ADP + phosphorylated alpha-casein
ATP + alpha-synuclein
ADP + phosphorylated alpha-synuclein
the enzyme phosphorylates alpha-synuclein at Ser-129
-
-
?
ATP + Ame1
ADP + phosphorylated Ame1
-
-
-
-
?
ATP + amyloid precursor protein
ADP + phosphorylated amyloid precursor protein
polo-like kinase 2 directly binds and phosphorylates threonine-668 and serine-675 of amyloid precursor protein in vitro
-
-
?
ATP + Asterless protein
ADP + phosphorylated Asterless protein
isoform Plk4 phosphorylates the N-terminal domain of Asterless protein
-
-
?
ATP + Bcl-xL
ADP + phosphorylated Bcl-xL
-
-
-
-
?
ATP + Bem3
ADP + phosphorylated Bem3
-
bound by the polo-box domain of Cdc5
-
-
?
ATP + beta-casein
ADP + phosphorylated beta-casein
-
-
-
-
?
ATP + bovine serum albumin
ADP + phosphorylated bovine serum albumin
-
very weak phosphorylation
-
-
?
ATP + Brd4
ADP + phosphorylated Brd4
the E2 binding domain of Brd4 is phosphorylated by Plk1 in vitro
-
-
?
ATP + BubR1
ADP + phosphorylated BubR1
ATP + casein
ADP + a phosphorylated casein
-
activity assay
-
-
?
ATP + casein
ADP + phosphocasein
ATP + casein
ADP + phosphorylated casein
ATP + Cdc14A
ADP + phosphorylated Cdc14A
-
-
-
?
ATP + Cdc25
ADP + phosphorylated Cdc25
ATP + Cdc25A
ADP + phosphorylated Cdc25A
-
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25
-
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
ATP + Cdh1
ADP + phosphorylated Cdh1
-
-
-
-
?
ATP + CENP-Q
ADP + phosphorylated CENP-Q
ATP + centromeric protein PBIP1
ADP + phosphorylated centromeric protein PBIP1
ATP + Chk2
ADP + phosphorylated Chk2
ATP + cJun peptide
ADP + phosphorylated cJun peptide
strong preference of PLK1 versus PLK2 and PLK3
-
-
?
ATP + CLASP
ADP + phosphorylated CLASP
-
-
-
?
ATP + claspin
ADP + phosphorylated claspin
ATP + cohesin
ADP + phosphorylated cohesin
ATP + CRAF protein
ADP + phosphorylated CRAF protein
-
-
-
?
ATP + Cse4
ADP + phosphorylated Cse4
-
-
-
-
?
ATP + cyclin B
ADP + phosphorylated cyclin B
ATP + cyclin B1
ADP + phosphorylated cyclin B
-
phosphorylation at S101, not at S113 in the cytoplasmic retention sequence
-
-
?
ATP + dephospho-beta-tubulin
ADP + phosphorylated beta-tubulin
ATP + Ecm25
ADP + phosphorylated Ecm25
-
bound by the polo-box domain of Cdc5
-
-
?
ATP + Ect2
ADP + phosphorylated Ect2
-
-
-
?
ATP + Emi2
ADP + phosphorylated Emi2
ATP + Fkh2p
ADP + phosphorylated Fkh2p
-
Fkh2p is only poorly phosphorylated by Cdc5p, Fkh2p has a function in nucleating the formation of a Fkh2p-Ndd1p-Cdc5p complex on CLB2 cluster promoters, and the subsequent Cdc5p-dependent phosphorylation of Ndd1p at Ser 85
-
-
?
ATP + gammaBD of IKKbeta
ADP + phosphorylated gammaBD of IKKbeta
Plk1 phosphorylates serines 733, 740 and 750 in the IKKgammaNEMO-binding domain, gammaBD, of IKKbeta
-
-
?
ATP + giantin
ADP + phosphorylated giantin
-
-
-
-
?
ATP + Hice1 subunit of Augmin complex
ADP + phosphorylated Hice1 subunit of Augmin complex
ATP + histone H1
ADP + phosphorylated histone H1
ATP + histone H1 kinase
ADP + phosphorylated histone H1 kinase
-
activation
-
-
?
ATP + HsCdc14A
ADP + phosphorylated HsCdc14A
HsCdc14A binds to PLK1 via its C-terminus, phosphorylation partially releases the auto-inhibition of HsCdc14A, PLK1-mediated phospho-regulation promotes HsCdc14A phosphatase activity
-
-
?
ATP + HTP-1 protein
ADP + phosphorylated HTP-1 protein
-
-
-
-
?
ATP + kinesin-like protein 2
ADP + phosphorylated kinesin-like protein 2
ATP + Mad1
ADP + phosphorylated Mad1
-
the results suggest that Plk1 is influential of Mad1 phosphorylation, Mad1, mitotic arrest deficiency protein 1
-
-
?
ATP + Mad3
ADP + phosphorylated Mad3
ATP + MEI-S332 protein
ADP + phosphorylated MEI-S332 protein
ATP + MEX-5
ADP + phosphorylated MEX-5
-
-
-
-
?
ATP + Mid1p
ADP + phosphorylated Mid1p
ATP + mitotic centromere-associated kinesin
ADP + phosphorylated mitotic centromere-associated kinesin
ATP + Mtw1
ADP + phosphorylated Mtw1
-
-
-
-
?
ATP + Mus81-Mms4 resolvase
ADP + phosphorylated Mus81-Mms4 resolvase
-
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
-
very weak phosphorylation
-
-
?
ATP + Myt1
ADP + phosphorylated Myt1
ATP + Ndc80
ADP + phosphorylated Ndc80
-
-
-
-
?
ATP + Ndd1p
ADP + phosphorylated Ndd1p
-
phosphorylation of Ser 85, phosphorylation is required for the normal temporal expression of cell-cycle-regulated genes such as CLB2 and SWI5 in G2/M phase
-
-
?
ATP + Nud1
ADP + phosphorylated Nud1
Cdc5 and Cdc28 activities are required for proper phosphorylation of Nud1
-
-
?
ATP + NudC
ADP + phosphorylated kinesin-like protein 2
-
i.e. nuclear distribution protein C, Plk1 phosphorylates Ser274 and Ser326
-
-
?
ATP + p125
ADP + phosphorylated p125
ATP + p53
ADP + phosphorylated p53
ATP + PBIP1
ADP + phosphorylated PBIP1
ATP + Pin1
ADP + phosphorylated Pin1
ATP + Plk1 polo box 1-derived peptide
ADP + phosphorylated Plk1 polo box 1-derived peptide
synthetic substrate
-
-
?
ATP + PLKtide
ADP + phosphorylated PLKtide
ATP + protein
ADP + phosphoprotein
ATP + protein MAVS
ADP + phosphorylated protein MAVS
phosphorylation of the mitochondria-bound adapter protein MAVS, MAVS, mitochondrial antiviral signaling
-
-
?
ATP + protein p110
ADP + ?
-
-
-
-
?
ATP + Rom2
ADP + phosphorylated Rom2
-
bound by the polo-box domain of Cdc5
-
-
?
ATP + Sac7
ADP + phosphorylated Sac7
-
bound by the polo-box domain of Cdc5
-
-
?
ATP + SCC1 cohesin
ADP + phosphorylated SCC1 cohesin
-
-
-
?
ATP + SCFFbw7 ubiquitin ligase
ADP + phosphorylated SCFFbw7 ubiquitin ligase
-
-
-
?
ATP + Slk19
ADP + phosphorylated Slk19
ATP + Stu2
ADP + phosphorylated Stu2
ATP + SYK tyrosine kinase
ADP + phosphorylated SYK tyrosine kinase
-
-
-
?
ATP + SYP-4 protein
ADP + phosphorylated SYP-4 protein
-
-
-
-
?
ATP + TbCentrin2
ADP + ?
-
-
-
-
?
ATP + TPSDSLIYDDGLS
ADP + phosphorylated TPSDSLIYDDGLS
-
-
-
?
ATP + TRF1
ADP + phosphorylated TRF1
ATP + Tus1
ADP + phosphorylated Tus1
-
bound by the polo-box domain of Cdc5
-
-
?
ATP + viral phosphoprotein P
ADP + phosphorylated viral phosphoprotein P
PLK1 directly phosphorylates viral phosphoprotein P of paramyxovirus in vitro
-
-
?
ATP + Wee1
ADP + phosphorylated Wee1
-
-
-
-
?
additional information
?
-
ATP + 3F3/2 kinase
ADP + phosphorylated 3F3/2 kinase
-
the enzyme creates the 3F3/2 kinase phosphoepitope on mitotic kinetichores, depletion of enzyme in M phase cell extract leads to loss of 3F3/2 kinase activity
-
-
?
ATP + 3F3/2 kinase
ADP + phosphorylated 3F3/2 kinase
-
purified recombinant Plk1 or M phase cell extract, phosphoepitope mapping reveals that the 3F3/2 kinase phosphoepitope overlaps the enzyme consensus phosphorylation seqence, overview
-
-
?
ATP + 3F3/2 kinase
ADP + phosphorylated 3F3/2 kinase
-
the enzyme creates the 3F3/2 kinase phosphoepitope on mitotic kinetichores, depletion of enzyme in M phase cell extract leads to loss of 3F3/2 kinase activity
-
-
?
ATP + 3F3/2 kinase
ADP + phosphorylated 3F3/2 kinase
-
purified recombinant Plk1 or M phase cell extract, phosphoepitope mapping reveals that the 3F3/2 kinase phosphoepitope overlaps the enzyme consensus phosphorylation seqence, overview
-
-
?
ATP + 53BP1
ADP + phosphorylated 53BP1
53BP1 is phosphorylated by Plk1 in mitosis
-
-
?
ATP + 53BP1
ADP + phosphorylated 53BP1
53BP1 is phosphorylated by Plk1 in its C-terminal domain at Ser1618 in the UDR domain
-
-
?
ATP + 85kDa microtubule-associated protein
ADP + phosphorylated 85kDa microtubule-associated protein
-
-
-
-
?
ATP + 85kDa microtubule-associated protein
ADP + phosphorylated 85kDa microtubule-associated protein
-
protein is released from microtubules after phosphorylation
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
Saccharomyces pombe
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + abnormal spindle pole protein
ADP + phosphorylated abnormal spindle pole protein
-
-
-
-
?
ATP + abnormal spindle pole protein
ADP + phosphorylated abnormal spindle pole protein
-
i.e. abnormal spindle pole protein, activation of abnormal spindle pole protein by phosphorylation
-
-
?
ATP + alpha-casein
ADP + phosphorylated alpha-casein
-
-
-
-
?
ATP + alpha-casein
ADP + phosphorylated alpha-casein
-
high activity of wild-type enzyme
-
-
?
ATP + alpha-casein
ADP + phosphorylated alpha-casein
-
-
-
-
?
ATP + BubR1
ADP + phosphorylated BubR1
-
-
-
?
ATP + BubR1
ADP + phosphorylated BubR1
S676 is an in vivo Plk1 phosphorylation site in BubR1
-
-
?
ATP + BubR1
ADP + phosphorylated BubR1
BubR1 interacts with Plk1 during prometaphase, binds to the C-terminal, complete polo-box domain of Plk1
-
-
?
ATP + BubR1
ADP + phosphorylated BubR1
Plk1-BubR1 interaction is mediated by polo-box domain binding to pT620 of BubR1. S676 is a Plk1-specific phosphorylation site, site is phosphorylated during prometaphase, but dephosphorylated at metaphase upon establishment of tension between sister chromatids. Phosphorylation is not required for spindle checkpoint function but instead is important for the stability of kinetochore-microtubule interactions, timely mitotic progression, and chromosome alignment onto the metaphase plate
-
-
?
ATP + BubR1
ADP + phosphorylated BubR1
-
Plk1 is responsible for the hyperphosphorylation of BubR1 during prometaphase
-
-
?
ATP + casein
ADP + phosphocasein
substrate in biochemical activity assay
-
-
?
ATP + casein
ADP + phosphocasein
-
substrate in biochemical activity assay
-
-
?
ATP + casein
ADP + phosphocasein
-
-
-
?
ATP + casein
ADP + phosphorylated casein
-
-
-
-
?
ATP + casein
ADP + phosphorylated casein
-
-
-
?
ATP + casein
ADP + phosphorylated casein
-
-
-
?
ATP + casein
ADP + phosphorylated casein
kinase assay
-
-
?
ATP + casein
ADP + phosphorylated casein
-
-
-
-
?
ATP + casein
ADP + phosphorylated casein
-
-
-
-
?
ATP + casein
ADP + phosphorylated casein
-
best in vitro substrate
-
-
?
ATP + Cdc25
ADP + phosphorylated Cdc25
-
-
-
?
ATP + Cdc25
ADP + phosphorylated Cdc25
-
-
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
-
-
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
-
-
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
-
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
-
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
-
phosphorylation by Plk1 on Ser198 in a nuclear export signal sequence promoting its nuclear translocation, inhibition of Cdc25 activation resulting in a delay in Cdc2 activation
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
-
Plk3 activity in vitro, phosphorylation by Plk1 on Ser198
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
preferentially phosphorylates Ser 198 and 191
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
the polo box domain displays a similar affinity for non-phosphorylated and phosphorylated Cdc25C target peptides, full-length Plk1 shows ca. 7fold more affinity for the phosphorylated peptide
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
substrate in activity assay
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
the protein phosphatase is directly phosphorylated by Plk1
-
-
?
ATP + CENP-Q
ADP + phosphorylated CENP-Q
-
-
-
?
ATP + CENP-Q
ADP + phosphorylated CENP-Q
-
-
-
-
?
ATP + CENP-Q
ADP + phosphorylated CENP-Q
phosphorylation of nine CENP-Q residues Thr123, Thr135, Ser138, Ser139, Ser248, Ser249, Ser253, Ser255, and Thr256, clustered in two regions, mutation of all nine residues to Ala completely eliminated Plk1-dependent CENP-Q phosphorylation in vitro
-
-
?
ATP + centromeric protein PBIP1
ADP + phosphorylated centromeric protein PBIP1
Plk1 phosphorylates PBIP1 at T78, GST-PBIPtide is used as in vitro substrate
-
-
?
ATP + centromeric protein PBIP1
ADP + phosphorylated centromeric protein PBIP1
-
Plk1 phosphorylates PBIP1 at T78, GST-PBIPtide is used as in vitro substrate
-
-
?
ATP + Chk2
ADP + phosphorylated Chk2
-
-
-
-
?
ATP + Chk2
ADP + phosphorylated Chk2
-
phosphorylation at Thr68
-
-
?
ATP + Chk2
ADP + phosphorylated Chk2
-
substrate is a protein kinase, phosphorylated by Plk1 at Ser28, Thr68, and Thr26 in vitro
-
-
?
ATP + claspin
ADP + phosphorylated claspin
-
Plx1 is involved in alleviating DNA replication checkpoint response by inactivation of claspin through phosphorylation
-
-
?
ATP + claspin
ADP + phosphorylated claspin
-
checkpoint protein, interaction and phosphorylation at Thr906 and Ser934
-
-
?
ATP + cohesin
ADP + phosphorylated cohesin
-
-
-
-
?
ATP + cohesin
ADP + phosphorylated cohesin
-
phosphorylation by Cdc5 required for removal of cohesin from chromosomes
-
-
?
ATP + cohesin
ADP + phosphorylated cohesin
-
phosphorylation adjacent to the cleavage site of Scc1 by Cdc5
-
-
?
ATP + cyclin B
ADP + phosphorylated cyclin B
-
-
-
?
ATP + cyclin B
ADP + phosphorylated cyclin B
-
phosphorylation at S126, S128, S133, and S147 for nuclear translocation of cyclin B
-
-
?
ATP + cyclin B
ADP + phosphorylated cyclin B
-
no phosphorylation of cyclin B1
-
-
?
ATP + cyclin B
ADP + phosphorylated cyclin B
-
-
-
-
?
ATP + dephospho-beta-tubulin
ADP + phosphorylated beta-tubulin
-
-
-
-
?
ATP + dephospho-beta-tubulin
ADP + phosphorylated beta-tubulin
-
the enzyme is required for beta-tubulin recruitment to the centrosome
-
-
?
ATP + Emi2
ADP + phosphorylated Emi2
-
-
-
-
?
ATP + Emi2
ADP + phosphorylated Emi2
-
CaMKII and polo-like kinase 1 sequentially phosphorylate the cytostatic factor Emi2/XErp1 to trigger its destruction and meiotic exit, in response to increased free Ca2+ levels CaMKII acts as a priming kinase mediating the interaction between Emi2 and Plx1 polo box domain via phosphorylation at a specific motif
-
-
?
ATP + Emi2
ADP + phosphorylated Emi2
-
Emi2, i.e. XErp1, is a cytostatic factor
-
-
?
ATP + Emi2
ADP + phosphorylated Emi2
-
CaMKII specifically directs Plx1 activity toward Emi2 by functioning as a priming kinase, creating a phosphoepitope on Emi2 that recruits the polo box domain of Plx1, allowing subsequent phosphorylation of Emi2s degron and its recognition by SCFbetaTrCP for ubiquitination and destruction
-
-
?
ATP + Hice1 subunit of Augmin complex
ADP + phosphorylated Hice1 subunit of Augmin complex
-
-
-
-
?
ATP + Hice1 subunit of Augmin complex
ADP + phosphorylated Hice1 subunit of Augmin complex
-
via the formation of the Nedd1-Plk1 complex and subsequent Augmin phosphorylation, Plk1 regulates spindle microtubule-based microtubule nucleation to accomplish normal bipolar spindle formation and mitotic progression
-
-
?
ATP + histone H1
ADP + phosphorylated histone H1
substrate used in kinase assay
-
-
?
ATP + histone H1
ADP + phosphorylated histone H1
-
substrate used in kinase assay
-
-
?
ATP + kinesin-like protein 2
ADP + phosphorylated kinesin-like protein 2
-
Plk1, essential for cytokinesis
-
-
?
ATP + kinesin-like protein 2
ADP + phosphorylated kinesin-like protein 2
-
Plk1
-
-
?
ATP + Mad3
ADP + phosphorylated Mad3
-
-
-
-
?
ATP + Mad3
ADP + phosphorylated Mad3
-
phosphorylation of Mad3 isozymes at 5 serine residues, S222, S380, S466, S504, and especially at S268, during spindle checkpoint activation, Mad3 is an inhibitor of Cdc20/APC ubiquitin ligase, overview
-
-
?
ATP + Mad3
ADP + phosphorylated Mad3
-
recombinant HA-tagged wild-type and mutant Mad3 substrate proteins, the activity with mutants in which phorylation site Ser is replaced by Ala is highly reduced, Mad3 is a homologue to the human BubR1 protein
-
-
?
ATP + MEI-S332 protein
ADP + phosphorylated MEI-S332 protein
-
substrate is a protein essential in meiosis for maintaining cohesion at centromers until sister chromatids separate at the metaphase II/anaphase II transition, phosphorylation by polo kinase removes the protein from centromeres and antagonizes the MEI-S332 function, MEI-S332 phosphorylation by polo kinase is essential for viability of the cells
-
-
?
ATP + MEI-S332 protein
ADP + phosphorylated MEI-S332 protein
-
enzyme requires residues T331 and possibly in combination with S234 for activity, no activity with MEI-S332 protein mutants T331A and S234A/T331A in S2 cells
-
-
?
ATP + MEI-S332 protein
ADP + phosphorylated MEI-S332 protein
-
phosphorylation/polo box binding is required for chromosomal dissociation of MEI-S332
-
-
?
ATP + MEI-S332 protein
ADP + phosphorylated MEI-S332 protein
-
enzyme requires residues T331 and possibly in combination with S234 for activity, no activity with MEI-S332 protein mutants T331A and S234A/T331A
-
-
?
ATP + Mid1p
ADP + phosphorylated Mid1p
-
-
-
-
?
ATP + Mid1p
ADP + phosphorylated Mid1p
-
required for positioning of division sites in cytokinesis
-
-
?
ATP + mitotic centromere-associated kinesin
ADP + phosphorylated mitotic centromere-associated kinesin
i.e. MCAK, residue S621 in MCAK is the major phosphorylation site of Plk1, residues S632/S633 are also phoshorylated by Plk1. S632/S633 phosphorylation significantly enhances the microtubule depolymerizing activity of MCAK in vivo and in vitro
-
-
?
ATP + mitotic centromere-associated kinesin
ADP + phosphorylated mitotic centromere-associated kinesin
i.e. MCAK, residue S621 in MCAK is the major phosphorylation site of Plk1, residues S632/S633 are also phoshorylated by Plk1
-
-
?
ATP + Myt1
ADP + phosphorylated Myt1
-
-
-
?
ATP + Myt1
ADP + phosphorylated Myt1
-
phosphorylation of Myt1 during M phase
-
-
?
ATP + Myt1
ADP + phosphorylated Myt1
-
i.e. membrane-associated tyrosine- and threonine-specific cdc2-inhibitory kinase, no activity with a Myt1 mutant in which the 4 C-terminal phosphorylation sites are mutated to alanine
-
-
?
ATP + Myt1
ADP + phosphorylated Myt1
-
-
-
-
?
ATP + p125
ADP + phosphorylated p125
-
peptide fragment of DNA polymerase delta, phosphorylation at Ser60 by Plk3
-
-
?
ATP + p125
ADP + phosphorylated p125
-
peptide fragment of DNA polymerase delta, phosphorylation at Ser60 by Plk3, wild-type and mutant GST-tagged or His6-tagged Plk3
-
-
?
ATP + p53
ADP + phosphorylated p53
-
-
Plk3, Plk1 inhibits tumor suppressor p53 transactivating activity in lung carcinoma cells
-
?
ATP + p53
ADP + phosphorylated p53
-
Plk1 binds tumor suppressor p53, dependent on DNA-binding to the specific DNA binding domain within residues 102-292 of p53, and inhibits its transactivation activity
-
-
?
ATP + p53
ADP + phosphorylated p53
-
phosphorylation at Ser20
-
-
?
ATP + p53
ADP + phosphorylated p53
-
Plk3 phosphorylates S20 in vitro, Plk1 inhibits p53 by phosphorylation
-
-
?
ATP + p53
ADP + phosphorylated p53
Plk1 apparently phosphorylates other residues than Plk3
-
-
?
ATP + p53
ADP + phosphorylated p53
Plk3 apparently phosphorylates other residues than Plk1
-
-
?
ATP + PBIP1
ADP + phosphorylated PBIP1
-
-
-
?
ATP + PBIP1
ADP + phosphorylated PBIP1
phosphorylation on Thr78 by Plk1
-
-
?
ATP + PBIP1
ADP + phosphorylated PBIP1
Plk1 efficiently phosphorylates and binds to the Thr78 motif of PBIP1 through a self-priming and binding mechanism
-
-
?
ATP + Pin1
ADP + phosphorylated Pin1
Plk1-mediated phosphorylation at Ser65 stabilizes Pin1 by inhibiting its ubiquitination in cells
-
-
?
ATP + Pin1
ADP + phosphorylated Pin1
recombinant isomerase Pin1 expressed in Escherichia coli, phosphorylation at Ser65, wild-type and truncated mutant Pin1 comprising residues 1-70
-
-
?
ATP + PLKtide
ADP + phosphorylated PLKtide
substrate corresponds to the consensus sequence for positions -7 to +6 supplemented with residues from Cdc25C for positions -23 to -8. PLK1 displays greatly enhanced activity and a strong preference for the residue corresponding to Ser198 in the optimized substrate
-
-
?
ATP + PLKtide
ADP + phosphorylated PLKtide
substrate corresponds to the consensus sequence for positions -7 to +6 supplemented with residues from Cdc25C for positions -23 to -8. PLK2 displays greatly enhanced activity and a strong preference for the residue corresponding to Ser198 in the optimized substrate
-
-
?
ATP + PLKtide
ADP + phosphorylated PLKtide
substrate corresponds to the consensus sequence for positions -7 to +6 supplemented with residues from Cdc25C for positions -23 to -8. PLK3 displays greatly enhanced activity and a strong preference for the residue corresponding to Ser198 in the optimized substrate
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
?
ATP + Slk19
ADP + phosphorylated Slk19
-
-
-
-
?
ATP + Slk19
ADP + phosphorylated Slk19
Cdc5 and Cdc28 activities are required for proper phosphorylation of Slk19
-
-
?
ATP + Stu2
ADP + phosphorylated Stu2
-
-
-
-
?
ATP + Stu2
ADP + phosphorylated Stu2
Cdc5 and Cdc28 activities are required for proper phosphorylation of Stu2
-
-
?
ATP + TRF1
ADP + phosphorylated TRF1
-
the cell-cycle-dependent TRF1 recruitment to telomere chromatin is regulated by the enzyme, TRF1 binds the telomere via the telomeric repeats, process overview
-
-
?
ATP + TRF1
ADP + phosphorylated TRF1
-
endogenous TRF1 associated to telomeres during mitosis, phosphorylation by Plx1 in vitro
-
-
?
ATP + TRF1
ADP + phosphorylated TRF1
-
is phosphorylated by Plx1 upon transition from interphase to M phase, and is recruited to mitotic telomere chromatin
-
-
?
additional information
?
-
required for nuclear envelope breakdown and the completion of meiosis
-
-
?
additional information
?
-
-
required for nuclear envelope breakdown and the completion of meiosis
-
-
?
additional information
?
-
-
the polo-loke kinase activates cyclase-dependent hyphal-like growth acting like a switch between yeast and hyphal growth forms, mechanism, overview
-
-
?
additional information
?
-
normal bipolar spindles with polyploid complements of chromosomes, bipolar spindles in which one pole can be unusually broad, and monopolar spindles
-
-
?
additional information
?
-
mutation in polo leads to a variety of abnormal mitoses in Drosophila larval neuroblasts. These include otherwise normal looking mitotic spindles upon which chromosomes appear overcondensed
-
-
?
additional information
?
-
-
the enzyme is a mitotic kinase and is required for centrosome maturation at mitotic M-phase entry in order to recruit the gamma-tubulin ring complex and activate abnormal spindle pole protein, Asp, the enzyme is involved in mitotic networks and cytokinesis, e.g. in spermatogenesis, overview, functional modeling of polo kinase in mitotic phases
-
-
?
additional information
?
-
-
the enzyme is pivotal in cell division as a regulator of cell cycle checkpoints in mitotic progression, regulation of cytokinesis, overview
-
-
?
additional information
?
-
autophosphorylation of wild-type full-length enzyme and isolated kinase domain
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
no phosphorylation of histone H1
-
-
?
additional information
?
-
playing an important role in regulating the onset and/or progression of mitosis in mammalian cells
-
-
?
additional information
?
-
the enzyme is involved in regulating M phase functions during the cell cycle. Prk's role in mitosis is at least partly mediated through direct regulation of Cdc25C
-
-
?
additional information
?
-
expression appears to be down-regulated in lung carcinomas
-
-
?
additional information
?
-
expression of PLK mRNA appeared to be strongly correlated with the mitotic activity of cells
-
-
?
additional information
?
-
Plk1 is likely to function in cell cycle progression
-
-
?
additional information
?
-
-
Chk2 phosphorylation at Thr68 is enhanced by overexpression of Plk1 in vivo
-
-
?
additional information
?
-
Plk1 depletion induces apoptosis in cancer cells and stabilizes p53 tumor-suppressor protein
-
-
?
additional information
?
-
-
Plk1 inhibits Wee1 inactivation resulting in a delay in Cdc2 activation, the enzyme is pivotal in cell division as a regulator of cell cycle checkpoints in mitotic progression, modeling of major Plk metabolism pathways, spindle checkpoint machinery, overview
-
-
?
additional information
?
-
-
Plk1 is involved in regulating centrosome maturation, mitotic entry, sister chromatid cohesion, the anaphase-promoting complex/cyclosome, and cytokinesis, as well as in chromosome orientation, detailed overview of physiological functions of the enzyme
-
-
?
additional information
?
-
-
Plk1 is involved in the regulation of M-phase of the cell cycle and might also be involved in tumorigenesis
-
-
?
additional information
?
-
-
Plk3 is involved in regulating Golgi fragmentation during the cell cycle
-
-
?
additional information
?
-
-
polo-like kinase 1 creates the tension-sensing 3F3/2 phosphoepitope and modulates the association of spindle-checkpoint proteins at kinetochores, the enzym is required for association of Cdc20 to kinetochores
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of centriole duplication cycle by protein phosphorylation
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of Nek2-induced centrosome separation after DNA damage
-
-
?
additional information
?
-
the enzyme plays an essential role in promoting mitosis and cytokinesis, the kinase activity is regulated by the conserved C-terminal polo box domain which acts as both an autoinhibitory domain and a subcellular localization domain, structure analysis
-
-
?
additional information
?
-
-
the enzyme plays an essential role in promoting mitosis and cytokinesis, the kinase activity is regulated by the conserved C-terminal polo box domain which acts as both an autoinhibitory domain and a subcellular localization domain, structure analysis
-
-
?
additional information
?
-
-
determination of enzyme consensus sequence
-
-
?
additional information
?
-
-
Plk1 interacts with the 20S and the 26S proteasomes, Plk3 interacts with DNA polymerase delta and Plk1 with the Golgi specific protein GRASP65
-
-
?
additional information
?
-
-
the protein phosphatase 1 is no substrate of Plk1
-
-
?
additional information
?
-
consensus substrate sequences for PLK2
-
-
?
additional information
?
-
consensus substrate sequences for PLK2
-
-
?
additional information
?
-
consensus substrate sequences for PLK2
-
-
?
additional information
?
-
consensus substrate sequences for PLK2
-
-
?
additional information
?
-
consensus substrate sequences for PLK3
-
-
?
additional information
?
-
consensus substrate sequences for PLK3
-
-
?
additional information
?
-
consensus substrate sequences for PLK3
-
-
?
additional information
?
-
consensus substrate sequences for PLK3
-
-
?
additional information
?
-
consensus substrate sequences for PLK4
-
-
?
additional information
?
-
consensus substrate sequences for PLK4
-
-
?
additional information
?
-
consensus substrate sequences for PLK4
-
-
?
additional information
?
-
consensus substrate sequences for PLK4
-
-
?
additional information
?
-
expanded consensus substrate sequence for PLK1
-
-
?
additional information
?
-
expanded consensus substrate sequence for PLK1
-
-
?
additional information
?
-
expanded consensus substrate sequence for PLK1
-
-
?
additional information
?
-
expanded consensus substrate sequence for PLK1
-
-
?
additional information
?
-
Plk1 can interact with hTERT independently of its kinase activity
-
-
?
additional information
?
-
-
Plk1 can interact with hTERT independently of its kinase activity
-
-
?
additional information
?
-
selective association between PLK1 and Fbw7 proteins. The WD40 domain of Fbw7 interacts with PLK1 as strongly as the full-length protein, the WD40 domain is responsible for Fbw7 association with PLK1, and the C-terminal Polobox domain (PBD), but not the N-terminal kinase domain (KD), within PLK1 selectively interacts with Fbw7 WD40 domain
-
-
?
additional information
?
-
-
selective association between PLK1 and Fbw7 proteins. The WD40 domain of Fbw7 interacts with PLK1 as strongly as the full-length protein, the WD40 domain is responsible for Fbw7 association with PLK1, and the C-terminal Polobox domain (PBD), but not the N-terminal kinase domain (KD), within PLK1 selectively interacts with Fbw7 WD40 domain
-
-
?
additional information
?
-
polo-box domain of polo-like kinase 2, residues 451-685, PBD2 binds phosphopeptides containing a SerpSer/pThr motif
-
-
?
additional information
?
-
the enzyme can be successfully encapsulated in PLGA nanoparticles. The encapsulated enzyme remains bioactive and can phosphorylate intracellular alpha-synuclein at Ser-129 of SH-SY5Y cells
-
-
-
additional information
?
-
the enzyme may be involved in the early signaling events required for growth factor-stimulated cell cycle progression
-
-
?
additional information
?
-
-
the enzyme may be involved in the early signaling events required for growth factor-stimulated cell cycle progression
-
-
?
additional information
?
-
has two functions, one during the entry of cells into the cell cycle and a second during mitosis of cycling cells
-
-
?
additional information
?
-
cell cycle- and terminal differentiation-associated regulation
-
-
?
additional information
?
-
enzyme is involved in cell proliferation, expression is associated with mitotic and meiotic cell division
-
-
?
additional information
?
-
-
enzyme is involved in cell proliferation, expression is associated with mitotic and meiotic cell division
-
-
?
additional information
?
-
the enzyme is regulated dynamically with synaptic plasticity
-
-
?
additional information
?
-
the enzyme is involved in regulation of cytokinesis and microtubule polymerization modulation during oocyte meiotic maturation, fertilization and early embryonic mitosis
-
-
?
additional information
?
-
required for the initiation of chromosomal DNA replication in Saccharomyces cerevisiae and interaction with the CDC7 protein kinase
-
-
?
additional information
?
-
-
Cdc5 plays a role in chromosomes segregation during meiosis I, it is required for phosphorylation and removal of cohesin from chromosomes, it is required for sister-kinetochore orientation with associated Mam1 protein, mechanism, overview
-
-
?
additional information
?
-
-
Plk1 is important in activation and regulation of spindle assembly during mitosis
-
-
?
additional information
?
-
-
polo kinase Cdc5 is involved as part of the FEAR network, i.e. fourteen early anaphase release network, and of MEN network, i.e. mitotic exit network, in controlling protein phosphatase Cdc14 localization and activity, the enzyme induces phosphorylation of Cdc14 and Cfi1/Net1 by activating the networks, overview
-
-
?
additional information
?
-
-
the enzyme is pivotal in cell division as a regulator of cell cycle checkpoints in mitotic progression, Cdc5 is part of mitotic networks, e.g. the fourteen early anaphase release network FEAR for Cdc14 release, overview
-
-
?
additional information
?
-
the enzyme is required to form a bipolar spindle, the actin ring, and septum, can drive septum formation in G1 and G2 cells
-
-
?
additional information
?
-
-
cytokinetic actomyosin ring formation and septation in fission yeast are dependent on the full recruitment of the polo-like kinase PLO1 to the spindle pole body, regulated by Mad2, and a functional spindle assembly checkpoint which requires an intact microtubule cytoskeleton, overview
-
-
?
additional information
?
-
-
physical and functional interactions between polo kinase and the spindle pole component Cut12 regulate mitotic commitment by feedback control of the MPF complex, overview
-
-
?
additional information
?
-
-
the enzyme is involved in spindle formation and septation playing an important role in cell cycle regulation
-
-
?
additional information
?
-
-
the enzyme is pivotal in cell division as a regulator of cell cycle checkpoints in mitotic progression, Plo1 is involved in cytokinesis
-
-
?
additional information
?
-
-
the enzyme recruitment to the spindle pole body influences the balance between Cdc25 and Wee1 activities on mitosis-promoting factor, MPF
-
-
?
additional information
?
-
-
the enzyme interacts with diverse proteins via its poloboxes, overview
-
-
?
additional information
?
-
-
the enzyme interacts with DNA polymerase delta
-
-
?
additional information
?
-
-
the enzyme is involved in regulation of cytokinesis and microtubule polymerization modulation during oocyte meiotic maturation, fertilization and early embryonic mitosis
-
-
?
additional information
?
-
-
no activity against myelin basic protein or histone H1
-
-
?
additional information
?
-
-
polo-like kinase 1 creates the tension-sensing 3F3/2 phosphoepitope and modulates the association of spindle-checkpoint proteins at kinetochores
-
-
?
additional information
?
-
-
the enzyme is essential for Ca2+-induced meiotic exit of fertilized eggs after arrest in metaphase II before fertilization
-
-
?
additional information
?
-
-
the enzyme is pivotal in cell division as a regulator of cell cycle checkpoints in mitotic progression, mechanism
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + 20S proteasome
ADP + phosphorylated S20 proteasome
-
phosphorylation by Plk1 enhances the proteolytic activity
-
-
?
ATP + 3F3/2 kinase
ADP + phosphorylated 3F3/2 kinase
ATP + 53BP1
ADP + phosphorylated 53BP1
53BP1 is phosphorylated by Plk1 in mitosis
-
-
?
ATP + 85kDa microtubule-associated protein
ADP + phosphorylated 85kDa microtubule-associated protein
-
protein is released from microtubules after phosphorylation
-
-
?
ATP + a protein
ADP + a phosphoprotein
ATP + abnormal spindle pole protein
ADP + phosphorylated abnormal spindle pole protein
-
i.e. abnormal spindle pole protein, activation of abnormal spindle pole protein by phosphorylation
-
-
?
ATP + BubR1
ADP + phosphorylated BubR1
ATP + casein
ADP + phosphorylated casein
kinase assay
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
ATP + CENP-Q
ADP + phosphorylated CENP-Q
ATP + Chk2
ADP + phosphorylated Chk2
ATP + CLASP
ADP + phosphorylated CLASP
-
-
-
?
ATP + claspin
ADP + phosphorylated claspin
-
Plx1 is involved in alleviating DNA replication checkpoint response by inactivation of claspin through phosphorylation
-
-
?
ATP + cohesin
ADP + phosphorylated cohesin
-
phosphorylation by Cdc5 required for removal of cohesin from chromosomes
-
-
?
ATP + cyclin B
ADP + phosphorylated cyclin B
-
phosphorylation at S126, S128, S133, and S147 for nuclear translocation of cyclin B
-
-
?
ATP + cyclin B1
ADP + phosphorylated cyclin B
-
phosphorylation at S101, not at S113 in the cytoplasmic retention sequence
-
-
?
ATP + dephospho-beta-tubulin
ADP + phosphorylated beta-tubulin
-
the enzyme is required for beta-tubulin recruitment to the centrosome
-
-
?
ATP + Emi2
ADP + phosphorylated Emi2
ATP + giantin
ADP + phosphorylated giantin
-
-
-
-
?
ATP + Hice1 subunit of Augmin complex
ADP + phosphorylated Hice1 subunit of Augmin complex
-
via the formation of the Nedd1-Plk1 complex and subsequent Augmin phosphorylation, Plk1 regulates spindle microtubule-based microtubule nucleation to accomplish normal bipolar spindle formation and mitotic progression
-
-
?
ATP + HTP-1 protein
ADP + phosphorylated HTP-1 protein
-
-
-
-
?
ATP + kinesin-like protein 2
ADP + phosphorylated kinesin-like protein 2
-
Plk1, essential for cytokinesis
-
-
?
ATP + Mad3
ADP + phosphorylated Mad3
-
phosphorylation of Mad3 isozymes at 5 serine residues, S222, S380, S466, S504, and especially at S268, during spindle checkpoint activation, Mad3 is an inhibitor of Cdc20/APC ubiquitin ligase, overview
-
-
?
ATP + MEI-S332 protein
ADP + phosphorylated MEI-S332 protein
ATP + Mid1p
ADP + phosphorylated Mid1p
-
required for positioning of division sites in cytokinesis
-
-
?
ATP + mitotic centromere-associated kinesin
ADP + phosphorylated mitotic centromere-associated kinesin
i.e. MCAK, residue S621 in MCAK is the major phosphorylation site of Plk1, residues S632/S633 are also phoshorylated by Plk1. S632/S633 phosphorylation significantly enhances the microtubule depolymerizing activity of MCAK in vivo and in vitro
-
-
?
ATP + Mus81-Mms4 resolvase
ADP + phosphorylated Mus81-Mms4 resolvase
-
-
-
?
ATP + Myt1
ADP + phosphorylated Myt1
-
phosphorylation of Myt1 during M phase
-
-
?
ATP + NudC
ADP + phosphorylated kinesin-like protein 2
-
i.e. nuclear distribution protein C, Plk1 phosphorylates Ser274 and Ser326
-
-
?
ATP + p125
ADP + phosphorylated p125
-
peptide fragment of DNA polymerase delta, phosphorylation at Ser60 by Plk3
-
-
?
ATP + p53
ADP + phosphorylated p53
ATP + PBIP1
ADP + phosphorylated PBIP1
ATP + Pin1
ADP + phosphorylated Pin1
Plk1-mediated phosphorylation at Ser65 stabilizes Pin1 by inhibiting its ubiquitination in cells
-
-
?
ATP + protein
ADP + phosphoprotein
ATP + Rom2
ADP + phosphorylated Rom2
-
bound by the polo-box domain of Cdc5
-
-
?
ATP + SCFFbw7 ubiquitin ligase
ADP + phosphorylated SCFFbw7 ubiquitin ligase
-
-
-
?
ATP + SYP-4 protein
ADP + phosphorylated SYP-4 protein
-
-
-
-
?
ATP + TRF1
ADP + phosphorylated TRF1
-
the cell-cycle-dependent TRF1 recruitment to telomere chromatin is regulated by the enzyme, TRF1 binds the telomere via the telomeric repeats, process overview
-
-
?
ATP + Tus1
ADP + phosphorylated Tus1
-
bound by the polo-box domain of Cdc5
-
-
?
additional information
?
-
ATP + 3F3/2 kinase
ADP + phosphorylated 3F3/2 kinase
-
the enzyme creates the 3F3/2 kinase phosphoepitope on mitotic kinetichores, depletion of enzyme in M phase cell extract leads to loss of 3F3/2 kinase activity
-
-
?
ATP + 3F3/2 kinase
ADP + phosphorylated 3F3/2 kinase
-
the enzyme creates the 3F3/2 kinase phosphoepitope on mitotic kinetichores, depletion of enzyme in M phase cell extract leads to loss of 3F3/2 kinase activity
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
Saccharomyces pombe
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + BubR1
ADP + phosphorylated BubR1
-
-
-
?
ATP + BubR1
ADP + phosphorylated BubR1
S676 is an in vivo Plk1 phosphorylation site in BubR1
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
-
phosphorylation by Plk1 on Ser198 in a nuclear export signal sequence promoting its nuclear translocation, inhibition of Cdc25 activation resulting in a delay in Cdc2 activation
-
-
?
ATP + Cdc25C
ADP + phosphorylated Cdc25C
the protein phosphatase is directly phosphorylated by Plk1
-
-
?
ATP + CENP-Q
ADP + phosphorylated CENP-Q
-
-
-
?
ATP + CENP-Q
ADP + phosphorylated CENP-Q
-
-
-
-
?
ATP + Chk2
ADP + phosphorylated Chk2
-
-
-
-
?
ATP + Chk2
ADP + phosphorylated Chk2
-
phosphorylation at Thr68
-
-
?
ATP + Emi2
ADP + phosphorylated Emi2
-
-
-
-
?
ATP + Emi2
ADP + phosphorylated Emi2
-
CaMKII and polo-like kinase 1 sequentially phosphorylate the cytostatic factor Emi2/XErp1 to trigger its destruction and meiotic exit, in response to increased free Ca2+ levels CaMKII acts as a priming kinase mediating the interaction between Emi2 and Plx1 polo box domain via phosphorylation at a specific motif
-
-
?
ATP + MEI-S332 protein
ADP + phosphorylated MEI-S332 protein
-
substrate is a protein essential in meiosis for maintaining cohesion at centromers until sister chromatids separate at the metaphase II/anaphase II transition, phosphorylation by polo kinase removes the protein from centromeres and antagonizes the MEI-S332 function, MEI-S332 phosphorylation by polo kinase is essential for viability of the cells
-
-
?
ATP + MEI-S332 protein
ADP + phosphorylated MEI-S332 protein
-
phosphorylation/polo box binding is required for chromosomal dissociation of MEI-S332
-
-
?
ATP + p53
ADP + phosphorylated p53
-
-
Plk3, Plk1 inhibits tumor suppressor p53 transactivating activity in lung carcinoma cells
-
?
ATP + p53
ADP + phosphorylated p53
-
Plk1 binds tumor suppressor p53, dependent on DNA-binding to the specific DNA binding domain within residues 102-292 of p53, and inhibits its transactivation activity
-
-
?
ATP + PBIP1
ADP + phosphorylated PBIP1
-
-
-
?
ATP + PBIP1
ADP + phosphorylated PBIP1
phosphorylation on Thr78 by Plk1
-
-
?
ATP + PBIP1
ADP + phosphorylated PBIP1
Plk1 efficiently phosphorylates and binds to the Thr78 motif of PBIP1 through a self-priming and binding mechanism
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
?
ATP + protein
ADP + phosphoprotein
-
-
-
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ATP + protein
ADP + phosphoprotein
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ATP + protein
ADP + phosphoprotein
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ATP + protein
ADP + phosphoprotein
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ATP + protein
ADP + phosphoprotein
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ATP + protein
ADP + phosphoprotein
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ATP + protein
ADP + phosphoprotein
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ATP + protein
ADP + phosphoprotein
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additional information
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required for nuclear envelope breakdown and the completion of meiosis
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additional information
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required for nuclear envelope breakdown and the completion of meiosis
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additional information
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the polo-loke kinase activates cyclase-dependent hyphal-like growth acting like a switch between yeast and hyphal growth forms, mechanism, overview
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additional information
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normal bipolar spindles with polyploid complements of chromosomes, bipolar spindles in which one pole can be unusually broad, and monopolar spindles
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additional information
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mutation in polo leads to a variety of abnormal mitoses in Drosophila larval neuroblasts. These include otherwise normal looking mitotic spindles upon which chromosomes appear overcondensed
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additional information
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the enzyme is a mitotic kinase and is required for centrosome maturation at mitotic M-phase entry in order to recruit the gamma-tubulin ring complex and activate abnormal spindle pole protein, Asp, the enzyme is involved in mitotic networks and cytokinesis, e.g. in spermatogenesis, overview, functional modeling of polo kinase in mitotic phases
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additional information
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the enzyme is pivotal in cell division as a regulator of cell cycle checkpoints in mitotic progression, regulation of cytokinesis, overview
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additional information
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additional information
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playing an important role in regulating the onset and/or progression of mitosis in mammalian cells
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additional information
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the enzyme is involved in regulating M phase functions during the cell cycle. Prk's role in mitosis is at least partly mediated through direct regulation of Cdc25C
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additional information
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expression appears to be down-regulated in lung carcinomas
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additional information
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expression of PLK mRNA appeared to be strongly correlated with the mitotic activity of cells
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additional information
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Plk1 is likely to function in cell cycle progression
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additional information
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Chk2 phosphorylation at Thr68 is enhanced by overexpression of Plk1 in vivo
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additional information
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Plk1 depletion induces apoptosis in cancer cells and stabilizes p53 tumor-suppressor protein
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additional information
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Plk1 inhibits Wee1 inactivation resulting in a delay in Cdc2 activation, the enzyme is pivotal in cell division as a regulator of cell cycle checkpoints in mitotic progression, modeling of major Plk metabolism pathways, spindle checkpoint machinery, overview
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additional information
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Plk1 is involved in regulating centrosome maturation, mitotic entry, sister chromatid cohesion, the anaphase-promoting complex/cyclosome, and cytokinesis, as well as in chromosome orientation, detailed overview of physiological functions of the enzyme
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additional information
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Plk1 is involved in the regulation of M-phase of the cell cycle and might also be involved in tumorigenesis
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additional information
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Plk3 is involved in regulating Golgi fragmentation during the cell cycle
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additional information
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polo-like kinase 1 creates the tension-sensing 3F3/2 phosphoepitope and modulates the association of spindle-checkpoint proteins at kinetochores, the enzym is required for association of Cdc20 to kinetochores
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additional information
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the enzyme is involved in regulation of centriole duplication cycle by protein phosphorylation
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additional information
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the enzyme is involved in regulation of Nek2-induced centrosome separation after DNA damage
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additional information
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the enzyme plays an essential role in promoting mitosis and cytokinesis, the kinase activity is regulated by the conserved C-terminal polo box domain which acts as both an autoinhibitory domain and a subcellular localization domain, structure analysis
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additional information
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the enzyme plays an essential role in promoting mitosis and cytokinesis, the kinase activity is regulated by the conserved C-terminal polo box domain which acts as both an autoinhibitory domain and a subcellular localization domain, structure analysis
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additional information
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Plk1 can interact with hTERT independently of its kinase activity
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additional information
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Plk1 can interact with hTERT independently of its kinase activity
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additional information
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selective association between PLK1 and Fbw7 proteins. The WD40 domain of Fbw7 interacts with PLK1 as strongly as the full-length protein, the WD40 domain is responsible for Fbw7 association with PLK1, and the C-terminal Polobox domain (PBD), but not the N-terminal kinase domain (KD), within PLK1 selectively interacts with Fbw7 WD40 domain
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additional information
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selective association between PLK1 and Fbw7 proteins. The WD40 domain of Fbw7 interacts with PLK1 as strongly as the full-length protein, the WD40 domain is responsible for Fbw7 association with PLK1, and the C-terminal Polobox domain (PBD), but not the N-terminal kinase domain (KD), within PLK1 selectively interacts with Fbw7 WD40 domain
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additional information
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the enzyme may be involved in the early signaling events required for growth factor-stimulated cell cycle progression
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additional information
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the enzyme may be involved in the early signaling events required for growth factor-stimulated cell cycle progression
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additional information
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has two functions, one during the entry of cells into the cell cycle and a second during mitosis of cycling cells
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additional information
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cell cycle- and terminal differentiation-associated regulation
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additional information
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enzyme is involved in cell proliferation, expression is associated with mitotic and meiotic cell division
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additional information
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enzyme is involved in cell proliferation, expression is associated with mitotic and meiotic cell division
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additional information
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the enzyme is regulated dynamically with synaptic plasticity
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additional information
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the enzyme is involved in regulation of cytokinesis and microtubule polymerization modulation during oocyte meiotic maturation, fertilization and early embryonic mitosis
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additional information
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required for the initiation of chromosomal DNA replication in Saccharomyces cerevisiae and interaction with the CDC7 protein kinase
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additional information
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Cdc5 plays a role in chromosomes segregation during meiosis I, it is required for phosphorylation and removal of cohesin from chromosomes, it is required for sister-kinetochore orientation with associated Mam1 protein, mechanism, overview
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additional information
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Plk1 is important in activation and regulation of spindle assembly during mitosis
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additional information
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polo kinase Cdc5 is involved as part of the FEAR network, i.e. fourteen early anaphase release network, and of MEN network, i.e. mitotic exit network, in controlling protein phosphatase Cdc14 localization and activity, the enzyme induces phosphorylation of Cdc14 and Cfi1/Net1 by activating the networks, overview
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additional information
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the enzyme is pivotal in cell division as a regulator of cell cycle checkpoints in mitotic progression, Cdc5 is part of mitotic networks, e.g. the fourteen early anaphase release network FEAR for Cdc14 release, overview
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additional information
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the enzyme is required to form a bipolar spindle, the actin ring, and septum, can drive septum formation in G1 and G2 cells
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additional information
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cytokinetic actomyosin ring formation and septation in fission yeast are dependent on the full recruitment of the polo-like kinase PLO1 to the spindle pole body, regulated by Mad2, and a functional spindle assembly checkpoint which requires an intact microtubule cytoskeleton, overview
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additional information
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physical and functional interactions between polo kinase and the spindle pole component Cut12 regulate mitotic commitment by feedback control of the MPF complex, overview
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additional information
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the enzyme is involved in spindle formation and septation playing an important role in cell cycle regulation
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additional information
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the enzyme is pivotal in cell division as a regulator of cell cycle checkpoints in mitotic progression, Plo1 is involved in cytokinesis
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additional information
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the enzyme recruitment to the spindle pole body influences the balance between Cdc25 and Wee1 activities on mitosis-promoting factor, MPF
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additional information
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the enzyme is involved in regulation of cytokinesis and microtubule polymerization modulation during oocyte meiotic maturation, fertilization and early embryonic mitosis
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?
additional information
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polo-like kinase 1 creates the tension-sensing 3F3/2 phosphoepitope and modulates the association of spindle-checkpoint proteins at kinetochores
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?
additional information
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the enzyme is essential for Ca2+-induced meiotic exit of fertilized eggs after arrest in metaphase II before fertilization
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additional information
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the enzyme is pivotal in cell division as a regulator of cell cycle checkpoints in mitotic progression, mechanism
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(1R)-1-[(3S,6S,9S,12S,15S)-19-(6-[[2-(1-acetyl-1H-indol-3-yl)ethyl]amino]-6-oxohexyl)-3-carbamoyl-9-(hydroxymethyl)-12-(1H-imidazol-5-ylmethyl)-15-(2-methylpropyl)-5,8,11,14,17,20-hexaoxo-1-thia-4,7,10,13,16,19-hexaazacyclohenicosan-6-yl]ethyl phosphate
PL-116
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(1R)-1-[(3S,6S,9S,12S,15S)-19-(6-[[2-(1-acetyl-1H-indol-3-yl)ethyl]amino]-6-oxohexyl)-3-carbamoyl-9-(hydroxymethyl)-15-(2-methylpropyl)-5,8,11,14,17,20-hexaoxo-12-[[1-(9-phenylnonyl)-1H-imidazol-5-yl]methyl]-1-thia-4,7,10,13,16,19-hexaazacyclohenicosan-6-yl]ethyl phosphate
PL-120
(2Z)-2-(5-bromo-2-methoxybenzylidene)-6-methyl-7H-[1,3]thiazolo[3,2-b][1,2,4]triazine-3,7(2H)-dione
-
(3-[5-methyl-2-[(3,4,5-trimethoxyphenyl)amino]imidazo[5,1-f][1,2,4]triazin-7-yl]phenyl)(phenyl)methanone
-
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(3S)-4-amino-4-oxo-3-([[2-(4-phenylbutyl)-1-(2-phenylethyl)-1H-benzimidazol-5-yl]carbonyl]amino)butan-2-yl phosphate
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(4E)-4-(hydroxyimino)-5-methyl-2-(propan-2-yl)cyclohexa-2,5-dien-1-one
(4E)-5-methyl-4-[[(2-methylbenzoyl)oxy]imino]-2-(propan-2-yl)cyclohexa-2,5-dien-1-one
(4E)-5-methyl-4-{[(2-methylbenzoyl)oxy]imino}-2-(propan-2-yl)cyclohexa-2,5-dien-1-one
(4R)-1-acetyl-4-(4-phenylbutoxy)prolyl-L-leucyl-L-histidyl-L-seryl-O-phosphono-L-threoninamide
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(4R)-1-acetyl-4-[[(E)-(3-phenylpropylidene)amino]oxy]prolyl-L-leucyl-L-histidyl-L-seryl-O-phosphono-L-threoninamide
-
(7R)-2-[5-(2,4-difluorophenyl)-1H-pyrazol-4-yl]-7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
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(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-3-yl)-7,8-dihydropteridin-6(5H)-one
good selectivity over Plk-1 (193-fold), good permeability and moderate microsomal stability. When dosed orally in rats, the inhibitor demonstrates a 41-45% reduction of pS129-a-synuclein levels in the cerebral cortex
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
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(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-5-yl)-7,8-dihydropteridin-6(5H)-one
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(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
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(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
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(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(oxetan-3-yl)-7,8-dihydropteridin-6(5H)-one
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(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-[(3S)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
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(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
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(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(propan-2-yl)-7,8-dihydropteridin-6(5H)-one
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(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(pyrimidin-5-yl)-7,8-dihydropteridin-6(5H)-one
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(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-[(3R)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
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(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-[(3S)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
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(7R)-7-ethyl-5-methyl-8-(1H-pyrazol-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
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(7R)-7-ethyl-5-methyl-8-(tetrahydro-2H-pyran-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
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(7R)-7-ethyl-5-methyl-8-(tetrahydrofuran-3-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
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(7R)-8-(3,3-difluorocyclobutyl)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
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(R)-4-[(8-cyclopentyl-7-ethyl-5,6,7,8-tetrahydro-5-methyl-6-oxo-2-pteridinyl)amino]-3-methoxy-N-(1-methyl-4-piperidinyl)benzamide
i.e. BI2536
1-(1-methylpiperidin-4-yl)-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
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1-(2-fluorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
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1-(2-hydroxyethyl)-2-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1,5,6,7-tetrahydro-4H-pyrrolo[3,2-c]pyridin-4-one
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1-(2-hydroxyethyl)-5-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1H-pyrrole-3-carboxamide
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1-(2-methoxyphenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
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1-(26-oxo-2,5,8,11,14,17,20,23-octaoxahexacosan-26-yl)-L-prolyl-L-leucyl-3-(8-phenyloctyl)-L-histidyl-L-seryl-(3R)-4-phosphono-L-valinamide
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1-(3,5-dichlorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
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1-(3,5-dimethylphenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
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1-(3-bromo-5-chlorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
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1-(3-chlorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
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1-(3-fluorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
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1-(3-methoxyphenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
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1-(4-fluorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
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1-(4-methoxyphenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
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1-(5-methyl-2-trifluoro-methyl-furan-3-yl)-3-(5-[2-[6-(1H-[1,2,4]triazol-3-ylamino)-pyrimidin-4-ylamino]-ethyl]-thiazol-2-yl)urea
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1-acetyl-L-prolyl-L-leucyl-3-(5-[[(Z)-([2-[acetyl(phenyl)amino]-1,3-thiazol-4-yl]methylidene)amino]oxy]pentyl)-L-histidyl-L-seryl-O-phosphono-L-threoninamide
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1-acetyl-L-prolyl-L-leucyl-3-(5-[[(Z)-([2-[benzyl(methyl)amino]-1,3-thiazol-5-yl]methylidene)amino]oxy]pentyl)-L-histidyl-L-seryl-O-phosphono-L-threoninamide
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1-acetyl-L-prolyl-L-leucyl-3-(5-[[(Z)-benzylideneamino]oxy]pentyl)-L-histidyl-L-seryl-O-phosphono-L-threoninamide
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1-acetyl-L-prolyl-L-leucyl-3-(6-[[(Z)-([1-[4-(thiophen-2-yl)pyrimidin-2-yl]-1H-pyrrol-2-yl]methylidene)amino]oxy]hexyl)-L-histidyl-L-seryl-O-phosphono-L-threoninamide
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1-acetyl-L-prolyl-L-leucyl-3-(6-[[(Z)-([2-[acetyl(phenyl)amino]-1,3-thiazol-4-yl]methylidene)amino]oxy]hexyl)-L-histidyl-L-seryl-O-phosphono-L-threoninamide
-
1-acetyl-L-prolyl-L-leucyl-3-(6-[[(Z)-([2-[benzyl(methyl)amino]-1,3-thiazol-5-yl]methylidene)amino]oxy]hexyl)-L-histidyl-L-seryl-O-phosphono-L-threoninamide
-
1-acetyl-L-prolyl-L-leucyl-3-(6-[[(Z)-([5-chloro-2-[(pyridin-2-yl)methoxy]phenyl]methylidene)amino]oxy]hexyl)-L-histidyl-L-seryl-O-phosphono-L-threoninamide
-
1-acetyl-L-prolyl-L-leucyl-3-(6-[[(Z)-benzylideneamino]oxy]hexyl)-L-histidyl-L-seryl-O-phosphono-L-threoninamide
-
1-acetyl-L-prolyl-L-leucyl-3-(8-phenyloctyl)-L-histidyl-L-seryl-O-phosphono-L-threoninamide
1-acetyl-L-prolyl-L-leucyl-3-[3-(2-hydroxyethyl)-1-(8-phenyloctyl)-1H-imidazol-3-ium-5-yl]-L-alanyl-L-seryl-O-phosphono-L-threoninamide
-
1-acetyl-L-prolyl-L-leucyl-3-[3-(2-hydroxyethyl)-1-(8-phenyloctyl)-1H-imidazol-3-ium-5-yl]-L-alanyl-L-seryl-O-[[[(2,2-dimethylpropanoyl)oxy]methoxy](hydroxy)phosphoryl]-L-threoninamide
-
1-acetyl-L-prolyl-L-leucyl-3-[5-([(Z)-[(2-fluoro-6-phenoxyphenyl)methylidene]amino]oxy)pentyl]-L-histidyl-L-seryl-O-phosphono-L-threoninamide
-
1-acetyl-L-prolyl-L-leucyl-3-[6-(2-phenoxyphenyl)hexyl]-L-histidyl-L-seryl-O-phosphono-L-threoninamide
-
1-acetyl-L-prolyl-L-leucyl-3-[6-([(Z)-[(2-fluoro-6-phenoxyphenyl)methylidene]amino]oxy)hexyl]-L-histidyl-L-seryl-O-phosphono-L-threoninamide
-
1-acetyl-L-prolyl-L-leucyl-3-[6-([(Z)-[(4'-fluoro[1,1'-biphenyl]-2-yl)methylidene]amino]oxy)hexyl]-L-histidyl-L-seryl-O-phosphono-L-threoninamide
-
1-acetyl-L-prolyl-L-leucyl-3-[8-(2-fluoro-6-phenoxyphenyl)octyl]-L-histidyl-L-seryl-O-phosphono-L-threoninamide
-
1-acetyl-L-prolyl-L-leucyl-3-[8-(2-phenoxyphenyl)octyl]-L-histidyl-L-seryl-O-phosphono-L-threoninamide
-
1-acetyl-L-prolyl-L-leucyl-3-[8-([1,1'-biphenyl]-2-yl)octyl]-L-histidyl-L-seryl-O-phosphono-L-threoninamide
-
1-acetyl-L-prolyl-L-leucyl-3-[8-[2-(benzyloxy)phenyl]octyl]-L-histidyl-L-seryl-O-phosphono-L-threoninamide
-
1-acetyl-L-prolyl-L-leucyl-3-[9-(2-fluoro-6-phenoxyphenyl)nonyl]-L-histidyl-L-seryl-O-phosphono-L-threoninamide
-
1-acetyl-L-prolyl-L-leucyl-L-histidyl-L-seryl-O-phosphono-L-threoninamide
-
1-cyclohexyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
1-methyl-2-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1,5,6,7-tetrahydro-4H-pyrrolo[3,2-c]pyridin-4-one
high levels of selectivity on a panel of unrelated kinases, as well as against PLK2 and PLK3 isoforms, acceptable oral bioavailability in mice making this inhibitor a suitable candidate for further in vivo activity studies
1-methyl-5-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1H-pyrrole-3-carboxamide
high levels of selectivity on a panel of unrelated kinases, as well as against PLK2 and PLK3 isoforms, acceptable oral bioavailability in mice making this inhibitor a suitable candidate for further in vivo activity studies
1-methyl-5-(2-[[5-(piperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1H-pyrrole-3-carboxamide
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1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxylic acid
-
1-methyl-8-[(2-methylphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
1-methyl-8-[(2-nitrophenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
1-methyl-8-[(2-phenoxyphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
1-methyl-8-[(2-sulfamoylphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
1-methyl-8-[(3-nitrophenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
1-methyl-8-[(4-nitrophenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
1-methyl-8-[[2-(methylamino)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
1-methyl-8-[[2-(methylsulfanyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
1-methyl-8-[[2-(phenylamino)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
1-methyl-8-[[2-(phenylcarbonyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
1-methyl-8-[[2-(phenylsulfanyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
1-methyl-8-[[2-(propan-2-yl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
1-methyl-8-[[2-(trifluoromethyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
1-methyl-8-[[3-(trifluoromethyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
1-methyl-8-[[4-(trifluoromethyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
1-methyl-N-phenyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
1-phenyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
1-[2-hydroxy-3-(4-methylpiperazin-1-yl)propyl]-1H-indole-3-carboxylic acid
-
1-[2-hydroxy-3-(piperidin-1-yl)propyl]-1H-indole-3-carboxylic acid
-
1-[2-hydroxy-3-(pyrrolidin-1-yl)propyl]-1H-indole-3-carboxylic acid
-
1-[3-(3-aminopropyl)phenyl]-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
1-[3-(diethylamino)-2-hydroxypropyl]-1H-indole-3-carboxylic acid
-
1-[3-(dimethylamino)phenyl]-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
2'-(2-hydroxyethoxy)-5'-methyl-(1,1':3',1''-terphenyl)-4,4''-dinitrile
-
0.3 mM, 11% inhibition, full-length enzyme Plk1 with the mutation T210D in the active-site loop of kinase domain
2'-(2-hydroxyethoxy)-5'-methyl-(1,1':3':1''-terphenyl)-4''-(1H-tetrazol-5-yl)-4-nitrile
-
0.3 mM, 66% inhibition, full-length enzyme Plk1 with the mutation T210D in the active-site loop of kinase domain
2'-(2-hydroxyethoxy)-5'-methyl-[1,1':3',1''-terphenyl]-3,3'',5,5''-tetrafluoro-4,4''-diol
-
0.3 mM, 61% inhibition, full-length enzyme Plk1 with the mutation T210D in the active-site loop of kinase domain
2'-(2-hydroxyethoxy)-5'-methyl-[1,1':3',1''-terphenyl]-4,4''-diacetic acid
-
0.3 mM, 53% inhibition, full-length enzyme Plk1 with the mutation T210D in the active-site loop of kinase domain
2'-(2-hydroxyethoxy)-5'-methyl-[1,1':3',1''-terphenyl]-4,4''-dicarboxylic acid
-
0.3 mM, 14% inhibition, full-length enzyme Plk1 with the mutation T210D in the active-site loop of kinase domain
2'-(2-hydroxyethoxy)-5'-methyl-[1,1':3',1''-terphenyl]-4,4''-dipropionic acid
-
0.3 mM, 26% inhibition, full-length enzyme Plk1 with the mutation T210D in the active-site loop of kinase domain
2'-hydroxy-5'-methyl-[1,1':3',1''-terphenyl]-4,4''-dicarboxylic acid
-
0.3 mM, 36% inhibition, full-length enzyme Plk1 with the mutation T210D in the active-site loop of kinase domain
2'-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5'-methyl-8'-(propan-2-yl)-5',8'-dihydro-6'H-spiro[cyclobutane-1,7'-pteridin]-6'-one
-
2,3,4,6-tetrahydroxy-5H-benzo[7]annulen-5-one
HeLa cells treated with purpurogallin exhibit delayed onset of mitosis and prolonged mitosis progression
2-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1-(2,2,2-trifluoroethyl)-1,5,6,7-tetrahydro-4H-pyrrolo[3,2-c]pyridin-4-one
-
2-cyano-3-hydroxy-3-methyl-N-[4-(trifluoromethoxy)phenyl]-propenamide
LFM-A12
2-methyl-5-(propan-2-yl)cyclohexa-2,5-diene-1,4-dione
2-[(3-cyano-6-methoxyquinolin-2-yl)sulfanyl]-N-(2-methoxy-5-methylphenyl)acetamide
i.e. I2
2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5,7,7-trimethyl-8-(propan-2-yl)-7,8-dihydropteridin-6(5H)-one
-
2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7-(2,2,2-trifluoroethyl)-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
-
2-[5'-methyl-4,4''-ditetrazol-5-yl-(1,1':3',1''-terphenyl)-2'-oxy]ethanol
-
0.3 mM, 47% inhibition, full-length enzyme Plk1 with the mutation T210D in the active-site loop of kinase domain
3-(1,3-benzodioxol-5-yl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
-
3-(1-[2-chloro-4-[(3-hydroxypyrrolidin-1-yl)methyl]phenyl]ethoxy)-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-(2-methylcyclohexyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
-
3-(3,4-dimethoxyphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
-
3-(3,4-dimethylphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
-
3-(3-chlorophenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
-
3-(3-methyl-6-[[(1S)-1-phenylethyl]amino]-1H-pyrazolo[4,3-c]pyridin-1-yl)benzonitrile
-
-
3-(3-methylphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
>0.01
3-(4-methylphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
-
3-(4-methylthiophen-3-yl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
-
3-benzyl-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
>0.020
3-methyl-1-(2-methylphenyl)-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
3-methyl-1-(3-methylphenyl)-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
3-methyl-1-(4-methylphenyl)-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
3-methyl-1-phenyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
3-methyl-1-[3-(1-methylethyl)phenyl]-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
3-methyl-1-[3-(methylsulfonyl)phenyl]-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
-
-
3-phenyl-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
-
3-[(1R)-1-(2-chloro-4-[[(1-methylethyl)amino]methyl]phenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-(2-chloro-4-[[(2-hydroxy-1,1-dimethylethyl)amino]methyl]phenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-(2-chloro-4-[[(2-hydroxyethyl)amino]methyl]phenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-(2-chloro-4-[[(3-hydroxypropyl)amino]methyl]phenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-methoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(2R)-2,3-dihydroxypropyl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(2R)-2-hydroxy-3-pyrrolidin-1-ylpropyl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(4R)-1-methylazepan-4-yl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(4S)-1-methylazepan-4-yl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[5-(1-methyl-1H-pyrrol-3-yl)-1H-benzo[3,4]cyclobuta[1,2-d]imidazol-1-yl]thiophene-2-carboxamide
GSK580432A, little inhibitory activity
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[5-[2-(4-methylpiperazin-1-yl)pyridin-4-yl]-1H-benzo[3,4]cyclobuta[1,2-d]imidazol-1-yl]thiophene-2-carboxamide
GSK641502A
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-(hydroxymethyl)imidazo[1,2-a]pyridin-3-yl]thiophene-2-carboxamide
-
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-(pyridin-4-yl)-1H-benzo[3,4]cyclobuta[1,2-d]imidazol-1-yl]thiophene-2-carboxamide
GSK483724A
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)methoxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)methoxy]-1H-benzo[3,4]cyclobuta[1,2-d]imidazol-1-yl]thiophene-2-carboxamide
GSK571989A
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
-
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzo[3,4]cyclobuta[1,2-d]imidazol-1-yl]thiophene-2-carboxamide
GSK579289A
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[3-(dimethylamino)propoxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
-
3-[(1R)-1-[2-(hydroxymethyl)phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-(hydroxymethyl)phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-[(1,1-dioxidothiomorpholin-4-yl)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-[(3-oxopiperazin-1-yl)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-[(4-fluoropiperidin-1-yl)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-[(4-hydroxypiperidin-1-yl)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-[(4-methylpiperazin-1-yl)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-[(cyclopentylamino)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-[(cyclopropylamino)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-[(dimethylamino)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-[(ethylamino)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[2-chloro-4-[(methylamino)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-(difluoromethoxy)phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
tested in rat xenograft model
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-(difluoromethyl)phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-chlorophenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-cyclopropylphenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-fluorophenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-methylphenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(1S)-1-(2-chlorophenyl)ethoxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
3-[(1S)-1-(2-chlorophenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[(2-chlorobenzyl)oxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
-
3-[(2-chlorobenzyl)oxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[1-(2-chlorophenyl)ethoxy]-5-[7-(hydroxymethyl)imidazo[1,2-a]pyridin-3-yl]thiophene-2-carboxamide
-
-
3-[1-(5-[[(1S)-1-phenylethyl]amino]isoxazolo[5,4-c]pyridin-3-yl)piperidin-3-yl]propanamide
-
3-[1-[2-chloro-5-(hydroxymethyl)phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
-
-
3-[1-[2-hydroxy-3-(piperidin-1-yl)propyl]-1H-indol-3-yl]propanoic acid
-
3-[1-[2-hydroxy-3-(pyrrolidin-1-yl)propyl]-1H-indol-3-yl]propanoic acid
-
3-[3-(3-methyl-6-[[(1S)-1-phenylethyl]amino]-1H-pyrazolo[4,3-c]pyridin-1-yl)phenyl]propanamide
-
-
3-[3-(3-methyl-6-[[(1S)-1-phenylethyl]amino]-1H-pyrazolo[4,3-c]pyridin-1-yl)phenyl]propanoic acid
-
-
3-[3-chloro-5-(5-[[(1S)-1-phenylethyl]amino]isoxazolo[5,4-c]pyridin-3-yl)phenyl]propan-1-ol
-
3-[3-chloro-5-(5-[[(1S)-1-phenylethyl]amino]isoxazolo[5,4-c]pyridin-3-yl)phenyl]propanamide
-
4-((R)-8-cyclopentyl-7-ethyl-5-methyl-6-oxo-5,6,7,8-tetrahydro-pteridin-2-ylamino)-3-methoxy-N-(1-methyl-piperidin-4-yl)-benzamide
BI 2536
4-amino-5-fluoro-3-[6-(4-methylpiperazin-1-yl)-1H-benzimidazol-2-yl]quinolin-2-ol
selectivity profile of PLK2/4 over PLK1/3
4-[(5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-yl)amino]benzenesulfonamide
-
-
4-[7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-6-oxo-6,7-dihydropteridin-8(5H)-yl]benzonitrile
-
5-(1-methyl-1H-imidazol-5-yl)-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
5-(1H-benzimidazol-1-yl)-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
5-(2-amino-1,3-thiazol-5-yl)-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
5-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1-(2,2,2-trifluoroethyl)-1H-pyrrole-3-carboxamide
-
5-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1-[2-(tetrahydro-2H-pyran-4-yloxy)ethyl]-1H-pyrrole-3-carboxamide
-
5-(5,6-dimethoxy-1H-benzimidazol-1-yl)-3-[2-(trifluoromethyl)-benzyloxy]-thiophene-2-carboxamide
-
-
5-(5,6-dimethoxy-1H-benzimidazol-1-yl)-3-[2-(trifluoromethyl)-benzyl]oxythiophene-2-carboxamide
-
GW843682X
5-(5,6-dimethoxy-1H-benzimidazol-1-yl)-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
5-(5,6-dimethoxy-1H-benzimidazol-1-yl)-3-{[2-(trifluoromethyl)phenyl]methoxy}thiophene-2-carboxamide
-
i.e. GW843682X, inhibition of PLK1 activity abrogates mitotic activation of AMP-activated protein kinasealpha through direct or indirect mechanisms
5-(5,6-dimethoxy-1H-benzimidazole-1-yl)-3-[2-(trifluoromethyl)-benzyloxy]-thiophene-2-carboxamide
-
GW843682X
5-(6-methoxy-1H-benzimidazol-1-yl)-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
5-imidazo[1,2-a]pyridin-3-yl-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
5-methyl-7-(2-nitrophenyl)-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
5-methyl-7-(3-phenoxyphenyl)-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
5-methyl-7-phenyl-N-(2-pyridin-4-ylethyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
>0.010
5-methyl-7-phenyl-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
5-methyl-7-phenyl-N-[3-(trifluoromethyl)phenyl]imidazo[5,1-f][1,2,4]triazin-2-amine
-
>0.010
5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
>0.010
5-methyl-7-[3-(trifluoromethyl)phenyl]-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
5-methyl-7-[4-(trifluoromethyl)phenyl]-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
5-methyl-N,7-diphenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
5-methyl-N-(3-morpholin-4-ylpropyl)-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
>0.010
5-methyl-N-(4-nitrophenyl)-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
5-pyrazolo[1,5-a]pyridin-3-yl-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
5-[2-(phenylamino)-1,3-thiazol-5-yl]-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
5-[2-[(phenylcarbonyl)amino]-1,3-thiazol-5-yl]-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
-
-
5-[6-(piperidin-4-yloxy)-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
5-[6-[(1-methylpiperidin-4-yl)methoxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
5-[6-[(1-methylpiperidin-4-yl)methoxy]-1H-benzo[3,4]cyclobuta[1,2-d]imidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
GSK326090A
5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
-
7-(2-bromophenyl)-5-methyl-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
7-(2-methoxyphenyl)-5-methyl-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
7-(3-bromophenyl)-5-methyl-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
7-(4-fluorophenyl)-5-methyl-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
-
-
7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5,7-dimethyl-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
-
7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1H-pyrazol-3-yl)-7,8-dihydropteridin-6(5H)-one
-
7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
-
7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-2-[5-(pyridin-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
-
7-ethyl-5-methyl-8-phenyl-2-(2-phenyl-1H-imidazol-1-yl)-7,8-dihydropteridin-6(5H)-one
-
7-ethyl-8-(4-fluorophenyl)-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
-
8-(3,3-difluorocyclopentyl)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
-
8-(biphenyl-2-ylamino)-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
8-(phenylamino)-1-(2,2,2-trifluoroethyl)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
8-(phenylamino)-1-(propan-2-yl)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
8-(phenylamino)-1-[2-(piperidin-1-yl)ethyl]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
8-[(2-acetylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
8-[(2-aminophenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
8-[(2-benzylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
8-[(2-carbamoylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
8-[(2-fluorophenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
8-[(2-methoxyphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
8-[(3-acetylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
8-[(3-methoxyphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
8-[(4-acetylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
8-[(4-methoxyphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
8-[[2-(acetylamino)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
8-[[2-acetyl-3-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
8-[[2-acetyl-4-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
8-[[2-acetyl-5-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
8-[[2-methoxy-4-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
8-[[2-methoxy-5-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
AG-013736
selective inhibition of PLK4 relative to PLK1-3
Asterless-A-13PM
phosphomimetic Asterless-A (13PM) inhibits isoform Plk4 activity by autophosphorylation of isoform Plk4 s kinase domain
-
ataxia-telangiectasia mutant
-
i.e. ATM, inhibits p53 phosphorylation by Plk1 in vivo
-
BAY 439006
selective inhibition of PLK4 relative to PLK1-3
Ca2+
-
5 mM Ca2+ inhibits the enzyme activity
CHIR-258
selectivity profile of PLK2/4 over PLK1/3; selectivity profile of PLK2/4 over PLK1/3
CP 547632
selective inhibition of PLK4 relative to PLK1-3
cyclic (-CH2-CO-Pro-Leu-His-Ser-pThr-Cys-S-)
-
cyclic [-CH2-CO-N[2-(1H-indol-3-yl)ethyl]-CH2-CO-Leu-His-Ser-pThr-NH-CH[CONH2]-CH2-S-]
-
cyclic [-CH2-CO-N[3-[[2-(1H-indol-3-yl)ethyl]amino]-3-oxopropyl]-CH2-CO-Leu-His-Ser-p-Thr-NH-CH[CONH2]-CH2-S-]
-
cyclic [-CH2-CO-N[6-[[2-(1-acetyl-1H-indol-3-yl)ethyl]amino]-6-oxohexyl]-CH2-CO-Leu-His-Ser-pThr-NH-CH[CONH2]-CH2-S-]
-
cyclic [-CH2-CO-N[6-[[2-(1-acetyl-1H-indol-3-yl)ethyl]amino]-6-oxohexyl]-CH2-CO-Leu-His[N3-(8-phenyloctyl)]-Ser-pThr-NH-CH[CONH2]-CH2-S-]
-
ethyl 1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxylate
-
FDPPLHSpTA
a PBIP1-derived phosphopeptide, the N-terminal phenylalanine sits in the hydrophobic pocket
genistein
-
decreases Plk1 expression
GO 6976
loses PLK1 activity by at least an order of magnitude, relative to staurosporine; loses PLK2 activity by at least an order of magnitude, relative to staurosporine; loses PLK3 activity by at least an order of magnitude, relative to staurosporine
H-1152
selective inhibition of PLK4 relative to PLK1-3
hesperadin
almost complete inhibition
imatinib
selective inhibition of PLK4 relative to PLK1-3
indirubin
-
decreases Plk1 expression
MAGPMQSpTPLNGAKK
the peptide inhibitor blocks the interaction between the Plk1 PBD and Cdc25C
Map205
-
Map205 can stabilize Polo and inhibit its cellular activity in vivo
-
matrimony
the matrimony protein acts as a negative regulator of polo during the later stages of G2 arrest during meiosis
-
methyl 2-[(3-carbamoyl-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazolin-8-yl)amino]benzoate
-
methyl 5-(5,6-dimethoxy-1H-benzo[3,4]cyclobuta[1,2-d]imidazol-1-yl)-3-[[2-(trifluoromethyl)phenyl]methoxy]thiophene-2-carboxylate
GSK1030058A
Mn2+
-
10 mM Ca2+ inhibits the enzyme activity, 5 mM is used in assay conditions
N,1-dimethyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-2-methylbenzamide
-
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-2-nitrobenzamide
-
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-4-chlorobenzylaniline
-
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-4-methoxybenzamide
-
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-4-methoxybenzylaniline
-
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-4-methylbenzamide
-
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-4-methylbenzylaniline
-
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-4-nitrobenzamide
-
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-4-nitrobenzylaniline
-
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-acetamide
-
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-benzamide
-
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-benzylaniline
-
N-(2-(3-(1H-indol-1-yl)propoxy)phenyl)-2-methylbenzamide
-
N-(2-(3-(1H-indol-1-yl)propoxy)phenyl)-2-nitrobenzamide
-
N-(2-(3-(1H-indol-1-yl)propoxy)phenyl)-4-methoxybenzamide
a highly selective inhibitor of Plk1, in vitro kinase inhibitory profile of 5i, overview
N-(2-(3-(1H-indol-1-yl)propoxy)phenyl)-4-nitrobenzamide
-
N-(2-(3-(1H-indol-1-yl)propoxy)phenyl)acetamide
-
N-(2-(3-(1H-indol-1-yl)propoxy)phenyl)benzamide
-
N-(2-(3-(1H-indol-1-yl)propoxy)phenyl)benzylaniline
-
N-(2-hydroxyethyl)-3-[3-(3-methyl-6-[[(1S)-1-phenylethyl]amino]-1H-pyrazolo[4,3-c]pyridin-1-yl)phenyl]propanamide
-
-
N-(26-(4-[(4-[[(7S)-8-cyclopentyl-7-ethyl-5-methyl-6-oxo-5,6,7,8-tetrahydropteridin-2-yl]amino]-3-methoxybenzoyl)amino]piperidin-1-yl)-19-oxo-3,6,9,12,15-pentaoxa-18-azahexacosan-1-oyl)glycyl-L-prolyl-L-leucyl-L-histidyl-L-seryl-O-phosphono-L-threonyl-L-alaninamide
-
N-(3,4-dimethoxyphenyl)-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
N-(3-(2-[(8-[4-[(4-[[(7S)-8-cyclopentyl-7-ethyl-5-methyl-6-oxo-5,6,7,8-tetrahydropteridin-2-yl]amino]-3-methoxybenzoyl)amino]piperidin-1-yl]octanoyl)amino]ethoxy)propanoyl)glycyl-L-prolyl-L-leucyl-L-histidyl-L-seryl-O-phosphono-L-threonyl-L-alaninamide
-
N-(3-methoxyphenyl)-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
N-(4-methoxyphenyl)-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
N-(48-(4-[(4-[[(7S)-8-cyclopentyl-7-ethyl-5-methyl-6-oxo-5,6,7,8-tetrahydropteridin-2-yl]amino]-3-methoxybenzoyl)amino]piperidin-1-yl)-41-oxo-4,7,10,13,16,19,22,25,28,31,34,37-dodecaoxa-40-azaoctatetracontan-1-oyl)glycyl-L-prolyl-L-leucyl-L-histidyl-L-seryl-O-phosphono-L-threonyl-L-alaninamide
-
N-(72-(4-[(4-[[(7S)-8-cyclopentyl-7-ethyl-5-methyl-6-oxo-5,6,7,8-tetrahydropteridin-2-yl]amino]-3-methoxybenzoyl)amino]piperidin-1-yl)-65-oxo-4,7,10,13,16,19,22,25,28,31,34,37,40,43,46,49,52,55,58,61-icosaoxa-64-azadoheptacontan-1-oyl)glycyl-L-prolyl-L-leucyl-L-histidyl-L-seryl-O-phosphono-L-threonyl-L-alaninamide
-
N-acetyl-N-(6-phenylhexyl)glycyl-L-leucyl-L-histidyl-L-seryl-O-phosphono-L-threoninamide
-
N-adamantylacetyl-L-prolyl-L-leucyl-L-histidyl-L-seryl-O-phosphono-L-threonyl-L-methioninamide
i.e PL-55, PLHSpT-based peptide
N-benzyl-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
N-cyclohexyl-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
>0.010
N-cyclopentyl-1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
N-cyclopropyl-1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
-
N-[(1S)-1-phenylethyl]-3-thiophen-2-ylisoxazolo[5,4-c]pyridin-5-amine
-
N-[2-(3-methyl-6-[[(1S)-1-phenylethyl]amino]-1H-pyrazolo[4,3-c]pyridin-1-yl)phenyl]-2-phenylacetamide
-
-
N-[2-methoxy-5-({[(E)-2-(2,4,6-trimethoxyphenyl)ethenyl]sulfonyl}methyl)phenyl]glycine
N-[3-(1-benzothiophen-2-yl)propanoyl]-alpha-aspartyl-L-prolyl-L-prolyl-L-leucyl-L-histidyl-L-seryl-O-phosphono-L-threonyl-L-alaninamide
-
N-[4-[(6-chloropyridin-3-yl)methoxy]-3-methoxybenzyl]-2-(3,4-dimethoxyphenyl)ethanamine
SBE13
N-[4-[2-(dimethylamino)ethoxy]phenyl]-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
-
-
NMS-P937
inhibition via binding in the ATP-binding site
ON01910
little inhibitory activity
ONO1910
does not significantly impacting Plk3 activity in vitro; inhibits Plk1 activity without significantly impacting Plk3 activity in vitro
PHA-680626
selective against Plk1
phenylmethylsulfonyl fluoride
-
-
PL-49
cyclohexylmethyl-PLHSpTM
purpurogallin
-
polo box inhibitor
silibinin
-
decreases Plk1 expression
SU11248
selective inhibition of PLK4 relative to PLK1-3
TAK960
little inhibitory activity
-
tert-butyl 1-methyl-2-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-4-oxo-1,4,6,7-tetrahydro-5H-pyrrolo[3,2-c]pyridine-5-carboxylate
-
trichostatin A
-
decreases Plk1 expression
Vanillin
-
decreases Plk1 expression
Volasertib
BI6727, inhibition via binding in the ATP-binding site
VX-680
selective inhibition of PLK4 relative to PLK1-3
[1-[2-hydroxy-3-(4-methylpiperazin-1-yl)propyl]-1H-indol-3-yl]acetic acid
a highly selective inhibitor of Plk1, poor inhibition of Plk2 and Plk3
[1-[2-hydroxy-3-(morpholin-4-yl)propyl]-1H-indol-3-yl]acetic acid
-
[1-[2-hydroxy-3-(piperidin-1-yl)propyl]-1H-indol-3-yl]acetic acid
-
[1-[2-hydroxy-3-(pyrrolidin-1-yl)propyl]-1H-indol-3-yl]acetic acid
-
[1-[3-(diethylamino)-2-hydroxypropyl]-1H-indol-3-yl]acetic acid
-
(4E)-4-(hydroxyimino)-5-methyl-2-(propan-2-yl)cyclohexa-2,5-dien-1-one
i.e. poloxime, PXE
(4E)-4-(hydroxyimino)-5-methyl-2-(propan-2-yl)cyclohexa-2,5-dien-1-one
-
(4E)-5-methyl-4-[[(2-methylbenzoyl)oxy]imino]-2-(propan-2-yl)cyclohexa-2,5-dien-1-one
-
(4E)-5-methyl-4-[[(2-methylbenzoyl)oxy]imino]-2-(propan-2-yl)cyclohexa-2,5-dien-1-one
poloxin
(4E)-5-methyl-4-{[(2-methylbenzoyl)oxy]imino}-2-(propan-2-yl)cyclohexa-2,5-dien-1-one
i.e. poloxin
(4E)-5-methyl-4-{[(2-methylbenzoyl)oxy]imino}-2-(propan-2-yl)cyclohexa-2,5-dien-1-one
-
1-acetyl-L-prolyl-L-leucyl-3-(8-phenyloctyl)-L-histidyl-L-seryl-O-phosphono-L-threoninamide
-
1-acetyl-L-prolyl-L-leucyl-3-(8-phenyloctyl)-L-histidyl-L-seryl-O-phosphono-L-threoninamide
-
2-methyl-5-(propan-2-yl)cyclohexa-2,5-diene-1,4-dione
i.e. thymoquinone
2-methyl-5-(propan-2-yl)cyclohexa-2,5-diene-1,4-dione
-
BI 2536
time-dependent inhibition; time-dependent inhibition; time-dependent inhibition of PLK1
BI 2536
-
potent and selective inhibitor of Plk1, delays prophase and entrance into prometaphase, initiates cyclin A destruction without degrading Emi1, leads to spindle-assembly-checkpoint-induced prometaphase arrest, prevents Plk1s enrichment at kinetochores and centrosomes, in metaphase cells induces detachment of microtubules from kinetochores and leads to spindle collapse, the inhibitor may serve as a powerful tool in mitosis research
BI 2536
remarkable potency and selectivity towards Plk1, HeLa cells treated with BI 2536 are first delayed in prophase, after reluctantly entering mitosis, cells become blocked in prometaphase with aberrant monopolar spindles that fail to attach stably to chromosomes
BI 2536
a dihydropteridinone and a ATP-competitive Plk1 inhibitor
BI 2536
inhibition via binding in the ATP-binding site
BI 6727
a ATP-competitive Plk1 inhibitor
BI-2536
potential anti-cancer therapeutic agent, shows strong selectivity for Plk1
BI-2536
blocks contractile ring assembly by preventing the localization of Rho and Rho-GEF without affecting the assembly of the central spindle
BI-2536
inhibits the wild-type enzyme but not mutant Plk1as
BI2536
-
-
BI6727
-
-
BTO-1
-
BTO-1
blocks contractile ring assembly by preventing the localization of Rho and Rho-GEF without affecting the assembly of the central spindle
GSK461364
-
GSK461364A
-
ATP-competitive inhibitor
GSK461364A
inhibition via binding in the ATP-binding site
GW843682X
-
-
GW843682X
potent inhibitor
GW843682X
little inhibitory activity
HMN-214
-
-
HMN-214
little inhibitory activity
LY294002
selective inhibition of PLK4 relative to PLK1-3
morin
-
-
morin
-
enzymatic inhibitor
N-[2-methoxy-5-({[(E)-2-(2,4,6-trimethoxyphenyl)ethenyl]sulfonyl}methyl)phenyl]glycine
i.e. ON01910, exhibits little activity against Plk1 in vitro, effective in inhibiting the cell proliferation
N-[2-methoxy-5-({[(E)-2-(2,4,6-trimethoxyphenyl)ethenyl]sulfonyl}methyl)phenyl]glycine
-
quercetin
-
-
quercetin
-
enzymatic inhibitor
RNA
RNA interference abrogates centrosome maturation, spindle bipolarization, and silencing of the spindle assembly checkpoint
RNA
-
downregulates PLK, in procyclic forms inhibition of kinetoplast division, in bloodstream form also delayed kinetoplast division, which is further observed to inhibit furrow ingression during cytokinesis
RNAi
induces Plk3 depletion, which causes a large fraction of cells to become quiescent, Plk3-depleted cells appear to pass through mitosis normally and complete cell division, but failed to reenter the cell cycle
-
RNAi
down-regulation of Plk1 protein level by ca. 90%, abolishes the mobility-shifted, hyperphosphorylated form of BubR1 in the prometaphase-arrested cells
-
RNAi
-
specific down-regulation of Plk1
-
SBE13
-
selective type II Plk1 inhibitor
scytonemin
-
scytonemin
-
enzymatic inhibitor
scytonemin
-
strongest inhibitory effect against Plk1 expression in mouse one-cell stage embryos, cleavage rate decreases and phosphorylation level of Tyr15 of Cdc2 increases
shRNA
-
-
shRNA
-
inhibits G2/M transition, cleavage rate decreases and phosphorylation level of Tyr15 of Cdc2 increases
-
siRNA
depletion of Plk1, which leads to loss of BubR1 hyperphosphorylation, but has no significant effects on BubR1 localization
-
siRNA
reduces serine phosphorylation of HsCdc14A but not HsCdc14 protein level
-
staurosporine
specific for PLK4
staurosporine
-
enzymatic inhibitor
thymoquinone
-
thymoquinone
-
polo box inhibitor
Wortmannin
-
Wortmannin
time-dependent irreversible inhibition with PLK1
Wortmannin
-
enzymatic inhibitor
additional information
Plk4 possesses an autoinhibitory mechanism mediated by a linker (L1) near the kinase domain, newly synthesized Plk4 is autoinhibited by L1. Autoinhibition is a conserved feature of Plks. In the case of Plk4, autoinhibition is relieved after homodimerization and is accomplished by PB3 and by autophosphorylation of L1. In contrast, autophosphorylation of the second linker promotes separation of the Plk4 homodimer. Mechanism for Plk4 autoinhibition, overview
-
additional information
-
Plk1 depletion in HeLa Plk RNAi cells by Aurora B inhibitor hesperadin, enzyme depletion delays entry into mitosis and arrest in prometaphase activating the spindle checkpoint
-
additional information
the kinase activity is regulated by the conserved C-terminal polo box domain which acts as both an autoinhibitory domain and a subcellular localization domain
-
additional information
-
the kinase activity is regulated by the conserved C-terminal polo box domain which acts as both an autoinhibitory domain and a subcellular localization domain
-
additional information
-
Plk1 expression is decreased during ciplatin-induced apoptosis while p53 is stabilized
-
additional information
-
in vivo inhibition of Plk1 by DNA damage is ATM- or ATR-dependent
-
additional information
-
Plk1 activity is inhibited upon DNA damage involving ATM or ATR, caffeine blocks the inhibition
-
additional information
GO 6976 retains PLK4 activity
-
additional information
GO 6976 retains PLK4 activity
-
additional information
GO 6976 retains PLK4 activity
-
additional information
GO 6976 retains PLK4 activity
-
additional information
inhibited by Plk1-specific antibodies
-
additional information
-
inhibited by Plk1-specific antibodies
-
additional information
1-NM-PP1 and 3-MB-PP1 have little effect on wild-type
-
additional information
-
1-NM-PP1 and 3-MB-PP1 have little effect on wild-type
-
additional information
design and synthesis of series of small-molecule non-ATP-competitive Plk1 inhibitors targeting the substrate-binding pocket are designed through rational drug design, molecular docking. Some comound are selective against inhibitory selectivity against polo kinases Plk2 and Plk3. Growth inhibition activity with HeLa and MCF-7 cells
-
additional information
identification of indole-3-carboxylic acids as non-ATP-competitive Plk1 inhibitors
-
additional information
the polo-box domain is unique to the five-member family of polo-like kinases, and its inhibition is sufficient to inhibit the enzyme. Small molecule and peptide-based inhibitors of the Plk1 polo-box domain, PBD, detailed overview
-
additional information
-
the enzyme activity is inhibited upon DNA damage
-
additional information
-
not inhibited by dithiothreitol
-
additional information
GSK479719A, albendazole, albendazole sulfoxide, MLN0905, HMN-214 and SBE13 display no inhibitory activity
-
additional information
-
GSK479719A, albendazole, albendazole sulfoxide, MLN0905, HMN-214 and SBE13 display no inhibitory activity
-
additional information
-
only simultaneous mutation of both motifs 192RSST195 and 333RLST336 of Emi2 abrogates polo box domain binding of Plx1
-
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0.00256
(1R)-1-[(3S,6S,9S,12S,15S)-19-(6-[[2-(1-acetyl-1H-indol-3-yl)ethyl]amino]-6-oxohexyl)-3-carbamoyl-9-(hydroxymethyl)-12-(1H-imidazol-5-ylmethyl)-15-(2-methylpropyl)-5,8,11,14,17,20-hexaoxo-1-thia-4,7,10,13,16,19-hexaazacyclohenicosan-6-yl]ethyl phosphate
Homo sapiens
pH and temperature not specified in the publication
-
0.00108
(1R)-1-[(3S,6S,9S,12S,15S)-19-(6-[[2-(1-acetyl-1H-indol-3-yl)ethyl]amino]-6-oxohexyl)-3-carbamoyl-9-(hydroxymethyl)-15-(2-methylpropyl)-5,8,11,14,17,20-hexaoxo-12-[[1-(9-phenylnonyl)-1H-imidazol-5-yl]methyl]-1-thia-4,7,10,13,16,19-hexaazacyclohenicosan-6-yl]ethyl phosphate
Homo sapiens
pH and temperature not specified in the publication
0.0032
(2Z)-2-(5-bromo-2-methoxybenzylidene)-6-methyl-7H-[1,3]thiazolo[3,2-b][1,2,4]triazine-3,7(2H)-dione
Homo sapiens
pH and temperature not specified in the publication
0.00041
(3-[5-methyl-2-[(3,4,5-trimethoxyphenyl)amino]imidazo[5,1-f][1,2,4]triazin-7-yl]phenyl)(phenyl)methanone
Mammalia
-
-
0.0045
(3S)-4-amino-4-oxo-3-([[2-(4-phenylbutyl)-1-(2-phenylethyl)-1H-benzimidazol-5-yl]carbonyl]amino)butan-2-yl phosphate
Homo sapiens
pH and temperature not specified in the publication
0.00114 - 0.00136
(4E)-5-methyl-4-[[(2-methylbenzoyl)oxy]imino]-2-(propan-2-yl)cyclohexa-2,5-dien-1-one
0.000014
(4R)-1-acetyl-4-(4-phenylbutoxy)prolyl-L-leucyl-L-histidyl-L-seryl-O-phosphono-L-threoninamide
Homo sapiens
pH and temperature not specified in the publication
122
(4R)-1-acetyl-4-[[(E)-(3-phenylpropylidene)amino]oxy]prolyl-L-leucyl-L-histidyl-L-seryl-O-phosphono-L-threoninamide
Homo sapiens
pH and temperature not specified in the publication
0.000103 - 0.00126
(7R)-2-[5-(2,4-difluorophenyl)-1H-pyrazol-4-yl]-7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
0.000007 - 0.00135
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-3-yl)-7,8-dihydropteridin-6(5H)-one
0.000021 - 0.00327
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
0.000532 - 0.0288
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-5-yl)-7,8-dihydropteridin-6(5H)-one
0.000012 - 0.00867
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
0.000042 - 0.00355
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
0.00104
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(oxetan-3-yl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000033 - 0.00753
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-[(3S)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
0.000009 - 0.00025
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
0.000025 - 0.00087
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(propan-2-yl)-7,8-dihydropteridin-6(5H)-one
0.000044 - 0.00776
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(pyrimidin-5-yl)-7,8-dihydropteridin-6(5H)-one
0.000021 - 0.00048
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-[(3R)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
0.000008 - 0.00038
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-[(3S)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
0.000092 - 0.00303
(7R)-7-ethyl-5-methyl-8-(1H-pyrazol-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
0.000036 - 0.00025
(7R)-7-ethyl-5-methyl-8-(tetrahydro-2H-pyran-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
0.000039 - 0.00141
(7R)-7-ethyl-5-methyl-8-(tetrahydrofuran-3-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
0.000012 - 0.00939
(7R)-8-(3,3-difluorocyclobutyl)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
0.01
1-(1-methylpiperidin-4-yl)-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
larger than 0.010, pH 7.9, 25°C
0.004516
1-(2-fluorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
Danio rerio
-
-
0.000102
1-(2-hydroxyethyl)-2-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1,5,6,7-tetrahydro-4H-pyrrolo[3,2-c]pyridin-4-one
Homo sapiens
pH and temperature not specified in the publication
0.000151
1-(2-hydroxyethyl)-5-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1H-pyrrole-3-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.01445
1-(2-methoxyphenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
Danio rerio
-
-
0.38
1-(26-oxo-2,5,8,11,14,17,20,23-octaoxahexacosan-26-yl)-L-prolyl-L-leucyl-3-(8-phenyloctyl)-L-histidyl-L-seryl-(3R)-4-phosphono-L-valinamide
Homo sapiens
pH and temperature not specified in the publication
0.000641
1-(3,5-dichlorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
Danio rerio
-
-
0.000149
1-(3,5-dimethylphenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
Danio rerio
-
-
0.000274
1-(3-bromo-5-chlorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
Danio rerio
-
-
0.000121
1-(3-chlorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
Danio rerio
-
-
0.000464
1-(3-fluorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
Danio rerio
-
-
0.005928
1-(3-methoxyphenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
Danio rerio
-
-
0.003241
1-(4-fluorophenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
Danio rerio
-
-
0.000703
1-(4-methoxyphenyl)-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
Danio rerio
-
-
0.009
1-acetyl-L-prolyl-L-leucyl-3-(5-[[(Z)-benzylideneamino]oxy]pentyl)-L-histidyl-L-seryl-O-phosphono-L-threoninamide
Homo sapiens
at pH 7.4 and 25°C
0.00505
1-acetyl-L-prolyl-L-leucyl-3-(6-[[(Z)-benzylideneamino]oxy]hexyl)-L-histidyl-L-seryl-O-phosphono-L-threoninamide
Homo sapiens
at pH 7.4 and 25°C
0.0000025 - 0.000121
1-acetyl-L-prolyl-L-leucyl-3-(8-phenyloctyl)-L-histidyl-L-seryl-O-phosphono-L-threoninamide
0.085
1-acetyl-L-prolyl-L-leucyl-3-[3-(2-hydroxyethyl)-1-(8-phenyloctyl)-1H-imidazol-3-ium-5-yl]-L-alanyl-L-seryl-O-phosphono-L-threoninamide
Homo sapiens
pH and temperature not specified in the publication
0.055
1-acetyl-L-prolyl-L-leucyl-3-[3-(2-hydroxyethyl)-1-(8-phenyloctyl)-1H-imidazol-3-ium-5-yl]-L-alanyl-L-seryl-O-[[[(2,2-dimethylpropanoyl)oxy]methoxy](hydroxy)phosphoryl]-L-threoninamide
Homo sapiens
pH and temperature not specified in the publication
0.00155
1-acetyl-L-prolyl-L-leucyl-3-[5-([(Z)-[(2-fluoro-6-phenoxyphenyl)methylidene]amino]oxy)pentyl]-L-histidyl-L-seryl-O-phosphono-L-threoninamide
Homo sapiens
at pH 7.4 and 25°C
0.000139
1-acetyl-L-prolyl-L-leucyl-3-[6-(2-phenoxyphenyl)hexyl]-L-histidyl-L-seryl-O-phosphono-L-threoninamide
Homo sapiens
at pH 7.4 and 25°C
0.00067
1-acetyl-L-prolyl-L-leucyl-3-[6-([(Z)-[(2-fluoro-6-phenoxyphenyl)methylidene]amino]oxy)hexyl]-L-histidyl-L-seryl-O-phosphono-L-threoninamide
Homo sapiens
at pH 7.4 and 25°C
0.000066
1-acetyl-L-prolyl-L-leucyl-3-[8-(2-fluoro-6-phenoxyphenyl)octyl]-L-histidyl-L-seryl-O-phosphono-L-threoninamide
Homo sapiens
at pH 7.4 and 25°C
0.000052
1-acetyl-L-prolyl-L-leucyl-3-[8-(2-phenoxyphenyl)octyl]-L-histidyl-L-seryl-O-phosphono-L-threoninamide
Homo sapiens
at pH 7.4 and 25°C
0.000043
1-acetyl-L-prolyl-L-leucyl-3-[8-([1,1'-biphenyl]-2-yl)octyl]-L-histidyl-L-seryl-O-phosphono-L-threoninamide
Homo sapiens
at pH 7.4 and 25°C
0.000032
1-acetyl-L-prolyl-L-leucyl-3-[8-[2-(benzyloxy)phenyl]octyl]-L-histidyl-L-seryl-O-phosphono-L-threoninamide
Homo sapiens
at pH 7.4 and 25°C
0.000139
1-acetyl-L-prolyl-L-leucyl-3-[9-(2-fluoro-6-phenoxyphenyl)nonyl]-L-histidyl-L-seryl-O-phosphono-L-threoninamide
Homo sapiens
at pH 7.4 and 25°C
0.3
1-acetyl-L-prolyl-L-leucyl-L-histidyl-L-seryl-O-phosphono-L-threoninamide
Homo sapiens
IC50 above 0.3 mM, at pH 7.4 and 25°C
0.000143
1-cyclohexyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000009
1-methyl-2-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1,5,6,7-tetrahydro-4H-pyrrolo[3,2-c]pyridin-4-one
Homo sapiens
pH and temperature not specified in the publication
0.000015
1-methyl-5-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1H-pyrrole-3-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000018
1-methyl-5-(2-[[5-(piperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1H-pyrrole-3-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000009 - 0.000068
1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
0.00011
1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxylic acid
Homo sapiens
pH 7.9, 25°C
0.000002 - 0.000015
1-methyl-8-[(2-methylphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
0.000488
1-methyl-8-[(2-nitrophenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000051 - 0.002666
1-methyl-8-[(2-phenoxyphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
0.003733
1-methyl-8-[(2-sulfamoylphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.01
1-methyl-8-[(3-nitrophenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
larger than 0.010, pH 7.9, 25°C
0.01
1-methyl-8-[(4-nitrophenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
larger than 0.010, pH 7.9, 25°C
0.000011 - 0.00011
1-methyl-8-[[2-(methylamino)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
0.000014 - 0.000097
1-methyl-8-[[2-(methylsulfanyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
0.000949
1-methyl-8-[[2-(phenylamino)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.001969
1-methyl-8-[[2-(phenylcarbonyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.002033
1-methyl-8-[[2-(phenylsulfanyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000146 - 0.000509
1-methyl-8-[[2-(propan-2-yl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
0.000095 - 0.000432
1-methyl-8-[[2-(trifluoromethyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
0.000051
1-methyl-8-[[3-(trifluoromethyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000872
1-methyl-8-[[4-(trifluoromethyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.01
1-methyl-N-phenyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
larger than 0.010, pH 7.9, 25°C
0.01
1-phenyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
larger than 0.010, pH 7.9, 25°C
0.00347
1-[2-hydroxy-3-(4-methylpiperazin-1-yl)propyl]-1H-indole-3-carboxylic acid
Homo sapiens
pH 7.5, 30°C
0.0021
1-[2-hydroxy-3-(piperidin-1-yl)propyl]-1H-indole-3-carboxylic acid
Homo sapiens
pH 7.5, 30°C
0.00484
1-[2-hydroxy-3-(pyrrolidin-1-yl)propyl]-1H-indole-3-carboxylic acid
Homo sapiens
pH 7.5, 30°C
0.000059
1-[3-(3-aminopropyl)phenyl]-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
Danio rerio
-
-
0.00191
1-[3-(diethylamino)-2-hydroxypropyl]-1H-indole-3-carboxylic acid
Homo sapiens
pH 7.5, 30°C
0.000977
1-[3-(dimethylamino)phenyl]-3-methyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
Danio rerio
-
-
0.00115 - 0.0253
2'-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5'-methyl-8'-(propan-2-yl)-5',8'-dihydro-6'H-spiro[cyclobutane-1,7'-pteridin]-6'-one
0.000028
2-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1-(2,2,2-trifluoroethyl)-1,5,6,7-tetrahydro-4H-pyrrolo[3,2-c]pyridin-4-one
Homo sapiens
pH and temperature not specified in the publication
0.00218
2-methyl-5-(propan-2-yl)cyclohexa-2,5-diene-1,4-dione
Homo sapiens
pH 7.5, 30°C
0.00271
2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5,7,7-trimethyl-8-(propan-2-yl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00012 - 0.00348
2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7-(2,2,2-trifluoroethyl)-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
0.000004 - 0.000214
3-(1,3-benzodioxol-5-yl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
0.00002
3-(1-[2-chloro-4-[(3-hydroxypyrrolidin-1-yl)methyl]phenyl]ethoxy)-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.005689
3-(2-methylcyclohexyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Homo sapiens
-
0.004927
3-(3,4-dimethoxyphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Homo sapiens
-
0.00033
3-(3,4-dimethylphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Homo sapiens
-
0.000625
3-(3-chlorophenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Homo sapiens
-
0.000412
3-(3-methyl-6-[[(1S)-1-phenylethyl]amino]-1H-pyrazolo[4,3-c]pyridin-1-yl)benzonitrile
Danio rerio
-
-
0.000549 - 0.01
3-(3-methylphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
0.00117
3-(4-methylphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Homo sapiens
-
0.000779
3-(4-methylthiophen-3-yl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Homo sapiens
-
0.02
3-benzyl-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Homo sapiens
>0.020
0.007685
3-methyl-1-(2-methylphenyl)-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
Danio rerio
-
-
0.000474
3-methyl-1-(3-methylphenyl)-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
Danio rerio
-
-
0.004528
3-methyl-1-(4-methylphenyl)-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
Danio rerio
-
-
0.001301
3-methyl-1-phenyl-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
Danio rerio
-
-
0.001476
3-methyl-1-[3-(1-methylethyl)phenyl]-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
Danio rerio
-
-
0.000225
3-methyl-1-[3-(methylsulfonyl)phenyl]-N-[(1S)-1-phenylethyl]-1H-pyrazolo[4,3-c]pyridin-6-amine
Danio rerio
-
-
0.001616
3-phenyl-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Homo sapiens
-
0.000028
3-[(1R)-1-(2-chloro-4-[[(1-methylethyl)amino]methyl]phenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.000023
3-[(1R)-1-(2-chloro-4-[[(2-hydroxy-1,1-dimethylethyl)amino]methyl]phenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.000021
3-[(1R)-1-(2-chloro-4-[[(2-hydroxyethyl)amino]methyl]phenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.000019
3-[(1R)-1-(2-chloro-4-[[(3-hydroxypropyl)amino]methyl]phenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.0000008 - 0.000025
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
0.000001 - 0.000321
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-methoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
0.000001 - 0.000073
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(2R)-2,3-dihydroxypropyl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
0.000003 - 0.00061
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(2R)-2-hydroxy-3-pyrrolidin-1-ylpropyl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
0.000004 - 0.00025
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(4R)-1-methylazepan-4-yl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
0.000003 - 0.00024
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(4S)-1-methylazepan-4-yl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
0.000007
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.0000073
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-(hydroxymethyl)imidazo[1,2-a]pyridin-3-yl]thiophene-2-carboxamide
Mammalia
-
-
0.000006 - 0.0011
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)methoxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
0.000002 - 0.00063
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
0.000004 - 0.00046
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[3-(dimethylamino)propoxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
0.000088
3-[(1R)-1-[2-(hydroxymethyl)phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.0000049
3-[(1R)-1-[2-chloro-4-(hydroxymethyl)phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.000016
3-[(1R)-1-[2-chloro-4-[(1,1-dioxidothiomorpholin-4-yl)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.000012
3-[(1R)-1-[2-chloro-4-[(3-oxopiperazin-1-yl)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.000013
3-[(1R)-1-[2-chloro-4-[(4-fluoropiperidin-1-yl)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.000027
3-[(1R)-1-[2-chloro-4-[(4-hydroxypiperidin-1-yl)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.000017
3-[(1R)-1-[2-chloro-4-[(4-methylpiperazin-1-yl)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.000025
3-[(1R)-1-[2-chloro-4-[(cyclopentylamino)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.000012
3-[(1R)-1-[2-chloro-4-[(cyclopropylamino)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.000022
3-[(1R)-1-[2-chloro-4-[(dimethylamino)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.000021
3-[(1R)-1-[2-chloro-4-[(ethylamino)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.000016
3-[(1R)-1-[2-chloro-4-[(methylamino)methyl]phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.0000098
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-(difluoromethoxy)phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.00002
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-(difluoromethyl)phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.000021
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-chlorophenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.00021
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-cyclopropylphenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.000046
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-fluorophenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.00015
3-[(1R)-1-[4-[(tert-butylamino)methyl]-2-methylphenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.00003 - 0.000994
3-[(1S)-1-(2-chlorophenyl)ethoxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
0.0003
3-[(1S)-1-(2-chlorophenyl)ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.000002 - 0.00114
3-[(2-chlorobenzyl)oxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
0.000035
3-[(2-chlorobenzyl)oxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.000092
3-[1-(2-chlorophenyl)ethoxy]-5-[7-(hydroxymethyl)imidazo[1,2-a]pyridin-3-yl]thiophene-2-carboxamide
Mammalia
-
-
0.007479
3-[1-(5-[[(1S)-1-phenylethyl]amino]isoxazolo[5,4-c]pyridin-3-yl)piperidin-3-yl]propanamide
Homo sapiens
-
0.000039
3-[1-[2-chloro-5-(hydroxymethyl)phenyl]ethoxy]-5-imidazo[1,2-a]pyridin-3-ylthiophene-2-carboxamide
Mammalia
-
-
0.00571
3-[1-[2-hydroxy-3-(piperidin-1-yl)propyl]-1H-indol-3-yl]propanoic acid
Homo sapiens
pH 7.5, 30°C
0.0029
3-[1-[2-hydroxy-3-(pyrrolidin-1-yl)propyl]-1H-indol-3-yl]propanoic acid
Homo sapiens
pH 7.5, 30°C
0.000032
3-[3-(3-methyl-6-[[(1S)-1-phenylethyl]amino]-1H-pyrazolo[4,3-c]pyridin-1-yl)phenyl]propanamide
Danio rerio
-
-
0.000021
3-[3-(3-methyl-6-[[(1S)-1-phenylethyl]amino]-1H-pyrazolo[4,3-c]pyridin-1-yl)phenyl]propanoic acid
Danio rerio
-
-
0.000099
3-[3-chloro-5-(5-[[(1S)-1-phenylethyl]amino]isoxazolo[5,4-c]pyridin-3-yl)phenyl]propan-1-ol
Homo sapiens
-
0.000051 - 0.001382
3-[3-chloro-5-(5-[[(1S)-1-phenylethyl]amino]isoxazolo[5,4-c]pyridin-3-yl)phenyl]propanamide
0.00000083
4-((R)-8-cyclopentyl-7-ethyl-5-methyl-6-oxo-5,6,7,8-tetrahydro-pteridin-2-ylamino)-3-methoxy-N-(1-methyl-piperidin-4-yl)-benzamide
Homo sapiens
-
0.00274
4-[(5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-yl)amino]benzenesulfonamide
Mammalia
-
-
0.000031 - 0.00376
4-[7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-6-oxo-6,7-dihydropteridin-8(5H)-yl]benzonitrile
0.00043
5-(1-methyl-1H-imidazol-5-yl)-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
Mammalia
-
-
0.000035
5-(1H-benzimidazol-1-yl)-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
Mammalia
-
-
0.003
5-(2-amino-1,3-thiazol-5-yl)-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
Mammalia
-
larger than 0.003
0.0000018
5-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1-(2,2,2-trifluoroethyl)-1H-pyrrole-3-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000272
5-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-1-[2-(tetrahydro-2H-pyran-4-yloxy)ethyl]-1H-pyrrole-3-carboxamide
Homo sapiens
pH and temperature not specified in the publication
0.000002 - 0.000009
5-(5,6-dimethoxy-1H-benzimidazol-1-yl)-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
0.0000022 - 0.0013
5-(5,6-dimethoxy-1H-benzimidazole-1-yl)-3-[2-(trifluoromethyl)-benzyloxy]-thiophene-2-carboxamide
0.000003 - 0.000476
5-(6-methoxy-1H-benzimidazol-1-yl)-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
0.000022
5-imidazo[1,2-a]pyridin-3-yl-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
Mammalia
-
-
0.00198
5-methyl-7-(2-nitrophenyl)-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
-
0.0005
5-methyl-7-(3-phenoxyphenyl)-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
-
0.01
5-methyl-7-phenyl-N-(2-pyridin-4-ylethyl)imidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
>0.010
0.00004
5-methyl-7-phenyl-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
-
0.01
5-methyl-7-phenyl-N-[3-(trifluoromethyl)phenyl]imidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
>0.010
0.01
5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
>0.010
0.00003
5-methyl-7-[3-(trifluoromethyl)phenyl]-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
-
0.00106
5-methyl-7-[4-(trifluoromethyl)phenyl]-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
-
0.0012
5-methyl-N,7-diphenylimidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
-
0.01
5-methyl-N-(3-morpholin-4-ylpropyl)-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
>0.010
0.00281
5-methyl-N-(4-nitrophenyl)-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
-
0.00013
5-pyrazolo[1,5-a]pyridin-3-yl-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
Mammalia
-
-
0.003
5-[2-(phenylamino)-1,3-thiazol-5-yl]-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
Mammalia
-
larger than 0.003
0.0021
5-[2-[(phenylcarbonyl)amino]-1,3-thiazol-5-yl]-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
Mammalia
-
-
0.000003 - 0.00035
5-[6-(piperidin-4-yloxy)-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
0.000007 - 0.00055
5-[6-[(1-methylpiperidin-4-yl)methoxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
0.000002 - 0.00027
5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
0.00267
7-(2-bromophenyl)-5-methyl-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
-
0.00566
7-(2-methoxyphenyl)-5-methyl-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
-
0.00007
7-(3-bromophenyl)-5-methyl-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
-
0.00008
7-(4-fluorophenyl)-5-methyl-N-(3,4,5-trimethoxyphenyl)imidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
-
0.00003 - 0.00716
7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5,7-dimethyl-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
0.000009 - 0.00342
7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1H-pyrazol-3-yl)-7,8-dihydropteridin-6(5H)-one
0.00013 - 0.00182
7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
0.000168 - 0.00182
7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-2-[5-(pyridin-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
0.000017 - 0.00283
7-ethyl-5-methyl-8-phenyl-2-(2-phenyl-1H-imidazol-1-yl)-7,8-dihydropteridin-6(5H)-one
0.000015 - 0.00234
7-ethyl-8-(4-fluorophenyl)-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
0.000013 - 0.00032
8-(3,3-difluorocyclopentyl)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
0.001565
8-(biphenyl-2-ylamino)-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000006
8-(phenylamino)-1-(2,2,2-trifluoroethyl)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.00043
8-(phenylamino)-1-(propan-2-yl)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.01
8-(phenylamino)-1-[2-(piperidin-1-yl)ethyl]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
larger than 0.010, pH 7.9, 25°C
0.000248
8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000103 - 0.000346
8-[(2-acetylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
0.000012 - 0.00015
8-[(2-aminophenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
0.000943
8-[(2-benzylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.002076
8-[(2-carbamoylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000027 - 0.000125
8-[(2-fluorophenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
0.000013 - 0.000042
8-[(2-methoxyphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
0.0001
8-[(3-acetylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000135
8-[(3-methoxyphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000197
8-[(4-acetylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000256
8-[(4-methoxyphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000049 - 0.002523
8-[[2-(acetylamino)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
0.002051 - 0.01
8-[[2-acetyl-3-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
0.000464 - 0.01
8-[[2-acetyl-4-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
0.000109 - 0.01
8-[[2-acetyl-5-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
0.00004 - 0.000082
8-[[2-methoxy-4-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
0.000007 - 0.00045
8-[[2-methoxy-5-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
0.00000087
BI 6727
Homo sapiens
pH 7.5, 30°C
0.0008
BI-2536
Homo sapiens
-
0.0000008
BI2536
Homo sapiens
-
-
0.00000087
BI6727
Homo sapiens
-
-
0.008
BTO-1
Homo sapiens
-
0.0098
cyclic (-CH2-CO-Pro-Leu-His-Ser-pThr-Cys-S-)
Homo sapiens
25°C, pH not specified in the publication
0.0085
cyclic [-CH2-CO-N[2-(1H-indol-3-yl)ethyl]-CH2-CO-Leu-His-Ser-pThr-NH-CH[CONH2]-CH2-S-]
Homo sapiens
25°C, pH not specified in the publication
0.0048
cyclic [-CH2-CO-N[3-[[2-(1H-indol-3-yl)ethyl]amino]-3-oxopropyl]-CH2-CO-Leu-His-Ser-p-Thr-NH-CH[CONH2]-CH2-S-]
Homo sapiens
25°C, pH not specified in the publication
0.0026
cyclic [-CH2-CO-N[6-[[2-(1-acetyl-1H-indol-3-yl)ethyl]amino]-6-oxohexyl]-CH2-CO-Leu-His-Ser-pThr-NH-CH[CONH2]-CH2-S-]
Homo sapiens
25°C, pH not specified in the publication
0.0011
cyclic [-CH2-CO-N[6-[[2-(1-acetyl-1H-indol-3-yl)ethyl]amino]-6-oxohexyl]-CH2-CO-Leu-His[N3-(8-phenyloctyl)]-Ser-pThr-NH-CH[CONH2]-CH2-S-]
Homo sapiens
25°C, pH not specified in the publication
0.01
ethyl 1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxylate
Homo sapiens
larger than 0.010, pH7.9, 25°C
0.00000005
GSK461364A
Homo sapiens
-
less than 50 nM
0.00525
LY294002
Homo sapiens
-
-
0.001117
methyl 2-[(3-carbamoyl-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazolin-8-yl)amino]benzoate
Homo sapiens
pH 7.9, 25°C
0.004215
N,1-dimethyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.0026
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-2-methylbenzamide
Homo sapiens
pH 7.5, 30°C
0.01
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-2-nitrobenzamide
Homo sapiens
pH 7.5, 30°C
0.00322
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-4-chlorobenzylaniline
Homo sapiens
pH 7.5, 30°C
0.00093
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-4-methoxybenzamide
Homo sapiens
pH 7.5, 30°C
0.00205
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-4-methoxybenzylaniline
Homo sapiens
pH 7.5, 30°C
0.00709
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-4-methylbenzamide
Homo sapiens
pH 7.5, 30°C
0.00466
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-4-methylbenzylaniline
Homo sapiens
pH 7.5, 30°C
0.01
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-4-nitrobenzamide
Homo sapiens
pH 7.5, 30°C
0.01
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-4-nitrobenzylaniline
Homo sapiens
pH 7.5, 30°C
0.00683
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-acetamide
Homo sapiens
pH 7.5, 30°C
0.00633
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-benzamide
Homo sapiens
pH 7.5, 30°C
0.00948
N-(2-(3-(1H-benzo[d]imidazol-1-yl)propoxy)phenyl)-benzylaniline
Homo sapiens
pH 7.5, 30°C
0.00559
N-(2-(3-(1H-indol-1-yl)propoxy)phenyl)-2-methylbenzamide
Homo sapiens
pH 7.5, 30°C
0.01
N-(2-(3-(1H-indol-1-yl)propoxy)phenyl)-2-nitrobenzamide
Homo sapiens
pH 7.5, 30°C
0.00068
N-(2-(3-(1H-indol-1-yl)propoxy)phenyl)-4-methoxybenzamide
Homo sapiens
pH 7.5, 30°C
0.01
N-(2-(3-(1H-indol-1-yl)propoxy)phenyl)-4-nitrobenzamide
Homo sapiens
pH 7.5, 30°C
0.0047
N-(2-(3-(1H-indol-1-yl)propoxy)phenyl)acetamide
Homo sapiens
pH 7.5, 30°C
0.01
N-(2-(3-(1H-indol-1-yl)propoxy)phenyl)benzamide
Homo sapiens
pH 7.5, 30°C
0.00702
N-(2-(3-(1H-indol-1-yl)propoxy)phenyl)benzylaniline
Homo sapiens
pH 7.5, 30°C
0.000048
N-(2-hydroxyethyl)-3-[3-(3-methyl-6-[[(1S)-1-phenylethyl]amino]-1H-pyrazolo[4,3-c]pyridin-1-yl)phenyl]propanamide
Danio rerio
-
-
0.00009
N-(3,4-dimethoxyphenyl)-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
-
0.0003
N-(3-methoxyphenyl)-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
-
0.00068
N-(4-methoxyphenyl)-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
-
0.00082
N-adamantylacetyl-L-prolyl-L-leucyl-L-histidyl-L-seryl-O-phosphono-L-threonyl-L-methioninamide
Homo sapiens
pH and temperature not specified in the publication
0.0015
N-benzyl-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
-
0.01
N-cyclohexyl-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
>0.010
0.01
N-cyclopentyl-1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
larger than 0.010, pH 7.9, 25°C
0.01
N-cyclopropyl-1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
larger than 0.010, pH 7.9, 25°C
0.003007
N-[(1S)-1-phenylethyl]-3-thiophen-2-ylisoxazolo[5,4-c]pyridin-5-amine
Homo sapiens
-
0.000207
N-[2-(3-methyl-6-[[(1S)-1-phenylethyl]amino]-1H-pyrazolo[4,3-c]pyridin-1-yl)phenyl]-2-phenylacetamide
Danio rerio
-
-
0.00025
N-[3-(1-benzothiophen-2-yl)propanoyl]-alpha-aspartyl-L-prolyl-L-prolyl-L-leucyl-L-histidyl-L-seryl-O-phosphono-L-threonyl-L-alaninamide
Homo sapiens
pH and temperature not specified in the publication
0.0000002
N-[4-[(6-chloropyridin-3-yl)methoxy]-3-methoxybenzyl]-2-(3,4-dimethoxyphenyl)ethanamine
Homo sapiens
-
0.00038
N-[4-[2-(dimethylamino)ethoxy]phenyl]-5-methyl-7-phenylimidazo[5,1-f][1,2,4]triazin-2-amine
Mammalia
-
-
0.00034 - 0.00053
PHA-680626
0.0018
PL-42
Homo sapiens
pH and temperature not specified in the publication
0.00036
PL-49
Homo sapiens
pH and temperature not specified in the publication
0.0000002
SBE13
Homo sapiens
-
immunoprecipitated Plk1 from HeLa cells
0.0008
staurosporine
Mammalia
-
-
0.000817
tert-butyl 1-methyl-2-(2-[[5-(4-methylpiperazin-1-yl)-2-(trifluoromethoxy)phenyl]amino]pyrimidin-4-yl)-4-oxo-1,4,6,7-tetrahydro-5H-pyrrolo[3,2-c]pyridine-5-carboxylate
Homo sapiens
pH and temperature not specified in the publication
0.00218
thymoquinone
Homo sapiens
pH 7.5, 30°C
0.00188
[1-[2-hydroxy-3-(4-methylpiperazin-1-yl)propyl]-1H-indol-3-yl]acetic acid
Homo sapiens
pH 7.5, 30°C
0.00096
[1-[2-hydroxy-3-(morpholin-4-yl)propyl]-1H-indol-3-yl]acetic acid
Homo sapiens
pH 7.5, 30°C
0.00041
[1-[2-hydroxy-3-(piperidin-1-yl)propyl]-1H-indol-3-yl]acetic acid
Homo sapiens
pH 7.5, 30°C
0.00013
[1-[2-hydroxy-3-(pyrrolidin-1-yl)propyl]-1H-indol-3-yl]acetic acid
Homo sapiens
pH 7.5, 30°C
0.00264
[1-[3-(diethylamino)-2-hydroxypropyl]-1H-indol-3-yl]acetic acid
Homo sapiens
pH 7.5, 30°C
additional information
additional information
Homo sapiens
IC50 values for cell growth inhibition of HeLa and MCF-7 cells
-
0.00114
(4E)-5-methyl-4-[[(2-methylbenzoyl)oxy]imino]-2-(propan-2-yl)cyclohexa-2,5-dien-1-one
Homo sapiens
pH and temperature not specified in the publication
0.00136
(4E)-5-methyl-4-[[(2-methylbenzoyl)oxy]imino]-2-(propan-2-yl)cyclohexa-2,5-dien-1-one
Homo sapiens
pH and temperature not specified in the publication
0.000103
(7R)-2-[5-(2,4-difluorophenyl)-1H-pyrazol-4-yl]-7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00126
(7R)-2-[5-(2,4-difluorophenyl)-1H-pyrazol-4-yl]-7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000007
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-3-yl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00135
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-3-yl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000021
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00327
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000532
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-5-yl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.0288
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1-methyl-1H-pyrazol-5-yl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000012
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00867
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1H-pyrazol-4-yl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000042
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00355
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000033
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-[(3S)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00753
(7R)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-[(3S)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000009
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00025
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000025
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(propan-2-yl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00087
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(propan-2-yl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000044
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(pyrimidin-5-yl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00776
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-(pyrimidin-5-yl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000021
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-[(3R)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00048
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-[(3R)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000008
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-[(3S)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00038
(7R)-7-ethyl-5-methyl-2-(2-phenyl-1H-imidazol-1-yl)-8-[(3S)-tetrahydrofuran-3-yl]-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000092
(7R)-7-ethyl-5-methyl-8-(1H-pyrazol-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00303
(7R)-7-ethyl-5-methyl-8-(1H-pyrazol-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000036
(7R)-7-ethyl-5-methyl-8-(tetrahydro-2H-pyran-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00025
(7R)-7-ethyl-5-methyl-8-(tetrahydro-2H-pyran-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000039
(7R)-7-ethyl-5-methyl-8-(tetrahydrofuran-3-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00141
(7R)-7-ethyl-5-methyl-8-(tetrahydrofuran-3-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000012
(7R)-8-(3,3-difluorocyclobutyl)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00939
(7R)-8-(3,3-difluorocyclobutyl)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.0000025 - 0.000017
1-acetyl-L-prolyl-L-leucyl-3-(8-phenyloctyl)-L-histidyl-L-seryl-O-phosphono-L-threoninamide
Homo sapiens
pH and temperature not specified in the publication
0.000121
1-acetyl-L-prolyl-L-leucyl-3-(8-phenyloctyl)-L-histidyl-L-seryl-O-phosphono-L-threoninamide
Homo sapiens
at pH 7.4 and 25°C
0.000009
1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000014
1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000068
1-methyl-8-(phenylamino)-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000002
1-methyl-8-[(2-methylphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000006
1-methyl-8-[(2-methylphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000015
1-methyl-8-[(2-methylphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000051
1-methyl-8-[(2-phenoxyphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000278
1-methyl-8-[(2-phenoxyphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.002666
1-methyl-8-[(2-phenoxyphenyl)amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000011
1-methyl-8-[[2-(methylamino)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000012
1-methyl-8-[[2-(methylamino)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.00011
1-methyl-8-[[2-(methylamino)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000014
1-methyl-8-[[2-(methylsulfanyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000016
1-methyl-8-[[2-(methylsulfanyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000097
1-methyl-8-[[2-(methylsulfanyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000146
1-methyl-8-[[2-(propan-2-yl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000365
1-methyl-8-[[2-(propan-2-yl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000509
1-methyl-8-[[2-(propan-2-yl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000095
1-methyl-8-[[2-(trifluoromethyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000109
1-methyl-8-[[2-(trifluoromethyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000432
1-methyl-8-[[2-(trifluoromethyl)phenyl]amino]-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.00115
2'-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5'-methyl-8'-(propan-2-yl)-5',8'-dihydro-6'H-spiro[cyclobutane-1,7'-pteridin]-6'-one
Homo sapiens
22°C, pH not specified in the publication
0.0253
2'-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5'-methyl-8'-(propan-2-yl)-5',8'-dihydro-6'H-spiro[cyclobutane-1,7'-pteridin]-6'-one
Homo sapiens
22°C, pH not specified in the publication
0.00012
2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7-(2,2,2-trifluoroethyl)-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00348
2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7-(2,2,2-trifluoroethyl)-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000004
3-(1,3-benzodioxol-5-yl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Homo sapiens
-
0.000024
3-(1,3-benzodioxol-5-yl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Homo sapiens
-
0.000214
3-(1,3-benzodioxol-5-yl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Homo sapiens
-
0.000549
3-(3-methylphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Homo sapiens
-
0.001449
3-(3-methylphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Homo sapiens
-
0.01
3-(3-methylphenyl)-N-[(1S)-1-phenylethyl]isoxazolo[5,4-c]pyridin-5-amine
Homo sapiens
>0.01
0.0000008
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
-
0.000006
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
-
0.000025
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
HCT-116 cell
0.000001
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-methoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
-
0.000035
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-methoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
-
0.000321
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-methoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
HCT-116 cell
0.000001
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(2R)-2,3-dihydroxypropyl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
-
0.000061
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(2R)-2,3-dihydroxypropyl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
-
0.000073
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(2R)-2,3-dihydroxypropyl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
HCT-116 cell
0.000003
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(2R)-2-hydroxy-3-pyrrolidin-1-ylpropyl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
-
0.000045
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(2R)-2-hydroxy-3-pyrrolidin-1-ylpropyl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
HCT-116 cell
0.00061
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(2R)-2-hydroxy-3-pyrrolidin-1-ylpropyl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
-
0.000004
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(4R)-1-methylazepan-4-yl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
-
0.000013
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(4R)-1-methylazepan-4-yl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
HCT-116 cell
0.00025
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(4R)-1-methylazepan-4-yl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
-
0.000003
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(4S)-1-methylazepan-4-yl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
-
0.000017
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(4S)-1-methylazepan-4-yl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
HCT-116 cell
0.00024
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-(6-[[(4S)-1-methylazepan-4-yl]oxy]-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
-
0.000006
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)methoxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
Homo sapiens
-
0.000034
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)methoxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
Homo sapiens
HCT-116 cell
0.0011
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)methoxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
Homo sapiens
-
0.000002
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
Homo sapiens
-
0.000003
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
Homo sapiens
HT-29 cell
0.000005
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
Homo sapiens
Colo-205 cell
0.000009
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
Homo sapiens
MX-1 cell
0.000011
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
Homo sapiens
A-549 cell
0.000011
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
Homo sapiens
HCT-116 cell
0.000011
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
Homo sapiens
SKOV-3 cell
0.00063
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
Homo sapiens
-
0.000004
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[3-(dimethylamino)propoxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
Homo sapiens
-
0.000032
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[3-(dimethylamino)propoxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
Homo sapiens
HCT-116 cell
0.00046
3-[(1R)-1-(2-chlorophenyl)ethoxy]-5-[6-[3-(dimethylamino)propoxy]-1H-benzimidazol-1-yl]thiophene-2-carboxamide
Homo sapiens
-
0.00003
3-[(1S)-1-(2-chlorophenyl)ethoxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
-
0.000044
3-[(1S)-1-(2-chlorophenyl)ethoxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
-
0.000994
3-[(1S)-1-(2-chlorophenyl)ethoxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
HCT-116 cell
0.000002
3-[(2-chlorobenzyl)oxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
-
0.000009
3-[(2-chlorobenzyl)oxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
-
0.00114
3-[(2-chlorobenzyl)oxy]-5-(5,6-dimethoxy-1H-benzimidazol-1-yl)thiophene-2-carboxamide
Homo sapiens
HCT-116 cell
0.000051
3-[3-chloro-5-(5-[[(1S)-1-phenylethyl]amino]isoxazolo[5,4-c]pyridin-3-yl)phenyl]propanamide
Homo sapiens
-
0.000172
3-[3-chloro-5-(5-[[(1S)-1-phenylethyl]amino]isoxazolo[5,4-c]pyridin-3-yl)phenyl]propanamide
Homo sapiens
-
0.001382
3-[3-chloro-5-(5-[[(1S)-1-phenylethyl]amino]isoxazolo[5,4-c]pyridin-3-yl)phenyl]propanamide
Homo sapiens
-
0.000031
4-[7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-6-oxo-6,7-dihydropteridin-8(5H)-yl]benzonitrile
Homo sapiens
22°C, pH not specified in the publication
0.00376
4-[7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-6-oxo-6,7-dihydropteridin-8(5H)-yl]benzonitrile
Homo sapiens
22°C, pH not specified in the publication
0.000002
5-(5,6-dimethoxy-1H-benzimidazol-1-yl)-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
Homo sapiens
-
0.000009
5-(5,6-dimethoxy-1H-benzimidazol-1-yl)-3-[[2-(trifluoromethyl)benzyl]oxy]thiophene-2-carboxamide
Homo sapiens
-
0.0000022
5-(5,6-dimethoxy-1H-benzimidazole-1-yl)-3-[2-(trifluoromethyl)-benzyloxy]-thiophene-2-carboxamide
Trypanosoma brucei
-
-
0.0013
5-(5,6-dimethoxy-1H-benzimidazole-1-yl)-3-[2-(trifluoromethyl)-benzyloxy]-thiophene-2-carboxamide
Trypanosoma brucei
-
Escherichia coli-expressed recombinant GST-tagged TbPLK
0.000003
5-(6-methoxy-1H-benzimidazol-1-yl)-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
Homo sapiens
-
0.000041
5-(6-methoxy-1H-benzimidazol-1-yl)-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
Homo sapiens
-
0.000476
5-(6-methoxy-1H-benzimidazol-1-yl)-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
Homo sapiens
HCT-116 cell
0.000003
5-[6-(piperidin-4-yloxy)-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
Homo sapiens
-
0.000015
5-[6-(piperidin-4-yloxy)-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
Homo sapiens
HCT-116 cell
0.00035
5-[6-(piperidin-4-yloxy)-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
Homo sapiens
-
0.000007
5-[6-[(1-methylpiperidin-4-yl)methoxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
Homo sapiens
-
0.00003
5-[6-[(1-methylpiperidin-4-yl)methoxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
Homo sapiens
HCT-116 cell
0.00055
5-[6-[(1-methylpiperidin-4-yl)methoxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
Homo sapiens
-
0.000002
5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
Homo sapiens
-
0.000003
5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
Homo sapiens
HT-29 cell
0.000005
5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
Homo sapiens
Colo-205 cell
0.00001
5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
Homo sapiens
MX-1 cell
0.000012
5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
Homo sapiens
HCT-116 cell
0.000014
5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
Homo sapiens
A-549 cell
0.000032
5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
Homo sapiens
SKOV-3 cell
0.00027
5-[6-[(1-methylpiperidin-4-yl)oxy]-1H-benzimidazol-1-yl]-3-[(1R)-1-[2-(trifluoromethyl)phenyl]ethoxy]thiophene-2-carboxamide
Homo sapiens
-
0.00003
7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5,7-dimethyl-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00716
7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5,7-dimethyl-8-(3,3,3-trifluoropropyl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000009
7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1H-pyrazol-3-yl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00342
7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-8-(1H-pyrazol-3-yl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00013
7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00182
7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-2-[5-(1,3-thiazol-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000168
7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-2-[5-(pyridin-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00182
7-ethyl-5-methyl-8-(1-methyl-1H-pyrazol-4-yl)-2-[5-(pyridin-2-yl)-1H-pyrazol-4-yl]-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000017
7-ethyl-5-methyl-8-phenyl-2-(2-phenyl-1H-imidazol-1-yl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00283
7-ethyl-5-methyl-8-phenyl-2-(2-phenyl-1H-imidazol-1-yl)-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000015
7-ethyl-8-(4-fluorophenyl)-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00234
7-ethyl-8-(4-fluorophenyl)-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000013
8-(3,3-difluorocyclopentyl)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.00032
8-(3,3-difluorocyclopentyl)-7-ethyl-2-[2-(4-fluorophenyl)-1H-imidazol-1-yl]-5-methyl-7,8-dihydropteridin-6(5H)-one
Homo sapiens
22°C, pH not specified in the publication
0.000103
8-[(2-acetylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000261
8-[(2-acetylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000346
8-[(2-acetylphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000012
8-[(2-aminophenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000013
8-[(2-aminophenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.00015
8-[(2-aminophenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000027
8-[(2-fluorophenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000037
8-[(2-fluorophenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000125
8-[(2-fluorophenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000013
8-[(2-methoxyphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000024
8-[(2-methoxyphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000042
8-[(2-methoxyphenyl)amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000049
8-[[2-(acetylamino)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.002104
8-[[2-(acetylamino)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.002523
8-[[2-(acetylamino)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.002051
8-[[2-acetyl-3-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.01
8-[[2-acetyl-3-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
larger than 0.010
0.000464
8-[[2-acetyl-4-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.002292
8-[[2-acetyl-4-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.01
8-[[2-acetyl-4-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
larger than 0.010
0.000109
8-[[2-acetyl-5-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.01
8-[[2-acetyl-5-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
larger than 0.010
0.00004
8-[[2-methoxy-4-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000066
8-[[2-methoxy-4-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000082
8-[[2-methoxy-4-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.000007
8-[[2-methoxy-5-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
pH 7.9, 25°C
0.000238
8-[[2-methoxy-5-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.00045
8-[[2-methoxy-5-(4-methylpiperazin-1-yl)phenyl]amino]-1-methyl-4,5-dihydro-1H-pyrazolo[4,3-h]quinazoline-3-carboxamide
Homo sapiens
-
0.14
AMPPNP
Homo sapiens
mutant T210D
0.155
AMPPNP
Homo sapiens
mutant T210V
0.166
AMPPNP
Homo sapiens
wild-type
0.00000083
BI 2536
Homo sapiens
-
-
0.00000083
BI 2536
Homo sapiens
pH 7.5, 30°C
0.0126
morin
Mammalia
-
-
0.0126
morin
Homo sapiens
-
-
0.000009
ONO1910
Homo sapiens
-
0.00026
ONO1910
Homo sapiens
Plk2
0.01
ONO1910
Homo sapiens
-
0.00034
PHA-680626
Homo sapiens
mutant T210D
0.00044
PHA-680626
Homo sapiens
mutant T210V
0.00053
PHA-680626
Homo sapiens
-
0.00053
PHA-680626
Homo sapiens
wild-type
0.064
quercetin
Mammalia
-
-
0.064
quercetin
Homo sapiens
-
-
0.002
scytonemin
Mammalia
-
-
0.002
scytonemin
Mus musculus
-
-
0.002
scytonemin
Homo sapiens
-
0.000024
Wortmannin
Mammalia
-
-
0.000024
Wortmannin
Homo sapiens
-
0.000024
Wortmannin
Homo sapiens
-
-
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evolution
the enzyme is a member of the polo-like kinase family. Among the five members, PLK2 is the more closely related to PLK1. The overall structure of the PLK2 PBD is similar to that of the PLK1 PBD, which is composed by two polo boxes each contain b6a structures that form a 12-stranded b sandwich domain. The edge of the interface between the two polo boxes forms the phosphorylated Ser-pSer/pThr motifs binding cleft. On the hand, the peripheral regions around the core binding cleft of the PLK2 PBD is distinct from that of the PLK1 PBD, which might confer the substrate specificity of the PBDs of the polo-like kinase family. Comparison of PLK1 and PL2 substrate binding and structure, detailed overview
evolution
the polo-box domain, PBD, is unique to the five-member family of polo-like kinases, found in only Plk1, Plk2, Plk3 and Plk5. Plk4 does not have a PBD, as it has only a single polo box. Unlike the other family members, Plk5 does not contain a kinase domain
evolution
the serine/threonine kinase Polo-like kinase 1 (Plk1) is a member of the Polo-like kinases family
malfunction
-
depletion of PLK1 leads to a delay of cell cycle recovery, and apoptosis
malfunction
heterozygosity of Plk4 does not lead to polyploidization and centrosome amplification
malfunction
heterozygosity of Plk4 does not lead to polyploidization and centrosome amplification
malfunction
loss of plk-2 inhibits chromosome pairing and licenses synapsis between nonhomologous chromosomes
malfunction
partial functional loss leads to chromosome missegregation
malfunction
53BP1 is excluded from the chromatin in mitotic cells and did not colocalize with gH2AX in mitotic cells after damage through irradiation. Inhibition of Plk1 by BI2536 inhibitor arrests cells in mitosis and increases the mobility of 53BP. The removal of pS1618-53BP1 modification correlates to disappearance of pS10-histone H3 as well as degradation of cyclin B and Plk1 during mitotic exit
malfunction
a failure in Plk1 regulation of the timing of CENP-Q dissociation from kinetochores leads to chromosome missegregation. Inhibition of Plk1 activity greatly diminishes hyperphosphorylates, slow-migrating PBIP1 (but not the moderately phosphorylated PBIP1 forms because of the presence of Plk1-independent phosphorylation) and appears to eliminate slow-migrating CENP-Q forms
malfunction
combination treatment with PLK1 and Bcl2 pharmacological inhibitors specifically induces synergistic cell death, partly because of PLK1 inhibitor-mediated depletion of Myc and Mcl1 expression
malfunction
kinase activity is impaired in Plk4-DELTAPB3, polo box 3-mutated enzyme, reducing its ability to transautophosphorylate and recruit Slimb and thereby increasing its stability
malfunction
knockdown of Plk1 caused the reduction of telomerase activity, whereas overexpression of Plk1 increased telomerase activity. Overexpression of Plk1 leads to a significant increase of hTERT protein by prolonging its half-life but does not affect the level of hTERT mRNA
malfunction
phenotype of different polo allele combinations compared to the effect of chemical inhibition. The chromosomal passenger complex is mislocalized in polo mutant meiosis. This defective CPC localization is independent of the degree of disruption of the spindle midzone, as visualized by staining for microtubules
malfunction
reduced kinase activity of polo kinase Cdc5 affects chromosome stability and DNA damage response. Cdc5-T238A mutant cells have increased rate of chromosome loss and gross chromosomal rearrangements, indicating altered genome stability. The T238A mutation affects timely localization of Cdc5 to the spindle pole bodies and blocks cell cycle restart after one irreparable double-strand break. In cells responding to alkylating agent metylmethane sulfonate (MMS), the cdc5-T238A mutation reduces the phosphorylation of Mus81-Mms4 resolvase and exacerbates the MMS sensitivity of sgs1D cells that accumulate Holliday junctions. Rad53 dephosphorylation is severely impaired in cdc5-T238A cells till almost 20-22 hours, but the defect is less severe than in cdc5-ad mutant cells. Cdc5-T238A and Cdc5-ad mutant protein variants show altered localization to spindle pole bodies after one irreparable double strand break. Mutant phenotypes, overview
malfunction
upon PLK1 inhibition, phosphorylated histone H3 on Thr 3, a marker of Haspin activity, is reduced. PLK1 inhibition, together with partial inhibition of Aurora B, allows efficient spindle assembly checkpoint override to occur. This phenotype is more pronounced than the phenotype observed by combining the same PLK1 inhibitors with partial MPS1 inhibition. PLK1 inhibition does not obviously cooperate with Haspin inhibition to promote spindle assembly checkpoint override. Effects of the PLK1 inhibitors together with partial inhibition of the three major checkpoint kinases Aurora B, MPS1 and Haspin in maintaining the strength of the nocodazole induced mitotic arrest, overview
malfunction
complete inhibition of polo kinase 1 can prevent mitotic entry for hours in a vast majority of TERT-RPE1, HeLa or RKO cells, even without prior activation of the DNA damage checkpoint
malfunction
enzyme downregulation in metastatic prostate cancer cells enhances epithelial characteristics and inhibits cell motility
malfunction
-
loss of isoform plk-2 function partially rescues meiotic defects in homolog alignment 2 mutants
metabolism
cell cycle-dependent regulation of the PBIP1-CENP-Q complex involving the enzyme, overview
metabolism
the enzyme affects the Mus81-Mms4 mediated resolution pathway
metabolism
polo-like kinase 2 accelerates amyloid precursor protein amyloidogenic cleavage by beta-secretase at synapses and is required for neuronal overactivity-stimulated amyloid beta secretion
physiological function
-
Cdc5 plays multiple roles during the cell cycle, component of the fourteen early anaphase release, FEAR, pathway, degradation of the protein Swe1 is Cdc5 dependent
physiological function
conserved function in mitotic processes
physiological function
conserved function in mitotic processes and cytokinesis
physiological function
Plk1 function as a key regulator of mitotic events by phosphorylating substrate proteins of centrosomes, kinetochores, the mitotic spindle, and the midbody
physiological function
-
Plk1 functions in multiple steps of mitosis
physiological function
Plk1 is a critical regulator of many stages of mitosis
physiological function
Plk1 is a fundamental regulator of mitotic progression
physiological function
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Plk1 is a key regulator of mitosis
physiological function
PLK1 is a key regulator of multiple steps during mitotic progression
physiological function
Plk1 is a regulator of interferon induction
physiological function
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Plk1 is involved in the activation of Cdc2, chromosome segregation, centrosome maturation, bipolar spindle formation and execution of cytokinesis
physiological function
PLK1 is the upstream regulator of SYK tyrosine kinase in B-lineage acute lymphoblastic leukemia cells
physiological function
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PLK1 participates in multiple steps in mitosis
physiological function
PLK1 plays a critical role in regulating the cell cycle, PLK inhibition increases gene expression of paramyxovirus
physiological function
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Plk1 plays an essential role in regulating the many processes involved in mitotic entry and progression
physiological function
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Plk1 plays several crucial roles in cell cycle progression and cell division
physiological function
PLK1 represents the most studied member of this familiy and has known roles throughout mitosis, including mitotic entry, spindle formation, chromosome segregation, and cytokinesis
physiological function
PLK4 is a key regulator of centrosome duplication
physiological function
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Plks are potent regulators of M phase, their roles in mitotic entry, spindle pole functions and cytokinesis are broadly conserved
physiological function
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Plks are potent regulators of M phase, their roles in mitotic entry, spindle pole functions and cytokinesis are broadly conserved
physiological function
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Plks are potent regulators of M phase, their roles in mitotic entry, spindle pole functions and cytokinesis are broadly conserved
physiological function
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Plks are potent regulators of M phase, their roles in mitotic entry, spindle pole functions and cytokinesis are broadly conserved
physiological function
Saccharomyces pombe
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Plks are potent regulators of M phase, their roles in mitotic entry, spindle pole functions and cytokinesis are broadly conserved
physiological function
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promotes adaptation to the DNA damage checkpoint, in addition to its numerous roles in mitotic progression
physiological function
responsible for cell cycle progression
physiological function
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TbPLK regulates cytokinetic initiation
physiological function
during meiosis the polo kinases PLK-1 is targeted to the pairing center by ZIM/HIM-8-pairing proteins
physiological function
during meiosis the polo kinases PLK-2 is targeted to the pairing center by ZIM/HIM-8-pairing proteins. PLK-2 enzyme is required for pairing center-mediated interhomolog interactions and for meiosis-specific phosphorylation of SUN-1 and establishment of dynamic SUN/KASH (SUN-1/ZYG-12) modules that promote homolog pairing
physiological function
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enzyme Cdc5 is required for spindle integrity during checkpoint bypass, it is not required for meiosis checkpoint activation
physiological function
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PLK1 plays an important role in DNA damage recovery
physiological function
polo-like kinase 4 controls centriole duplication but does not directly regulate cytokinesis
physiological function
polo-like kinase 4 controls centriole duplication but does not directly regulate cytokinesis
physiological function
polo-like kinase 4 plays a key role in initiating centriole duplication. Kinase-mediated, autoregulated instability of Plk4 self-limits Plk4 activity so as to prevent centrosome amplification
physiological function
the dynamics of the enzyme at kinetochores control two critical mitotic processes: initially establishing correct kinetochore-microtubule attachments and subsequently silencing the spindle checkpoint
physiological function
the enzyme has multiple functions and substrates in mitosis
physiological function
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the enzyme plays a critical role in cell division
physiological function
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the enzyme plays a pivotal role in the regulation of cell cycle progression and the orchestration of cell division
physiological function
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via the formation of the Nedd1-Plk1 complex and subsequent Augmin phosphorylation, Plk1 regulates spindle microtubule-based microtubule nucleation to accomplish normal bipolar spindle formation and mitotic progression
physiological function
Cdc5 contributes to the timely release of Cdc14 in mitosis. Cdc5 acts in parallel with MEN during anaphase. The MEN-independent Cdc5 function requires active separase and activation by Cdk1-dependent phosphorylation. The Cdc5 function is regulated by sequential Cdk1 phosphorylation. Initial phosphorylation at T242 activates Cdc5, which, in turn, promotes Cdc14 release in the metaphase-to-anaphase transition. Cdc14 release on Cdc5 induction does require active Cdc5 kinase activity, and Cdc5-induced Cdc14 release requires Cdc28-Clb2 activity. Phosphorylation at T70 contributes to Cdc5-MEN function in late anaphase. Cdc5 requires separase to induce Cdc14 release from the nucleolus
physiological function
enzyme Plk1 acts as a regulator in multiple stages of mitotic progression
physiological function
hTERT plays a central role for telomerase activity and telomeric chromatin maintenance. Plk1 interacts with hTERT and regulates its stability. Overexpression of Plk1 up regulates the activity of telomerase. Plk1 enhances the chromatin loading of hTERT and inhibits its ubiquitination. Plk1 is a positive regulator of telomerase by enhancing the stability of hTERT, mechanism, overview. Plk1 can interact with hTERT and increase telomerase activity independently of its kinase activity
physiological function
Plk1 is a protein kinase that localizes to subcellular structures called kinetochores to promote mitotic progression. Plk1 interacts with and regulates a kinetochore-associated PBIP1-CENP-Q complex. This is a tightly regulated, cell cycle-dependent process, the deregulation of which leads to improper chromosome segregation and mitotic progression. The event is likely critical for maintaining genomic integrity and preventing aneuploidy. PBIP1 and CENP-Q are ubiquitinated in a manner that does not require Plk1. Plk1 dissociates CENP-Q from chromatin without disrupting the PBIP1-CENP-Q complex. Plk1-dependent CENP-Q phosphorylation negatively regulates the ability of the PBIP1-CENP-Q complex to associate with chromatin. Plk1 regulates the timing of CENP-Q dissociation from kinetochores. Plk1 efficiently phosphorylates and binds to the Thr78 motif of PBIP1 through a self-priming and binding mechanism and then phosphorylates the CENP-Q subunit of the PBIP1-CENP-Q complex
physiological function
PLK1 promotes Fbw7 phosphorylation, selfubiquitination, and proteasomal degradation, creating a PLK1-Myc feedforward activation loop in MYC overexpressing tumor cells. PLK1 specifically binds to the SCFFbw7 ubiquitin ligase, phosphorylates it, and promotes its autopolyubiquitination and proteasomal degradation, counteracting Fbw7-mediated degradation of N-Myc and additional substrates, including cyclin E and Mcl1. Stabilized N-Myc in turn directly activates PLK1 transcription, constituting a positive feedforward regulatory loop that reinforces Myc-regulated oncogenic programs, association between Myc deregulation and PLK1 dependence. Analysis of the molecular mechanism responsible for reciprocal activation between Polo-like kinase-1 and N-Myc, PLK1-Fbw7-Myc signaling circuit, overview. PLK1 Reduces Fbw7 stability through promotion of its phosphorylation and autopolyubiquitination, Fbw7 turnover is mediated by autocatalytic ubiquitin transfer
physiological function
polo kinase regulates the localization and activity of the chromosomal passenger complex in meiosis and mitosis, e.g. in larval neuroblast mitoses, significant differences in the localization and activity of the chromosomal passenger complex in diploid tissues. Polo kinase is required for the correct localization and activity of the CPC at all stages of male meiosis as well as in larval neuroblast mitoses
physiological function
polo-like kinase 1 (Plk1) is a core regulator of mitosis required for centrosome maturation, bipolar spindle formation, chromosome arm resolution, chromosome alignment and segregation, and cytokinesis. Protein kinase signaling along the kinetochore-centromere axis is crucial to assure mitotic fidelity. Deep within the centromere, Plk1 operates to assure proper chromosome alignment and segregation. Plk1 is recruited to the outer kinetochore by Bub1, NudC, and BubR1, where it phosphorylates BubR1 and CLASP to stabilize kinetochore-microtubule attachments, promoting chromosome alignment, and Kif2b to correct microtubule attachment errors, facilitating accurate chromosome segregation. At the inner kinetochore, Plk1's role in chromosome alignment and segregation also requires recruitment by and phosphorylation of CENP-U/50 (also called PBIP) and CENP-Q. Plk1 operates in pools within the kinetochore and the bulk pool is at the inner kinetochore/centromere, and it operates at chromatin and in the inner centromere in a manner that is distinct and separable from Plk1s role in stabilizing microtubule attachments at the outer kinetochore
physiological function
Polo-like kinase 1 (PLK1) plays many roles leading to cell division including promoting entry into, progression through and exit from mitosis. It regulates bipolar spindle formation, centrosome function and k-MT attachment in human cells. PLK1 kinase activity is required in the maintenance of a robust spindle assembly checkpoint. PLK1 kinase plays a major role in mitosis. In nocodazole-arrested U2OS cells, PLK1 activity is continuously required for maintaining Aurora B protein localisation and activity at kinetochores (Aurora B is required for the recruitment of outer kinetochore proteins). Aurora B inhibition causes PLK1 to relocalise from kinetochores into fewer and much larger foci, possibly due to incomplete recruitment of outer kinetochore proteins. PLK1 is directly involved in maintaining efficient spindle assembly checkpoint signalling, possibly by cooperating in a positive feedback loop with Aurora B, and that partially redundant mechanisms exist which reinforce the spindle assembly checkpoint. PLK1 activity appears to be required for continuous maintenance of levels of histone H3 phosphorylated at Thr3 and its accumulation at kinetochores. Upon disruption of microtubules in U2-OS cells PLK1 functions to cooperate with Aurora B to maintain a mitotic cell cycle arrest
physiological function
polo-like kinase 1 inhibits DNA damage response during mitosis, and Plk1 activity supresses DNA repair in mitotic cells. 53BP1 facilitates repair of DNA lesions through NHEJ especially when localized in the heterochromatin or at telomeres and is phosphorylated by Plk1 in mitosis, Upon phosphorylation of the N-terminal domain by ATM, 53BP1 recruits RIF1 and PTIP that block resection of DNA ends and promote repair through NHEJ. 53BP1 is recruited to the DNA damage foci through binding of its Tudor domain to the dimethylated histone H4K20-me2 and therefore 53BP1 is then recognized as a bivalent reader of posttranslationally modified mononucleosomes. Distinct behavior of 53BP1 in interphase and mitotic cells due to its phosphorylation. 53BP1 phosphorylation by Plk1 impairs its binding to ubiquitinated histones and localization to foci
physiological function
polo-like kinase 2 (PLK2) is a crucial regulator in cell cycle progression, DNA damage response, and neuronal activity
physiological function
polo-like kinase 4 is a master regulator of centriole duplication, and its hyperactivity induces centriole amplification. Homodimeric Plk4 is ubiquitinated as a result of autophosphorylation, promoting its own degradation and preventing centriole amplification. Speculative multistep model for Plk4 activation and regulation, overview
physiological function
polo-like kinases control several aspects of eukaryotic cell division and DNA damage response. Cdc5 is the only PLK in Saccharomyces cerevisiae, it has minor effect on cell growth in unperturbed conditions. It is important of regulate Cdc5 activity through T-loop phosphorylation to preserve genome integrity and respond to DNA damage. Cdc5 may phosphorylate and regulate several factors that can suppress gross chromosomal rearrangements
physiological function
the mitotic centromere-associated kinesin (MCAK), a potent microtubule depolymerase, is involved in regulating microtubule dynamics. The activity and subcellular localization of MCAK are tightly regulated by key mitotic kinases, such as Polo-like kinase 1 (Plk1) by phosphorylating multiple residues in MCAK. Plk1 phosphorylates very often different residues of substrates at different stages. Residue S621 in MCAK is the major phosphorylation site of Plk1, which is responsible for regulating MCAK's degradation by promoting the association of MCAK with APC/C_Cdc20. Plk1 also phosphorylates S632/S633 and regulates its catalytic activity in mitosis, this phosphorylation is required for proper spindle assembly during early phases of mitosis
physiological function
the Plk1 polo-box domain is involved in substrate binding and in determining the correct subcellular localization of Plk1, with phospho-dependent substrate recognition by the PBD being necessary for proper mitotic progression. Binding of Plk1 to PBIP1 mediates centromeric localization of Plk1 and is important for chromosome segregation
physiological function
polo kinase 1 is essential for mitotic entry in human cells
physiological function
the enzyme is a key regulator of epithelial-to-mesenchymal transition and cell motility in normal prostate epithelium and prostate cancer. The enzyme is a potent activator of MAPK signaling
additional information
in Plk1, the phosphopeptide binds to a shallow cleft formed between polo box 1 (PB1) and polo box 2 (PB2), which are clamped together by the Polo-cap
additional information
the three polo boxes of Plk4 not only are crucial for Plk4 homodimerization and ubiquitination but also relieve autoinhibition caused by linker 1. Polo box 3 is required for kinase activity
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N166A
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kinase dead mutant
L408A
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mutant for interaction studies with Map205
S374A/S378A
site-directed mutagenesis within L1 (GST-L1-Ala-602), the double mutant shows reduced enzyme activity compared to the wild-type enzyme
V396A
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mutant for interaction studies with Map205
W395F
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mutant for interaction studies with Map205
C67V/L130G
localizes to centrosomes and kinetochores in mitotic cells like the wild-type, is ca. 12fold less active than wild-type in the presence of ATP, both 1-NM-PP1 and 3-MB-PP1 inhibit rapidly, selectively, and reversibly its growth in a dose-dependent manner. Acute treatment during anaphase prevents recruitment of both Plk1 itself and the Rho guanine nucleotide exchange factor Ect2 to the central spindle, abolishes RhoA GTPase localization to the equatorial cortex, and suppresses cleavage furrow formation and cell division. 3-MB-PP1 elicits a more penetrant phenotype that is virtually identical to PLK1 deletion
DELTAKD
kinase domain deleted Plk1, residues 307-603
DELTAPlk1
polo box deleted Plk1, residues 1-400
EGFP-Plk1D176N
construct used in FRAP experiments, expressed in U2OS cells, kinase-dead mutant
EGFP-Plk1PBD
construct used in FRAP experiments, expressed in U2OS cells, only C-terminal PBD domain
EGFP-Plk1T210A
construct used in FRAP experiments, expressed in U2OS cells, nonphosphorylatable T-loop form of Plk1
EGFP-Plk1T210D
construct used in FRAP experiments, expressed in U2OS cells, constitutively active mutant
H629A
site-directed mutagenesis, the mutation eliminates the capability of PBD2 binding with the phosphopeptide
K111R
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site-directed mutagenesis, kinase inactive mutant, overexpression blocks the centriole duplication and arrests the cells in S-phase
K52R
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site-directed mutagenesis, kinase-defective mutant
K631M
site-directed mutagenesis, the mutation eliminates the capability of PBD2 binding with the phosphopeptide
K82R
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myc-tagged kinase inactive mutant
PBD
polo box domain, residues 401-603
PLK1-C
construct comprising amino acids 305-603
PLK1-N
construct comprising amino acids 1-300
PLK1-PBD H538A/K540M
PLK1 polo box domain double mutant, constructed for the determination of the specificity of the association of PLK1 with MAVS
PLK1-PBD W414F/H538A/K540M
PLK1 polo box domain triple mutant, constructed for the determination of the specificity of the association of PLK1 with MAVS
PLK4_1-285
fragment, kinase domain only
PLK4_1-367_K41M
N-terminal fragment that possesses a mutation within the catalytic domain
S137D
constitutively active mutant
S305A
mutation of the autophosphorylation site
S305E
mutation of the autophosphorylation site
T236E
constitutively active mutant
T82A
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site-directed mutagenesis
W507F
site-directed mutagenesis, the mutation eliminates the capability of PBD2 binding with the phosphopeptide
D154A
kinase-inactive mutant enzyme
K110A
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kinase-dead mutant
L251W
generation of mutant cdc5-ad that has a checkpoint adaptation defective allele, i.e. it blocks DNA damage checkpoint adaptation, cdc5-ad does not show reduced kinase activity, defective Mms4 phosphorylation and genetic interaction with sgs1DELTA
T238A
the substitution in the T-loop reduces the kinase activity of Cdc5. Mutant cdc5-T238A cells do not adapt to one irreparable double strand break and uncapped telomere, cdc5-T238A affects Mms4 phosphorylation and viability of sgs1D cells with alkylating agent metylmethane sulfonate
T242A
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kinase-deficient mutant
W565R
single point mutation within the PB1 motif of the highly conserved polo box domain, mutant exhibits a temperature-sensitive growth defect
SmPlk1DK
dead kinase version of SmPlk1, obtained by replacing the D166FG168 active motif by a D166NA168 inactive motif
SmPlk1T182D
constitutively active mutant
SmPlk1T182D-DK
double mutant
SmPlk1T182V
inactive mutant
D181N
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site-directed mutagenesis, mutation of the kinase domain, no complementation by plo1
D181R
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site-directed mutagenesis, mutation of the kinase domain, no complementation by plo1
D623A/H624A/K625A
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site-directed mutagenesis, mutation of polo box 3, mutant strain shows reduced mitotic activity, no complementation by plo1
E139K
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site-directed mutagenesis, mutation in the kinase domain, mutant enzyme is fully active with histone H1 kinase
E193V
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site-directed mutagenesis, mutation of the kinase domain, no complementation by plo1
F518A/N519A
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site-directed mutagenesis, mutation of polo box 1, mutant strain shows reduced mitotic activity
G505A
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site-directed mutagenesis, mutation of polo box 1, mutant strain shows reduced mitotic activity
K69R
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site-directed mutagenesis, mutation of the kinase domain, mutant is catalytically inactive, no complementation by plo1
L577A
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site-directed mutagenesis, mutation of polo box 2, mutant strain shows reduced mitotic activity
S402A
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site-directed mutagenesis, no phosphorylation of the mutant by the stress response machinery, leading to delay in cell tip growth and cell division
T197V
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site-directed mutagenesis, mutation of the kinase domain, no complementation by plo1
W49F
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site-directed mutagenesis, mutation of polo box 1, mutant strain shows reduced mitotic activity
Y506A/Q507A/L508A
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site-directed mutagenesis, mutation of polo box 1, mutant strain shows reduced mitotic activity, no complementation by plo1
F561A
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mutation does not affect kinase activity, the mutant enzyme is correctly localized to the anterior tip of the new flagellum attachment zone
H710A
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mutation does not affect kinase activity, the mutant enzyme is correctly localized to the anterior tip of the new flagellum attachment zone
K70R
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no kinase activity
K712A
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mutation does not affect kinase activity, the mutant enzyme is correctly localized to the anterior tip of the new flagellum attachment zone
N169A
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abrogates kinase activity, after PLK depletion the single kinetoplast is predominantly located between the two divided nuclei
T198A
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mutation disrupts the ability to phosphorylate the in vitro substrate TbCentrin2
T198D
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kinase activity of the mutant enzyme is several-fold higher than that of wild-type enzyme
T201A
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mutation disrupts the ability to phosphorylate the in vitro substrate TbCentrin2
T201D
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kinase activity of the mutant enzyme is several-fold higher than that of wild-type enzyme
W557F
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mutation does not affect kinase activity, the mutant enzyme is correctly localized to the anterior tip of the new flagellum attachment zone
T196D
variant containing an activating substitution
T196D
variant containing an activating substitution
H538A/K540M
localizes at the centrosome, when wild-type Plk1 and H538A/K540M are fused to EGFP. After photobleaching recovers its signal at the centrosome following very similar kinetics as the wild-type
H538A/K540M
double mutant, no differences in centrosomal localization compared to the wild-type protein are detected
K82M
mutant
K82M
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site-directed mutagenesis, kinase-defective mutant
K82M
site-directed mutagenesis, kinase-defective Plk1 mutant
K82M
kinase defective mutant
K82M
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Plk1 kinase-dead mutant
K82M
kinase-deficient PLK1
K82M
a kinase-inactive mutant
T210D
mutant
T210D
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site-directed mutagenesis, constitutively active mutant, overrides the irradiation-induced DNA damage and inhibition of centrosome separation in contrast to the wild-type enzyme
T210D
site-directed mutagenesis, hyperactive Plk1 mutant, shows reduced activity with truncated Pin1 compared to the wild-tpe Plk1
T210D
expression at low levels, no crystals obtained
T210D
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constitutively active mutant
T210D
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variant containing an activating substitution
T210D
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hyperactive mutant
T210D
mutation in sequence of full-lenght construct
T210V
mutant
T210V
mutation in sequence of full-lenght construct
W414F
abolishes molecular recognition and diminishes centrosomal localization
W414F
mutation abolishes polo box domain target peptide binding and reduces EGFP-Plk1 centrosomal localization
N209A
site-directed mutagenesis, inactive mutant
N209A
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Cdc5KD, kinase-dead mutant
additional information
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constructed mutant cells deficient in Cdc5p are blocked early in nuclear division with very short spindles and unseparated chromatin, the cell cycle defective mutants show also formation of hyphal-like filaments under yeast growth conditions
additional information
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male homozygous polo mutant flies die in the third instar larval stage, heterozygous mutants show affected centromer dissociation of MEI-S332, but not association resulting in chromosome segragation defects
additional information
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mutant phenotype analysis
additional information
complete inactivation of a kinase domain mutant. Expression of Plk4 phospho-mutants influences centriole numbers
additional information
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construction of an kinase-active deletion mutant lacking 32 amino acids of te N-terminus
additional information
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construction of Plk1 deletion mutants comprising residues 1-480, 1-330, or 1-408, deletion mutant 1-330 shows no kinase activity
additional information
down-regulation of Plk1 by expression of hairpin shRNA results in increased Pin1 ubiquitination and to down-regulation of pin 1 levels during mitosis
additional information
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down-regulation of Plk1 by expression of hairpin shRNA results in increased Pin1 ubiquitination and to down-regulation of pin 1 levels during mitosis
additional information
enzyme depletion using the vector-based small interfering RNA technique, Plk1 depletion leads to highly inhibited cell proliferation, decreased viability, and results in cell-cycle arrest with 4 n DNA content, formation of dumbbell-like chromatin structure due to impaired sister chromatin separation, induction of apoptosis, the apoptotic effect is reversible by co-transfection of murine Plk1
additional information
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enzyme inhibition by expression of siRNA or inhibition of enzyme expression in HeLa cells reducing the the level of 3F3/2 phosphoepitope and inhibiting normal kinetochore association, overview
additional information
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inhibition of p53 phosphorylation by Plk3 via siRNA transfection
additional information
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overexpression of dominant negative Plk2 mtant results in abolished centriole duplication in fibroblasts and in U2OS2 cells
additional information
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Plk1 depletion by siRNA transfection combined with Nek2 overexpression in U2OS cells
additional information
both copies of the PLK1 locus deleted in telomerase-immortalized human retinal pigment epithelial cells, more than 90% knockdown of Plk1 does not cause any cell cycle impairment, PLK1-null cells arrest in mitosis with immature centrosomes and monopolar spindles. Plk1 function and cell viability can be reconstituted by expressing either wildtype Plk1 or an analog-sensitive variant, the analog-sensitive variant is inhibited by 3-MB-PP1
additional information
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both copies of the PLK1 locus deleted in telomerase-immortalized human retinal pigment epithelial cells, more than 90% knockdown of Plk1 does not cause any cell cycle impairment, PLK1-null cells arrest in mitosis with immature centrosomes and monopolar spindles. Plk1 function and cell viability can be reconstituted by expressing either wildtype Plk1 or an analog-sensitive variant, the analog-sensitive variant is inhibited by 3-MB-PP1
additional information
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EGFP-Plk1 delta400-603 mutant, lacks the polo box domain, localizes to the centrosome and displays a similar fluorescence intensity to the W414F mutant
additional information
EGFP-Plk1 delta400-603 mutant, lacks the polo box domain, localizes to the centrosome and displays a similar fluorescence intensity to the W414F mutant
additional information
homozygous deletion of PLK1 fully abrogates its function in vivo, PLK1delta/delta cells have monopolar or disorganized bipolar spindles with adjacent and immature centrosomes
additional information
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homozygous deletion of PLK1 fully abrogates its function in vivo, PLK1delta/delta cells have monopolar or disorganized bipolar spindles with adjacent and immature centrosomes
additional information
polo-box domain mutant in which residues His 538 and Lys 540, critical for ligand binding, are changed to alanine, do not pull down BubR1 from mitotic cell lysates
additional information
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human full-length Plk1 with the mutation T210D in the active-site loop of kinase domain
additional information
enzyme knockdown in HeLa cells via transfection with Plk1-specific small interfering RNA (siRNA). Chromatin-bound hTERT is obviously decreased in Plk1 siRNA-transfected HeLa cells compared with that in control cells
additional information
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enzyme knockdown in HeLa cells via transfection with Plk1-specific small interfering RNA (siRNA). Chromatin-bound hTERT is obviously decreased in Plk1 siRNA-transfected HeLa cells compared with that in control cells
additional information
mutant Plk1as is resistant to inhibition by BI-2536
additional information
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mutant Plk1as is resistant to inhibition by BI-2536
additional information
PLK1 shRNA knockdown
additional information
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PLK1 shRNA knockdown
additional information
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in mutant cells in which the Cdc5 promoter is exchanged for the Clb2 promoter, the enzyme is degradated during G1 phase and is absent in meiosis, Cdc5-depleted cells progress through premeiotic S phase and enter metaphase I but arrest in metaphase I, mechanism
additional information
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overexpression of Cdc5 leads to Cdc14 release from the nucleolus in S-phase-arrested cells
additional information
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overexpression of mutant or wild-type Cdc5 results in multinucleated cells, Cdc5 overexpression overrides checkpoint-induced cell cycle arrest, Cdc5-defective mutant protein suppresses a Rad53 checkpoint defect
additional information
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mutants lacking Cdc5, contractile actin ring assembly is impaired
additional information
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several yeast Cdc5-mutant strains are used
additional information
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construction of C-terminal deletions, the deletion mutants comprise residues 1-633, 1-583, and 1-483, no complementation of the mutants by plo1
additional information
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generation of temperature-sensitive mutants of Plo1 which are inactivated at 35°C for 4 h, Plo1 activity is abolished in Cut12 loss-of-function mutant cells, but is increased in Cut12 gain-of-function mutant cells
additional information
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overexpression of Plo1 results in formation of multiple septa without nuclear division
additional information
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deletion of the C-terminal polo-box domain abolishes localization of polo-like kinase
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