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integrin alpha7 + NAD+
(ADP-D-ribosyl)-integrin alpha7 + nicotinamide
NAD+ + (ADP-D-ribosyl)n-(EF-2)
nicotinamide + (ADP-D-ribosyl)n+1-(EF-2)
-
in native conformation, CRM66 shows limited ability to modify EF-2 covalently. Upon activation with urea and dithiothreitol CRM66 loses ADP-ribosylation activity entirely, yet it retains the ability to bind NAD+. Replacement of Tyr-426 with histidine in CRM66 completely restores cytotoxicity and ADP-ribosyltransferase activity
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
NAD+ + (ADP-D-ribosyl)n-actin
nicotinamide + (ADP-D-ribosyl)n+1-actin
Q49TP5
VahC is shown to ADP-ribosylate Arg-177 of actin. VahC activity causes depolymerization of actin filaments, which induces caspase-mediated apoptosis in HeLa Tet-Off cells
-
-
?
NAD+ + (ADP-D-ribosyl)n-apolipoprotein
nicotinamide + (ADP-D-ribosyl)n+1-apolipoprotein
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-aryl hydrocarbon receptor
nicotinamide + (ADP-D-ribosyl)n+1-aryl hydrocarbon receptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-biotin
nicotinamide + (ADP-D-ribosyl)n+1-biotin + H+
NAD+ + (ADP-D-ribosyl)n-Crk-I
nicotinamide + (ADP-D-ribosyl)n+1-Crk-I
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-Crk-II
nicotinamide + (ADP-D-ribosyl)n+1-Crk-II
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-His6HRas
nicotinamide + (ADP-D-ribosyl)n+1-His6HRas
-
the enzyme preferentially ADP-ribosylates membrane-associated His6HRas relative to its cytosolic His6HRasDELTACAAX with a C-terminal deletion
-
-
?
NAD+ + (ADP-D-ribosyl)n-immunoglobulin A
nicotinamide + (ADP-D-ribosyl)n+1-immunoglobulin A
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-immunoglobulin G
nicotinamide + (ADP-D-ribosyl)n+1-immunoglobulin G
-
preferentially IgG3
-
-
?
NAD+ + (ADP-D-ribosyl)n-NEMO protein
nicotinamide + (ADP-D-ribosyl)n+1-NEMO protein + H+
-
the enzyme prevents poly-ubiquitination of NEMO protein
-
-
?
NAD+ + (ADP-D-ribosyl)n-p21ras
nicotinamide + (ADP-D-ribosyl)n+1-p21ras
NAD+ + (ADP-D-ribosyl)n-P2X7 ion channel
nicotinamide + (ADP-D-ribosyl)n+1-P2X7 ion channel + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-peptide LL-37
nicotinamide + (ADP-D-ribosyl)n+1-peptide LL-37 + H+
-
up to four of the five arginine residues present in peptide LL-37 can be ADP-ribosylated on the same peptide when incubated at a high NAD concentration
-
-
?
NAD+ + (ADP-D-ribosyl)n-Rab2
nicotinamide + (ADP-D-ribosyl)n+1-Rab2
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-Rab3
nicotinamide + (ADP-D-ribosyl)n+1-Rab3
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-rab4
nicotinamide + (ADP-D-ribosyl)n+1-rab4
NAD+ + (ADP-D-ribosyl)n-Rab5
nicotinamide + (ADP-D-ribosyl)n+1-Rab5
NAD+ + (ADP-D-ribosyl)n-RalA
nicotinamide + (ADP-D-ribosyl)n+1-RalA
NAD+ + (ADP-D-ribosyl)n-Rap1A
nicotinamide + (ADP-D-ribosyl)n+1-Rap1A
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-Ras
nicotinamide + (ADP-D-ribosyl)n+1-Ras
NAD+ + (ADP-D-ribosyl)n-Ras protein
nicotinamide + (ADP-D-ribosyl)n+1-Ras protein
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
NAD+ + (ADP-D-ribosyl)n-serine/arginine-rich protein-specific kinase 2
nicotinamide + (ADP-D-ribosyl)n+1-serine/arginine-rich protein-specific kinase 2 + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-soybean trypsin inhibitor
nicotinamide + (ADP-D-ribosyl)n+1-soybean trypsin inhibitor
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-soybean-trypsin-inhibitor
nicotinamide + (ADP-D-ribosyl)n+1-soybean-trypsin-inhibitor
-
-
-
-
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
NAD+ + GTPase RhoA
nicotinamide + (ADP-D-ribosyl)-GTPase RhoA
-
the exoenzyme modifies the low-molecular-mass GTPases RhoA, B, and C specifically at Asn41
-
-
?
NAD+ + GTPase RhoB
nicotinamide + (ADP-D-ribosyl)-GTPase RhoB
-
the exoenzyme modifies the low-molecular-mass GTPases RhoA, B, and C specifically at Asn41
-
-
?
NAD+ + GTPase RhoC
nicotinamide + (ADP-D-ribosyl)-GTPase RhoC
-
the exoenzyme modifies the low-molecular-mass GTPases RhoA, B, and C specifically at Asn41
-
-
?
NAD+ + H2O
nicotinamide + ADP-ribose
-
-
-
-
?
NAD+ + histone H1
nicotinamide + (ADP-D-ribosyl)-histone H1
-
-
-
-
?
NAD+ + histone H2A
nicotinamide + (ADP-D-ribosyl)-histone H2A
NAD+ + histone H2B
nicotinamide + (ADP-D-ribosyl)-histone H2B
NAD+ + lymphocyte function-associated antigen LFA-1
nicotinamide + ?
-
-
-
-
?
NAD+ + moesin
nicotinamide + (ADP-D-ribosyl)-moesin
NAD+ + p53
nicotinamide + (ADP-D-ribosyl)-p53
NAD+ + poly(ADP-ribose) polymerase-1
nicotinamide + (ADP-ribosyl)-poly(ADP-ribose) polymerase-1
-
the 40 kDa CD fragment of avian PARP-1 efficiently catalyzes a covalent auto-poly-(ADP-ribosyl)ation reaction via an intermolecular mechanism that is completely independent of DNA
-
-
?
NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
NAD+ + Ras
nicotinamide + (ADP-D-ribosyl)-Ras
-
interaction requires residue Leu428
-
-
?
NAD+ + Ras GTPase
nicotinamide + (ADP-D-ribosyl)-Ras GTPase
-
-
-
-
?
NAD+ + Ras2p
nicotinamide + (ADP-D-ribosyl)-Ras2p + H+
-
Ras2p is a yeast protein, activity absolutely requires the yeast protein Bmh1p
-
-
?
NAD+ + RhoA
nicotinamide (ADP-D-ribosyl)-RhoA
NAD+ + RhoB
nicotinamide (ADP-D-ribosyl)-RhoB
NAD+ + RhoC
nicotinamide (ADP-D-ribosyl)-RhoC
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
NAD+ + soybean trypsin inhibitor
nicotinamide + (ADP-D-ribosyl)-soybean trypsin inhibitor
-
the exoenzyme modifies the substrate at an arginine residue
-
-
?
NAD+ + topoisomerase I
nicotinamide + (ADP-D-ribosyl)-topoisomerase I
NAD+ + vimentin
nicotinamide + (ADP-D-ribosyl)-vimentin
-
-
-
-
?
NAD+ + wild-type exoenzyme C3
nicotinamide + (ADP-D-ribosyl)-wild-type exoenzyme C3
-
activity of the recombinant mutant Q217E exoenzyme C3, modification at Arg86
-
-
?
nicotinamide 1,N6-ethenoadenine dinucleotide + (ADP-D-ribosyl)n-vH-Ras protein
nicotinamide + ?
additional information
?
-
integrin alpha7 + NAD+

(ADP-D-ribosyl)-integrin alpha7 + nicotinamide
-
the extracellular domain of integrin alpha7 is ADP-ribosylated by an arginine-specific ecto-ADP-ribosyltransferase after adding exogenous NAD+ to intact C2C12 muscle cells, integrin alpha7 N-terminal ADP-ribosylation inhibits the binding of integrin alpha7beta1 to laminin activation status of integrin alpha7beta1 in intact myotubes, overview
-
-
?
integrin alpha7 + NAD+
(ADP-D-ribosyl)-integrin alpha7 + nicotinamide
-
the extracellular domain of integrin alpha7 is ADP-ribosylated by an arginine-specific ecto-ADP-ribosyltransferase after adding exogenous NAD+ to intact C2C12 muscle cells, integrin alpha7 ADP-ribosylation inhibits the binding of integrin alpha7beta1 to laminin, binding site, overview
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor

nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of histone H1
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
the enzyme is a DNA repair enzyme
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of 21000-24000 Da platelet membrane proteins
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
Cryptothecodinium cohnii
-
poly(ADP-ribosyl)ation of histone
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of histone H1
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation, i.e. PARylation, plays diverse roles in many molecular and cellular processes, including DNA damage detection and repair, chromatin modification, transcription, cell death pathways, insulator function, and mitotic apparatus function, connections between nuclear NAD+ metabolism and nuclear signaling through PARP-1, physiologic functions, detailed overview, synthesis and degradation of PAR on an acceptor protein, pathway overview, the enzyme is involved in regulation of the steady-state levels of PAR
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
linking a long negatively charged polymer to a protein, PARP catalyzes the polymerization of ADP-ribose units from donor NAD+ molecules on target proteins, resulting in the attachment of PAR, each residue in PAR contains an adenine moiety capable of base stacking and hydrogen bonding, as well as two phosphate groups that carry negative charges, substrate structure, overview
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of histone
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of topoisomerase I
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
auto-poly(ADP-ribosyl)ation
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of high mobility group proteins
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of DNA ligase
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of endonuclease
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of topoisomerase II
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of terminal deoxynucleotidyltransferase
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of histone H1
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of histone
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
catalyzes poly(ADP-ribosyl)ation of the synthetase itself, automodification
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation of ADP-ribosyltransferase
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation, i.e. PARylation, plays diverse roles in many molecular and cellular processes, including DNA damage detection and repair, chromatin modification, transcription, cell death pathways, insulator function, and mitotic apparatus function, connections between nuclear NAD+ metabolism and nuclear signaling through PARP-1, physiologic functions, detailed overview, synthesis and degradation of PAR on an acceptor protein, pathway overview, the enzyme is involved in regulation of the steady-state levels of PAR
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
linking a long negatively charged polymer to a protein, PARP-1 catalyzes the polymerization of ADP-ribose units from donor NAD+ molecules on target proteins, resulting in the attachment of PAR, each residue in PAR contains an adenine moiety capable of base stacking and hydrogen bonding, as well as two phosphate groups that carry negative charges, substrate structure, overview
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
agmatine as ADPribose acceptor is used
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ADPRT domain of ExoT is active in vivo and contributes to the pathogenesis of Pseudomonas aeruginosa infections
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
exoenzyme S is an ADP-ribosyltransferase produced and directly translocated into eukaryotic cells by the opportunistic pathogen Pseudomonas aeruginosa. Factors expressed by growing epithelial cells are required for the bacterial contact-dependent translocation of ExoS. As normal epithelial cells differentiate into polarized confluent monolayers, expression of these factors is altered, and cells in turn become more resistant to the effects of ExoS
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoS can modify multiple GTPases of the Ras superfamily in vivo. ExoS modulates the activity of several of GTP-binding proteins, such as Ras, Rap1, Rap2, Ral, Rac1, RhoA and Cdc42. It is suggested that ExoS is the major ADP-ribosyltransferase protein modulating small GTPase function encoded by Pseudomonas aeruginosa
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoT modifies and inactivates host cell proteins involved in maintaining the actin cytoskeleton in vivo by two independent mechanisms. ADP-ribosylation activity of ExoT induces an irreversible disruption of actin microfilaments of infected Hela cells
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
intracellular expression of the amino terminus of ExoS in eukaryotic cells stimulates actin reorganization without cytotoxicity, which involves small-molecular-weight GTPases of the Rho subfamily
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
intracellular Ras is modified by bacterially translocated ExoS, inhibition of target cell proliferation correlates with the efficiency of Ras modification
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoS has polysubstrate specificity and can ADP-ribosylate numerous host proteins, e.g. monomeric GTPase or vimentin. ExoS also undergoes auto-ADP-ribosylation. Ras has multiple alternative sites for ADP-ribosylation
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoS is a type III cytotoxin which modulates two eukaryotic signalling pathways. The N-terminus (residues 1-234) is a GTPase activating protein for RhoGTPases, while the C-terminus (residues 232-453) encodes an ADP-ribosyltransferase
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoT ADP-ribosylates a restricted subset of host proteins including the Crk proteins
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoS has polysubstrate specificity and can ADP-ribosylate numerous host proteins, e.g. monomeric GTPase or vimentin. ExoS also undergoes auto-ADP-ribosylation. Ras has multiple alternative sites for ADP-ribosylation
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoT ADP-ribosylates a restricted subset of host proteins including the Crk proteins
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoS has polysubstrate specificity and can ADP-ribosylate numerous host proteins, e.g. monomeric GTPase or vimentin. ExoS also undergoes auto-ADP-ribosylation. Ras has multiple alternative sites for ADP-ribosylation
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoT ADP-ribosylates a restricted subset of host proteins including the Crk proteins
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor

nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the enzyme labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the enzyme labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
the emzyme protects homologous DNA against thermal denaturation by lowering the amount of melted DNA and increasing melting temperature. The archaeal protein induces structural changes of the nucleic acid by modifying the dichroic spectra towards a shape typical of condensing DNA
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
the emzyme protects homologous DNA against thermal denaturation by lowering the amount of melted DNA and increasing melting temperature. The archaeal protein induces structural changes of the nucleic acid by modifying the dichroic spectra towards a shape typical of condensing DNA
-
-
?
NAD+ + (ADP-D-ribosyl)n-biotin

nicotinamide + (ADP-D-ribosyl)n+1-biotin + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-biotin
nicotinamide + (ADP-D-ribosyl)n+1-biotin + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-p21ras

nicotinamide + (ADP-D-ribosyl)n+1-p21ras
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-p21ras
nicotinamide + (ADP-D-ribosyl)n+1-p21ras
-
ADP-ribosylation of p21ras does not alter interactions with guanidine nucleotides. Possible function of the enzyme in pathogenesis
-
-
?
NAD+ + (ADP-D-ribosyl)n-rab4

nicotinamide + (ADP-D-ribosyl)n+1-rab4
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-rab4
nicotinamide + (ADP-D-ribosyl)n+1-rab4
-
ADP-ribosylation affects Rab4 function in membrane recycling
-
-
?
NAD+ + (ADP-D-ribosyl)n-Rab5

nicotinamide + (ADP-D-ribosyl)n+1-Rab5
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-Rab5
nicotinamide + (ADP-D-ribosyl)n+1-Rab5
-
ADP-ribosylation of Rab5 by ExoS affects endocytosis. Interaction of Rab5 with endosome antigen 1 is markedly diminished after Rab5 ADP-ribosylation by ExoS
-
-
?
NAD+ + (ADP-D-ribosyl)n-RalA

nicotinamide + (ADP-D-ribosyl)n+1-RalA
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-RalA
nicotinamide + (ADP-D-ribosyl)n+1-RalA
-
ADP-ribosylation of RalA by ExoS interferes with RalA activation and binding to its downstream effector in J774A.1 macrophages and suggests the potential of ExoS ADPRT activity to interfere with filiopodium formation through the inactivation of RalA and downstream effects mediated through the exocyst complex
-
-
?
NAD+ + (ADP-D-ribosyl)n-Ras

nicotinamide + (ADP-D-ribosyl)n+1-Ras
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-Ras
nicotinamide + (ADP-D-ribosyl)n+1-Ras
-
ADP-ribosylation of Ras at Arg41 disrupts Ras-Cdc25 interactions, which inhibits the rate-limiting step in Ras signal transduction, the activation of Ras by its guanine nucleotide exchange factor
-
-
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein

nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
-
-
-
?
NAD+ + cyclophilin A

nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
cytosolic protein of several human epithelial cells, modification at Arg55 and Arg69 of cyclophilin A, ADP-ribosylation of CpA efficiently inhibits CpA binding to calcineurin/PP2B phosphatase, overview
-
-
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
a non-G-protein substrate with peptidyl-prolyl isomerase activity, from several human epithelial cells, modification at Arg55 and Arg69, but not at Arg148, of cyclophilin A, i.e. CpA, ADP-ribosylation of CpA efficiently inhibits CpA binding to calcineurin/PP2B phosphatase, activity with CpA mutants, overview
-
-
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
cytosolic protein of several human epithelial cells, modification at Arg55 and Arg69 of cyclophilin A, ADP-ribosylation of CpA efficiently inhibits CpA binding to calcineurin/PP2B phosphatase, overview
-
-
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
a non-G-protein substrate with peptidyl-prolyl isomerase activity, from several human epithelial cells, modification at Arg55 and Arg69, but not at Arg148, of cyclophilin A, i.e. CpA, ADP-ribosylation of CpA efficiently inhibits CpA binding to calcineurin/PP2B phosphatase, activity with CpA mutants, overview
-
-
?
NAD+ + histone H2A

nicotinamide + (ADP-D-ribosyl)-histone H2A
-
the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B. Histone modification by TbSIR2RP1 is involved in DNA repair
-
-
?
NAD+ + histone H2A
nicotinamide + (ADP-D-ribosyl)-histone H2A
-
the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B
-
-
?
NAD+ + histone H2B

nicotinamide + (ADP-D-ribosyl)-histone H2B
-
-
-
-
?
NAD+ + histone H2B
nicotinamide + (ADP-D-ribosyl)-histone H2B
-
the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B. Histone modification by TbSIR2RP1 is involved in DNA repair
-
-
?
NAD+ + histone H2B
nicotinamide + (ADP-D-ribosyl)-histone H2B
-
the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B
-
-
?
NAD+ + moesin

nicotinamide + (ADP-D-ribosyl)-moesin
-
ADP-ribosylated-moesin is a poor target for phosphorylation by protein kinase C and Rho kinase, which shows that ADP-ribosylation directly inhibits ERM phosphorylation
-
-
?
NAD+ + moesin
nicotinamide + (ADP-D-ribosyl)-moesin
-
modification of Arg553, Arg560 and Arg563, activity with wild-type and mutant moesins, overview
-
-
?
NAD+ + p53

nicotinamide + (ADP-D-ribosyl)-p53
-
-
-
-
?
NAD+ + p53
nicotinamide + (ADP-D-ribosyl)-p53
-
PARP-1 interacts with and poly(ADP-ribosyl)ates p53, which participates in DNA recombination
-
-
?
NAD+ + Rab5 protein

nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
-
Rab5 mediates entry of the EGFR into early endosomes
-
-
?
NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
-
Rab5 mediates entry of the EGFR into early endosomes
-
-
?
NAD+ + Rab9 protein

nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
-
-
-
-
?
NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
-
-
-
-
?
NAD+ + RhoA

nicotinamide (ADP-D-ribosyl)-RhoA
-
-
-
-
?
NAD+ + RhoA
nicotinamide (ADP-D-ribosyl)-RhoA
-
-
-
-
?
NAD+ + RhoB

nicotinamide (ADP-D-ribosyl)-RhoB
-
-
-
-
?
NAD+ + RhoB
nicotinamide (ADP-D-ribosyl)-RhoB
-
-
-
-
?
NAD+ + RhoC

nicotinamide (ADP-D-ribosyl)-RhoC
-
weak activity
-
-
?
NAD+ + RhoC
nicotinamide (ADP-D-ribosyl)-RhoC
-
weak activity
-
-
?
NAD+ + RNA polymerase

nicotinamide + (ADP-D-ribosyl)-RNA polymerase
-
-
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
three ADP-ribosyltransferases, Alt, ModA, and ModB participate in the regulation of the T4 replication cycle by ADP-ribosylating a defined set of host proteins. ADP-ribosylation of RNA polymerase and of other host proteins allows initial phage-directed mRNA synthesis reactions to escape from host control
-
-
?
NAD+ + topoisomerase I

nicotinamide + (ADP-D-ribosyl)-topoisomerase I
-
-
-
-
?
NAD+ + topoisomerase I
nicotinamide + (ADP-D-ribosyl)-topoisomerase I
-
PARP-1 interacts with and poly(ADP-ribosyl)ates topoisomerase I, which participates in DNA recombination, I-SceI-meganuclease-mediated cleavage terminates the interaction, overview
-
-
?
nicotinamide 1,N6-ethenoadenine dinucleotide + (ADP-D-ribosyl)n-vH-Ras protein

nicotinamide + ?
-
-
-
-
?
nicotinamide 1,N6-ethenoadenine dinucleotide + (ADP-D-ribosyl)n-vH-Ras protein
nicotinamide + ?
-
-
-
-
?
additional information

?
-
-
cuts produced in vivo on DNA during DNA repair activate the enzyme, which then synthesiszes poly(ADP-ribose) on histone H1, in particular, and contributes to the opening of the 25 nm chromatin fiber, resulting in the increased accessibility of DNA to excision repair enzymes
-
-
-
additional information
?
-
-
the enzyme modifies eukaryotic 21000-24000 Da GTP-binding proteins
-
-
-
additional information
?
-
-
transcriptional regulation mechanism, overview
-
-
-
additional information
?
-
-
the enzyme also shows NAD+-hydrolase activity
-
-
-
additional information
?
-
-
ADP-ribosylation seems to be involved in regulation of differentiation, the enzyme may be centrally involved in tumorigenic cell transformation, the enzyme appears to be a central controller of cell processes: higher activities shift the cell towards proliferation, low activities shift the cell towards differentiation, role of the enzyme in DNA repair
-
-
-
additional information
?
-
-
role of the enzyme in DNA repair, the unmodified polymerase molecules bind tightly to DNA strand breaks: auto-poly(ADP-ribosyl)ation of the protein then effects its release and allows access to lesions for DNA repair enzymes
-
-
-
additional information
?
-
-
mechanistic basis for the physiological function of PARP-1 in the dynamics of the local modulation of chromatin structure. PARP-1 activation upon binding to base-unpaired regions and stem-loops structures in DNA leads to a local PAR modification of histones and non-histone proteins at genomic sites where such DNA structures are formed. Subsequent PARP-1 automodification results in its dissociation from DNA leading to an enzymatic self-inactivation thus ensuring a transient character of chromatin ADP-ribosylation. In combination with the PAR-glycohydrolase degradation of ADP-ribose polymers on acceptor proteins, PARP-1 interaction with DNA secondary structures provides a mechanism for local and transient chromatin modification by PAR during physiological nuclear processes
-
-
-
additional information
?
-
-
PARP-1 inhibits the transcription factor tonicity-responsive enhancer/osmotic response element-binding protein, TonEBP/OREBP. Inhibition of TonEBP/OREBP transcriptional activity by PARP-1 does not require PARP-1 catalytic activity, functional interaction anaylsis, overview
-
-
-
additional information
?
-
-
the enzyme is involved in pathogenesis of Parkinson's disease, analysis of polymorphisms, overview
-
-
-
additional information
?
-
-
the enzyme shows DNA-binding activity, and is physically associated with the transcription factor tonicity-responsive enhancer/osmotic response element-binding protein, TonEBP/OREBP
-
-
-
additional information
?
-
-
the enzyme has the ability to ADP-ribosylate itself
-
-
-
additional information
?
-
-
raft association focuses ART2.2 on specific targets that constitutively or inducibly assoiate with lipid rafts
-
-
-
additional information
?
-
-
ART1 is an arginine-specific transferase
-
-
-
additional information
?
-
-
PARP-1 is involved in modulation of NO-derived injury and response to genotoxic damage
-
-
-
additional information
?
-
-
PARP-1 plays an essential role in the control of cell repair and tissue remodeling after hyperoxia-induced lung injury, overview
-
-
-
additional information
?
-
-
PARP-1 plays fundamental roles in the recruitment and modulation of enzymatic and regulatory factors involved in transcription, DNA replication, repair and recombination, the enzyme antagonizes topoisomerase I-dependent recombination stimulation by P53
-
-
-
additional information
?
-
-
PARP-1 responds to DNA damage by transferring 50 to 200 molecules of ADP-ribose to various nuclear proteins, including transcription factors, histones and PARP-1 itself, interaction between ATM and PARP-1 in response to DNA damage and sensitization of ATM deficient cells through PARP inhibition, ATM and PARP-1 are two of the most important players in the cell's response to DNA damage, PARP-1 is needed for optimal activation of ATM, overview
-
-
-
additional information
?
-
-
role for PARP-1 in DNA double-strand break repair, the enzyme is not required for homologous recombination itself, it regulates the process through its involvement in the repair of DNA single-strand breaks, PARP-1 binds to DNA breaks to facilitate DNA repair, but the role of PARP-1 in DNA repair appears to not be critical since PARP-1 knockout mice are viable, fertile and do not develop early onset tumors, DNA binding and auto-modification of PARP-1 attracts the DNA repair proteins
-
-
-
additional information
?
-
-
the enzyme is involved in endothelial cell dysfunction
-
-
-
additional information
?
-
-
transcriptional regulation mechanism, overview
-
-
-
additional information
?
-
-
PARP-1 protein has an N-terminal DNA binding domain containing two large zinc fingers that bind to both DNA single-strand breaks and DNA double-strand breaks, DNA binding by PARP-1 triggers its activity and it adds poly(ADP-ribose) polymers to itself and to surrounding histones, overview
-
-
-
additional information
?
-
-
the enzyme itself is a target for P2X7-triggered ectodomain shedding at F239/S240
-
-
-
additional information
?
-
-
the enzyme is involved in endothelial cell dysfunction
-
-
-
additional information
?
-
-
PARP-1 plays an essential role in the control of cell repair and tissue remodeling after hyperoxia-induced lung injury, overview
-
-
-
additional information
?
-
-
narE possesses ADP-ribosylating and NAD-glycohydrolase activities
-
-
-
additional information
?
-
-
exoenzyme S and 14-3-3 interact in a direct fashion, interaction involves the conserved amphiphatic groove of 14-3-3
-
-
-
additional information
?
-
-
exoenzyme S is an important adhesin
-
-
-
additional information
?
-
-
ExoS is a virulence factor of the pathogen
-
-
-
additional information
?
-
-
Pseudomonas aeruginosa inhibits mammalian cytokinesis in a type III secretion system and exotoxin T-dependent manner, the ADP-ribosyl transferase domain inhibits late steps of cytokinesis by blocking syntaxin-2 localization to the midbody, an event essential for completion of cytokinesis, e.g. in Madin-Darby canine kidney cells, mechanism, overview
-
-
-
additional information
?
-
-
the bacterial enzyme shows the ability to mediate cell death in the host and is a toxin, residues 426-428 are required for this activity
-
-
-
additional information
?
-
-
exoenzyme S is a bifunctional type III secretion, TTS, effector protein, with GTPase-activating and ADP-ribosyltransferase activities
-
-
-
additional information
?
-
-
ExoS is a bifunctional toxin with an N-terminal Rho GTPase activating protein, GAP, domain, and a C-terminal ADP-ribosyltransferase domain which transfers ADP-ribose from NAD onto substrates such as the Ras GTPases and vimentin
-
-
-
additional information
?
-
-
ExoT is a bifunctional type III secretion system effector protein that contains an N-terminal GTPase-activating protein domain and a C-terminal ADP-ribosyl transferase domain
-
-
-
additional information
?
-
-
ExoS is a toxin playing a pivotal role during Pseudomonas aeruginosa infections, it is a virulence factor causing growth inhibition in Saccharomyces cerevisiae. Exoenzyme S ADP-ribosylates identical targets in both human and yeast
-
-
-
additional information
?
-
-
ExoS is a type III cytotoxin, that ADP-ribosylates Rab GTPases to inhibit host cell vesicle trafficking pathways by modulating HeLa host cell endocytosis, wild-type ExoS uncouples Rab5-early endosome antigen 1 interaction and inhibits fluid phase uptake, as well as Pseudomonas aeruginosa internalization, RhoGAP, but not ADPr, the ADPr domain is dispensable for anti-internalization function, but is required for inhibition of EGF-activated EGFR degradation in HeLa cells, mechanism, overview
-
-
-
additional information
?
-
-
ExoS is a bi-functional type III cytotoxin that possesses Rho GTPase activating protein and ADP-ribosyltransferase activities, no activity with Rab4 protein, overview
-
-
-
additional information
?
-
-
exoenzyme S is a bifunctional type III secretion, TTS, effector protein, with GTPase-activating and ADP-ribosyltransferase activities
-
-
-
additional information
?
-
-
ExoS is a type III cytotoxin, that ADP-ribosylates Rab GTPases to inhibit host cell vesicle trafficking pathways by modulating HeLa host cell endocytosis, wild-type ExoS uncouples Rab5-early endosome antigen 1 interaction and inhibits fluid phase uptake, as well as Pseudomonas aeruginosa internalization, RhoGAP, but not ADPr, the ADPr domain is dispensable for anti-internalization function, but is required for inhibition of EGF-activated EGFR degradation in HeLa cells, mechanism, overview
-
-
-
additional information
?
-
-
ExoS is a bi-functional type III cytotoxin that possesses Rho GTPase activating protein and ADP-ribosyltransferase activities, no activity with Rab4 protein, overview
-
-
-
additional information
?
-
the enzyme also targets deoxyguanosine
-
-
-
additional information
?
-
-
the enzyme also targets deoxyguanosine
-
-
-
additional information
?
-
the enzyme also targets deoxyguanosine
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
integrin alpha7 + NAD+
(ADP-D-ribosyl)-integrin alpha7 + nicotinamide
-
the extracellular domain of integrin alpha7 is ADP-ribosylated by an arginine-specific ecto-ADP-ribosyltransferase after adding exogenous NAD+ to intact C2C12 muscle cells, integrin alpha7 N-terminal ADP-ribosylation inhibits the binding of integrin alpha7beta1 to laminin activation status of integrin alpha7beta1 in intact myotubes, overview
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
NAD+ + (ADP-D-ribosyl)n-aryl hydrocarbon receptor
nicotinamide + (ADP-D-ribosyl)n+1-aryl hydrocarbon receptor + H+
Q7Z3E1
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-NEMO protein
nicotinamide + (ADP-D-ribosyl)n+1-NEMO protein + H+
-
the enzyme prevents poly-ubiquitination of NEMO protein
-
-
?
NAD+ + (ADP-D-ribosyl)n-p21ras
nicotinamide + (ADP-D-ribosyl)n+1-p21ras
-
ADP-ribosylation of p21ras does not alter interactions with guanidine nucleotides. Possible function of the enzyme in pathogenesis
-
-
?
NAD+ + (ADP-D-ribosyl)n-P2X7 ion channel
nicotinamide + (ADP-D-ribosyl)n+1-P2X7 ion channel + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-rab4
nicotinamide + (ADP-D-ribosyl)n+1-rab4
-
ADP-ribosylation affects Rab4 function in membrane recycling
-
-
?
NAD+ + (ADP-D-ribosyl)n-Rab5
nicotinamide + (ADP-D-ribosyl)n+1-Rab5
-
ADP-ribosylation of Rab5 by ExoS affects endocytosis. Interaction of Rab5 with endosome antigen 1 is markedly diminished after Rab5 ADP-ribosylation by ExoS
-
-
?
NAD+ + (ADP-D-ribosyl)n-RalA
nicotinamide + (ADP-D-ribosyl)n+1-RalA
-
ADP-ribosylation of RalA by ExoS interferes with RalA activation and binding to its downstream effector in J774A.1 macrophages and suggests the potential of ExoS ADPRT activity to interfere with filiopodium formation through the inactivation of RalA and downstream effects mediated through the exocyst complex
-
-
?
NAD+ + (ADP-D-ribosyl)n-Ras
nicotinamide + (ADP-D-ribosyl)n+1-Ras
-
ADP-ribosylation of Ras at Arg41 disrupts Ras-Cdc25 interactions, which inhibits the rate-limiting step in Ras signal transduction, the activation of Ras by its guanine nucleotide exchange factor
-
-
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
NAD+ + histone H2A
nicotinamide + (ADP-D-ribosyl)-histone H2A
-
the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B. Histone modification by TbSIR2RP1 is involved in DNA repair
-
-
?
NAD+ + histone H2B
nicotinamide + (ADP-D-ribosyl)-histone H2B
-
the enzyme catalyses both ADP-ribosylation and deacetylation of histones, particulary H2A and H2B. Histone modification by TbSIR2RP1 is involved in DNA repair
-
-
?
NAD+ + moesin
nicotinamide + (ADP-D-ribosyl)-moesin
-
ADP-ribosylated-moesin is a poor target for phosphorylation by protein kinase C and Rho kinase, which shows that ADP-ribosylation directly inhibits ERM phosphorylation
-
-
?
NAD+ + p53
nicotinamide + (ADP-D-ribosyl)-p53
-
-
-
-
?
NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
NAD+ + Ras
nicotinamide + (ADP-D-ribosyl)-Ras
-
interaction requires residue Leu428
-
-
?
NAD+ + Ras GTPase
nicotinamide + (ADP-D-ribosyl)-Ras GTPase
-
-
-
-
?
NAD+ + RNA polymerase
nicotinamide + (ADP-D-ribosyl)-RNA polymerase
P12726
three ADP-ribosyltransferases, Alt, ModA, and ModB participate in the regulation of the T4 replication cycle by ADP-ribosylating a defined set of host proteins. ADP-ribosylation of RNA polymerase and of other host proteins allows initial phage-directed mRNA synthesis reactions to escape from host control
-
-
?
NAD+ + topoisomerase I
nicotinamide + (ADP-D-ribosyl)-topoisomerase I
-
-
-
-
?
NAD+ + vimentin
nicotinamide + (ADP-D-ribosyl)-vimentin
-
-
-
-
?
additional information
?
-
NAD+ + (ADP-D-ribosyl)n-acceptor

nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
the enzyme is a DNA repair enzyme
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation, i.e. PARylation, plays diverse roles in many molecular and cellular processes, including DNA damage detection and repair, chromatin modification, transcription, cell death pathways, insulator function, and mitotic apparatus function, connections between nuclear NAD+ metabolism and nuclear signaling through PARP-1, physiologic functions, detailed overview, synthesis and degradation of PAR on an acceptor protein, pathway overview, the enzyme is involved in regulation of the steady-state levels of PAR
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
O95271, P09874, Q2NL67, Q460N5, Q8N5Y8, Q9NR21, Q9UGN5, Q9UKK3, Q9Y6F1
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
poly(ADP-ribosyl)ation, i.e. PARylation, plays diverse roles in many molecular and cellular processes, including DNA damage detection and repair, chromatin modification, transcription, cell death pathways, insulator function, and mitotic apparatus function, connections between nuclear NAD+ metabolism and nuclear signaling through PARP-1, physiologic functions, detailed overview, synthesis and degradation of PAR on an acceptor protein, pathway overview, the enzyme is involved in regulation of the steady-state levels of PAR
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ADPRT domain of ExoT is active in vivo and contributes to the pathogenesis of Pseudomonas aeruginosa infections
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
exoenzyme S is an ADP-ribosyltransferase produced and directly translocated into eukaryotic cells by the opportunistic pathogen Pseudomonas aeruginosa. Factors expressed by growing epithelial cells are required for the bacterial contact-dependent translocation of ExoS. As normal epithelial cells differentiate into polarized confluent monolayers, expression of these factors is altered, and cells in turn become more resistant to the effects of ExoS
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoS can modify multiple GTPases of the Ras superfamily in vivo. ExoS modulates the activity of several of GTP-binding proteins, such as Ras, Rap1, Rap2, Ral, Rac1, RhoA and Cdc42. It is suggested that ExoS is the major ADP-ribosyltransferase protein modulating small GTPase function encoded by Pseudomonas aeruginosa
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
ExoT modifies and inactivates host cell proteins involved in maintaining the actin cytoskeleton in vivo by two independent mechanisms. ADP-ribosylation activity of ExoT induces an irreversible disruption of actin microfilaments of infected Hela cells
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
intracellular expression of the amino terminus of ExoS in eukaryotic cells stimulates actin reorganization without cytotoxicity, which involves small-molecular-weight GTPases of the Rho subfamily
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor
-
intracellular Ras is modified by bacterially translocated ExoS, inhibition of target cell proliferation correlates with the efficiency of Ras modification
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor

nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Q9Y6F1
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
Q9JZ10
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
-
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
C9Z6T8
the enzyme labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA
-
-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
C9Z6T8
the enzyme labels the exocyclic amino group on guanine bases in either single-stranded or double-stranded DNA
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-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
-
the emzyme protects homologous DNA against thermal denaturation by lowering the amount of melted DNA and increasing melting temperature. The archaeal protein induces structural changes of the nucleic acid by modifying the dichroic spectra towards a shape typical of condensing DNA
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-
?
NAD+ + (ADP-D-ribosyl)n-acceptor
nicotinamide + (ADP-D-ribosyl)n+1-acceptor + H+
B3EWG9
the emzyme protects homologous DNA against thermal denaturation by lowering the amount of melted DNA and increasing melting temperature. The archaeal protein induces structural changes of the nucleic acid by modifying the dichroic spectra towards a shape typical of condensing DNA
-
-
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein

nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
W2E3J5
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-
-
?
NAD+ + (ADP-D-ribosyl)n-RhoA protein
nicotinamide + (ADP-D-ribosyl)n+1-RhoA protein + H+
W2E3J5
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-
-
?
NAD+ + cyclophilin A

nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
cytosolic protein of several human epithelial cells, modification at Arg55 and Arg69 of cyclophilin A, ADP-ribosylation of CpA efficiently inhibits CpA binding to calcineurin/PP2B phosphatase, overview
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-
?
NAD+ + cyclophilin A
nicotinamide + (ADP-D-ribosyl)-cyclophilin A
-
cytosolic protein of several human epithelial cells, modification at Arg55 and Arg69 of cyclophilin A, ADP-ribosylation of CpA efficiently inhibits CpA binding to calcineurin/PP2B phosphatase, overview
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-
?
NAD+ + Rab5 protein

nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
-
Rab5 mediates entry of the EGFR into early endosomes
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?
NAD+ + Rab5 protein
nicotinamide + (ADP-D-ribosyl)-Rab5 protein + H+
-
Rab5 mediates entry of the EGFR into early endosomes
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-
?
NAD+ + Rab9 protein

nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
-
-
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?
NAD+ + Rab9 protein
nicotinamide + (ADP-D-ribosyl)-Rab9 protein + H+
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?
additional information

?
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cuts produced in vivo on DNA during DNA repair activate the enzyme, which then synthesiszes poly(ADP-ribose) on histone H1, in particular, and contributes to the opening of the 25 nm chromatin fiber, resulting in the increased accessibility of DNA to excision repair enzymes
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additional information
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the enzyme modifies eukaryotic 21000-24000 Da GTP-binding proteins
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additional information
?
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transcriptional regulation mechanism, overview
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additional information
?
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ADP-ribosylation seems to be involved in regulation of differentiation, the enzyme may be centrally involved in tumorigenic cell transformation, the enzyme appears to be a central controller of cell processes: higher activities shift the cell towards proliferation, low activities shift the cell towards differentiation, role of the enzyme in DNA repair
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additional information
?
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role of the enzyme in DNA repair, the unmodified polymerase molecules bind tightly to DNA strand breaks: auto-poly(ADP-ribosyl)ation of the protein then effects its release and allows access to lesions for DNA repair enzymes
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additional information
?
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mechanistic basis for the physiological function of PARP-1 in the dynamics of the local modulation of chromatin structure. PARP-1 activation upon binding to base-unpaired regions and stem-loops structures in DNA leads to a local PAR modification of histones and non-histone proteins at genomic sites where such DNA structures are formed. Subsequent PARP-1 automodification results in its dissociation from DNA leading to an enzymatic self-inactivation thus ensuring a transient character of chromatin ADP-ribosylation. In combination with the PAR-glycohydrolase degradation of ADP-ribose polymers on acceptor proteins, PARP-1 interaction with DNA secondary structures provides a mechanism for local and transient chromatin modification by PAR during physiological nuclear processes
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additional information
?
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PARP-1 inhibits the transcription factor tonicity-responsive enhancer/osmotic response element-binding protein, TonEBP/OREBP. Inhibition of TonEBP/OREBP transcriptional activity by PARP-1 does not require PARP-1 catalytic activity, functional interaction anaylsis, overview
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additional information
?
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the enzyme is involved in pathogenesis of Parkinson's disease, analysis of polymorphisms, overview
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additional information
?
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the enzyme has the ability to ADP-ribosylate itself
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additional information
?
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raft association focuses ART2.2 on specific targets that constitutively or inducibly assoiate with lipid rafts
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additional information
?
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PARP-1 is involved in modulation of NO-derived injury and response to genotoxic damage
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additional information
?
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PARP-1 plays an essential role in the control of cell repair and tissue remodeling after hyperoxia-induced lung injury, overview
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additional information
?
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PARP-1 plays fundamental roles in the recruitment and modulation of enzymatic and regulatory factors involved in transcription, DNA replication, repair and recombination, the enzyme antagonizes topoisomerase I-dependent recombination stimulation by P53
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additional information
?
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PARP-1 responds to DNA damage by transferring 50 to 200 molecules of ADP-ribose to various nuclear proteins, including transcription factors, histones and PARP-1 itself, interaction between ATM and PARP-1 in response to DNA damage and sensitization of ATM deficient cells through PARP inhibition, ATM and PARP-1 are two of the most important players in the cell's response to DNA damage, PARP-1 is needed for optimal activation of ATM, overview
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additional information
?
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role for PARP-1 in DNA double-strand break repair, the enzyme is not required for homologous recombination itself, it regulates the process through its involvement in the repair of DNA single-strand breaks, PARP-1 binds to DNA breaks to facilitate DNA repair, but the role of PARP-1 in DNA repair appears to not be critical since PARP-1 knockout mice are viable, fertile and do not develop early onset tumors, DNA binding and auto-modification of PARP-1 attracts the DNA repair proteins
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additional information
?
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the enzyme is involved in endothelial cell dysfunction
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additional information
?
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transcriptional regulation mechanism, overview
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additional information
?
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the enzyme itself is a target for P2X7-triggered ectodomain shedding at F239/S240
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additional information
?
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the enzyme is involved in endothelial cell dysfunction
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additional information
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PARP-1 plays an essential role in the control of cell repair and tissue remodeling after hyperoxia-induced lung injury, overview
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additional information
?
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exoenzyme S and 14-3-3 interact in a direct fashion, interaction involves the conserved amphiphatic groove of 14-3-3
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additional information
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exoenzyme S is an important adhesin
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additional information
?
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ExoS is a virulence factor of the pathogen
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additional information
?
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Pseudomonas aeruginosa inhibits mammalian cytokinesis in a type III secretion system and exotoxin T-dependent manner, the ADP-ribosyl transferase domain inhibits late steps of cytokinesis by blocking syntaxin-2 localization to the midbody, an event essential for completion of cytokinesis, e.g. in Madin-Darby canine kidney cells, mechanism, overview
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additional information
?
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the bacterial enzyme shows the ability to mediate cell death in the host and is a toxin, residues 426-428 are required for this activity
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additional information
?
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ExoS is a toxin playing a pivotal role during Pseudomonas aeruginosa infections, it is a virulence factor causing growth inhibition in Saccharomyces cerevisiae. Exoenzyme S ADP-ribosylates identical targets in both human and yeast
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additional information
?
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ExoS is a type III cytotoxin, that ADP-ribosylates Rab GTPases to inhibit host cell vesicle trafficking pathways by modulating HeLa host cell endocytosis, wild-type ExoS uncouples Rab5-early endosome antigen 1 interaction and inhibits fluid phase uptake, as well as Pseudomonas aeruginosa internalization, RhoGAP, but not ADPr, the ADPr domain is dispensable for anti-internalization function, but is required for inhibition of EGF-activated EGFR degradation in HeLa cells, mechanism, overview
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-
additional information
?
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-
ExoS is a type III cytotoxin, that ADP-ribosylates Rab GTPases to inhibit host cell vesicle trafficking pathways by modulating HeLa host cell endocytosis, wild-type ExoS uncouples Rab5-early endosome antigen 1 interaction and inhibits fluid phase uptake, as well as Pseudomonas aeruginosa internalization, RhoGAP, but not ADPr, the ADPr domain is dispensable for anti-internalization function, but is required for inhibition of EGF-activated EGFR degradation in HeLa cells, mechanism, overview
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(2S)-2-[[3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoyl]amino]-3-phenylpropanamide
-
(beta,beta-dimethylacryl)shikonin
64% inhibition at 0.01 mM; 64% inhibition at 0.01 mM
0469-0796
-
restores yeast growth after treatment with ExoS
1(2H)-phthalazinone
-
IC50: 0.012 mM
1,2-benzopyrone
-
IC50: 2.8 mM
1,3-benzodiazine
-
IC50: 2.0 mM
1,3-dihydroxynaphthalene
-
IC50: 1.3 mM
1,4-benzoquinone
-
IC50: 0.4 mM
1,4-naphthalenedione
-
IC50: 0.25 mM
1,5-dihydroxyisoquinoline
-
IC50: 0.00039 mM
1,8-naphthalimide
-
IC50: 0.0014 mM
1-hydroxy-2-methyl-4-aminonaphthalene
-
IC50: 1.3 mM
1-hydroxyisoquinoline
-
IC50: 0.007 mM
1-Indanone
-
IC50: 0.81 mM
1-methylnicotinamide chloride
2,3-benzodiazine
-
IC50: 0.15 mM
2,3-dichloro-1,4-naphthoquinone
-
IC50: 0.26 mM
2,3-dihydro-1,4-phthalazinedione
-
IC50: 0.03 mM
2,3-dihydro-5-hydroxy-1,4-phthalazinedione
-
0.001 mM, 95% inhibition of the 116000 Da enzyme
-
2,4(1H,3H)-quinazolinedione
-
IC50: 0.0081 mM
2,6-difluorobenzamide
-
IC50: 0.18 mM
2-(3-hydroxypropyl)-3,5,6,7-tetrahydro-4H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-4-one
-
-
2-(3-hydroxypropyl)-5,6,7,8-tetrahydro[1]benzothieno[2,3-d]pyrimidin-4(3H)-one
-
-
2-(4-[4-[(2,4-dimethoxyphenyl)amino]quinazolin-2-yl]piperazin-1-yl)ethanol
Q49TP5
-
2-acetamidobenzamide
-
IC50: 1.0 mM
2-amino-3-chloro-1,4-naphthoquinone
-
IC50: 0.82 mM
2-bromobenzamide
-
IC50: 2.9 mM
2-chlorobenzamide
-
IC50: 1.0 mM
2-fluorobenzamide
-
IC50: 0.12 mM
2-Hydroxy-1,4-naphthoquinone
-
IC50: 0.33 mM
2-hydroxybenzamide
-
IC50: 0.82 mM
2-mercapto-4(3H)-quinazolinone
-
IC50: 0.044 mM
2-Methoxybenzamide
-
IC50: 0.2 mM
2-methyl-1,4-benzopyrone
-
IC50: 0.045 mM
2-methyl-1,4-naphthoquinone
-
IC50: 0.42 mM
2-methyl-3-phytyl-1,4-naphthoquinone
-
IC50: 0.52 mM
2-methyl-4(3H)-quinazolinone
-
IC50: 0.056 mM
2-methylbenzamide
-
IC50: 1.5 mM
2-methylchromone
-
IC50: 0.045 mM
2-nitro-6(5H)-phenanthridione
-
IC50: 0.00035 mM
2-phenylchromone
-
IC50: 0.022 mM
2-trichloromethyl-4(3H)-quinazolinone
-
IC50: 2.2 mM
2-[[3-(dimethylamino)-2-oxopropyl]amino]-5,6-dihydrophenanthridin-6-one
potent inhibitor
2H-benz[c]isoquinolin-1-one
-
IC50: 0.0003 mM
2H-benz[de]isoquinoline-1,3-dione
-
IC50: 0.0014 mM
3,4-dihydro-1(2H)-naphthalenone
-
IC50: 0.31 mM
3,5-dibromosalicylamide
-
IC50: 0.56 mM
3,5-dimethoxybenzamide
-
IC50: 1.2 mM
3,5-dinitrobenzamide
-
IC50: 2.5 mM
3-(4-methoxy-6,7-dihydro-5H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-2-yl)propanoic acid
-
-
3-(4-oxo-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl)propanoic acid
-
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1R)-1-(pyridin-2-yl)ethyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1R)-1-phenylethyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-(pyridin-2-yl)ethyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-phenylethyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-phenylpropyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[1-(4-sulfamoylphenyl)ethyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[1-(pyridin-2-yl)ethyl]propanamide
-
3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoic acid
-
-
3-(4-oxo-3,5,6,7-tetrahydro-4H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-2-yl)propanoic acid
-
inhibitor with micromolar potency
3-(N,N-dimethylamino)benzamide
-
IC50: 0.12 mM
3-Acetamidobenzamide
-
IC50: 0.012 mM
3-acetamidosalicylamide
-
IC50: 2.0 mM
3-amino-1,4-dimethyl-5H-pyrido[4,3-b]indole
-
i.e. Trp-P-1, 94% inhibition at 5 mM, IC50: 0.22 mM
3-amino-1-methyl-5H-pyrido[4,3-b]indole
-
i.e. Trp-P-2, 34% activation at 1 mM, 7% inhibition at 5 mM, IC50: 2.2 mM
3-aminobenzoic acid
-
1 mM, 12% inhibition
3-bromobenzamide
-
IC50: 0.055 mM
3-Chlorobenzamide
-
IC50: 0.22 mM
3-Fluorobenzamide
-
IC50: 0.2 mM
3-Guanidinobenzamide
-
0.1 mM, 71% inhibition of the 116000 Da enzyme
3-isobutyl-1-methylxanthine
-
IC50: 3.1 mM
3-Methylbenzamide
-
IC50: 0.19 mM
3-nitrobenzamide
-
IC50: 0.16 mM
3-nitrophthalhydrazide
-
IC50: 0.072 mM
3-nitrosalicylamide
-
IC50: 1.6 mM
4,8-dihydroxy-2-quinolinecarboxylic acid
-
IC50: 0.19 mM
4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanoic acid
-
-
4-amino-1,8-naphthalimide
-
IC50: 0.00018 mM
4-aminophthalhydrazide
-
IC50: 0.29 mM
4-bromobenzamide
-
IC50: 2.2 mM
4-chlorobenzamide
-
IC50: 0.3 mM
4-chromanone
-
IC50: 0.72 mM
4-fluorobenzamide
-
IC50: 0.2 mM
4-hydroxy-2-methylquinoline
-
IC50: 0.074 mM
4-hydroxy-2-quinolinecarboxylic acid
-
IC50: 0.67 mM
4-hydroxybenzamide
-
IC50: 0.28 mM
4-Hydroxycoumarin
-
IC50: 0.57 mM
4-hydroxypyridine
-
IC50: 2.3 mM
4-hydroxyquinazoline
-
IC50: 0.0095 mM
4-hydroxyquinoline
-
IC50: 0.08 mM
4-methoxybenzamide
-
IC50: 1.1 mM
4-methylbenzamide
-
IC50: 1.8 mM
4-nitrophthalhydrazide
-
IC50: 0.51 mM
4-[8-fluoro-6-oxo-1H,2H,3H,4H,5H,6H-benzo[c]1,6-naphthyridin-2-yl]butanoic acid
-
4-[[[6-cyano-1-[(1-methyl-1H-imidazol-5-yl)methyl]-1,2,3,4,6,7-hexahydroquinolin-3-yl](pyridin-2-ylsulfonyl)amino]methyl]-N,N-dimethylpiperidine-1-carboxamide
-
activates in presence of Mg2+, inhibits in absence of Mg2+
4296-1011
-
restores yeast growth after treatment with ExoS
5-acetamidosalicylamide
-
IC50: 0.045 mM
5-aminosalicylamide
-
IC50: 0.1 mM
5-bromodeoxyuridine
-
IC50: 0.015 mM
5-Bromouracil
-
IC50: 0.16 mM
5-Bromouridine
-
IC50: 0.21 mM
5-chlorosalicylamide
-
IC50: 0.19 mM
5-Chlorouracil
-
IC50: 0.27 mM
5-hydroxy-1,4-naphthoquinone
-
IC50: 0.25 mM
5-Hydroxy-2-methyl-1,4-naphthoquinone
-
IC50: 0.7 mM
5-Iodouracil
-
IC50: 0.071 mM
5-iodouridine
-
IC50: 0.043 mM
5-methyluracil
-
IC50: 0.29 mM
5-Nitrouracil
-
IC50: 0.43 mM
6(5H)-phenanthridinone
-
IC50: 0.0003 mM
6-aminocoumarin
-
IC50: 0.85 mM
6-aminonicotinamide
-
IC50: 1.1 mM
8-acetamidocarsalam
-
IC50: 1.4 mM
8-fluoro-2-[3-(piperidin-1-yl)propanesulfonyl]-1H,2H,3H,4H,5H,6H-benzo[c]1,6-naphthyridin-6-one
-
8-fluoro-2-[3-(piperidin-1-yl)propyl]-1H,2H,3H,4H,5H,6H-benzo[c]1,6-naphthyridin-6-one
-
8-Methylnicotinamide
-
IC50: 7.8 mM
acetophenone
-
IC50: 2.3 mM
ADP-D-ribose
-
5 mM, remaining activity: 7.3%
all-trans-retinal
-
IC50: 0.45 mM
Alpha-NAD+
-
0.5 mM, 40% inhibition of the 116000 Da enzyme, 44% inhibition of the 90000 Da enzyme
alpha-picolinamide
-
IC50: 0.25 mM
AMP
-
1 mM, remaining activity: 3.6%
benzoyleneurea
-
IC50: 0.0081 mM
bergapten
69% inhibition at 0.01 mM; 69% inhibition at 0.01 mM
carbonylsalicylamide
-
IC50: 0.46 mM
carsalam
-
5 mM, 88% inhibition in presence of Mg2+, 68% inhibition in absence of Mg2+
Chlorthenoxazin
-
IC50: 0.0085 mM
chromone-2-carboxylic acid
-
IC50: 0.56 mM
cyclohexanecarboxamide
-
IC50: 0.62 mM
deoxyshikonin
67% inhibition at 0.01 mM; 67% inhibition at 0.01 mM
diosmin
-
restores yeast growth after treatment with ExoS
DMSO
at 2% (v/v) DMSO isoform ARTD10 loses more than half of its activity; at 2% (v/v) DMSO isoform ARTD7 loses its activity completely
E216-5303
-
restores yeast growth after treatment with ExoS
EB-47
i.e. 5'-deoxy-5'-[4-[2-[(2,3-dihydro-1-oxo-1H-isoindol-4-yl)amino]-2-oxoethyl]-1-piperazinyl]-5'-oxoadenosine dihydrochloride; i.e. 5'-deoxy-5'-[4-[2-[(2,3-dihydro-1-oxo-1H-isoindol-4-yl)amino]-2-oxoethyl]-1-piperazinyl]-5'-oxoadenosine dihydrochloride
EDTA
-
5 mM, 41% inhibition in presence of Mg2+, 2% inhibition in absence of Mg2+
embelin
57% inhibition at 0.01 mM; 57% inhibition at 0.01 mM
everninic acid
-
restores yeast growth after treatment with ExoS
exosin
-
a small molecule inhibitor, that modulates ExoS ADP-ribosyltransferase activity in vitro, suggesting the inhibition is direct. Exosin and two of its analogues display a significant protective effect against Pseudomonas infection in vivo, competitive against NAD+
flavokawain B
-
restores yeast growth after treatment with ExoS
gambogic acid
75% inhibition at 0.01 mM; 75% inhibition at 0.01 mM
gamma-linolenic acid
-
IC50: 0.12 mM
gossypol
75% inhibition at 0.01 mM; 75% inhibition at 0.01 mM
GTP(gammaS)
-
in presence of Mg2+
hypoxanthine
-
IC50: 1.7 mM
Isonicotinamide
-
IC50: 0.99 mM
Isonicotinate hydrazide
-
IC50: 4.8 MM
Isoquinoline
-
5 mM, 47% inhibition in presence of Mg2+, 34% inhibition in absence of Mg2+
linoleic acid
-
IC50: 0.048 mM
linolenic acid
-
IC50: 0.11 mM
m-acetamidoacetophenone
-
IC50: 0.93 mM
m-aminoacetophenone
-
IC50: 1.9 mM
m-hydroxyacetophenone
-
IC50: 0.6 mM
m-phthalamide
-
IC50: 0.05 mM
menadione
55% inhibition at 0.01 mM; 55% inhibition at 0.01 mM
menadione sodium bisulfite
-
IC50: 0.72 mM
methyl (2S)-2-[[3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoyl]amino]-3-phenylpropanoate
-
myricetin
78% inhibition at 0.01 mM; 78% inhibition at 0.01 mM
N-(2-chloroethyl)1,8-naphthalamide
-
IC50: above 1.8 mM
N-(6-oxo-5,6-dihydrophenanthrolin-2-yl)-(N,N-dimethylamino)acetamide
-
0.1 mM, remaining activity: 36.2%
N-(acridin-9-yl)-4-nitrobenzamide
Q49TP5
-
N-hydroxynaphthalimide sodium salt
-
IC50: 0.45 mM
N-[(1R)-2,3-dihydro-1H-inden-1-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[(1S)-2,3-dihydro-1H-inden-1-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[(2S)-1-hydroxy-3-phenylpropan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[(2S)-1-hydroxybutan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[(2S)-1-hydroxypropan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[1-[4-(1H-imidazol-1-yl)phenyl]ethyl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
-
N-[2-oxo-4-(phenylamino)-3,8a-dihydro-2H-chromen-3-yl]acetamide
Q49TP5
-
N-[[1-(1H-pyrazolo[3,4-d]pyrimidin-4-yl)piperidin-3-yl]methyl]methanesulfonamide
-
novobiocin
-
IC50: 2.2 mM, 5 mM, 90% inhibition in presence of Mg2+, 59% inhibition in absence of Mg2+
olaparib
i.e. 4-[(3-[(4-cyclopropylcarbonyl)piperazin-4-yl]carbonyl)-4-fluorophenyl]methyl(2H)phthalazin-1-one; i.e. 4-[(3-[(4-cyclopropylcarbonyl)piperazin-4-yl]carbonyl)-4-fluorophenyl]methyl(2H)phthalazin-1-one
oleic acid
-
IC50: 0.082 mM
palmitoleic acid
-
IC50: 0.095 mM
phenanthridinone
-
5 mM, remaining activity: 35.1%
phenantridinone
i.e. 6(5H)-phenantridinone; i.e. 6(5H)-phenantridinone
phthalamide
-
IC50: 1.0 mM
Phthalazine
-
5 mM, 91% inhibition in presence of Mg2+, 79% inhibition in absence of Mg2+
PJ34
-
potent PARP inhibitor
Plumbagin
67% inhibition at 0.01 mM; 67% inhibition at 0.01 mM
Pyrazinamide
-
IC50: 0.13 mM
Quinazoline
-
5 mM, 63% inhibition in presence of Mg2+, 50% inhibition in absence of Mg2+
reserpine
-
IC50: 0.79 mM
thiobenzamide
-
IC50: 0.62 mM
Thionicotinamide
-
IC50: 1.8 mM
TIQ-A
i.e. 4H-thieno[2,3-c]isoquinolin-5-one; i.e. 4H-thieno[2,3-c]isoquinolin-5-one
trans-decahydro-1-naphthalenone
-
IC50: 4.3 mM
trimethylpsoralen
61% inhibition at 0.01 mM; 61% inhibition at 0.01 mM
vitamin K1
-
IC50: 0.0019 mM
vitamin K3
-
IC50: 0.42 mM
xanthurenic acid
-
5 mM, 88% inhibition in presence of Mg2+, 65% inhibition in absence of Mg2+
Zinc acetate
-
0.1 mM, remaining activity: 0.5%
1-methylnicotinamide chloride

-
IC50: 3.8 mM
1-methylnicotinamide chloride
-
IC50: 1.7 mM
2-Aminobenzamide

-
IC50: 0.65 mM
2-Aminobenzamide
-
IC50: 0.1 mM
3-aminobenzamide

-
IC50: 0.33 mM
3-aminobenzamide
-
IC50: 0.0054
3-aminobenzamide
-
1 mM, remaining activity: 3.9%
3-aminobenzamide
-
1 mM, 98% inhibition
3-aminobenzamide
-
1 mM, 99% inhibition
3-aminobenzamide
-
10 mM, 47% inhibition; 10 mM, 47% inhibition
3-Aminophthalhydrazide

-
IC50: 0.023 mM
3-Aminophthalhydrazide
-
0.1 mM, 98% inhibition of the 116000 Da enzyme
3-Hydroxybenzamide

-
IC50: 0.0091 mM
3-Hydroxybenzamide
-
0.1 mM, 89% inhibition of the 116000 Da enzyme
3-Methoxybenzamide

-
IC50: 0.017 mM
3-Methoxybenzamide
-
IC50: 0.0034 mM
3-Methoxybenzamide
-
0.01 mM, 85% inhibition of the 116000 Da enzyme, 84% inhibition of the 90000 Da enzyme; 1 mM, 96% inhibition of the 116000 Da enzyme, 95% inhibition of the 90000 Da enzyme
3-Methoxybenzamide
-
1 mM, 98% inhibition
4-Aminobenzamide

-
IC50: 1.8 mM
4-Aminobenzamide
-
IC50: 0.4 mM
5-Methylnicotinamide

-
IC50: 0.35 mM
5-Methylnicotinamide
-
IC50: 0.07
5-Methylnicotinamide
Cryptothecodinium cohnii
-
0.15 mM, 31% inhibition
Benzamide

-
IC50: 0.22 mM
Benzamide
-
IC50: 0.0033 mM
Benzamide
Cryptothecodinium cohnii
-
0.15 mM, 48% inhibition
Caffeine

-
IC50: 1.4 mM
Caffeine
-
1 mM, 86% inhibition of the 116000 Da enzyme, 57% inhibition of the 90000 Da enzyme
Caffeine
-
1 mM, 23% inhibition
KCl

-
0.05 mM, remaining activity: 6.8%
KCl
-
100 mM, 85% inhibition of the 90000 Da enzyme
nicotinamide

-
IC50: 0.21 mM
nicotinamide
-
IC50: 0.031 mM
nicotinamide
-
0.05 mM, remaining activity: 27.3%
nicotinamide
Cryptothecodinium cohnii
-
0.15 mM, 25% inhibition
nicotinamide
-
1 mM, 96% inhibition of the 116000 Da enzyme, 95% inhibition of the 90000 Da enzyme
nicotinamide
-
1 mM, 91% inhibition
nicotinamide
-
1 mM, 93% inhibition
nicotinamide
-
10 mM, 14% inhibition; 10 mM, 14% inhibition
Theobromine

-
IC50: 0.11 mM
Theobromine
-
1 mM, 76% inhibition
theophylline

-
IC50: 0.0046
theophylline
Cryptothecodinium cohnii
-
0.15 mM, 62% inhibition
theophylline
-
1 mM, 68% inhibition of the 116000 Da enzyme, 39% inhibition of the 90000 Da enzyme
theophylline
-
1 mM, 72% inhibition
thymidine

-
IC50: 0.18 mM
thymidine
Cryptothecodinium cohnii
-
0.15 mM, 39% inhibition
thymidine
-
1 mM, 94% inhibition of the 116000 Da enzyme, 88% inhibition of the 90000 Da enzyme
thymidine
-
1 mM, 70% inhibition
Zn2+

-
ZnCl2, IC50: 0.077 mM
Zn2+
-
0.5 mM, 47% inhibition; 0.5 mM, 50% inhibition
additional information

-
comparison of the effects of heterocyclic amines acting as potent carcinogens on PARP-1 and the arginine-specific mono-ADP-ribosyltransferase A, MART-A, EC 2.4.2.31, overview
-
additional information
-
PARP inhibitors promote ATM activation through induction of double strand breaks
-
additional information
-
identification of small molecule inhibitors of Pseudomonas aeruginosa exoenzyme S using a yeast phenotypic screening, overview
-
additional information
-
phenanthroline has no or a slightly activating effect
-
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0.0038
(2S)-2-[[3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoyl]amino]-3-phenylpropanamide
Homo sapiens
Q9Y6F1
pH and temperature not specified in the publication
0.012
1(2H)-phthalazinone
Bos taurus
-
IC50: 0.012 mM
2.8
1,2-benzopyrone
Bos taurus
-
IC50: 2.8 mM
2
1,3-benzodiazine
Bos taurus
-
IC50: 2.0 mM
1.3
1,3-dihydroxynaphthalene
Bos taurus
-
IC50: 1.3 mM
0.4
1,4-benzoquinone
Bos taurus
-
IC50: 0.4 mM
0.25
1,4-naphthalenedione
Bos taurus
-
IC50: 0.25 mM
0.00039
1,5-dihydroxyisoquinoline
Bos taurus
-
IC50: 0.00039 mM
0.0014
1,8-naphthalimide
Bos taurus
-
IC50: 0.0014 mM
1.3
1-hydroxy-2-methyl-4-aminonaphthalene
Bos taurus
-
IC50: 1.3 mM
0.007
1-hydroxyisoquinoline
Bos taurus
-
IC50: 0.007 mM
0.81
1-Indanone
Bos taurus
-
IC50: 0.81 mM
1.7 - 3.8
1-methylnicotinamide chloride
0.15
2,3-benzodiazine
Bos taurus
-
IC50: 0.15 mM
0.26
2,3-dichloro-1,4-naphthoquinone
Bos taurus
-
IC50: 0.26 mM
0.03
2,3-dihydro-1,4-phthalazinedione
Bos taurus
-
IC50: 0.03 mM
0.0081
2,4(1H,3H)-quinazolinedione
Bos taurus
-
IC50: 0.0081 mM
0.18
2,6-difluorobenzamide
Bos taurus
-
IC50: 0.18 mM
0.0524
2-(3-hydroxypropyl)-3,5,6,7-tetrahydro-4H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-4-one
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
0.169
2-(3-hydroxypropyl)-5,6,7,8-tetrahydro[1]benzothieno[2,3-d]pyrimidin-4(3H)-one
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
1
2-acetamidobenzamide
Bos taurus
-
IC50: 1.0 mM
0.82
2-amino-3-chloro-1,4-naphthoquinone
Bos taurus
-
IC50: 0.82 mM
0.1 - 0.65
2-Aminobenzamide
2.9
2-bromobenzamide
Bos taurus
-
IC50: 2.9 mM
1
2-chlorobenzamide
Bos taurus
-
IC50: 1.0 mM
0.12
2-fluorobenzamide
Bos taurus
-
IC50: 0.12 mM
0.33
2-Hydroxy-1,4-naphthoquinone
Bos taurus
-
IC50: 0.33 mM
0.82
2-hydroxybenzamide
Bos taurus
-
IC50: 0.82 mM
0.044
2-mercapto-4(3H)-quinazolinone
Bos taurus
-
IC50: 0.044 mM
0.2
2-Methoxybenzamide
Bos taurus
-
IC50: 0.2 mM
0.045
2-methyl-1,4-benzopyrone
Bos taurus
-
IC50: 0.045 mM
0.42
2-methyl-1,4-naphthoquinone
Bos taurus
-
IC50: 0.42 mM
0.52
2-methyl-3-phytyl-1,4-naphthoquinone
Bos taurus
-
IC50: 0.52 mM
0.056
2-methyl-4(3H)-quinazolinone
Bos taurus
-
IC50: 0.056 mM
1.5
2-methylbenzamide
Bos taurus
-
IC50: 1.5 mM
0.045
2-methylchromone
Bos taurus
-
IC50: 0.045 mM
0.00035
2-nitro-6(5H)-phenanthridione
Bos taurus
-
IC50: 0.00035 mM
0.022
2-phenylchromone
Bos taurus
-
IC50: 0.022 mM
2.2
2-trichloromethyl-4(3H)-quinazolinone
Bos taurus
-
IC50: 2.2 mM
0.0003
2H-benz[c]isoquinolin-1-one
Bos taurus
-
IC50: 0.0003 mM
0.0014
2H-benz[de]isoquinoline-1,3-dione
Bos taurus
-
IC50: 0.0014 mM
0.31
3,4-dihydro-1(2H)-naphthalenone
Bos taurus
-
IC50: 0.31 mM
0.56
3,5-dibromosalicylamide
Bos taurus
-
IC50: 0.56 mM
1.2
3,5-dimethoxybenzamide
Bos taurus
-
IC50: 1.2 mM
2.5
3,5-dinitrobenzamide
Bos taurus
-
IC50: 2.5 mM
0.294
3-(4-methoxy-6,7-dihydro-5H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-2-yl)propanoic acid
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
0.0479
3-(4-oxo-3,4,5,6,7,8-hexahydro[1]benzothieno[2,3-d]pyrimidin-2-yl)propanoic acid
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
0.1
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1R)-1-(pyridin-2-yl)ethyl]propanamide
Homo sapiens
Q9Y6F1
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.0152
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1R)-1-phenylethyl]propanamide
Homo sapiens
Q9Y6F1
pH and temperature not specified in the publication
0.0013
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-(pyridin-2-yl)ethyl]propanamide
Homo sapiens
Q9Y6F1
pH and temperature not specified in the publication
0.0009
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-phenylethyl]propanamide
Homo sapiens
Q9Y6F1
pH and temperature not specified in the publication
0.0022
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[(1S)-1-phenylpropyl]propanamide
Homo sapiens
Q9Y6F1
pH and temperature not specified in the publication
0.0144
3-(4-oxo-3,4-dihydroquinazolin-2-yl)-N-[1-(4-sulfamoylphenyl)ethyl]propanamide
Homo sapiens
Q9Y6F1
pH and temperature not specified in the publication
0.135
3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoic acid
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
0.019
3-(4-oxo-3,5,6,7-tetrahydro-4H-cyclopenta[4,5]thieno[2,3-d]pyrimidin-2-yl)propanoic acid
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
0.12
3-(N,N-dimethylamino)benzamide
Bos taurus
-
IC50: 0.12 mM
0.012
3-Acetamidobenzamide
Bos taurus
-
IC50: 0.012 mM
2
3-acetamidosalicylamide
Bos taurus
-
IC50: 2.0 mM
0.22
3-amino-1,4-dimethyl-5H-pyrido[4,3-b]indole
Bos taurus
-
i.e. Trp-P-1, 94% inhibition at 5 mM, IC50: 0.22 mM
2.2
3-amino-1-methyl-5H-pyrido[4,3-b]indole
Bos taurus
-
i.e. Trp-P-2, 34% activation at 1 mM, 7% inhibition at 5 mM, IC50: 2.2 mM
0.0054 - 0.33
3-aminobenzamide
0.023
3-Aminophthalhydrazide
Bos taurus
-
IC50: 0.023 mM
0.055
3-bromobenzamide
Bos taurus
-
IC50: 0.055 mM
0.22
3-Chlorobenzamide
Bos taurus
-
IC50: 0.22 mM
0.2
3-Fluorobenzamide
Bos taurus
-
IC50: 0.2 mM
0.0091
3-Hydroxybenzamide
Bos taurus
-
IC50: 0.0091 mM
3.1
3-isobutyl-1-methylxanthine
Bos taurus
-
IC50: 3.1 mM
0.0034 - 0.017
3-Methoxybenzamide
0.19
3-Methylbenzamide
Bos taurus
-
IC50: 0.19 mM
0.16
3-nitrobenzamide
Bos taurus
-
IC50: 0.16 mM
0.072
3-nitrophthalhydrazide
Bos taurus
-
IC50: 0.072 mM
1.6
3-nitrosalicylamide
Bos taurus
-
IC50: 1.6 mM
0.19
4,8-dihydroxy-2-quinolinecarboxylic acid
Bos taurus
-
IC50: 0.19 mM
0.0249
4-(4-oxo-3,4-dihydroquinazolin-2-yl)butanoic acid
Pseudomonas aeruginosa
-
at pH 7.5 and 22°C
0.00018
4-amino-1,8-naphthalimide
Bos taurus
-
IC50: 0.00018 mM
0.4 - 1.8
4-Aminobenzamide
0.29
4-aminophthalhydrazide
Bos taurus
-
IC50: 0.29 mM
2.2
4-bromobenzamide
Bos taurus
-
IC50: 2.2 mM
0.3
4-chlorobenzamide
Bos taurus
-
IC50: 0.3 mM
0.72
4-chromanone
Bos taurus
-
IC50: 0.72 mM
0.2
4-fluorobenzamide
Bos taurus
-
IC50: 0.2 mM
0.074
4-hydroxy-2-methylquinoline
Bos taurus
-
IC50: 0.074 mM
0.67
4-hydroxy-2-quinolinecarboxylic acid
Bos taurus
-
IC50: 0.67 mM
0.28
4-hydroxybenzamide
Bos taurus
-
IC50: 0.28 mM
0.57
4-Hydroxycoumarin
Bos taurus
-
IC50: 0.57 mM
2.3
4-hydroxypyridine
Bos taurus
-
IC50: 2.3 mM
0.0095
4-hydroxyquinazoline
Bos taurus
-
IC50: 0.0095 mM
0.08
4-hydroxyquinoline
Bos taurus
-
IC50: 0.08 mM
1.1
4-methoxybenzamide
Bos taurus
-
IC50: 1.1 mM
1.8
4-methylbenzamide
Bos taurus
-
IC50: 1.8 mM
0.51
4-nitrophthalhydrazide
Bos taurus
-
IC50: 0.51 mM
0.006
4296-1011
Pseudomonas aeruginosa
-
pH 6.0, 30°C
0.045
5-acetamidosalicylamide
Bos taurus
-
IC50: 0.045 mM
0.1
5-aminosalicylamide
Bos taurus
-
IC50: 0.1 mM
0.015
5-bromodeoxyuridine
Bos taurus
-
IC50: 0.015 mM
0.16
5-Bromouracil
Bos taurus
-
IC50: 0.16 mM
0.21
5-Bromouridine
Bos taurus
-
IC50: 0.21 mM
0.19
5-chlorosalicylamide
Bos taurus
-
IC50: 0.19 mM
0.27
5-Chlorouracil
Bos taurus
-
IC50: 0.27 mM
0.25
5-hydroxy-1,4-naphthoquinone
Bos taurus
-
IC50: 0.25 mM
0.7
5-Hydroxy-2-methyl-1,4-naphthoquinone
Bos taurus
-
IC50: 0.7 mM
0.071
5-Iodouracil
Bos taurus
-
IC50: 0.071 mM
0.043
5-iodouridine
Bos taurus
-
IC50: 0.043 mM
0.07 - 0.35
5-Methylnicotinamide
0.29
5-methyluracil
Bos taurus
-
IC50: 0.29 mM
0.43
5-Nitrouracil
Bos taurus
-
IC50: 0.43 mM
0.0003
6(5H)-phenanthridinone
Bos taurus
-
IC50: 0.0003 mM
0.85
6-aminocoumarin
Bos taurus
-
IC50: 0.85 mM
1.1
6-aminonicotinamide
Bos taurus
-
IC50: 1.1 mM
1.4
8-acetamidocarsalam
Bos taurus
-
IC50: 1.4 mM
7.8
8-Methylnicotinamide
Bos taurus
-
IC50: 7.8 mM
2.3
acetophenone
Bos taurus
-
IC50: 2.3 mM
0.45
all-trans-retinal
Bos taurus
-
IC50: 0.45 mM
0.25
alpha-picolinamide
Bos taurus
-
IC50: 0.25 mM
0.0081
benzoyleneurea
Bos taurus
-
IC50: 0.0081 mM
1.4
Caffeine
Bos taurus
-
IC50: 1.4 mM
0.46
carbonylsalicylamide
Bos taurus
-
IC50: 0.46 mM
0.0085
Chlorthenoxazin
Bos taurus
-
IC50: 0.0085 mM
0.56
chromone-2-carboxylic acid
Bos taurus
-
IC50: 0.56 mM
0.62
cyclohexanecarboxamide
Bos taurus
-
IC50: 0.62 mM
0.003
diosmin
Pseudomonas aeruginosa
-
pH 6.0, 30°C
0.023
E216-5303
Pseudomonas aeruginosa
-
pH 6.0, 30°C
0.00118
EB-47
Homo sapiens
Q460N3
isoform ARDT10, pH and temperature not specified in the publication
0.021
everninic acid
Pseudomonas aeruginosa
-
pH 6.0, 30°C
0.022
flavone
Bos taurus
-
IC50: 0.022 mM
0.12
gamma-linolenic acid
Bos taurus
-
IC50: 0.12 mM
1.7
hypoxanthine
Bos taurus
-
IC50: 1.7 mM
0.99
Isonicotinamide
Bos taurus
-
IC50: 0.99 mM
4.8
Isonicotinate hydrazide
Bos taurus
-
IC50: 4.8 mM
0.048
linoleic acid
Bos taurus
-
IC50: 0.048 mM
0.11
linolenic acid
Bos taurus
-
IC50: 0.11 mM
0.93
m-acetamidoacetophenone
Bos taurus
-
IC50: 0.93 mM
1.9
m-aminoacetophenone
Bos taurus
-
IC50: 1.9 mM
0.6
m-hydroxyacetophenone
Bos taurus
-
IC50: 0.6 mM
0.05
m-phthalamide
Bos taurus
-
IC50: 0.05 mM
0.72
menadione sodium bisulfite
Bos taurus
-
IC50: 0.72 mM
0.0022
methyl (2S)-2-[[3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanoyl]amino]-3-phenylpropanoate
Homo sapiens
Q9Y6F1
pH and temperature not specified in the publication
1.8
N-(2-chloroethyl)1,8-naphthalamide
Bos taurus
-
IC50: above 1.8 mM
0.0858
N-(acridin-9-yl)-4-nitrobenzamide
Aeromonas hydrophila
Q49TP5
25°C, pH not specified in the publication
0.45
N-hydroxynaphthalimide sodium salt
Bos taurus
-
IC50: 0.45 mM
0.1
N-[(1R)-2,3-dihydro-1H-inden-1-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
Q9Y6F1
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.1
N-[(1S)-2,3-dihydro-1H-inden-1-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
Q9Y6F1
IC50 above 0.1 mM, pH and temperature not specified in the publication
0.001
N-[(2S)-1-hydroxy-3-phenylpropan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
Q9Y6F1
pH and temperature not specified in the publication
0.0096
N-[(2S)-1-hydroxybutan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
Q9Y6F1
pH and temperature not specified in the publication
0.0111
N-[(2S)-1-hydroxypropan-2-yl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
Q9Y6F1
pH and temperature not specified in the publication
0.0132
N-[1-[4-(1H-imidazol-1-yl)phenyl]ethyl]-3-(4-oxo-3,4-dihydroquinazolin-2-yl)propanamide
Homo sapiens
Q9Y6F1
pH and temperature not specified in the publication
0.086
N-[2-oxo-4-(phenylamino)-3,8a-dihydro-2H-chromen-3-yl]acetamide
Aeromonas hydrophila
Q49TP5
25°C, pH not specified in the publication
0.031 - 0.21
nicotinamide
4.7
norharman
Bos taurus
-
IC50: 4.7 mM
2.2
novobiocin
Bos taurus
-
IC50: 2.2 mM, 5 mM, 90% inhibition in presence of Mg2+, 59% inhibition in absence of Mg2+
0.000925 - 0.00204
olaparib
0.082
oleic acid
Bos taurus
-
IC50: 0.082 mM
0.095
palmitoleic acid
Bos taurus
-
IC50: 0.095 mM
0.000745 - 0.00114
phenantridinone
1
phthalamide
Bos taurus
-
IC50: 1.0 mM
0.13
Pyrazinamide
Bos taurus
-
IC50: 0.13 mM
0.79
reserpine
Bos taurus
-
IC50: 0.79 mM
0.02
suramin
Aeromonas hydrophila
Q49TP5
25°C, pH not specified in the publication
0.11
Theobromine
Bos taurus
-
IC50: 0.11 mM
0.046
theophylline
Bos taurus
-
IC50: 0.046 mM
0.62
thiobenzamide
Bos taurus
-
IC50: 0.62 mM
1.8
Thionicotinamide
Bos taurus
-
IC50: 1.8 mM
0.000232
TIQ-A
Homo sapiens
Q460N3
isoform ARDT7, pH and temperature not specified in the publication
4.3
trans-decahydro-1-naphthalenone
Bos taurus
-
IC50: 4.3 mM
0.157
V8 protease
Aeromonas hydrophila
Q49TP5
25°C, pH not specified in the publication
-
0.0019
vitamin K1
Bos taurus
-
IC50: 0.0019 mM
0.42
vitamin K3
Bos taurus
-
IC50: 0.42 mM
0.077
Zn2+
Bos taurus
-
ZnCl2, IC50: 0.077 mM
1.7
1-methylnicotinamide chloride

Bos taurus
-
IC50: 1.7 mM
3.8
1-methylnicotinamide chloride
Bos taurus
-
IC50: 3.8 mM
0.1
2-Aminobenzamide

Bos taurus
-
IC50: 0.1 mM
0.65
2-Aminobenzamide
Bos taurus
-
IC50: 0.65 mM
0.0054
3-aminobenzamide

Bos taurus
-
IC50: 0.0054
0.33
3-aminobenzamide
Bos taurus
-
IC50: 0.33 mM