Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + protein tau
ADP + protein tau phosphate
the antagonist of GSK-3beta in protein tau phosphorylation is the phosphatase PP2A
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
ATP + beta-catenin
ADP + phosphorylated beta-catenin
ATP + c-Jun
ADP + phosphorylated c-Jun
-
substrate of isoform GSK-3alpha
-
-
?
ATP + CEP164
ADP + phospho-CEP164
-
-
-
?
ATP + CEP97
ADP + phospho-CEP97
-
-
-
?
ATP + eIF2B peptide
ADP + phosphorylated eIF2B peptide
-
-
-
-
?
ATP + histone H1
ADP + histone H1 phosphate
-
Cdk5 substrate
-
-
?
ATP + HLSNVSSTGSIDMVDSPQLATLADEVSASLAK
ADP + HLSNVSSTGSIDMVDpSPQLATLADEVSASLAK
-
-
-
?
ATP + HSPB6
ADP + phosphorylated HSPB6
-
phosphorylation at Ser16
-
-
?
ATP + phospho-glycogen synthase peptide-2
ADP + phosphorylated phospho-glycogen synthase peptide-2
-
GSK3 substrate
-
-
?
ATP + protein tau
ADP + protein tau phosphate
ATP + tau-protein
ADP + O-phospho-tau-protein
ATP + TDP-43
ADP + phospho-TDP-43
-
-
-
?
ATP + tubulin
ADP + phospho-tubulin
-
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
additional information
?
-
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
recombinant human tau protein expressed in transgenic mice
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
phosphorylation level of tau at Thr205, Thr231, Ser396 and tau-1 sites
-
-
?
ATP + beta-catenin
ADP + phosphorylated beta-catenin
-
-
-
-
?
ATP + beta-catenin
ADP + phosphorylated beta-catenin
-
substrate of isoform GSK-3beta
-
-
?
ATP + protein tau
ADP + protein tau phosphate
-
-
?
ATP + protein tau
ADP + protein tau phosphate
-
-
-
?
ATP + protein tau
ADP + protein tau phosphate
-
-
-
-
?
ATP + protein tau
ADP + protein tau phosphate
-
phosphorylation at Ser9
-
-
?
ATP + protein tau
ADP + protein tau phosphate
-
role of GSK3 as a key mediator of tau hyperphosphorylation, whereas Cdk5 acts as a modulator of tau hyperphosphorylation via the inhibitory regulation of GSK3
-
-
?
ATP + protein tau
ADP + protein tau phosphate
-
T231 is the primary phosphorylation site for GSK3beta, the tau227-237 (AVVRTPPKSPS) derived from tau containing T231P232 motif is the GSK3beta binding site with high affinity (Kd = 0.00082 mmol/L), tau mutant T231A completely abolishes tau phosphorylation by GSK3beta
-
-
?
ATP + protein tau
ADP + protein tau phosphate
-
phosphorylation occurs at Ser-396/Ser-404
-
-
?
ATP + protein tau
ADP + protein tau phosphate
-
PKA transfers about 2 mol of phosphate per mole of the shortest protein tau isoform and phosphorylates Ser156, 235, 267, 320 and 327 (corresponding to Ser214, 324, 356, 409 and 416 of the longest protein tau isoform)
-
-
?
ATP + tau-protein
ADP + O-phospho-tau-protein
-
-
-
-
?
ATP + tau-protein
ADP + O-phospho-tau-protein
-
-
-
?
ATP + tau-protein
ADP + O-phospho-tau-protein
isoform TTBK1 is the isoform responsible for tau phosphorylation at epitopes enriched in tauopathies such as serine 422
-
-
?
ATP + tau-protein
ADP + O-phospho-tau-protein
-
good substrate for protein kinase A which phosphorylates several key residues (Ser156, Ser235, Ser267, Ser320, Ser327) of tau-protein and induces its tight interaction with 14-3-3 proteins
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
-
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
activity in organisms with mutated APP and tau, not in wild-type, overview
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
cdk5 substrate in brain, cdk5 associated with p39, tau is a microtubule-associated and developmentally regulated protein involved in axonal development in neurons, tau phosphorylation by cyclin-dependent kinase 5/p39 during brain development reduces its affinity for microtubules
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
hyperphosphorylation of tau by CDK5 is involved in apoptosis and neurodegeneration in Alzheimer's disease, overview
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
regulation, overview
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
tau phosphorylation by GSK-3beta is involved in development of neurodegenerative Alzheimer's disease, the tau phosphorylation activity by GSK-3beta is further increased by soluble toxic beta-amyloid oligomers, overview
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
tau phosphorylation in vivo is stimulated by extracellular signal-regulated kinase Erk phosphorylation and apolipoprotein isozyme E4, to a lesser extent by isozyme apoE3, overview
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
phosphorylation of the PHF-1 epitope at Ser396 and Ser404 by CDK5
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
preferred substrate of cdk5 associated with p39, recombinant bacterially expressed human tau protein as substrate, phosphorylation at Ser202 and Thr205
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
AMPK is one of the main tau kinase phosphorylating tau at the epitopes Ser262/356 and Thr231 at basal conditions in neurons
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
AMPK phosphorylate tau in vitro at several epitopes including Thr231, Ser262/356, Ser396, Ser409 and Ser422, whereas Ser199, Ser202, Ser235, Ser400, and Ser404 are not phosphorylated by AMPK
-
-
?
additional information
?
-
-
naturally occurring V717I mutation of the amyloid precursor protein APP in a CT100 fragment of mutants leads to augmented age-dependent tau phosphorylation, followed by increased activation status of mitogen-activated protein kinase family members, e.g. ERK1/2, p38, and c-Jun NH2-terminal kinase, compared to the wild-type organism, naturally occurring V337M mutation of tau protein of mutants leads to age-dependent memory deficits
-
-
?
additional information
?
-
-
rapid, reversible cold-water stress-induced hyperphosphorylation of tau S199, S202, T205, T231, and S235 in hippocampal and cerebral region of the brain, hyperphosphorylation of tau is associated to the Alzheimer's disease
-
-
?
additional information
?
-
-
cdk5 also performs the kinase reaction of EC 2.7.11.22
-
-
?
additional information
?
-
the enzyme performs autophosphorylation
-
-
?
additional information
?
-
isoform TTBK1 is autophosphorylated
-
-
-
additional information
?
-
isoform TTBK1 is autophosphorylated
-
-
-
additional information
?
-
isoform TTBK2 is autophosphorylated
-
-
-
additional information
?
-
isoform TTBK2 is autophosphorylated
-
-
-
additional information
?
-
-
often protein kinase A works in pair with 14-3-3 since it phosphorylates target proteins at (R/K)RX(S/T) sequences (where X is any amino acid)
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
ATP + protein tau
ADP + protein tau phosphate
ATP + tau-protein
ADP + O-phospho-tau-protein
ATP + tubulin
ADP + phospho-tubulin
-
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
additional information
?
-
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
recombinant human tau protein expressed in transgenic mice
-
-
?
ATP + protein tau
ADP + protein tau phosphate
-
-
?
ATP + protein tau
ADP + protein tau phosphate
-
-
-
?
ATP + protein tau
ADP + protein tau phosphate
-
-
-
-
?
ATP + tau-protein
ADP + O-phospho-tau-protein
-
-
-
-
?
ATP + tau-protein
ADP + O-phospho-tau-protein
-
-
-
?
ATP + tau-protein
ADP + O-phospho-tau-protein
isoform TTBK1 is the isoform responsible for tau phosphorylation at epitopes enriched in tauopathies such as serine 422
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
activity in organisms with mutated APP and tau, not in wild-type, overview
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
cdk5 substrate in brain, cdk5 associated with p39, tau is a microtubule-associated and developmentally regulated protein involved in axonal development in neurons, tau phosphorylation by cyclin-dependent kinase 5/p39 during brain development reduces its affinity for microtubules
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
hyperphosphorylation of tau by CDK5 is involved in apoptosis and neurodegeneration in Alzheimer's disease, overview
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
regulation, overview
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
tau phosphorylation by GSK-3beta is involved in development of neurodegenerative Alzheimer's disease, the tau phosphorylation activity by GSK-3beta is further increased by soluble toxic beta-amyloid oligomers, overview
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
-
tau phosphorylation in vivo is stimulated by extracellular signal-regulated kinase Erk phosphorylation and apolipoprotein isozyme E4, to a lesser extent by isozyme apoE3, overview
-
-
?
ATP + [tau-protein]
ADP + O-phospho-[tau-protein]
AMPK is one of the main tau kinase phosphorylating tau at the epitopes Ser262/356 and Thr231 at basal conditions in neurons
-
-
?
additional information
?
-
-
naturally occurring V717I mutation of the amyloid precursor protein APP in a CT100 fragment of mutants leads to augmented age-dependent tau phosphorylation, followed by increased activation status of mitogen-activated protein kinase family members, e.g. ERK1/2, p38, and c-Jun NH2-terminal kinase, compared to the wild-type organism, naturally occurring V337M mutation of tau protein of mutants leads to age-dependent memory deficits
-
-
?
additional information
?
-
-
rapid, reversible cold-water stress-induced hyperphosphorylation of tau S199, S202, T205, T231, and S235 in hippocampal and cerebral region of the brain, hyperphosphorylation of tau is associated to the Alzheimer's disease
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
physiological function
stimulation of GSK-3beta both in vitro and in vivo induces tau hyperphosphorylation with impairments of the cognitive functions, whereas inhibition of GSK-3beta improves tau pathologies and memory deficits. Stimulation of EphB2 upregulates PI3K and Akt with inhibition of GSK-3beta. Stimulation of EphB2 attenuates tau phosphorylation both in vitro and in hippocampus of human tau transgenic mice
evolution
TTBK2 is a serine/threonine protein kinase of the CK1 superfamily
malfunction
functional status of glycogen synthase kinase-3 and correlated appearance of distinct tau phospho-epitopes: neurons displaying increases in activation of phosphorylation of glycogen synthase kinase-3alpha/beta at tyrosine 279/216 also show an intense rather than moderate AT8 (phospho-Ser202/Thr205 tau) immunoreactivity, and immunoreactivity for AT100 (phospho-Ser212/Thr214 tau) and phosphorylated Ser422, phospho-epitopes associated with fibrillar tau pathology. These neurons are rare in 8.5-month-old, but numerous in 18.5- and 28-month-old pR5 mice. Tau- rather than an amyloid-beta peptide-induced pathology is associated with increased neuronal tyrosine phosphorylation. Tyrosine phosphorylation only increases in neurons with fibrillar tau pathology
malfunction
Stimulation of EphB2 attenuates tau phosphorylation through PI3K/Akt-mediated inactivation of glycogen synthase kinase-3beta
malfunction
-
chronic inhibition of GSK-3 enhances glycolysis
malfunction
-
GSK-3beta heterozygote mice, which express GSK-3beta at 50% wild type levels, have impaired memory reconsolidation but normal memory consolidation
malfunction
-
inhibition of GSK-3beta abolishes Abeta-induced spine alterations
malfunction
-
inhibition of GSK-3beta abrogates glucocorticoid-induced bone loss by increasing beta-catenin- and Runx2-mediated osteoblast differentiation
malfunction
AMPK inhibition leads to a rapid decrease of tau phosphorylation. AMP-activated protein kinase (AMPK) is deregulated in the Alzheimer's disease brain where it co-localized with phosphorylated tau in pre-tangle and tangle bearing neurons. AMPK mice deficient for one of the catalytic alpha subunits display reduced endogenous tau phosphorylation. AMPK deficiency reduces tau pathology in the PS19 mouse model of tauopathy
malfunction
functional status of glycogen synthase kinase-3 and correlated appearance of distinct tau phospho-epitopes: neurons displaying increases in activation of phosphorylation of glycogen synthase kinase-3alpha/beta at tyrosine 279/216 also show an intense rather than moderate AT8 (phospho-Ser202/Thr205 tau) immunoreactivity, and immunoreactivity for AT100 (phospho-Ser212/Thr214 tau) and phosphorylated Ser422, phospho-epitopes associated with fibrillar tau pathology. These neurons are rare in 8.5-month-old, but numerous in 18.5- and 28-month-old pR5 mice. Tau- rather than an amyloid-beta peptide-induced pathology is associated with increased neuronal tyrosine phosphorylation. Tyrosine phosphorylation only increases in neurons with fibrillar tau pathology
malfunction
knockout TTBK2fmly1/fmly1 mice with homozygous mutants of truncated TTBK2 at residue 450 are embryonic lethal at embryonic day 10, with indistinct brain subdivisions, distorted caudal bodies, and delayed body and brain development. Heterozygous mutant TTBK2fmly1/+ mice are completely normal and exhibit a regular lifespan
physiological function
-
cisplatin-induced cytotoxicity may be associated with modulation of GSK-3 activation
physiological function
-
GSK-3 is necessary and sufficient for cardiomyocyte differentiation in mesenchymal stem cells, GSK-3beta in the cytosol induces cardiomyocyte differentiation of mesenchymal stem cells through down-regulation of beta-catenin. In contrast, GSK-3alpha in the nucleus inhibits cardiomyocyte differentiation through down-regulation of c-Jun
physiological function
-
GSK-3beta activation is required for memory reconsolidation in the adult brain
physiological function
-
GSK-3beta is a critical mediator of N-methyl-4-phenyl-1,2,3,6-tetrahydropyridine/1-methyl-4-phenylpyridinium iodide-induced neurotoxicity through its ability to regulate mitochondrial functions
physiological function
-
mitochondrial hexokinase II is a promoter of neuronal survival under the regulation of GSK-3
physiological function
AMP-activated protein kinase modulates tau phosphorylation and tau pathology in vivo. Tau functions, which include the regulation of microtubules dynamics, are dependent on its phosphorylation status, any changes in tau phosphorylation can have major impacts on synaptic plasticity and memory. Endogenous AMPK activation in mouse primary neurons induces an increase of tau at multiple sites. AMPK regulates tau phosphorylation in mouse primary neurons as well as in vivo, and thus suggest that AMPK could be a key player in the development of Alzheimer's disease pathology. The two alpha subunits of AMPK can have distinct roles. AMPKalpha2, which is the most highly expressed of the catalytic subunit in the brain, is responsible for the detrimental effects observed following ischemic stroke in mice. AMPK activation increases tau phosphorylation in primary neurons and affects tau binding to microtubules. AMPK controls basal tau phosphorylation levels
physiological function
TTBK2 is a multifunctional kinase. TTBK2 is essential for regulating the growth of axonemal microtubules in ciliogenesis. It also plays roles in resistance of cancer target therapies and in regulating glucose and GABA transport. The enzyme binds to CEP164, a centriolar protein, and EB1, a microtubule plus-end tracking protein. The TTBK2 pathway may be independent of the biogenesis of the ciliary transition zone. TTBK2 can also bind to EB1 through its SxIP motifs, where EB1 is a microtubule plus-end tracking protein required for ciliogenesis
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Tomizawa, K.; Omori, A.; Ohtake, A.; Sato, K.; Takahashi, M.
tau-Tubulin kinase phosphorylates tau at Ser-208 and Ser-210, sites found in paired helical filament-tau
FEBS Lett.
492
221-227
2001
Bos taurus, Mus musculus, Mus musculus (Q3UVR3), Rattus norvegicus, Rattus norvegicus Wistar
brenda
Mukai, F.; Ishiguro, K.; Sano, Y.; Fujita, S.C.
Alternative splicing isoform of tau protein kinase I/glycogen synthase kinase 3beta
J. Neurochem.
81
1073-1083
2002
Homo sapiens, Mus musculus, Rattus norvegicus
brenda
Okawa, Y.; Ishiguro, K.; Fujita, S.C.
Stress-induced hyperphosphorylation of tau in the mouse brain
FEBS Lett.
535
183-189
2003
Mus musculus
brenda
Takahashi, S.; Saito, T.; Hisanaga, S.; Pant, H.C.; Kulkarni, A.B.
Tau phosphorylation by cyclin-dependent kinase 5/p39 during brain development reduces its affinity for microtubules
J. Biol. Chem.
278
10506-10515
2003
Mus musculus
brenda
Harris, F.M.; Brecht, W.J.; Xu, Q.; Mahley, R.W.; Huang, Y.
Increased tau phosphorylation in apolipoprotein E4 transgenic mice is associated with activation of extracellular signal-regulated kinase: modulation by zinc
J. Biol. Chem.
279
44795-44801
2004
Mus musculus
brenda
Shelton, S.B.; Krishnamurthy, P.; Johnson, G.V.
Effects of cyclin-dependent kinase-5 activity on apoptosis and tau phosphorylation in immortalized mouse brain cortical cells
J. Neurosci. Res.
76
110-120
2004
Mus musculus
brenda
Ma, Q.L.; Lim, G.P.; Harris-White, M.E.; Yang, F.; Ambegaokar, S.S.; Ubeda, O.J.; Glabe, C.G.; Teter, B.; Frautschy, S.A.; Cole, G.M.
Antibodies against beta-amyloid reduce abeta oligomers, glycogen synthase kinase-3beta activation and tau phosphorylation in vivo and in vitro
J. Neurosci. Res.
83
374-384
2006
Homo sapiens, Mus musculus
brenda
Lambourne, S.L.; Sellers, L.A.; Bush, T.G.; Choudhury, S.K.; Emson, P.C.; Suh, Y.H.; Wilkinson, L.S.
Increased tau phosphorylation on mitogen-activated protein kinase consensus sites and cognitive decline in transgenic models for Alzheimer's disease and FTDP-17: evidence for distinct molecular processes underlying tau abnormalities
Mol. Cell. Biol.
25
278-293
2005
Homo sapiens, Mus musculus
brenda
Ikeda, Y.; Ishiguro, K.; Fujita, S.C.
Ether stress-induced Alzheimer-like tau phosphorylation in the normal mouse brain
FEBS Lett.
581
891-897
2007
Mus musculus
brenda
Plattner, F.; Angelo, M.; Giese, K.P.
The roles of cyclin-dependent kinase 5 and glycogen synthase kinase 3 in tau hyperphosphorylation
J. Biol. Chem.
281
25457-25465
2006
Mus musculus
brenda
Lin, Y.T.; Cheng, J.T.; Liang, L.C.; Ko, C.Y.; Lo, Y.K.; Lu, P.J.
The binding and phosphorylation of Thr231 is critical for Taus hyperphosphorylation and functional regulation by glycogen synthase kinase 3beta
J. Neurochem.
103
802-813
2007
Mus musculus
brenda
Sato, S.; Cerny, R.L.; Buescher, J.L.; Ikezu, T.
Tau-tubulin kinase 1 (TTBK1), a neuron-specific tau kinase candidate, is involved in tau phosphorylation and aggregation
J. Neurochem.
98
1573-1584
2006
Homo sapiens, Mus musculus
brenda
Fujio, J.; Hosono, H.; Ishiguro, K.; Ikegami, S.; Fujita, S.C.
Tau phosphorylation in the mouse brain during aversive conditioning
Neurochem. Int.
51
200-208
2007
Mus musculus, Mus musculus C57BL/6Njcl
brenda
Meske, V.; Albert, F.; Ohm, T.G.
Coupling of mammalian target of rapamycin with phosphoinositide 3-kinase signaling pathway regulates protein phosphatase 2A- and glycogen synthase kinase-3-dependent phosphorylation of Tau
J. Biol. Chem.
283
100-109
2008
Mus musculus (Q9WV60)
brenda
Shi, H.R.; Zhu, L.Q.; Wang, S.H.; Liu, X.A.; Tian, Q.; Zhang, Q.; Wang, Q.; Wang, J.Z.
17beta-Estradiol attenuates glycogen synthase kinase-3beta activation and tau hyperphosphorylation in Akt-independent manner
J. Neural Transm.
115
879-888
2008
Mus musculus
brenda
Wen, Y.; Planel, E.; Herman, M.; Figueroa, H.Y.; Wang, L.; Liu, L.; Lau, L.F.; Yu, W.H.; Duff, K.E.
Interplay between cyclin-dependent kinase 5 and glycogen synthase kinase 3 beta mediated by neuregulin signaling leads to differential effects on tau phosphorylation and amyloid precursor protein processing
J. Neurosci.
28
2624-2632
2008
Mus musculus
brenda
Lomoio, S.; Scherini, E.; Necchi, D.
beta-Amyloid overload does not directly correlate with SAPK/JNK activation and tau protein phosphorylation in the cerebellar cortex of Ts65Dn mice
Brain Res.
1297
198-206
2009
Mus musculus
brenda
Sluchanko, N.N.; Seit-Nebi, A.S.; Gusev, N.B.
Phosphorylation of more than one site is required for tight interaction of human tau protein with 14-3-3zeta
FEBS Lett.
583
2739-2742
2009
Mus musculus
brenda
Park, H.J.; Kim, H.J.; Bae, G.S.; Seo, S.W.; Kim, D.Y.; Jung, W.S.; Kim, M.S.; Song, M.Y.; Kim, E.K.; Kwon, K.B.; Hwang, S.Y.; Song, H.J.; Park, C.S.; Park, R.K.; Chong, M.S.; Park, S.J.
Selective GSK-3beta inhibitors attenuate the cisplatin-induced cytotoxicity of auditory cells
Hear. Res.
257
53-62
2009
Mus musculus
brenda
Crespo-Biel, N.; Camins, A.; Gutierrez-Cuesta, J.; Melchiorri, D.; Nicoletti, F.; Pallas, M.; Canudas, A.M.
Regulation of GSK-3beta by calpain in the 3-nitropropionic acid model
Hippocampus
20
962-970
2010
Mus musculus
brenda
Cho, J.; Rameshwar, P.; Sadoshima, J.
Distinct roles of glycogen synthase kinase (GSK)-3alpha and GSK-3beta in mediating cardiomyocyte differentiation in murine bone marrow-derived mesenchymal stem cells
J. Biol. Chem.
284
36647-36658
2009
Mus musculus
brenda
Miao, Y.; Chen, J.; Zhang, Q.; Sun, A.
Deletion of tau attenuates heat shock-induced injury in cultured cortical neurons
J. Neurosci. Res.
88
102-110
2010
Mus musculus
brenda
Tackenberg, C.; Brandt, R.
Divergent pathways mediate spine alterations and cell death induced by amyloid-beta, wild-type tau, and R406W tau
J. Neurosci.
29
14439-14450
2009
Mus musculus
brenda
Takashima, A.
Drug development targeting the glycogen synthase kinase-3beta (GSK-3beta)-mediated signal transduction pathway: role of GSK-3beta in adult brain
J. Pharmacol. Sci.
109
174-178
2009
Mus musculus
brenda
Wang, F.S.; Ko, J.Y.; Weng, L.H.; Yeh, D.W.; Ke, H.J.; Wu, S.L.
Inhibition of glycogen synthase kinase-3beta attenuates glucocorticoid-induced bone loss
Life Sci.
85
685-692
2009
Mus musculus
brenda
Manceur, A.P.; Driscoll, B.D.; Sun, W.; Audet, J.
Selective enhancement of the uptake and bioactivity of a TAT-conjugated peptide inhibitor of glycogen synthase kinase-3
Mol. Ther.
17
500-507
2009
Homo sapiens, Mus musculus
brenda
Min, W.W.; Yuskaitis, C.J.; Yan, Q.; Sikorski, C.; Chen, S.; Jope, R.S.; Bauchwitz, R.P.
Elevated glycogen synthase kinase-3 activity in Fragile X mice: key metabolic regulator with evidence for treatment potential
Neuropharmacology
56
463-472
2009
Mus musculus
brenda
Petit-Paitel, A.; Brau, F.; Cazareth, J.; Chabry, J.
Involvment of cytosolic and mitochondrial GSK-3beta in mitochondrial dysfunction and neuronal cell death of MPTP/MPP-treated neurons
PLoS ONE
4
e5491
2009
Mus musculus
brenda
Liao, J.C.; Yang, T.T.; Weng, R.R.; Kuo, C.T.; Chang, C.W.
TTBK2: a tau protein kinase beyond tau phosphorylation
BioMed Res. Int.
2015
575170
2015
Mus musculus (Q3UVR3), Homo sapiens (Q6IQ55)
brenda
Koehler, C.; Dinekov, M.; Goetz, J.
Active glycogen synthase kinase-3 and tau pathology-related tyrosine phosphorylation in pR5 human tau transgenic mice
Neurobiol. Aging
34
1369-1379
2013
Mus musculus (Q2NL51), Mus musculus (Q9WV60), Mus musculus C57BL/6 (Q2NL51), Mus musculus C57BL/6 (Q9WV60)
brenda
Jiang, J.; Wang, Z.H.; Qu, M.; Gao, D.; Liu, X.P.; Zhu, L.Q.; Wang, J.Z.
Stimulation of EphB2 attenuates tau phosphorylation through PI3K/Akt-mediated inactivation of glycogen synthase kinase-3beta
Sci. Rep.
5
11765
2015
Homo sapiens (P49841), Homo sapiens, Mus musculus (Q9WV60), Mus musculus
brenda
Domise, M.; Didier, S.; Marinangeli, C.; Zhao, H.; Chandakkar, P.; Buee, L.; Viollet, B.; Davies, P.; Marambaud, P.; Vingtdeux, V.
AMP-activated protein kinase modulates tau phosphorylation and tau pathology in vivo
Sci. Rep.
6
26758
2016
Mus musculus (Q5EG47), Mus musculus, Mus musculus C57BL6 (Q5EG47)
brenda
Bao, C.; Bajrami, B.; Marcotte, D.J.; Chodaparambil, J.V.; Kerns, H.M.; Henderson, J.; Wei, R.; Gao, B.; Dillon, G.M.
Mechanisms of regulation and diverse activities of tau-tubulin kinase (TTBK) isoforms
Cell. Mol. Neurobiol.
41
669-685
2021
Mus musculus (Q3UVR3), Mus musculus (Q6PCN3), Homo sapiens (Q5TCY1), Homo sapiens (Q6IQ55)
brenda
Yao, X.; Xian, X.; Fang, M.; Fan, S.; Li, W.
Loss of miR-369 promotes tau phosphorylation by targeting the Fyn and serine/threonine-protein kinase 2 signaling pathways in Alzheimer s disease mice
Front. Aging Neurosci.
11
365
2019
Mus musculus
brenda
Tugaeva, K.V.; Tsvetkov, P.O.; Sluchanko, N.N.
Bacterial co-expression of human Tau protein with protein kinase A and 14-3-3 for studies of 14-3-3/phospho-Tau interaction
PLoS ONE
12
e0178933
2017
Mus musculus
brenda