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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + Elk-1
ADP + phosphorylated Elk-1
an ETS family transcription factor
-
-
?
ATP + Net
ADP + phosphorylated Net
an ETS family transcription factor
-
-
?
ATP + a protein
ADP + a phosphoprotein
ATP + activating transcription factor 2
ADP + phosphorylated activating transcription factor 2
ATP + ATF-2
ADP + phosphorylated ATF-2
-
substrate in kinase assay
-
-
?
ATP + ATF2
ADP + phosphorylated ATF2
phosphorylation by p38 MAPK at threonine residues
-
-
?
ATP + ATF2DELTA109
ADP + phosphorylated ATF2DELTA109
-
-
-
-
?
ATP + c-Jun
ADP + phosphorylated c-Jun
-
-
-
-
?
ATP + EGF receptor peptide
ADP + phosphorylated EGF receptor peptide
-
-
-
-
?
ATP + Elk1
ADP + phosphorylated Elk1
-
recombinant GST-tagged Elk1, substrate of ERK2
-
-
?
ATP + MAPKAP-K2
ADP + phosphorylated MAPKAP-K2
-
-
-
-
?
ATP + MAPKAP-K3
ADP + phosphorylated MAPKAP-K3
-
-
-
-
?
ATP + MEF2
ADP + phosphorylated MEF2
-
-
-
-
?
ATP + myelin basic protein
ADP + phosphorylated myelin basic protein
-
substrate of ERK2
-
-
?
ATP + protein
ADP + phosphoprotein
Ser/Thr kinase
-
-
?
ATP + protein ATF2
ADP + phosphorylated protein ATF2
-
-
-
?
ATP + Smad3
ADP + phosphorylated Smad3
additional information
?
-
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
ATP + activating transcription factor 2
ADP + phosphorylated activating transcription factor 2
-
ATF2
-
-
?
ATP + activating transcription factor 2
ADP + phosphorylated activating transcription factor 2
-
ATF2, recombinant GST-tagged ATF2DELTA115
-
-
?
ATP + Smad3
ADP + phosphorylated Smad3
-
substrate of MAPKs, e.g. ERK2
-
-
?
ATP + Smad3
ADP + phosphorylated Smad3
-
substrate of MAPKs, e.g. ERK2, identification of phosphorylation sites Ser203, Ser207, and Thr187, Ser207 is the best phosphorylation site for ERK2, other MAPKs than ERK2 also phosphorylate Ser212
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
Jnk3-mediated signalling pathway is an important component in the pathogenesis of glutamate neurotoxicity
-
-
?
additional information
?
-
MKK4 is a JNK activator in vivo and an essential component of the JNK signal transduction pathway
-
-
?
additional information
?
-
JNK is necessary for T-cell differentiation but not for naive T-cell activation
-
-
?
additional information
?
-
-
JNK is necessary for T-cell differentiation but not for naive T-cell activation
-
-
?
additional information
?
-
the enzyme functions as a Scaffold factor in the JNK signaling pathway
-
-
?
additional information
?
-
the enzyme functions as a Scaffold factor in the JNK signaling pathway
-
-
?
additional information
?
-
the enzyme functions as a Scaffold factor in the JNK signaling pathway
-
-
?
additional information
?
-
-
the enzyme functions as a Scaffold factor in the JNK signaling pathway
-
-
?
additional information
?
-
-
ERK, but not p38 and JNK, is involved in TGF-beta production in macrophages, the phosphatidylserine-receptor is involved in the ERK signaling pathway, overview
-
-
?
additional information
?
-
-
regulation mechanism of p38 MAPK activity involving the protein kinases MKK3, MKK4, and MKK6, overview
-
-
?
additional information
?
-
-
signaling pathways overview, the enzyme is important in transduction of external stimuli and signals from the cell membrane to nuclear and other intracellular targets, the enzyme is involved in regulation of several cellular processes in cell growth, differentiation, development cell cycle, death and survival, the enzyme is also involved in pathogenesis of several processes in the heart, e.g. hypertrophy, ischemic and reperfusion injury, as well as in cardioprotection, the MAPK family enzymes have regulatory function in the myocardium, overview
-
-
?
additional information
?
-
-
measurement of ATPase activity of p38 MAPK in an NADH-coupled assay
-
-
?
additional information
?
-
-
activated p39 MAPK inhibits steroid synthesis in adrenocortical Y1-BS1 cells, overview
-
-
?
additional information
?
-
activated p39 MAPK inhibits steroid synthesis in adrenocortical Y1-BS1 cells, overview
-
-
?
additional information
?
-
activated p39 MAPK inhibits steroid synthesis in adrenocortical Y1-BS1 cells, overview
-
-
?
additional information
?
-
activation of JNK facilitates tumour necrosis factor-induced cell death. The p38 mitogen-activated protein kinase pathway is induced by TNF-stimulation, but it is not involved in TNF-induced cell death. p38alpha MAPK inhibits JNK activation and collaborates with IkappaB kinase 2 to prevent endotoxin-induced liver failure. p38alpha MAPK inhibits MKK4, and MKK3/6, regulation, overview
-
-
?
additional information
?
-
-
MAP kinases are essential signaling molecules that mediate many cellular effects of growth factors, cytokines, and stress stimuli
-
-
?
additional information
?
-
-
MAPKs are involved in the upstream regulation of inducible nitric oxide synthase, iNOS
-
-
?
additional information
?
-
-
p38 MAPK is induced in response to environmental stress, it is implicated in diverse cellular processes, including cell proliferation, differentiation, and survival of differentiated cells in the central nervous system, expression profile and roles of p38 MAPK in the developing brain, overview. Inhibitors of p38 mitogen-activated protein kinase enhance proliferation of mouse neural stem cells, overview
-
-
?
additional information
?
-
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modeling, overview
-
-
?
additional information
?
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modeling, overview
-
-
?
additional information
?
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modeling, overview
-
-
?
additional information
?
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modeling, overview
-
-
?
additional information
?
-
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modelling, overview
-
-
?
additional information
?
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modelling, overview
-
-
?
additional information
?
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modelling, overview
-
-
?
additional information
?
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modelling, overview
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ATP + Elk-1
ADP + phosphorylated Elk-1
an ETS family transcription factor
-
-
?
ATP + Net
ADP + phosphorylated Net
an ETS family transcription factor
-
-
?
ATP + a protein
ADP + a phosphoprotein
ATP + activating transcription factor 2
ADP + phosphorylated activating transcription factor 2
-
ATF2
-
-
?
ATP + MAPKAP-K2
ADP + phosphorylated MAPKAP-K2
-
-
-
-
?
ATP + MAPKAP-K3
ADP + phosphorylated MAPKAP-K3
-
-
-
-
?
ATP + MEF2
ADP + phosphorylated MEF2
-
-
-
-
?
ATP + Smad3
ADP + phosphorylated Smad3
-
substrate of MAPKs, e.g. ERK2
-
-
?
additional information
?
-
ATP + a protein
ADP + a phosphoprotein
-
-
-
-
?
ATP + a protein
ADP + a phosphoprotein
-
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
-
-
?
additional information
?
-
-
-
-
-
?
additional information
?
-
Jnk3-mediated signalling pathway is an important component in the pathogenesis of glutamate neurotoxicity
-
-
?
additional information
?
-
MKK4 is a JNK activator in vivo and an essential component of the JNK signal transduction pathway
-
-
?
additional information
?
-
JNK is necessary for T-cell differentiation but not for naive T-cell activation
-
-
?
additional information
?
-
-
JNK is necessary for T-cell differentiation but not for naive T-cell activation
-
-
?
additional information
?
-
the enzyme functions as a Scaffold factor in the JNK signaling pathway
-
-
?
additional information
?
-
the enzyme functions as a Scaffold factor in the JNK signaling pathway
-
-
?
additional information
?
-
the enzyme functions as a Scaffold factor in the JNK signaling pathway
-
-
?
additional information
?
-
-
the enzyme functions as a Scaffold factor in the JNK signaling pathway
-
-
?
additional information
?
-
-
ERK, but not p38 and JNK, is involved in TGF-beta production in macrophages, the phosphatidylserine-receptor is involved in the ERK signaling pathway, overview
-
-
?
additional information
?
-
-
regulation mechanism of p38 MAPK activity involving the protein kinases MKK3, MKK4, and MKK6, overview
-
-
?
additional information
?
-
-
signaling pathways overview, the enzyme is important in transduction of external stimuli and signals from the cell membrane to nuclear and other intracellular targets, the enzyme is involved in regulation of several cellular processes in cell growth, differentiation, development cell cycle, death and survival, the enzyme is also involved in pathogenesis of several processes in the heart, e.g. hypertrophy, ischemic and reperfusion injury, as well as in cardioprotection, the MAPK family enzymes have regulatory function in the myocardium, overview
-
-
?
additional information
?
-
-
activated p39 MAPK inhibits steroid synthesis in adrenocortical Y1-BS1 cells, overview
-
-
?
additional information
?
-
activated p39 MAPK inhibits steroid synthesis in adrenocortical Y1-BS1 cells, overview
-
-
?
additional information
?
-
activated p39 MAPK inhibits steroid synthesis in adrenocortical Y1-BS1 cells, overview
-
-
?
additional information
?
-
activation of JNK facilitates tumour necrosis factor-induced cell death. The p38 mitogen-activated protein kinase pathway is induced by TNF-stimulation, but it is not involved in TNF-induced cell death. p38alpha MAPK inhibits JNK activation and collaborates with IkappaB kinase 2 to prevent endotoxin-induced liver failure. p38alpha MAPK inhibits MKK4, and MKK3/6, regulation, overview
-
-
?
additional information
?
-
-
MAP kinases are essential signaling molecules that mediate many cellular effects of growth factors, cytokines, and stress stimuli
-
-
?
additional information
?
-
-
MAPKs are involved in the upstream regulation of inducible nitric oxide synthase, iNOS
-
-
?
additional information
?
-
-
p38 MAPK is induced in response to environmental stress, it is implicated in diverse cellular processes, including cell proliferation, differentiation, and survival of differentiated cells in the central nervous system, expression profile and roles of p38 MAPK in the developing brain, overview. Inhibitors of p38 mitogen-activated protein kinase enhance proliferation of mouse neural stem cells, overview
-
-
?
additional information
?
-
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modeling, overview
-
-
?
additional information
?
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modeling, overview
-
-
?
additional information
?
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modeling, overview
-
-
?
additional information
?
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modeling, overview
-
-
?
additional information
?
-
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modelling, overview
-
-
?
additional information
?
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modelling, overview
-
-
?
additional information
?
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modelling, overview
-
-
?
additional information
?
-
trauma-hemorrhage suppresses MAPK phosphorylation and activation in lipopolysaccharide-unstimulated splenic dendritic cells, in lipopolysaccharide-unstimulated cells the activation is increased, modelling, overview
-
-
?
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.
(E)-3-(2,4-dimethoxyphenyl)-N-(4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]pyridin-2-yl)acrylamide
-
(E)-3-(2,4-dimethoxyphenyl)-N-(4-[5-(4-fluorophenyl)-2-methanesulfinyl-3H-imidazol-4-yl]pyridin-2-yl)acrylamide
-
(E)-3-(2,4-dimethoxyphenyl)-N-(4-[5-(4-fluorophenyl)-2-methylsulfanyl-3H-imidazol-4-yl]pyridin-2-yl)acrylamide
-
1-(2,6-dichloro-phenyl)-5-(2,4-difluoro-phenyl)-7-piperazin-1-yl-3,4-dihydro-1H-quinazolin-2-one
highly selective for p38 isozyme alpha wild-type with IC50 of 3.2 nM, the IC50 for mutants G110A and G110D are 37 nM and 56 nM, respectively, no inhibition of JNK3, JNK2, and ERK
1-(2,6-dichloro-phenyl)-5-(2,4-difluoro-phenyl)-7-piperidin-4-yl-3,4-dihydro-1H-quinolin-2-one
highly selective for p38 isozyme alpha wild-type with IC50 of 0.74 nM, the IC50 for mutants G110A and G110D are 26 nM and 67 nM, respectively, no inhibition of JNK3, JNK2, and ERK
1-(2,6-dichloro-phenyl)-6-(2,4-difluoro-phenylsulfanyl)-7-(1,2,3,6-tetrahydro-pyridin-4-yl)-3,4-dihydro-1H-pyrido[3,2-d]pyrimidin-2-one
highly selective for p38 isozyme alpha wild-type with IC50 of 4.3 nM, the IC50 for mutants G110A and G110D are 61 nM and 160 nM, respectively, no inhibition of JNK3, JNK2, and ERK
2-(4-fluorophenyl)-3-(2-isopropylaminopyridin-4-yl)pyrido[2,3-b]pyrazine
-
-
2-(4-fluorophenyl)-3-(pyridin-4-yl)pyrido[2,3-b]pyrazine
-
-
2-(4-fluorophenyl)-3-(pyridin-4-yl)quinoxaline
-
-
2-(4-fluorophenyl)-3-pyridin-4-ylpyrido[3,4-b]pyrazine
-
-
2-(4-fluorophenyl)-6,7-dimethyl-3-pyridin-4-ylquinoxaline
-
-
2-(4-fluorophenyl)-6-methoxy-3-(pyridin-4-yl)quinoxaline
-
-
2-(4-fluorophenyl)-N-[4-(3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl)pyridin-2-yl]acetamide
-
3-(4-fluorophenyl)-2-(2-isopropylaminopyridin-4-yl)pyrido[2,3-b]pyrazine
-
-
3-(4-fluorophenyl)-2-(pyridin-4-yl)pyrido[2,3-b]pyrazine
-
-
3-(4-fluorophenyl)-2-pyridin-4-ylpyrido[3,4-b]pyrazine
-
-
3-(4-fluorophenyl)-6-methoxy-2-(pyridin-4-yl)quinoxaline
-
-
4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]-N-(1(R)-phenylethyl)pyridin-2-amine
-
4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]-N-(1(S)-phenylethyl)pyridin-2-amine
-
4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]-N-(tetrahydro-2H-pyran-4-yl)pyridin-2-amine
-
4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]-N-(1-methylethyl)pyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-(1-phenylethyl)pyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-(3-methylbutan-2-yl)pyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-isobutylpyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-isopropylpyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(1R)-1-phenylethyl]pyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(1S)-1-phenylethyl]pyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(R)-3-methylbutan-2-yl]pyridin-2-amine
-
-
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(S)-3-methylbutan-2-yl]pyridin-2-amine
-
-
4-[4-[3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-ylamine]-cyclohexanol
-
-
4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]-N-(1,2-dimethylpropyl)pyridin-2-amine
-
-
4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]-N-(1-methylethyl)pyridin-2-amine
-
-
6,7-dichloro-2-(4-fluorophenyl)-3-pyridin-4-ylquinoxaline
-
-
7-(6-N-phenylaminohexyl)amino-2H-anthra[1,9-cd]pyrazol-6-one
-
AV-7
adenylyl-beta,gamma-methylene diphosphonic acid
-
i.e. AMP-PCP, MgAMP-PCP shows a mixed inhibition pattern in the kinase reaction, and a competitive pattern in the ATPase reaction
ADP
-
MgADP- shows an uncompetitive inhibition pattern
alsterpaullone
-
36% inhibition of MAPK2/ERK2 at 0.01 mM
BIRB796
binding structure with isozyme p38alpha
II/SP600125
inhibits SAPK/JNK
kenpaullone
-
30% inhibition of MAPK2/ERK2 at 0.01 mM
lignocaine
-
the enzyme inhibition by lignocine may involve voltage-sensitive sodium channels, the enzyme attenuates the induction of MAPK activation by lipopolysaccharides, overview
N-(1,2-dimethylpropyl)-4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-amine
-
-
N-(4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]pyridin-2-yl)2-phenoxypropanamide
-
N-benzyl-4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-amine
-
-
N-benzyl-4-[3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-amine
-
-
N-benzyl-4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-amine
-
-
N-sec-butyl-4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]pyridin-2-amine
-
N-sec-butyl-4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-amine
-
-
N-sec-butyl-4-[3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-amine
-
-
N-tert-butyl-4-[2-(4-fluorophenyl)pyrido[3,4-b]pyrazin-3-yl]pyridin-2-amine
-
-
N-tert-butyl-4-[3-(4-fluorophenyl)pyrido[3,4-b]pyrazin-2-yl]pyridin-2-amine
-
-
N-[4-(3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl)pyridin-2-yl]acetamide
-
purvalanol
-
74% inhibition of MAPK2/ERK2 at 0.01 mM
pyridinyl imidazole-type inhibitors
IC50 of 15-48 nM
-
roscovitine
-
19% inhibition of MAPK2/ERK2 at 0.01 mM
skepinone-L
-
the specificity by which SCD-1 modulates the phospholipid composition and inhibits p38 MAPK signaling (among survival/stress pathways), thereby preventing endoplasmic reticulum stress (but not other SCD-1-dependent responses), suggests selective protein-lipid interactions
trans-4-([4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-yl]amino)cyclohexanol
-
-
trans-4-([4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-yl]amino)cyclohexanol
-
-
U0126
-
specific inhibitor of ERK
[4-[3-methyl-2-piperidin-4-yl-5-(3-trifluoromethyl-phenyl)-3H-imidazol-4-yl]-pyrimidin-2-yl]-((S)-1-phenyl-ethyl)-amine
highly selective for p38 isozyme alpha wild-type and mutants with IC50 of 0.10-0.14 nM, IC50 for JNK2 is 680 nM, for JNK3 970 nM and for ERK 660 nM
SB202190
-
a p38 MAPK specific inhibitor
SB202190
inhibitor of p38 MAPKalpha, little or no inhibition of p38 MAPK beta, gamma, and delta
SB203580
inhibits the p38 isozymes isozymes alpha, beta, and gamma
SB203580
-
noncompetitive in the kinase reaction, competitive versus ATP in the ATPase reaction, no classical linear inhibition kinetics at concentrations below 100 nM
SB203580
-
specific inhibitor of p38alpha MAP kinase, interaction analysis with immobilized enzyme in a surface plasmon resonance study, binding structure from the cyrstal structure of the enzyme-inhibitor complex
SB203580
-
inhibits p38 MAP kinase in T cells, administration of the pharmacological inhibitor of the kinase during the course of infection with the spirochete Borrelia burgdorferi results in reduced levels of IFN-gamma in the sera of infected mice
SB203580
-
a p38 MAPK specific inhibitor
SB203580
inhibitor of p38 MAPKalpha, little or no inhibition of p38 MAPK beta, gamma, and delta
SP600125
-
-
SP600125
inhibitor of JNK
SP600125
-
SP600125 inhibits lipopolysaccharide- and lipoteichoic acid-induced iNOS/NO production by reducing lipopolysaccharide- and lipoteichoic acid-induced JNK protein phosphorylation
additional information
-
indirubin-3'-monoxime is no inhibitor of MAPK2/ERK2
-
additional information
-
no inhibition by AMP and adenine
-
additional information
-
PD98059 and U0126 inhibit EGF-induced phosphorylation of Smad3
-
additional information
structural basis for inhibitor selectivity for p38 over other MAPKs such as ERK or JNK, overview
-
additional information
-
downregulation of MAP kinase activity can be initiated by dephosphorylation through multiple serine/threonine phosphatases, tyrosine-specific phosphatases, and dual specificity phosphatases, i.e. MAP kinase phosphatases, leading to the formation of monophosphorylated MAP kinases
-
additional information
-
PD98059 inhibits the activation of ERK1/2 with a IC50 value of 0.002 mM
-
additional information
PD98059 inhibits the activation of ERK1/2 with a IC50 value of 0.002 mM
-
additional information
PD98059 inhibits the activation of ERK1/2 with a IC50 value of 0.002 mM
-
additional information
PD98059 inhibits the activation of ERK1/2 with a IC50 value of 0.002 mM
-
additional information
-
some monounsaturated fatty acids inhibit p38 MAPK via selective protein-lipid interactions
-
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.
0.00252
(E)-3-(2,4-dimethoxyphenyl)-N-(4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]pyridin-2-yl)acrylamide
Mus musculus
-
0.000041
(E)-3-(2,4-dimethoxyphenyl)-N-(4-[5-(4-fluorophenyl)-2-methanesulfinyl-3H-imidazol-4-yl]pyridin-2-yl)acrylamide
Mus musculus
-
0.000019
(E)-3-(2,4-dimethoxyphenyl)-N-(4-[5-(4-fluorophenyl)-2-methylsulfanyl-3H-imidazol-4-yl]pyridin-2-yl)acrylamide
Mus musculus
-
0.0000043 - 0.00016
1-(2,6-dichloro-phenyl)-6-(2,4-difluoro-phenylsulfanyl)-7-(1,2,3,6-tetrahydro-pyridin-4-yl)-3,4-dihydro-1H-pyrido[3,2-d]pyrimidin-2-one
0.000333
2-(4-fluorophenyl)-3-(2-isopropylaminopyridin-4-yl)pyrido[2,3-b]pyrazine
Mus musculus
-
-
0.00315
2-(4-fluorophenyl)-3-(pyridin-4-yl)quinoxaline
Mus musculus
-
-
0.0037
2-(4-fluorophenyl)-6,7-dimethyl-3-pyridin-4-ylquinoxaline
Mus musculus
-
-
0.00156
2-(4-fluorophenyl)-N-[4-(3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl)pyridin-2-yl]acetamide
Mus musculus
-
0.000038
3-(4-fluorophenyl)-2-(2-isopropylaminopyridin-4-yl)pyrido[2,3-b]pyrazine
Mus musculus
-
-
0.00319
3-(4-fluorophenyl)-2-(pyridin-4-yl)pyrido[2,3-b]pyrazine
Mus musculus
-
-
0.00614
3-(4-fluorophenyl)-6-methoxy-2-(pyridin-4-yl)quinoxaline
Mus musculus
-
-
0.00045
4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]-N-(1(R)-phenylethyl)pyridin-2-amine
Mus musculus
-
0.000006
4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]-N-(1(S)-phenylethyl)pyridin-2-amine
Mus musculus
-
0.00006
4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]-N-(tetrahydro-2H-pyran-4-yl)pyridin-2-amine
Mus musculus
-
0.000238
4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]-N-(1-methylethyl)pyridin-2-amine
Mus musculus
-
-
0.00072
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-(1-phenylethyl)pyridin-2-amine
Mus musculus
-
-
0.000794
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-(3-methylbutan-2-yl)pyridin-2-amine
Mus musculus
-
-
0.000642
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-isobutylpyridin-2-amine
Mus musculus
-
-
0.000081
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-isopropylpyridin-2-amine
Mus musculus
-
-
0.00479
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(1R)-1-phenylethyl]pyridin-2-amine
Mus musculus
-
-
0.000431
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(1S)-1-phenylethyl]pyridin-2-amine
Mus musculus
-
-
0.00159
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(R)-3-methylbutan-2-yl]pyridin-2-amine
Mus musculus
-
-
0.00576
4-[3-(4-fluorophenyl)quinoxalin-2-yl]-N-[(S)-3-methylbutan-2-yl]pyridin-2-amine
Mus musculus
-
-
0.000211
4-[4-[3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-ylamine]-cyclohexanol
Mus musculus
-
-
0.00946
4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]-N-(1,2-dimethylpropyl)pyridin-2-amine
Mus musculus
-
-
0.000412
4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]-N-(1-methylethyl)pyridin-2-amine
Mus musculus
-
-
0.00004 - 0.00009
II/SP600125
0.00138
N-(1,2-dimethylpropyl)-4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-amine
Mus musculus
-
-
0.00089
N-(4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]pyridin-2-yl)2-phenoxypropanamide
Mus musculus
-
0.00153
N-benzyl-4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-amine
Mus musculus
-
-
0.00003
N-sec-butyl-4-[3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl]pyridin-2-amine
Mus musculus
-
0.000595
N-sec-butyl-4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-amine
Mus musculus
-
-
0.000114
N-sec-butyl-4-[3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-amine
Mus musculus
-
-
0.000522
N-tert-butyl-4-[2-(4-fluorophenyl)pyrido[3,4-b]pyrazin-3-yl]pyridin-2-amine
Mus musculus
-
mixture of N-tert-butyl-4-[3-(4-fluorophenyl)pyrido[3,4-b]pyrazin-2-yl]pyridin-2-amine and N-tert-butyl-4-[2-(4-fluorophenyl)pyrido[3,4-b]pyrazin-3-yl]pyridin-2-amine
0.000522
N-tert-butyl-4-[3-(4-fluorophenyl)pyrido[3,4-b]pyrazin-2-yl]pyridin-2-amine
Mus musculus
-
mixture of N-tert-butyl-4-[3-(4-fluorophenyl)pyrido[3,4-b]pyrazin-2-yl]pyridin-2-amine and N-tert-butyl-4-[2-(4-fluorophenyl)pyrido[3,4-b]pyrazin-3-yl]pyridin-2-amine
0.0003
N-[4-(3-(4-fluorophenyl)-5-isopropylisoxazol-4-yl)pyridin-2-yl]acetamide
Mus musculus
-
0.000015 - 0.000048
pyridinyl imidazole-type inhibitors
Mus musculus
IC50 of 15-48 nM
-
0.000025 - 0.00005
skepinone-L
Mus musculus
-
pH 7.4, 22°C
0.000259
trans-4-([4-[3-(4-fluorophenyl)-6,7-dimethylquinoxalin-2-yl]pyridin-2-yl]amino)cyclohexanol
Mus musculus
-
-
0.000608
trans-4-([4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-yl]amino)cyclohexanol
Mus musculus
-
-
0.0000001 - 0.00097
[4-[3-methyl-2-piperidin-4-yl-5-(3-trifluoromethyl-phenyl)-3H-imidazol-4-yl]-pyrimidin-2-yl]-((S)-1-phenyl-ethyl)-amine
additional information
2-(4-fluorophenyl)-3-(pyridin-4-yl)pyrido[2,3-b]pyrazine
0.0000043
1-(2,6-dichloro-phenyl)-6-(2,4-difluoro-phenylsulfanyl)-7-(1,2,3,6-tetrahydro-pyridin-4-yl)-3,4-dihydro-1H-pyrido[3,2-d]pyrimidin-2-one
Mus musculus
highly selective for p38 isozyme alpha wild-type with IC50 of 4.3 nM, respectively, no inhibition of JNK3, JNK2, and ERK
0.000061
1-(2,6-dichloro-phenyl)-6-(2,4-difluoro-phenylsulfanyl)-7-(1,2,3,6-tetrahydro-pyridin-4-yl)-3,4-dihydro-1H-pyrido[3,2-d]pyrimidin-2-one
Mus musculus
IC50 for mutant G110A 61 nM
0.00016
1-(2,6-dichloro-phenyl)-6-(2,4-difluoro-phenylsulfanyl)-7-(1,2,3,6-tetrahydro-pyridin-4-yl)-3,4-dihydro-1H-pyrido[3,2-d]pyrimidin-2-one
Mus musculus
IC50 mutant G110D 160 nM, respectively, no inhibition of JNK3, JNK2, and ERK
0.00004
II/SP600125
Mus musculus
inhibition of JNK1
0.00004
II/SP600125
Mus musculus
inhibition of JNK2
0.00009
II/SP600125
Mus musculus
inhibition of JNK3
0.0000001 - 0.00000014
[4-[3-methyl-2-piperidin-4-yl-5-(3-trifluoromethyl-phenyl)-3H-imidazol-4-yl]-pyrimidin-2-yl]-((S)-1-phenyl-ethyl)-amine
Mus musculus
highly selective for p38 isozyme alpha wild-type and mutants with IC50 of 0.10-0.14 nM
0.00066
[4-[3-methyl-2-piperidin-4-yl-5-(3-trifluoromethyl-phenyl)-3H-imidazol-4-yl]-pyrimidin-2-yl]-((S)-1-phenyl-ethyl)-amine
Mus musculus
Ic50 for ERK 660 nM
0.00068
[4-[3-methyl-2-piperidin-4-yl-5-(3-trifluoromethyl-phenyl)-3H-imidazol-4-yl]-pyrimidin-2-yl]-((S)-1-phenyl-ethyl)-amine
Mus musculus
IC50 for JNK2 is 680 nM
0.00097
[4-[3-methyl-2-piperidin-4-yl-5-(3-trifluoromethyl-phenyl)-3H-imidazol-4-yl]-pyrimidin-2-yl]-((S)-1-phenyl-ethyl)-amine
Mus musculus
IC50 for JNK3 970 nM
additional information
2-(4-fluorophenyl)-3-(pyridin-4-yl)pyrido[2,3-b]pyrazine
Mus musculus
-
46% at 10 microM
additional information
2-(4-fluorophenyl)-3-pyridin-4-ylpyrido[3,4-b]pyrazine
Mus musculus
-
33% at 10 microM, mixture of 3-(4-fluorophenyl)-2-pyridin-4-ylpyrido[3,4-b]pyrazine and 2-(4-fluorophenyl)-3-pyridin-4-ylpyrido[3,4-b]pyrazine
additional information
2-(4-fluorophenyl)-6-methoxy-3-(pyridin-4-yl)quinoxaline
Mus musculus
-
33% at 10 microM
additional information
3-(4-fluorophenyl)-2-pyridin-4-ylpyrido[3,4-b]pyrazine
Mus musculus
-
33% at 10 microM, mixture of 3-(4-fluorophenyl)-2-pyridin-4-ylpyrido[3,4-b]pyrazine and 2-(4-fluorophenyl)-3-pyridin-4-ylpyrido[3,4-b]pyrazine
additional information
6,7-dichloro-2-(4-fluorophenyl)-3-pyridin-4-ylquinoxaline
Mus musculus
-
39% at 10 microM
additional information
N-benzyl-4-[3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-amine
Mus musculus
-
9% at 10 microM
additional information
N-benzyl-4-[6,7-dichloro-3-(4-fluorophenyl)quinoxalin-2-yl]pyridin-2-amine
Mus musculus
-
37% at 10 microM
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.
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.
Ershler, M.; Nagorskaya, T.V.; Visser, J.W.; Belyavsky, A.V.
Novel CDC2-related protein kinases produced in murine hematopoietic stem cells
Gene
124
305-306
1993
Mus musculus (P47811), Mus musculus (P63085), Mus musculus (Q61532)
brenda
Canagarajah, B.J.; Khokhlatchev, A.; Cobb, M.H.; Goldsmith, E.J.
Activation mechanism of the MAP kinase ERK2 by dual phosphorylation
Cell
90
859-869
1997
Mus musculus (P63085)
brenda
Zhang, F.; Strand, A.; Robbins, D.; Cobb, M.H.; Goldsmith, E.J.
Atomic structure of the MAP kinase ERK2 at 2.3 A resolution
Nature
367
704-711
1994
Mus musculus (P63085)
brenda
Payne, D.M.; Rossomando, A.J.; Martino, P.; Erickson, A.K.; Her, J.H.; Shabanowitz, J.; Hunt, D.F.; Weber, M.J.; Sturgill, T.W.
Identification of the regulatory phosphorylation sites in pp42/mitogen-activated protein kinase (MAP kinase)
EMBO J.
10
885-892
1991
Mus musculus (P63085)
brenda
Her, J.H.; Wu, J.; Rall, T.B.; Sturgill, T.W.; Weber, M.J.
Sequence of pp42/MAP kinase, a serine/threonine kinase regulated by tyrosine phosphorylation
Nucleic Acids Res.
19
3743
1991
Mus musculus (P63085)
brenda
Boulton, T.G.; Nye, S.H.; Robbins, D.J.; Ip, N.Y.; Radziejewska, E.; Morgenbesser, S.D.; DePinho, R.A.; Panayotatos, N.; Cobb, M.H.; Yancopoulos, G.D.
ERKs: a family of protein-serine/threonine kinases that are activated and tyrosine phosphorylated in response to insulin and NGF
Cell
65
663-675
1991
Rattus norvegicus (P27704), Mus musculus (P63085)
brenda
Derijard, B.; Raingeaud, J.; Barrett, T.; Wu, I.H.; Han, J.; Ulevitch, R.J.; Davis, R.J.
Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms
Science
267
682-685
1995
Homo sapiens (P45983), Homo sapiens, Mus musculus (P47811)
brenda
Wang, Z.; Harkins, P.C.; Ulevitch, R.J.; Han, J.; Cobb, M.H.; Goldsmith, E.J.
The structure of mitogen-activated protein kinase p38 at 2.1-A resolution
Proc. Natl. Acad. Sci. USA
94
2327-2332
1997
Mus musculus (P47811)
brenda
Han, J.; Lee, J.D.; Bibbs, L.; Ulevitch, R.J.
A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells
Science
265
808-811
1994
Mus musculus (P47811)
brenda
Turgeon, B.; Saba-El-Leil, M.K.; Meloche, S.
Cloning and characterization of mouse extracellular-signal-regulated protein kinase 3 as a unique gene product of 100 kDa
Biochem. J.
346
169-175
2000
Mus musculus (Q61532)
-
brenda
Ito, M.; Yoshioka, K.; Akechi, M.; Yamashita, S.; Takamatsu, N.; Sugiyama, K.; Hibi, M.; Nakabeppu, Y.; Shiba, T.; Yamamoto, K.I.
JSAP1, a novel jun N-terminal protein kinase (JNK)-binding protein that functions as a Scaffold factor in the JNK signaling pathway
Mol. Cell. Biol.
19
7539-7548
1999
Mus musculus (Q61831), Mus musculus (Q91Y86), Mus musculus (Q9WTU6), Mus musculus
brenda
Yang, D.D.; Kuan, C.Y.; Whitmarsh, A.J.; Rincon, M.; Zheng, T.S.; Davis, R.J.; Rakic, P.; Flavell, R.A.
Absence of excitotoxicity-induced apoptosis in the hippocampus of mice lacking the Jnk3 gene
Nature
389
865-870
1997
Mus musculus (Q61831)
brenda
Martin, J.H.; Mohit, A.A.; Miller, C.A.
Developmental expression in the mouse nervous system of the p493F12 SAP kinase
Brain Res. Mol. Brain Res.
35
47-57
1996
Mus musculus (Q61831), Mus musculus
brenda
Whitmarsh, A.J.; Kuan, C.Y.; Kennedy, N.J.; Kelkar, N.; Haydar, T.F.; Mordes, J.P.; Appel, M.; Rossini, A.A.; Jones, S.N.; Flavell, R.A.; Rakic, P.; Davis, R.J.
Requirement of the JIP1 scaffold protein for stress-induced JNK activation
Genes Dev.
15
2421-2432
2001
Mus musculus (Q91Y86)
brenda
Dong, C.; Yang, D.D.; Tournier, C.; Whitmarsh, A.J.; Xu, J.; Davis, R.J.; Flavell, R.A.
JNK is required for effector T-cell function but not for T-cell activation
Nature
405
91-94
2000
Mus musculus (Q91Y86), Mus musculus
brenda
Yang, D.; Tournier, C.; Wysk, M.; Lu, H.T.; Xu, J.; Davis, R.J.; Flavell, R.A.
Targeted disruption of the MKK4 gene causes embryonic death, inhibition of c-Jun NH2-terminal kinase activation, and defects in AP-1 transcriptional activity
Proc. Natl. Acad. Sci. USA
94
3004-3009
1997
Mus musculus (Q91Y86)
brenda
Tournier, C.; Whitmarsh, A.J.; Cavanagh, J.; Barrett, T.; Davis, R.J.
Mitogen-activated protein kinase kinase 7 is an activator of the c-Jun NH2-terminal kinase
Proc. Natl. Acad. Sci. USA
94
7337-7342
1997
Mus musculus (Q91Y86)
brenda
Bain, J.; McLauchlan, H.; Elliott, M.; Cohen, P.
The specificities of protein kinase inhibitors: an update
Biochem. J.
371
199-204
2003
Homo sapiens, Mus musculus
brenda
Matsuura, I.; Wang, G.; He, D.; Liu, F.
Identification and characterization of ERK MAP kinase phosphorylation sites in Smad3
Biochemistry
44
12546-12553
2005
Mus musculus
brenda
Otsuka, M.; Goto, K.; Tsuchiya, S.; Aramaki, Y.
Phosphatidylserine-specific receptor contributes to TGF-beta production in macrophages through a MAP kinase, ERK
Biol. Pharm. Bull.
28
1707-1710
2005
Mus musculus
brenda
Szafranska, A.E.; Dalby, K.N.
Kinetic mechanism for p38 MAP kinase alpha. A partial rapid-equilibrium random-order ternary-complex mechanism for the phosphorylation of a protein substrate
FEBS J.
272
4631-4645
2005
Mus musculus
brenda
Brancho, D.; Tanaka, N.; Jaeschke, A.; Ventura, J.J.; Kelkar, N.; Tanaka, Y.; Kyuuma, M.; Takeshita, T.; Flavell, R.A.; Davis, R.J.
Mechanism of p38 MAP kinase activation in vivo
Genes Dev.
17
1969-1978
2003
Mus musculus
brenda
Ravingerova, T.; Barancik, M.; Strniskova, M.
Mitogen-activated protein kinases: a new therapeutic target in cardiac pathology
Mol. Cell. Biochem.
247
127-138
2003
Canis lupus familiaris, Oryctolagus cuniculus, Homo sapiens, Mus musculus, Rattus norvegicus, Sus scrofa
brenda
Fitzgerald, C.E.; Patel, S.B.; Becker, J.W.; Cameron, P.M.; Zaller, D.; Pikounis, V.B.; O'Keefe, S.J.; Scapin, G.
Structural basis for p38alpha MAP kinase quinazolinone and pyridol-pyrimidine inhibitor specificity
Nat. Struct. Biol.
10
764-769
2003
Mus musculus (P47811)
brenda
Bukhtiyarova, M.; Northrop, K.; Chai, X.; Casper, D.; Karpusas, M.; Springman, E.
Improved expression, purification, and crystallization of p38alpha MAP kinase
Protein Expr. Purif.
37
154-161
2004
Mus musculus
brenda
Diskin, R.; Engelberg, D.; Livnah, O.
High-resolution diffracting crystals of intrinsically active p38alpha MAP kinase: a case study for low-throughput approaches
Acta Crystallogr. Sect. D
63
260-265
2007
Mus musculus
brenda
Hedrick, M.N.; Olson, C.M.; Conze, D.B.; Bates, T.C.; Rincon, M.; Anguita, J.
Control of Borrelia burgdorferi-specific CD4+-T-cell effector function by interleukin-12- and T-cell receptor-induced p38 mitogen-activated protein kinase activity
Infect. Immun.
74
5713-5717
2006
Mus musculus, Mus musculus C3H/HEN
brenda
Kawasaki, T.; Choudhry, M.A.; Schwacha, M.G.; Fujimi, S.; Lederer, J.A.; Bland, K.I.; Chaudry, I.H.
Trauma-hemorrhage inhibits splenic dendritic cell proinflammatory cytokine production via a mitogen-activated protein kinase process
Am. J. Physiol. Cell Physiol.
294
C754-C764
2008
Mus musculus, Mus musculus (Q61831), Mus musculus (Q91Y86), Mus musculus (Q9WTU6)
brenda
Lee, P.Y.; Tsai, P.S.; Huang, Y.H.; Huang, C.J.
Inhibition of toll-like receptor-4, nuclear factor-kappaB and mitogen-activated protein kinase by lignocaine may involve voltage-sensitive sodium channels
Clin. Exp. Pharmacol. Physiol.
35
1052-1058
2008
Mus musculus
brenda
Heinrichsdorff, J.; Luedde, T.; Perdiguero, E.; Nebreda, A.R.; Pasparakis, M.
p38alpha MAPK inhibits JNK activation and collaborates with IkappaB kinase 2 to prevent endotoxin-induced liver failure
EMBO Rep.
9
1048-1054
2008
Mus musculus (P47811), Mus musculus C57BL/6 (P47811)
brenda
Zhang, Y.Y.; Mei, Z.Q.; Wu, J.W.; Wang, Z.X.
Enzymatic activity and substrate specificity of mitogen-activated protein kinase p38alpha in different phosphorylation states
J. Biol. Chem.
283
26591-26601
2008
Mus musculus
brenda
Abidi, P.; Zhang, H.; Zaidi, S.M.; Shen, W.J.; Leers-Sucheta, S.; Cortez, Y.; Han, J.; Azhar, S.
Oxidative stress-induced inhibition of adrenal steroidogenesis requires participation of p38 mitogen-activated protein kinase signaling pathway
J. Endocrinol.
198
193-207
2008
Mus musculus, Mus musculus (Q91Y86), Mus musculus (Q9WTU6)
brenda
Sato, K.; Hamanoue, M.; Takamatsu, K.
Inhibitors of p38 mitogen-activated protein kinase enhance proliferation of mouse neural stem cells
J. Neurosci. Res.
86
2179-2189
2008
Mus musculus
brenda
Pocivavsek, A.; Rebeck, G.W.
Inhibition of c-Jun N-terminal kinase increases apoE expression in vitro and in vivo
Biochem. Biophys. Res. Commun.
387
516-520
2009
Mus musculus
brenda
Beck, I.M.; Berghe, W.V.; Gerlo, S.; Bougarne, N.; Vermeulen, L.; De Bosscher, K.; Haegeman, G.
Glucocorticoids and mitogen- and stress-activated protein kinase 1 inhibitors: possible partners in the combat against inflammation
Biochem. Pharmacol.
77
1194-1205
2009
Mus musculus
brenda
Lin, H.Y.; Shen, S.C.; Lin, C.W.; Wu, M.S.; Chen, Y.C.
Cobalt protoporphyrin inhibition of lipopolysaccharide or lipoteichoic acid-induced nitric oxide production via blocking c-Jun N-terminal kinase activation and nitric oxide enzyme activity
Chem. Biol. Interact.
180
202-210
2009
Mus musculus
brenda
Yao, K.; Cho, Y.Y.; Bode, A.M.; Vummenthala, A.; Park, J.G.; Liu, K.; Pang, Y.P.; Dong, Z.
A selective small-molecule inhibitor of c-Jun N-terminal kinase 1
FEBS Lett.
583
2208-2212
2009
Mus musculus, Homo sapiens (P45983)
brenda
Peifer, C.; Abadleh, M.; Bischof, J.; Hauser, D.; Schattel, V.; Hirner, H.; Knippschild, U.; Laufer, S.
3,4-Diaryl-isoxazoles and -imidazoles as potent dual inhibitors of p38alpha mitogen activated protein kinase and casein kinase 1delta
J. Med. Chem.
52
7618-7630
2009
Mus musculus (P47811)
brenda
Koch, P.; Jahns, H.; Schattel, V.; Goettert, M.; Laufer, S.
Pyridinylquinoxalines and pyridinylpyridopyrazines as lead compounds for novel p38 alpha mitogen-activated protein kinase inhibitors
J. Med. Chem.
53
1128-1137
2010
Mus musculus
brenda
Koeberle, A.; Pergola, C.; Shindou, H.; Koeberle, S.C.; Shimizu, T.; Laufer, S.A.; Werz, O.
Role of p38 mitogen-activated protein kinase in linking stearoyl-CoA desaturase-1 activity with endoplasmic reticulum homeostasis
FASEB J.
29
2439-2449
2015
Mus musculus
brenda
Bardwell, A.J.; Bardwell, L.
Two hydrophobic residues can determine the specificity of mitogen-activated protein kinase docking interactions
J. Biol. Chem.
290
26661-26674
2015
Homo sapiens (P45983), Homo sapiens (P45984), Homo sapiens (Q15759), Mus musculus (P63085)
brenda