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AHSA1 — JUN
Text-mined interactions from Literome
Arnould et al., Mol Cell Biol 1999
(Polycystic Kidney, Autosomal Dominant) :
The PKD2 mediated
AP-1 activity was
dependent upon activation of the mitogen activated protein kinases
p38 and JNK1 and protein kinase C (PKC) epsilon, a calcium independent PKC isozyme
Bhattacharyya et al., Biochem J 2002
:
While ERK1/2 activation could be linked to enhanced DNA binding of activator protein-1 (AP-1),
p38 MAPK signalling did not
affect AP-1 DNA binding
Chen et al., J Neurochem 2003
(MAP Kinase Signaling System) :
These results suggest a prominent role of JNK and
p38 , as well as their downstream
AP-1 binding
activation and p53 phosphorylation in mediating glutamate excitotoxicity
Silvers et al., Neoplasia (New York, N.Y.) 2003
(Skin Neoplasms) :
The role of JNK and
p38 MAPK activities in UVA induced signaling pathways
leading to
AP-1 activation and c-Fos expression
Parameswaran et al., Cell Physiol Biochem 2003
:
Both an AM-induced increase in AP-1 mRNA expression and
AP-1 luciferase activities were
inhibited by H89 ( protein kinase-A inhibitor ) and SB203580 (
p38 MAPK inhibitor )
Han et al., FEBS Lett 2005
:
While extracellular signal regulated kinase ( ERK ) and
p38 activation was detected in Prx II ( -/- ) MEF, ERK and
c-Jun N-terminal kinase (JNK) activation was
detected in Prx II ( -/- ) skin
Kim et al., Eur J Immunol 2005
(Bacteroides Infections...) :
The
p38 inhibitor SB203580 and the ERK inhibitor U0126
reduced not only
AP-1 activity, but also decreased IL-8 and MCP-1 expression
Lahti et al., BMC pharmacology 2006
:
Inhibition of
p38 mitogen activated protein kinase
enhances c-Jun N-terminal kinase activity : implication in inducible nitric oxide synthase expression
Hong et al., J Biol Chem 2006
(MAP Kinase Signaling System...) :
The homophilic interactions of CD151 increased motility and MMP-9 expression of CD151 transfected MelJuSo cells, along with FAK-, Src-,
p38 MAPK-, and JNK mediated
activation of
c-Jun in an adhesion dependent manner
Peng et al., Toxicology 2007
(Glioma) :
Inhibition of ERK,
p38 and JNK
block the activation of
AP-1 and NF-kappaB, suggesting these MAPKs are involved in ( Ac ) ( 5 ) GP-induced transcription regulation
Humar et al., Int J Biochem Cell Biol 2007
:
The mitogen activated protein kinase
p38 regulates
activator protein 1 by direct phosphorylation of c-Jun
Lim et al., Planta Med 2007
(Inflammation) :
Moreover, quercetin inhibited extracellular signal regulated protein kinase ( ERK ) and
p38 mitogen activated protein kinase ( MAPK ) activation, and kaempferol
inhibited p38 MAPK and
c-Jun N-terminal kinase (JNK) activation among the MAPKs tested
Jiao et al., Zhonghua lao dong wei sheng zhi ye bing za zhi = Zhonghua laodong weisheng zhiyebing zazhi = Chinese journal of industrial hygiene and occupational diseases 2007
:
Moreover, B ( a ) P-induced activation of
c-Jun was
inhibited by stable expression of dominant negative mutants of JNK or ERK, but not by dominant negative mutant of
p38
Ding et al., FEMS Immunol Med Microbiol 2008
:
extracellular signal related kinase ( ERK ),
p38 , and c-Jun N-terminal kinase (JNK) each selectively
regulated AP-1 subcomponent expression and DNA binding activity
Lee et al., Immunology 2009
:
Anti-P mAb
enhanced phosphorylation of Akt ( PKB ; protein kinase B ), extracellular signal regulated kinase 1/2 ( ERK1/2 ) and
c-Jun NH2-terminal kinase 1/2 (JNK1/2) , while phosphorylation of
p38 remained unaltered
Truter et al., Cardiology 2009
(Aortic Valve Insufficiency...) :
JNK and
p38MAPK inhibition
reduced c-Jun and ATF2 phosphorylation to NL ; ERK inhibition had no effect
Shim et al., J Med Food 2009
:
Moreover, inhibition of phosphorylated ERK, JNK, and
p38 by K. pandurata extract
resulted in decreased c-Fos expression and
c-Jun phosphorylation induced by UV light
Loesch et al., J Biol Chem 2010
:
p38gamma requires phosphorylation and its C terminus to bind
c-Jun , whereas both c-Jun and p38gamma are required for the trans-activation of MMP9
Liu et al., Particle and fibre toxicology 2012
:
Our data also demonstrated that the stimulation of cocultures with SiO2 particles strongly
enhanced c-Jun NH2-terminal kinase (JNK) phosphorylation and NF-?B activation in both HUVECs and THP-1 cells, whereas the phosphorylation of
p38 was not affected
Yi et al., J Immunol 1998
(Lymphoma, B-Cell) :
Inhibition of
p38 led to the suppression of CpG DNA induced
AP-1 DNA binding activity and cytokine production, indicating that the p38 pathway is required for mediating these immune stimulatory effects of CpG DNA