◀ Back to JUN

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