Results 11 to 20 of about 49,266 (275)

Role of p38 and JNK Mitogen-Activated Protein Kinases in the Activation of Ternary Complex Factors [PDF]

open access: yesMolecular and Cellular Biology, 1997
The transcription factors Elk-1 and SAP-1 bind together with serum response factor to the serum response element present in the c-fos promoter and mediate increased gene expression. The ERK, JNK, and p38 groups of mitogen-activated protein (MAP) kinases phosphorylate and activate Elk-1 in response to a variety of extracellular stimuli. In contrast, SAP-
Whitmarsh, Alan J.   +4 more
core   +6 more sources

Roles of JNK, p38 and ERK mitogen-activated protein kinases in the growth inhibition and apoptosis induced by cadmium [PDF]

open access: yesCarcinogenesis, 2000
Cadmium (Cd), a human carcinogen, can induce apoptosis in various cell types. Three major mitogen-activated protein kinases (MAPKs), c-JUN N-terminal kinase (JNK), p38 and extracellular signal-regulated kinase (ERK), have been shown to regulate apoptosis.
Show-Mei Chuang   +2 more
exaly   +5 more sources

Mitogen Activated Protein kinase signal transduction pathways in the prostate

open access: yesCell Communication and Signaling, 2004
The biochemistry of the mitogen activated protein kinases ERK, JNK, and p38 have been studied in prostate physiology in an attempt to elucidate novel mechanisms and pathways for the treatment of prostatic disease.
Koul Sweaty   +3 more
doaj   +2 more sources

Mechanism and Therapeutic Targets of c-Jun-N-Terminal Kinases Activation in Nonalcoholic Fatty Liver Disease

open access: yesBiomedicines, 2022
Non-alcoholic fatty liver (NAFL) is the most common chronic liver disease. Activation of mitogen-activated kinases (MAPK) cascade, which leads to c-Jun N-terminal kinase (JNK) activation occurs in the liver in response to the nutritional and metabolic ...
Robert W. M. Min   +4 more
doaj   +1 more source

Interacting JNK-docking Sites in MKK7 Promote Binding and Activation of JNK Mitogen-activated Protein Kinases [PDF]

open access: yesJournal of Biological Chemistry, 2006
D-sites are a class of MAPK-docking sites that have been found in many MAPK regulators and substrates. A single functional, high affinity D-site has been identified near the N terminus of each of the MAPK kinases (MKKs or MEKs) MEK1, MEK2, MKK3, MKK4, and MKK6.
David T, Ho   +4 more
openaire   +2 more sources

Scaffold Role of DUSP22 in ASK1-MKK7-JNK Signaling Pathway. [PDF]

open access: yesPLoS ONE, 2016
Mitogen-activated protein kinases (MAPKs) are involved in a variety of intracellular events such as gene expression, cell proliferation, and programmed cell death.
Anna Ju   +8 more
doaj   +1 more source

Scaffold Role of a Mitogen-activated Protein Kinase Phosphatase, SKRP1, for the JNK Signaling Pathway [PDF]

open access: yesJournal of Biological Chemistry, 2002
Stress-activated protein kinase (SAPK) pathway-regulating phosphatase 1 (SKRP1) has been identified as a member of the mitogen-activated protein kinase (MAPK) phosphatase (MKP) family that interacts physically with the MAPK kinase (MAPKK) MKK7, a c-Jun N-terminal kinase (JNK) activator, and inactivates the MAPK JNK pathway.
Takeru, Zama   +5 more
openaire   +2 more sources

The JNK Signaling Pathway in Inflammatory Skin Disorders and Cancer

open access: yesCells, 2020
The c-Jun N-terminal kinases (JNKs), with its members JNK1, JNK2, and JNK3, is a subfamily of (MAPK) mitogen-activated protein kinases. JNK signaling regulates a wide range of cellular processes, including cell proliferation, differentiation, survival ...
Manel B. Hammouda   +3 more
doaj   +1 more source

Corticosterone‐induced rapid phosphorylation of p38 and JNK mitogen‐activated protein kinases in PC12 cells [PDF]

open access: yesFEBS Letters, 2001
The present study showed that corticosterone (B) could induce a rapid activation of p38 and c‐Jun NH2‐terminal protein kinase (JNK) in PC12 cells. The dose–response and time–response curves were bell‐shaped with maximal activation at 10−9 M and at 15 min. RU38486 had no effect, and bovine serum albumin‐coupled B could induce the activation.
Li, Xiaoyu   +5 more
openaire   +2 more sources

Co-regulation of the transcription controlling ATF2 phosphoswitch by JNK and p38

open access: yesNature Communications, 2020
The ATF2 transcription factor is phosphorylated by different mitogen-activated protein (MAP) kinases. Here, the authors show that the functionally distinct MAP kinases JNK and p38 control ATF2 through different binding sites and differential ...
Klára Kirsch   +13 more
doaj   +1 more source

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