Results 1 to 10 of about 98,842 (86)

A human MAP kinase interactome. [PDF]

open access: yesNature Methods, 2010
Mitogen-activated protein kinase (MAPK) pathways form the backbone of signal transduction in the mammalian cell. Here we applied a systematic experimental and computational approach to map 2,269 interactions between human MAPK-related proteins and other ...
A Friedman   +51 more
core   +8 more sources

Interaction of MAP kinase with MAP kinase kinase: its possible role in the control of nucleocytoplasmic transport of MAP kinase [PDF]

open access: yesThe EMBO Journal, 1997
The mitogen-activated protein kinase (MAPK) cascade consisting of MAPK and its direct activator, MAPK kinase (MAPKK), is essential for signaling of various extracellular stimuli to the nucleus. Upon stimulation, MAPK is translocated to the nucleus, whereas MAPKK stays in the cytoplasm.
Yukiko Gotoh   +2 more
openaire   +3 more sources

Conserved Docking Site Is Essential for Activation of Mammalian MAP Kinase Kinases by Specific MAP Kinase Kinase Kinases [PDF]

open access: yesMolecular Cell, 2005
Mammalian mitogen-activated protein kinase (MAPK) cascades control various cellular events, ranging from cell growth to apoptosis, in response to external stimuli. A conserved docking site, termed DVD, is found in the mammalian MAP kinase kinases (MAPKKs) belonging to the three major subfamilies, namely MEK1, MKK4/7, and MKK3/6.
Kazuo Tatebayashi   +3 more
openaire   +3 more sources

Activation of p21-activated Kinase 6 by MAP Kinase Kinase 6 and p38 MAP Kinase [PDF]

open access: yesJournal of Biological Chemistry, 2005
The p21-activated kinases (PAKs) contain an N-terminal Cdc42/Rac interactive binding domain, which in the group 1 PAKs (PAK1, 2, and 3) regulates the activity of an adjacent conserved autoinhibitory domain. In contrast, the group 2 PAKs (PAK4, 5, and 6) lack this autoinhibitory domain and are not activated by Cdc42/Rac binding, and the mechanisms that ...
Ole Gjoerup   +7 more
openaire   +3 more sources

Concentration-dependent positive and negative regulation of a MAP kinase by a MAP kinase kinase [PDF]

open access: yesOncogene, 1999
There are at least three distinct MAP kinase signaling modules in mammalian cells, distinguished by the family of kinases (Erk, SAPK/JNK, or p38) that is ultimately activated. Many input signals activate multiple MAP kinase cascades, and the mechanisms that control the specificity of signal output are not well understood.
Bruce J. Mayer   +4 more
openaire   +3 more sources

c-Jun N-Terminal Kinase in Inflammation and Rheumatic Diseases. [PDF]

open access: yes, 2012
The c-Jun N-terminal kinases (JNKs) are members of the mitogen-activated protein kinase (MAPK) family and are activated by environmental stress. JNK is also activated by proinflammatory cytokines, such as TNF and IL-1, and Toll-like receptor ligands ...
Firestein, Gary S, Guma, Monica
core   +1 more source

Expressed in the yeast Saccharomyces cerevisiae, human ERK5 is a client of the Hsp90 chaperone that complements loss of the Slt2p (Mpk1p) cell integrity stress-activated protein kinase [PDF]

open access: yes, 2006
ERK5 is a mitogen-activated protein (MAP) kinase regulated in human cells by diverse mitogens and stresses but also suspected of mediating the effects of a number of oncogenes.
King, Victoria   +7 more
core   +2 more sources

Phosphorylation of Xenopus mitogen-activated protein (MAP) kinase kinase by MAP kinase kinase kinase and MAP kinase.

open access: yesJournal of Biological Chemistry, 1993
Xenopus 45-kDa mitogen-activated protein (MAP) kinase kinase (MAPKK) is a serine/threonine/tyrosine kinase, which activates MAP kinase (MAPK) by phosphorylating its threonine and tyrosine residues. MAPKK is active only when its threonine and/or serine residues are phosphorylated.
Satoshi Matsuda   +2 more
openaire   +3 more sources

Identification of a MAP kinase kinase kinase in phaeochromocytoma (PC12) cells [PDF]

open access: yesFEBS Letters, 1992
A MAP kinase kinase kinase (MAPKKK) was identified in phaeochromocytoma (PC12) cells which reactivated homogeneous MAP kinase kinase (MAPKK) from rabbit skeletal muscle that had been inactivated by incubation with protein phosphatase 2A. Reactivation was accompanied by stoichiometric phosphorylation of MAPKK on a serine residue(s).
Gomez, Nestor   +2 more
openaire   +4 more sources

The structural basis for the specificity of pyridinylimidazole inhibitors of p38 MAP kinase [PDF]

open access: yes, 1997
Background: The p38 mitogen-activated protein (MAP) kinase regulates signal transduction in response to environmental stress. Pyridinylimidazole compounds are specific inhibitors of p38 MAP kinase that block the production of the cytokines interleukin-1 ...
Bemis, Guy W.   +9 more
core   +1 more source

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