Results 351 to 360 of about 3,607,204 (411)

Kinase Inhibitors:  Not Just for Kinases Anymore

Journal of Medicinal Chemistry, 2003
Kinase inhibitors are widely employed as biological reagents and as leads for drug design. Their use is often complicated by their lack of specificity. Although binding conserved ATP sites accounts for some of their nonspecificity, some compounds inhibit proteins not known to bind ATP.
Susan Lynne McGovern, Brian K. Shoichet
openaire   +3 more sources

Coupling of stress in the ER to activation of JNK protein kinases by transmembrane protein kinase IRE1.

Science, 2000
Malfolded proteins in the endoplasmic reticulum (ER) induce cellular stress and activate c-Jun amino-terminal kinases (JNKs or SAPKs). Mammalian homologs of yeast IRE1, which activate chaperone genes in response to ER stress, also activated JNK, and ...
F. Urano, Xiaozhong Wang, A. Bertolotti, Yuhong Zhang, Peter Chung, H. Harding, D. Ron   +6 more
semanticscholar   +1 more source

NAK is an IκB kinase-activating kinase

Nature, 2000
Phosphorylation of IkappaB by the IkappaB kinase (IKK) complex is a critical step leading to IkappaB degradation and activation of transcription factor NF-kappaB. The IKK complex contains two catalytic subunits, IKKalpha and IKKbeta, the latter being indispensable for NF-kappaB activation by pro-inflammatory cytokines.
Atsushi Fujimoto, Shigetsugu Hatakeyama, Yuji Nimura, Yi Chen, Yuichiro Tojima, Yoko S. Kaneko, Kyoji Ikeda, Noboru Motoyama, Michael Karin, Mireille Delhase, Keiichi I. Nakayama, Makoto Nakanishi   +11 more
openaire   +2 more sources

Mitogen-activated protein kinase: conservation of a three-kinase module from yeast to human.

Physiological Reviews, 1999
Mitogen-activated protein kinases (MAPK) are serine-threonine protein kinases that are activated by diverse stimuli ranging from cytokines, growth factors, neurotransmitters, hormones, cellular stress, and cell adherence.
C. Widmann, S. Gibson, M. Jarpe, G. Johnson   +3 more
semanticscholar   +1 more source

Characterization of KLBCK1, encoding a MAP kinase kinase kinase of Kluyveromyces lactis

Journal of Molecular Biology, 1999
The cellular integrity and response to hypoosmotic conditions in the yeast Saccharomyces cerevisiae are ensured by a MAP kinase signal transduction pathway mediated by the yeast homolog of mammalian protein kinase C. Bck1p functions as the MAP kinase kinase kinase of this pathway.
Jörg J. Jacoby, Ute Gengenbacher, Lutz Kirchrath, Jürgen J. Heinisch   +3 more
openaire   +3 more sources

Phosphatidylinositol 3-kinase related kinases

Current Opinion in Immunology, 1996
Studies in yeast, files and mammalian cells have uncovered a novel family of signal-transducing kinases which bear an evolutionary relationship to phosphatidylinositol 3-kinase. These phosphatidylinositol 3-kinase related enzymes play critical roles in DNA repair, V(D)J recombination and cell-cycle checkpoints, and their dysfunction leads to clinical ...
openaire   +3 more sources

Regulation of a Mitogen-Activated Protein Kinase Kinase Kinase, MLTK by PKN

Journal of Biochemistry, 2003
PKNalpha is a fatty acid- and Rho-activated serine/threonine protein kinase having a catalytic domain homologous to members of the protein kinase C family. Recently it was reported that PKNalpha is involved in the p38 mitogen-activated protein kinase (MAPK) signaling pathway.
Takayuki Isagawa, Tamako Nishimura, Yusuke Gotoh, Hon-Song Kim, Mikiko Takahashi, Hideyuki Mukai, Yoshitaka Ono, Emiko Goyama   +7 more
openaire   +3 more sources

Protein Kinases

2011
Enzymes that move phosphate groups from ATP to serine, threonine, or tyrosine residues in another protein.
openaire   +5 more sources

Casein Kinases—Multipotential Protein Kinases

1982
Publisher Summary Casein kinase I and casein kinase II are unique protein kinases that have been described in a number of mammalian and avian cells; an enzyme with properties similar to those of casein kinase I has been described in yeast and plants.
Gary M. Hathaway, Jolinda A. Traugh
openaire   +3 more sources

A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells.

Science, 1994
Mammalian cells respond to endotoxic lipopolysaccharide (LPS) by activation of protein kinase cascades that lead to new gene expression. A protein kinase, p38, that was tyrosine phosphorylated in response to LPS, was cloned.
Jiahuai Han, J.-D. Lee, L. Bibbs, R. Ulevitch   +3 more
semanticscholar   +1 more source