Results 321 to 330 of about 2,849,925 (342)

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
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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
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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
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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 ...
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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
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Protein Kinases

2011
Enzymes that move phosphate groups from ATP to serine, threonine, or tyrosine residues in another protein.
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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
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Cyclin dependent kinase activating kinases

Current Opinion in Cell Biology, 1996
The cyclin dependent kinase activating kinase (CAK) has roles in both cell cycle regulation and transcription. CAK assembly is regulated either by additional protein binding or by phosphorylation. A recent comparison of this kinase from two yeast species shows that different proteins perform distinct roles and that the most studied CAK may function ...
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Diacylglycerol kinases

Cellular Signalling, 2004
Diacylglycerol kinases (DGKs) phosphorylate diacylglycerol to form phosphatidic acid. In most cases, members of this large family of enzymes appear to bind and regulate proteins activated by either diacylglycerol or phosphatidic acid. Proteins that appear to be regulated, in part, by DGKs include protein kinase Cs, RasGRPs, and phosphatidylinositol ...
Bai, Luo, Debra S, Regier, Stephen M, Prescott, Matthew K, Topham   +3 more
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Phosphatases and Kinases [PDF]

Current Protocols in Molecular Biology, 1987
AbstractThe reaction conditions and applications of two phosphatases and one kinase are described in this unit. Bacterial alkaline phosphatase (BAP) from E. coli and calf intestine phosphatase (CIP) from veal are commonly used in nucleic acid research.
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