Results 381 to 390 of about 3,327,333 (431)
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2011
Enzymes that move phosphate groups from ATP to serine, threonine, or tyrosine residues in another protein.
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Enzymes that move phosphate groups from ATP to serine, threonine, or tyrosine residues in another protein.
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Characterization of KLBCK1, encoding a MAP kinase kinase kinase of Kluyveromyces lactis
Journal of Molecular Biology, 1999The 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 +3 more
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Phosphatidylinositol 3-kinase related kinases
Current Opinion in Immunology, 1996Studies 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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A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells.
Science, 1994Mammalian 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 +3 more
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Casein Kinases—Multipotential Protein Kinases
1982Publisher 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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Protein kinase C and lipid signaling for sustained cellular responses
The FASEB Journal, 1995Since the second messenger role was proposed for the products of inositol phospholipid hydrolysis, considerable progress has been made in our understanding of the biochemical mechanism of the intracellular signaling network.
Y. Nishizuka
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Regulation of a Mitogen-Activated Protein Kinase Kinase Kinase, MLTK by PKN
Journal of Biochemistry, 2003PKNalpha 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 +7 more
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Cyclin dependent kinase activating kinases
Current Opinion in Cell Biology, 1996The 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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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 +3 more
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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 +3 more
openaire +2 more sources