Results 1 to 10 of about 856,952 (362)

AGC protein kinase phosphorylation and protein kinase C

Biochemical Society Transactions, 2001
Protein kinase cascades feature in many signal transduction pathways. For those discussed here, a single upstream protein kinase appears to be responsible for the control of multiple downstream targets. So how is specificity introduced into these events?
Parker, P J, Parkinson, S J
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Protein Kinase C

Journal of Cellular Physiology, 1986
The combined application of protein structural techniques, immunochemistry, and molecular biology has permitted an analysis of the differential expression of the genes for the three related protein kinases, C-alpha, -beta, and gamma. The evidence now suggests that the type of protein kinase C in a cell may govern the nature and mechanisms of functional
Axel Ullrich, Peter J. Parker
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A new family of protein kinases— The mitochondrial protein kinases

Advances in Enzyme Regulation, 1995
Molecular cloning has provided evidence for a new family of protein kinases in eukaryotic cells. These kinases show no sequence similarity with other eukaryotic protein kinases, but are related by sequence to the histidine protein kinases found in prokaryotes. These protein kinases, responsible for phosphorylation and inactivation of the branched-chain
Yu Zhao, Kirill M. Popov, David W. Crabb, Robert A. Harris, Yoshiharu Shimomura, Natalia Y. Kedishvili   +5 more
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Protein kinase ofAcetabularia [PDF]

Protoplasma, 1975
Acetabularia cells contain a protein kinase activity which transfers phosphate from ATP to serine or threonine residues of proteins. The enzyme does not respond to cAMP or cGMP. The specific activity increased during development and reached a maximum just before beginning of cap formation. The kinase appears to be a chloroplast associated enzyme.
Manfred Schweiger, P. Dehm, H. J. Rahmsdorf, Monica Hirsch-Kauffmann, Helmut Ponta, Hans-Georg Schweiger, H. S. Pai   +6 more
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cAMP-dependent protein kinase and the protein kinase family

Faraday Discussions, 1992
The structure of the catalytic subunit of cAMP-dependent protein kinase, the first protein kinase structure to be solved, is reviewed. The general architecture of the enzyme is described as well as the active site regions associated with substrate binding and catalysis.
Jianhua Zheng, Susan S. Taylor, Daniel R. Knighton, Janusz M. Sowadski, Lynn F. Ten Eyck   +4 more
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A-kinase anchoring protein targeting of protein kinase A in the heart

Journal of Molecular and Cellular Cardiology, 2004
There is increasing evidence that subcellular targeting of signaling molecules is an important means of regulating the protein kinase A (PKA) pathway. Subcellular organization of the signaling molecules in the PKA pathway insures that a signal initiated at the receptor level is transferred efficiently to a PKA substrate eliciting some cellular response.
Meredith Bond, Mary A. Russell, Mary L. Ruehr   +2 more
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Protein Kinase InhibitorsThe Tyrosine-Specific Protein Kinases

Pharmacology & Therapeutics, 1998
Inhibitors for tyrosine-specific protein kinases ultimately may constitute a novel family of medicinally active agents. Unfortunately, the challenges associated with the acquisition of inhibitors for these enzyme targets are unlike any that have ever been encountered in medicinal chemistry.
David S. Lawrence, Jinkui Niu
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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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Protein kinase C

Pharmacology & Therapeutics, 1991
Based on the molecular structure of the individual members of the protein kinase C family, general properties and the mode of activation of this enzyme family are discussed. Examples are presented of how the investigation of protein kinase C function in vivo has been approached at the molecular level.
Peter J. Parker, Silvia Stabel
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Method for Simultaneous Detection of Protein Kinase A, Protein Kinase C, Protein Tyrosine Kinase, and Calmodulin-Dependent Protein Kinase Activities

Analytical Biochemistry, 1993
We report a simple method that permits simultaneous detection of multiple protein kinase activities using postnuclear supernatant of v-src transformed NIH3T3 cells. A supernatant is incubated with activators of protein kinases and [gamma-32P]ATP, and the phosphorylated proteins are analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis ...
Hidesuke Fukazawa, Satoshi Mizuno, Yoshimasa Uehara, Pei-Ming Li   +3 more
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