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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
openaire   +3 more sources

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
openaire   +3 more sources

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   +3 more
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Protein Kinases

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

The stereospecificity of protein kinases

Archives of Biochemistry and Biophysics, 1987
To test whether cellular protein kinases exist that phosphorylate D-amino acid residues, a method was developed for separating O-phospho-D-serine from O-phospho-L-serine and O-phospho-L-tyrosine from O-phospho-D-tyrosine. This was accomplished by converting these amino acids to the L-leucyl dipeptide derivatives followed by separation of the ...
Lillian L. Lou   +3 more
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Nuclear protein kinases

Molecular and Cellular Biochemistry, 1984
Nuclear protein kinases include enzymes that transfer the gamma-phosphate of ATP to serine, threonine, lysine or histidine in proteins. Nuclear kinases with a preference for basic proteins are known as histone kinases; those preferring acidic protein substrates are casein kinases.
Harry R. Matthews, Verena D. Huebner
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The structural basis for control of eukaryotic protein kinases.

Annual Review of Biochemistry, 2012
Eukaryotic protein kinases are key regulators of cell processes. Comparison of the structures of protein kinase domains, both alone and in complexes, allows generalizations to be made about the mechanisms that regulate protein kinase activation.
J. Endicott, M. Noble, L. Johnson
semanticscholar   +1 more source

Bacterial Protein Kinases

2021
Bacteria are able to inhabit and survive vastly diverse environments. This enormous adaptive capacity depend on their ability to perceive cues from the micro-environment and process this information accordingly to mount appropriate metabolic responses and ultimately sustain homeostasis.
openaire   +2 more sources

New directions in targeting protein kinases: focusing upon true allosteric and bivalent inhibitors.

Current pharmaceutical design, 2012
Over the past decade, therapeutics that target subsets of the 518 human protein kinases have played a vital role in the fight against cancer. Protein kinases are typically targeted at the adenosine triphosphate (ATP) binding cleft by type I and II ...
Vandana Lamba, I. Ghosh
semanticscholar   +1 more source

The Chk2 protein kinase

DNA Repair, 2004
Checkpoint kinase 2 (Chk2) is a multifunctional enzyme whose functions are central to the induction of cell cycle arrest and apoptosis by DNA damage. Insight into Chk2 has derived from multiple approaches. Biochemical studies have addressed Chk2 structure, domain organization and regulation by phosphorylation.
Jinwoo Ahn, Marshall Urist, Carol Prives
openaire   +2 more sources

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