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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 +6 more
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cAMP-dependent protein kinase and the protein kinase family
Faraday Discussions, 1992The 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 +4 more
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A-kinase anchoring protein targeting of protein kinase A in the heart
Journal of Molecular and Cellular Cardiology, 2004There 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 +2 more
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Protein Kinase InhibitorsThe Tyrosine-Specific Protein Kinases
Pharmacology & Therapeutics, 1998Inhibitors 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
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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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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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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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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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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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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The stereospecificity of protein kinases
Archives of Biochemistry and Biophysics, 1987To 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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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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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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