Results 311 to 320 of about 2,670,458 (365)
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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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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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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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Science, 2000
Malfolded proteins in the endoplasmic reticulum (ER) induce cellular stress and activate c-Jun amino-terminal kinases (JNKs or SAPKs). Mammalian homologs of yeast IRE1, which activate chaperone genes in response to ER stress, also activated JNK, and ...
F. Urano +6 more
semanticscholar +1 more source
Malfolded proteins in the endoplasmic reticulum (ER) induce cellular stress and activate c-Jun amino-terminal kinases (JNKs or SAPKs). Mammalian homologs of yeast IRE1, which activate chaperone genes in response to ER stress, also activated JNK, and ...
F. Urano +6 more
semanticscholar +1 more source
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.
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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.
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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
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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
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Regulation of a heart potassium channel by protein kinase A and C.
Science, 1988The enzymes adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase (protein kinase A) and protein kinase C regulate the activity of a diverse group of cellular proteins including membrane ion channel proteins.
K. Walsh, R. Kass
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Networking with protein kinases
Current Biology, 1993It is taken for granted nowadays that extracellular signals are amplified and transduced inside cells by protein kinase cascades. Hundreds of different protein kinases have already been identified and the rate of discovery of new kinases shows no sign of slowing. Until recently, however, relatively little was known about how all these different protein
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