Results 221 to 230 of about 2,111,356 (267)
Some of the next articles are maybe not open access.
AGC protein kinase phosphorylation and protein kinase C
Biochemical Society Transactions, 2001Protein 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
openaire +2 more sources
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.
Mary L, Ruehr +2 more
openaire +2 more sources
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 ...
H, Fukazawa +3 more
openaire +2 more sources
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 ...
H, Fukazawa +3 more
openaire +2 more sources
2011
Enzymes that move phosphate groups from ATP to serine, threonine, or tyrosine residues in another protein.
openaire +5 more sources
Enzymes that move phosphate groups from ATP to serine, threonine, or tyrosine residues in another protein.
openaire +5 more sources
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 +2 more
openaire +2 more sources
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 +2 more
openaire +2 more sources
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
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
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.
H S, Pai +6 more
openaire +2 more sources
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.
H S, Pai +6 more
openaire +2 more sources
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.
H R, Matthews, V D, Huebner
openaire +2 more sources
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.
H R, Matthews, V D, Huebner
openaire +2 more sources
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 ...
P N, McFadden +3 more
openaire +2 more sources
The International Journal of Biochemistry & Cell Biology, 1997
Protein kinase CK2 is a ubiquitous protein kinase responsible for the phosphorylation of Ser and Thr residues specified by acidic side chains in many proteins, including several key enzymes, growth factor receptors, transcription factors and cytoskeletal proteins.
openaire +2 more sources
Protein kinase CK2 is a ubiquitous protein kinase responsible for the phosphorylation of Ser and Thr residues specified by acidic side chains in many proteins, including several key enzymes, growth factor receptors, transcription factors and cytoskeletal proteins.
openaire +2 more sources

