Results 321 to 330 of about 856,952 (362)
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A-kinase anchoring proteins: protein kinase A and beyond
Current Opinion in Cell Biology, 2000Compartmentalization of kinases and phosphatases is a key determinant in the specificity of second messenger mediated signaling events. Localization of the cAMP-dependent protein kinase (PKA) and other signaling enzymes is mediated by interaction with A-kinase anchoring proteins (AKAPs).
Amelia S. Edwards, John D. Scott
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Current Opinion in Structural Biology, 1994
The structures of four serine/threonine protein kinases have been determined recently. By comparing these structures with that of the cAMP-dependent protein kinase (cAPK), it is now possible to see how the activity of these regulatory enzymes is controlled. Low activity is maintained through the conformation of the phosphorylation lip, domain rotations,
E J, Goldsmith, M H, Cobb
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The structures of four serine/threonine protein kinases have been determined recently. By comparing these structures with that of the cAMP-dependent protein kinase (cAPK), it is now possible to see how the activity of these regulatory enzymes is controlled. Low activity is maintained through the conformation of the phosphorylation lip, domain rotations,
E J, Goldsmith, M H, Cobb
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2021
Recently, aging has been tried to be explained with large numbers of theories, but none of them can elucidate the changes occurring in the aging process alone. A unified theory encompassing the mechanisms of genetic factors and repair systems in aging is becoming increasingly required.
ENGİN, ATİLLA, ENGİN, AYŞE BAŞAK
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Recently, aging has been tried to be explained with large numbers of theories, but none of them can elucidate the changes occurring in the aging process alone. A unified theory encompassing the mechanisms of genetic factors and repair systems in aging is becoming increasingly required.
ENGİN, ATİLLA, ENGİN, AYŞE BAŞAK
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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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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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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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2011
Major progress has been made in unravelling of regulatory mechanisms in eukaryotic cells. Modification of target protein properties by reversible phosphorylation events has been found to be one of the most prominent cellular control processes in all organisms.
Nico Dissmeyer, Arp Schnittger
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Major progress has been made in unravelling of regulatory mechanisms in eukaryotic cells. Modification of target protein properties by reversible phosphorylation events has been found to be one of the most prominent cellular control processes in all organisms.
Nico Dissmeyer, Arp Schnittger
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