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The function of serine/threonine-specific protein kinases in B cells [PDF]

open access: yesFrontiers in Immunology
The serine/threonine-specific protein kinases (STKs) are important for cell survival, proliferation, differentiation, and apoptosis. In B cells, these kinases play indispensable roles in regulating important cellular functions.
Zhennan Han   +8 more
doaj   +3 more sources

Correlated mutation analysis on the catalytic domains of serine/threonine protein kinases. [PDF]

open access: goldPLoS ONE, 2009
BACKGROUND:Protein kinases (PKs) have emerged as the largest family of signaling proteins in eukaryotic cells and are involved in every aspect of cellular regulation.
Feng Xu   +6 more
doaj   +6 more sources

Impact of Serine/Threonine Protein Kinases on the Regulation of Sporulation in Bacillus subtilis. [PDF]

open access: yesFrontiers in Microbiology, 2016
Bacteria possess many kinases that catalyze phosphorylation of proteins on diverse amino acids including arginine, cysteine, histidine, aspartate, serine, threonine and tyrosine.
Frédérique ePompeo   +2 more
doaj   +6 more sources

Mycobacterium tuberculosis Serine/Threonine Protein Kinases [PDF]

open access: yesMicrobiology Spectrum, 2014
The Mycobacterium tuberculosis genome encodes 11 serine/threonine protein kinases (STPKs). A similar number of two-component systems are also present, indicating that these two signal transduction mechanisms are both important in the adaptation of this ...
S. Prisic, R. Husson
semanticscholar   +4 more sources

Protein serine/threonine kinases (PKA, PKC and CaMKII) involved in ischemic brain pathology

open access: hybridActa Neurobiologiae Experimentalis, 1996
The protein serine/threonine kinases which are highly expressed in the central nervous system (CNS) are severely affected by brain ischemia. Irrespective of substantial differences among the particular members of this group of kinases, their responses to
Krystyna Domańska‐Janik
openalex   +3 more sources

Structural basis and prediction of substrate specificity in protein serine/threonine kinases

open access: greenProceedings of the National Academy of Sciences of the United States of America, 2002
The large number of protein kinases makes it impractical to determine their specificities and substrates experimentally. Using the available crystal structures, molecular modeling, and sequence analyses of kinases and substrates, we developed a set of ...
Ross I. Brinkworth   +2 more
openalex   +2 more sources

Cross-phosphorylation of bacterial serine/threonine and tyrosine protein kinases on key regulatory residues

open access: yesFrontiers in Microbiology, 2014
Bacteria possess protein serine/threonine and tyrosine kinases which resemble eukaryal kinases in their capacity to phosphorylate multiple substrates. We hypothesized that the analogy might extend further, and bacterial kinases may also undergo mutual ...
Lei eShi   +7 more
doaj   +2 more sources

Coordinate regulation of pp90rsk and a distinct protein-serine/threonine kinase activity that phosphorylates recombinant pp90rsk in vitro. [PDF]

open access: greenMolecular and Cellular Biology, 1991
Protein kinase assays that use recombinant pp90rsk as a substrate were developed in an attempt to identify growth-regulated enzymes responsible for the phosphorylation and activation of pp90rsk S6 phosphotransferase activity.
Jongkyeong Chung   +2 more
openalex   +2 more sources

Mitogen‐activated protein kinases activate the serine/threonine kinases Mnk1 and Mnk2 [PDF]

open access: yesThe EMBO Journal, 1997
Mitogen‐activated protein (MAP) kinases bind tightly to many of their physiologically relevant substrates. We have identified a new subfamily of murine serine/threonine kinases, whose members, MAP kinase‐interacting kinase 1 (Mnk1) and Mnk2, bind tightly
A. Waskiewicz   +3 more
semanticscholar   +4 more sources

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