Results 11 to 20 of about 148,098 (212)
Frontiers 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
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Bioinformatic search of plant microtubule-and cell cycle related serine-threonine protein kinases
BMC Genomics, 2010 A bioinformatic search was carried for plant homologues of human serine-threonine protein kinases involved in regulation of cell division and microtubule protein phosphorylation (SLK, PAK6, PAK7, MARK1, MAST2, TTBK1, TTBK2, AURKA, PLK1, PLK4 and PASK). A
Nyporko Alexey +6 more
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Impact of Serine/Threonine Protein Kinases on the Regulation of Sporulation in Bacillus subtilis.
Frontiers 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
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Química Nova, 2009 Protein kinases are one of the largest protein families and they are responsible for regulation of a great number of signal transduction pathways in cells, through the phosphorylation of serine, threonine, or tyrosine residues.
Bárbara V. Silva +3 more
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SnRK2 Protein Kinases-Key Regulators of Plant Response to Abiotic Stresses [PDF]
, 2011 The SnRK2 family members are plant-specific serine/threonine kinases involved in plant response to abiotic stresses and abscisic acid (ABA)-dependent plant development.
Wawer, Izabela +9 more
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Mechanism of activation of NDR protein kinase by the HMOB1 protein [PDF]
, 2005 Serine/threonine kinases of the nuclear Dbf2-related (NDR) family are highly conserved throughout the eukaryotic world. Members of this kinase family are implicated in various aspects of the regulation of cell division and cell morphology. It has been
Bichsel, Samuel J.
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Role of serine/threonine protein phosphatase PrpN in the life cycle of Bacillus anthracis.
PLoS Pathogens, 2022 Reversible protein phosphorylation at serine/threonine residues is one of the most common protein modifications, widely observed in all kingdoms of life.
Aakriti Gangwal +10 more
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Exploring downstream pathways of aberrantly activated kinases for targeted leukemia therapy [PDF]
, 2008 Genetic alterations resulting in uncontrolled protein tyrosine kinases (PTKs) activity are frequently found in leukemia and in human solid cancers. Although the development of small molecule kinase inhibitors has revolutionized therapy for PTKinduced ...
Gasser, Christelle
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STRUCTURE, ACTIVATION AND BIOLOGICAL EFFECTS OF AKT OR PROTEIN KINASE B [PDF]
Romanian Journal of Medical Practice, 2019 AKT or protein kinase B is a serine / threonine kinase that plays a crucial role in cell proliferation, survival, growth, and glucose metabolism. So far, there have been discovered 3 isoforms of AKT, the most widespread in the tissues is AKT1.
Daniela Miricescu +8 more
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Phosphoinositide-dependent protein kinase-1 (PDK1)-independent activation of the protein kinase C substrate, protein kinase D [PDF]
, 2007 Phosphoinoisitide dependent kinase l (PDK1) is proposed to phosphorylate a key threonine residue within the catalytic domain of the protein kinase C (PKC) superfamily that controls the stability and catalytic competence of these kinases.
Kelly, April P. +3 more
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