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Protein Serine-Threonine Kinases
1992Abstract In nature, a broad range of proteins become modified via the covalent bonding of phosphate to nucleophilic functional groups located on the side-chains of their constituent amino acids. Although numerous amino acids can be modified in this way, by far the most widespread and quantitatively significant phosphorylation events take
Peter J Kennelly, Arthur M Edelman
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Recent advances in bacterial signaling by serine/threonine protein kinases
Trends in Microbiology, 2022Sathya Narayanan Nagarajan +1 more
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Protein Serine/Threonine Kinases of the MAPK Cascade
Annals of the New York Academy of Sciences, 1995J D, Graves, J S, Campbell, E G, Krebs
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Substrate and Docking Interactions in Serine/Threonine Protein Kinases
Chemical Reviews, 2007Elizabeth J Goldsmith +2 more
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Identification and characterization of the serine/threonine protein kinases in Bifidobacterium
Archives of Microbiology, 2014Natalia V Zakharevich
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