Results 301 to 310 of about 11,155,248 (357)

The origins of protein phosphorylation

Nature Cell Biology, 2002
The reversible phosphorylation of proteins is central to the regulation of most aspects of cell function but, even after the first protein kinase was identified, the general significance of this discovery was slow to be appreciated. Here I review the discovery of protein phosphorylation and give a personal view of the key findings that have helped to ...
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Identification of Phosphorylated Proteins

2006
Reversible protein phosphorylation is crucially involved in all aspects of plant cell physiology. The highly challenging task of revealing and characterizing the dynamic protein phosphorylation networks in plants has only recently begun to become feasible, owing to application of dedicated proteomics and mass spectrometry techniques.
Maria V, Turkina, Alexander V, Vener
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Protein tyrosine phosphorylation in streptomycetes

FEMS Microbiology Letters, 1994
Using phosphotyrosine-specific antibodies, we demonstrate that in several Streptomyces spp. a variety of proteins are phosphorylated on tyrosine residues. Tyrosine phosphorylation was found in a number of Streptomyces species including Streptomyces lividans, Streptomyces hygroscopicus and Streptomyces lavendulae. Each species exhibited a unique pattern
Waters, Barbara, Vujaklija, Dušica, Gold, Michael R., Davies, Julian   +3 more
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Protein arginine phosphorylation in organisms

International Journal of Biological Macromolecules, 2021
Protein arginine phosphorylation (pArg), a novel molecular switch, plays a key role in regulating cellular processes. The intrinsic acid lability, hot sensitivity, and hot-alkali instability of "high-energy" phosphoamidate (PN bond) in pArg, make the investigation highly difficult and challenging.
Biling, Huang, Zhixing, Zhao, Yufen, Zhao, Shaohua, Huang   +3 more
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The regulation of protein phosphorylation

Biochemical Society Transactions, 2009
Phosphorylation plays essential roles in nearly every aspect of cell life. Protein kinases regulate signalling pathways and cellular processes that mediate metabolism, transcription, cell-cycle progression, differentiation, cytoskeleton arrangement and cell movement, apoptosis, intercellular communication, and neuronal and immunological functions ...
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Overview of Protein Phosphorylation

Current Protocols in Cell Biology, 1998
AbstractPhosphorylation is the most common and important mechanism of acute and reversible regulation of protein function. Studies of mammalian cells metabolically labeled with [32P]orthophosphate suggest that as many as one‐third of all cellular proteins are covalently modified by protein phosphorylation.
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Platelet Protein Phosphorylation

1985
As can be seen from this review, protein phosphorylation appears involved in both positive and negative regulation of platelets. To date, good evidence has been presented for the involvement of protein phosphorylation in the regulation of granule centralization (i.e. myosin light chain phosphorylation).
J M, Gerrard, L L, Friesen, J M, McCrea, S J, Israels, P, Robinson   +4 more
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Protein phosphorylation and dephosphorylation

Current Opinion in Cell Biology, 1990
The involvement of protein phosphorylation in cellular regulation has advanced far beyond its origins in the study of metabolic enzymes. Indeed, the current literature abounds with studies demonstrating the importance of phosphorylation events in both prokaryotic and eukaryotic species and in virtually every aspect of cellular function. This makes life
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Protein Dephosphorylation and Protein Phosphorylation

2002
The phosphorylation of proteins, at serine, threonine or tyrosine residues, serves multiple roles in the regulation of cell function. However, dephosphorylation is as important as phosphorylation, and it follows that the phosphoprotein phosphatases are integral components of the signaling systems operated by protein kinases.
Bastien D. Gomperts, Ijsbrand M. Kramer, Peter E.R. Tatham   +2 more
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Phosphorylation of nuclear proteins

Philosophical Transactions of the Royal Society of London. B, Biological Sciences, 1983
Abstract Many nuclear proteins are phosphorylated: they range from enzymes to several structural proteins such as histones, non-histone chromosomal proteins and the nuclear lamins. The pattern of phosphorylation varies through the cell cycle. Although histone H1 is phosphorylated during interphase its phosphorylation increases sharply
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