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Overview of Protein Phosphorylation

Current Protocols in Protein Science, 1995
AbstractThis overview provides a history of protein phosphorylation research and provides the reader with an understanding of how and why labeling studies are performed. The various sites of protein phosphorylation are described along with the roles of the many kinases and phosphatases that regulate phosphorylation.
B M, Sefton, S, Shenolikar
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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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Highly phosphorylated bacterial proteins

PROTEOMICS, 2004
AbstractWe show in Gram‐negative and Gram‐positive bacteria the appearance of highly acidic proteins, which are highly phosphorylated. This group of proteins includes many cellular proteins, such as chaperones, biosynthetic, and metabolic enzymes. These proteins accumulate under stress conditions or under conditions, which overload the proteolytic ...
Ran, Rosen   +5 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   +3 more
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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   +3 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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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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Protein Phosphorylation

1999
Abstract Reversible phosphorylation is one of the major mechanisms of controlling protein activity in all eukaryotic cells. This new edition of Protein Phosphorylation: A Practical Approach provides a comprehensive description of current methods used to study protein phosphorylation and the kinases and phosphatases which catalyse it ...
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Protein Phosphorylation

1993
Abstract Reversible phosphorylation is one of the major mechanisms by which protein activity is controlled in all eukaryotic cells. Networks of protein kinases and phosphatases, which catalyse phosphorylation and dephosphorylation respectively, are responsible for switching between different pathways of cell division, development, or ...
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Phosphorylation of nuclear proteins

Philosophical Transactions of the Royal Society of London. B, Biological Sciences, 1983
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 during mitosis. Histone H3,
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