Results 221 to 230 of about 897,439 (267)

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 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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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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The phosphorylation of myelin proteins

Progress in Neurobiology, 1988
Abbreviations I. Overview 2. General introduction 2.1. Myelin 2.2. Myelination 2.3. Myelin basic protein 2.4. Protein phosphorylation 3. Protein kinases that act on myelin basic protein 3.1. Cyclic AMP-dependent kinase 3.2. Calcium-dependent kinases 3.3. Other kinases 4. Phosphoprotein phosphatases that act on myelin basic protein 5. Phosphorylation of
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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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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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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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The Phosphorylation of Presenilin Proteins

2003
The phosphorylation of presenilin (PS) proteins was initially analyzed in cultured cells overexpressing the respective proteins. These studies revealed that the homologous PS proteins are differentially phosphorylated in vivo. Fulllength PS2 was found to be constitutively phosphorylated on serine residues (1,2). In contrast, very little if any (1) or a
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Extracellular Phosphorylation and Phosphorylated Proteins: Not Just Curiosities But Physiologically Important

Science Signaling, 2012
Proteomic data indicate that the phosphorylation of extracellular proteins and extracellular protein domains is a widespread phenomenon.
Yalak G, Vogel V
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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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