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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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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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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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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   +2 more
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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 Phosphorylation in Plant Cell Signaling.

Methods in molecular biology, 2021
Ping Li, Junzhong Liu
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Inhibition of protein phosphorylation by chloroquine

Archives of Microbiology, 1987
The rapid phase of fructose-1,6-bisphosphatase (FBPase) inactivation following glucose addition to starved yeast cells [reported previously] is inhibited on addition of 10 mM chloroquine (CQ) at about pH 8. This inhibition of inactivation was shown to be due to the prevention of phosphorylation of the enzyme.
H, Kalisz, G, Pohlig, H, Holzer
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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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Regulating centrosomes by protein phosphorylation

1999
Publisher Summary Phosphorylation plays a vital role in regulating centrosome architecture and function during progression of the animal cell cycle. Many of the centrosome-associated protein kinases that catalyze the events are described. This chapter discusses the role of reversible protein phosphorylation in controlling many different aspects of ...
Fry, A. M., Mayor, T., Nigg, E. A.
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Sequence and structure-based prediction of eukaryotic protein phosphorylation sites.

Journal of Molecular Biology, 1999
Nikolaj S. Blom   +2 more
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