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Protein phosphorylation

About: Protein phosphorylation is a research topic. Over the lifetime, 13320 publications have been published within this topic receiving 769601 citations. The topic is also known as: GO:0006468 & protein amino acid phosphorylation.


Papers
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Journal ArticleDOI
TL;DR: Genistein inhibited the EGF-stimulated increase in phosphotyrosine level in A431 cells and scarcely inhibited the enzyme activities of serine- and threonine-specific protein kinases such as cAMP-dependent protein kinase, phosphorylase kinases, and the Ca2+/phospholipid-dependent enzymeprotein kinase C.

3,761 citations

Journal ArticleDOI
03 Nov 2006-Cell
TL;DR: A general mass spectrometric technology is developed and applied for identification and quantitation of phosphorylation sites as a function of stimulus, time, and subcellular location to provide a missing link in a global, integrative view of cellular regulation.

3,404 citations

Journal ArticleDOI
13 Nov 1998-Science
TL;DR: In this paper, the kinase Akt and p21-Ras, an Akt activator, induced phosphorylation of pro-caspase-9 (pro-Casp9) in cells.
Abstract: Caspases are intracellular proteases that function as initiators and effectors of apoptosis. The kinase Akt and p21-Ras, an Akt activator, induced phosphorylation of pro-caspase-9 (pro-Casp9) in cells. Cytochrome c-induced proteolytic processing of pro-Casp9 was defective in cytosolic extracts from cells expressing either active Ras or Akt. Akt phosphorylated recombinant Casp9 in vitro on serine-196 and inhibited its protease activity. Mutant pro-Casp9(Ser196Ala) was resistant to Akt-mediated phosphorylation and inhibition in vitro and in cells, resulting in Akt-resistant induction of apoptosis. Thus, caspases can be directly regulated by protein phosphorylation.

3,280 citations

Journal ArticleDOI
TL;DR: An artificial neural network method is presented that predicts phosphorylation sites in independent sequences with a sensitivity in the range from 69 % to 96 % and predicts novel phosphorylated sites in the p300/CBP protein that may regulate interaction with transcription factors and histone acetyltransferase activity.

2,984 citations

Journal ArticleDOI
27 Jan 1995-Cell
TL;DR: Although the use of PP inhibitors shows that there is significant basal PP activity in cells, it has become apparent that the activities of PPs are regulated in a sophisticated manner by a combination of targeting and regulatory subunits and by specific inhibitors.

2,863 citations


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Performance
Metrics
No. of papers in the topic in previous years
YearPapers
202344
2022133
2021221
2020238
2019224
2018207