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Cooperativity within proximal phosphorylation sites is revealed from large-scale proteomics data

Overview of attention for article published in Biology Direct, January 2010
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Title
Cooperativity within proximal phosphorylation sites is revealed from large-scale proteomics data
Published in
Biology Direct, January 2010
DOI 10.1186/1745-6150-5-6
Pubmed ID
Authors

Regev Schweiger, Michal Linial

Abstract

Phosphorylation is the most prevalent post-translational modification on eukaryotic proteins. Multisite phosphorylation enables a specific combination of phosphosites to determine the speed, specificity and duration of biological response. Until recent years, the lack of high quality data limited the possibility for analyzing the properties of phosphorylation at the proteome scale and in the context of a wide range of conditions. Thanks to advances of mass spectrometry technologies, thousands of phosphosites from in-vivo experiments were identified and archived in the public domain. Such resource is appropriate to derive an unbiased view on the phosphosites properties in eukaryotes and on their functional relevance.

Mendeley readers

Mendeley readers

The data shown below were compiled from readership statistics for 95 Mendeley readers of this research output. Click here to see the associated Mendeley record.

Geographical breakdown

Country Count As %
Switzerland 1 1%
Brazil 1 1%
Israel 1 1%
India 1 1%
United Kingdom 1 1%
Canada 1 1%
Spain 1 1%
United States 1 1%
Unknown 87 92%

Demographic breakdown

Readers by professional status Count As %
Student > Ph. D. Student 22 23%
Researcher 17 18%
Student > Master 13 14%
Professor 6 6%
Professor > Associate Professor 6 6%
Other 15 16%
Unknown 16 17%
Readers by discipline Count As %
Agricultural and Biological Sciences 38 40%
Biochemistry, Genetics and Molecular Biology 22 23%
Chemistry 5 5%
Pharmacology, Toxicology and Pharmaceutical Science 2 2%
Computer Science 2 2%
Other 6 6%
Unknown 20 21%