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Phosphorylation at the Interface

descriptionPublicationkeyboard_double_arrow_right Article 01 Dec 2011 English Publisher:Elsevier BVJournal:Structure, volume 19, pages 1,726-1,727 (issn: 0969-2126, Copyright policy )
Authors: Davis, Fred P.;

doi: 10.1016/j.str.2011.11.006

pmid: 22153492

Phosphorylation at the Interface

Abstract

Proteomic studies have identified thousands of eukaryotic phosphorylation sites (phosphosites), but few are functionally characterized. Nishi et al., in this issue of Structure, characterize phosphosites at protein-protein interfaces and estimate the effect of their phosphorylation on interaction affinity, by combining proteomics data with protein structures.

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Keywords

Structural Biology, Molecular Biology

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    popularity
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    influence
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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
7
Average
Average
Average
hybrid