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Peptidyl-prolyl cis-trans isomerases: structure and functions.

descriptionPublicationkeyboard_double_arrow_right Article 30 Aug 1999 English Journal:Biochemistry. Biokhimiia, volume 64 (issn: 0006-2979, Copyright policy )
Authors: B K, Pliyev; B Y, Gurvits;

pmid: 10424896

Peptidyl-prolyl cis-trans isomerases: structure and functions.

Abstract

Peptidyl-prolyl cis-trans isomerases (PPI) catalyze cis-trans isomerization of imide bonds in peptides and proteins. This review summarizes the literature on the structure and functions of PPIs, their involvement in protein folding, and organization of PPI-containing receptors and membrane channels. A possible role of several PPIs in distant interactions between cells is discussed.

Related Organizations
Keywords

Models, Molecular, Protein Folding, Protein Conformation, Membrane Proteins, Amino Acid Sequence, Peptidylprolyl Isomerase

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    		 15
    popularity
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    influence
    This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
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    impulse
    This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
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Powered by OpenAIRE graph
Found an issue? Give us feedback
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!
15
Average
Average
Average
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