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BioArchitecture
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PubMed Central
Other literature type . 2012
License: CC BY NC
Data sources: PubMed Central
BioArchitecture
Article . 2012 . Peer-reviewed
Data sources: Crossref
BioArchitecture
Article . 2014
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Structural biology of the PCI-protein fold

Authors: Ellisdon, Andrew M.; Stewart, Murray;

Structural biology of the PCI-protein fold

Abstract

The PCI fold is based on a stack of α-helices topped with a winged-helix domain and is found in a range of proteins that form central parts of large complexes such as the proteasome lid, the COP9 signalosome, elongation factor eIF3, and the TREX-2 complex. Recent structural determinations have given intriguing insight into how these folds function both to facilitate the generation of larger proteinaceous assembles and also to interact functionally with nucleic acids.

Keywords

Models, Molecular, Proteasome Endopeptidase Complex, Protein Folding, Saccharomyces cerevisiae Proteins, Mini Review, Nucleic Acids, Humans, Protein Structure, Secondary, Protein C Inhibitor

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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!
35
Top 10%
Top 10%
Top 10%
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bronze