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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Proteins Structure F...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
Proteins Structure Function and Bioinformatics
Article . 2009 . Peer-reviewed
License: Wiley Online Library User Agreement
Data sources: Crossref
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Comparative modeling of human NSF reveals a possible binding mode of GABARAP and GATE‐16

Authors: Yvonne, Thielmann; Oliver H, Weiergräber; Peixiang, Ma; Melanie, Schwarten; Jeannine, Mohrlüder; Dieter, Willbold;

Comparative modeling of human NSF reveals a possible binding mode of GABARAP and GATE‐16

Abstract

AbstractVesicular trafficking is an important homeostatic process in eukaryotic cells which critically relies on membrane fusion. One of the essential components of the universal membrane fusion machinery is NSF (N‐ethylmaleimide‐sensitive factor), a large hexameric ATPase involved in disassembly of SNARE (soluble NSF attachment protein receptor) complexes. To improve our understanding of this sophisticated molecular machine, we have modeled the structure of the NSF hexamer in two alternative assemblies. Our data suggest a mechanistic concept of the operating mode of NSF which helps to explain the functional impact of post‐translational modifications and mutations reported previously. Furthermore, we propose a binding site for the ubiquitin‐like proteins GABARAP and GATE‐16, which is supported by experimental evidence, yielding a complex with favorable surface complementarity. Proteins 2009. © 2009 Wiley‐Liss, Inc.

Keywords

Models, Molecular, Binding Sites, Protein Conformation, Ubiquitin, Hydrolysis, Microfilament Proteins, Autophagy-Related Protein 8 Family, Protein Structure, Tertiary, Adenosine Triphosphate, Protein Interaction Mapping, Humans, Phosphorylation, Apoptosis Regulatory Proteins, Peptides, Microtubule-Associated Proteins, N-Ethylmaleimide-Sensitive Proteins, Adaptor Proteins, Signal Transducing, Protein Binding

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citations
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!
17
Average
Average
Top 10%