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Cited by 206

The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.

Three SNARE complexes cooperate to mediate membrane fusion

Open access
Hua, Yuanyuan, Scheller, Richard H.·2001·Proceedings of the National Academy of Sciences

Abstract

Soluble N- ethylmaleimide-sensitive factor attachment protein receptor (SNARE) proteins of the syntaxin, SNAP-25, and VAMP families mediate intracellular membrane fusion through the formation of helical bundles that span opposing membranes. Soluble SNARE domains that lack their integral membrane anchors inhibit membrane fusion by forming nonfunctional complexes with endogenous SNARE proteins. In this study we investigate the dependence of membrane fusion on the concentration of a soluble SNARE coil domain derived from VAMP2. The increase in the inhibition of fusion observed with increasing concentration of inhibitor is best fit to a function that suggests three SNARE complexes cooperate to mediate fusion of a single vesicle. These three complexes likely contribute part of a protein and lipidic fusion pore.

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Crossref · 10.1073/pnas.131214798

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Metadata

Authors
Hua, Y., & Scheller, R. H.
Venue
Proceedings of the National Academy of Sciences
Published
2001-06-26
Volume
98
Issue
14
Pages
8065-8070
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1975642381
Cited by
206
References
1
FWCI
3.77
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Three SNARE complexes cooperate to mediate membrane fusion. https://app.cochat.ai/papers/10.1073/pnas.131214798
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Hua, Y., & Scheller, R. H. (2001). Three SNARE complexes cooperate to mediate membrane fusion. Proceedings of the National Academy of Sciences. https://doi.org/10.1073/pnas.131214798

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