Low-resolution solution structures of Munc18:Syntaxin protein complexes indicate an open binding mode driven by the Syntaxin N-peptide-Reference-Cited by-同舟云学术

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Low-resolution solution structures of Munc18:Syntaxin protein complexes indicate an open binding mode driven by the Syntaxin N-peptide

Published:2012-06-05 Issue:25 Volume:109 Page:9816-9821
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Christie M. P.,Whitten A. E.,King G. J.,Hu S.-H.,Jarrott R. J.,Chen K.-E.,Duff A. P.,Callow P.,Collins B. M.,James D. E.,Martin J. L.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference44 articles.

1. SNAREs — engines for membrane fusion

2. Synaptic vesicle fusion

3. Crystal structure of a SNARE complex involved in synaptic exocytosis at 2.4 Å resolution

4. Energetics and dynamics of SNAREpin folding across lipid bilayers

5. SNAREpins: Minimal Machinery for Membrane Fusion

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1. The DDHD2-STXBP1 interaction mediates long-term memory via generation of saturated free fatty acids;The EMBO Journal;2024-02-05

2. Regulation of Syntaxin3B-Mediated Membrane Fusion by T14, Munc18, and Complexin;Biomolecules;2023-09-28

3. VAMP2/Munc18-1 domain 3a interaction controls the nanoscale reorganization underpinning vesicular priming;2023-09-11

4. DDHD2 interacts with STXBP1 to mediate long-term memory via the generation of myristic acid;2023-05-11

5. Interrogation and validation of the interactome of neuronal Munc18-interacting Mint proteins with AlphaFold2;2023-02-21

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