Evidence map›Paper›PMID 27911771›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2016

Stability, folding dynamics, and long-range conformational transition of the synaptic t-SNARE complex.

Xinming Zhang, Aleksander A Rebane, Lu Ma, Feng Li, Junyi Jiao, Hong Qu, Frederic Pincet, James E Rothman, Yongli Zhang

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

27 citing papers in PubMed, 41 citations in OpenAlex.

  1. Article
  2. Article
  3. SNARE Proteins in Synaptic Vesicle Fusion.Advances in neurobiology · 2023
    Article
  4. A dynamic template complex mediates Munc18-chaperoned SNARE assembly.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  5. Review
  6. Review
  7. Article
  8. Energetics, kinetics, and pathways of SNARE assembly in membrane fusion.Critical reviews in biochemistry and molecular biology · 2022
    Review
  9. Review
  10. Article
  11. Chaperoning SNARE Folding and Assembly.Annual review of biochemistry · 2021
    Review
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. SNARE zippering requires activation by SNARE-like peptides in Sec1/Munc18 proteins.Proceedings of the National Academy of Sciences of the United States of America · 2018
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

9 authors at 2 institutions in 2 countries.

Xinming ZhangDepartment of Cell Biology, Yale School of Medicine, New Haven, CT 06520.
Aleksander A RebaneDepartment of Cell Biology, Yale School of Medicine, New Haven, CT 06520.
Lu MaDepartment of Cell Biology, Yale School of Medicine, New Haven, CT 06520.
Feng LiDepartment of Cell Biology, Yale School of Medicine, New Haven, CT 06520.
Junyi JiaoDepartment of Cell Biology, Yale School of Medicine, New Haven, CT 06520.
Hong QuDepartment of Cell Biology, Yale School of Medicine, New Haven, CT 06520.
Frederic PincetDepartment of Cell Biology, Yale School of Medicine, New Haven, CT 06520.
James E RothmanDepartment of Cell Biology, Yale School of Medicine, New Haven, CT 06520.
Yongli ZhangDepartment of Cell Biology, Yale School of Medicine, New Haven, CT 06520; yongli.zhang@yale.edu.ORCID 0000-0001-5424-3022
Yale University · USCentre National de la Recherche Scientifique · FR

Funding

Yale Clinical and Translational Science Award (U Component)UL1TR001863 · NCATS · YALE UNIVERSITY · PI John H. Krystal, LUCILA OHNO-MACHADO · 2016 to 2026
$102.9M
Skill Development for Diverse Scientific Careers: A New Course Predoctoral Program in Cellular and Molecular BiologyT32GM007223 · NIGMS · YALE UNIVERSITY · PI BASERGA, SUSAN J · 1985 to 2019
$31.0M
REGULATION OF EXOCYTOSIS STUDIES WITH FLIPPED SNARESR01GM071458 · NIGMS · YALE UNIVERSITY · PI ROTHMAN, JAMES · 2004 to 2015
$8.5M
Regulation of Membrane Fusion in ExocytosisR01DK027044 · NIDDK · YALE UNIVERSITY · PI KRISHNAKUMAR, SHYAM S · 1986 to 2021
$8.2M
Single-molecule manipulation of SNAREsR01GM093341 · NIGMS · YALE UNIVERSITY · PI ZHANG, YONGLI · 2010 to 2018
$3.1M
NCATS NIH HHS UL1 TR001863NIDDK NIH HHS R01 DK027044NIGMS NIH HHS R01 GM071458NIGMS NIH HHS R01 GM093341NIGMS NIH HHS T32 GM007223
6 · The paper itself

Abstract

Synaptic soluble N-ethylmaleimide-sensitive factor attachment protein receptors (SNAREs) couple their stepwise folding to fusion of synaptic vesicles with plasma membranes. In this process, three SNAREs assemble into a stable four-helix bundle. Arguably, the first and rate-limiting step of SNARE assembly is the formation of an activated binary target (t)-SNARE complex on the target plasma membrane, which then zippers with the vesicle (v)-SNARE on the vesicle to drive membrane fusion. However, the t-SNARE complex readily misfolds, and its structure, stability, and dynamics are elusive. Using single-molecule force spectroscopy, we modeled the synaptic t-SNARE complex as a parallel three-helix bundle with a small frayed C terminus. The helical bundle sequentially folded in an N-terminal domain (NTD) and a C-terminal domain (CTD) separated by a central ionic layer, with total unfolding energy of ∼17 k

Indexed as

Amino Acid SequenceAnimalsMembrane FusionMiceMicroscopy, Atomic ForceMolecular Dynamics SimulationMunc18 ProteinsOptical TweezersProtein ConformationProtein DomainsProtein FoldingProtein StabilityQa-SNARE ProteinsSNARE ProteinsSynaptic TransmissionSynaptosomal-Associated Protein 25Munc18 ProteinsQa-SNARE ProteinsSnap25 protein, mouseSNARE ProteinsSynaptosomal-Associated Protein 25Vesicle-Associated Membrane Protein 2vesicle-associated membrane protein 2, mousemembrane fusionoptical tweezersSNARE assemblySNARE four-helix bundlet-SNARE complex

Identifiers

PMID27911771
PMCPMC5167175
OpenAlexW2557708678

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.