Evidence map›Paper›PMID 10831610›Full record

ArticleThe Journal of cell biology2000

SNAREpins are functionally resistant to disruption by NSF and alphaSNAP.

T Weber, F Parlati, J A McNew, R J Johnston, B Westermann, T H Söllner, J E Rothman

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

53 citing papers in PubMed, 113 citations in OpenAlex.

  1. Article
  2. Article
  3. GLUT4 On the move.The Biochemical journal · 2022
    Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Proteomics Analysis ofInternational journal of molecular sciences · 2019
    Article
  11. Article
  12. Article
  13. Mechanism of neurotransmitter release coming into focus.Protein science : a publication of the Protein Society · 2018
    Review
  14. Arrest ofThe Journal of biological chemistry · 2018
    Article
  15. SolubleFrontiers in immunology · 2018
    Article
  16. Article
  17. Article
  18. Chaperoning SNARE assembly and disassembly.Nature reviews. Molecular cell biology · 2016
    Review
  19. Article
  20. 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

7 authors at 1 institution in 1 country.

T WeberCellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10021, USA.
F Parlati
J A McNew
R J Johnston
B Westermann
T H Söllner
J E Rothman
Memorial Sloan Kettering Cancer Center · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

SNARE (SNAP [soluble NSF (N-ethylmaleimide-sensitive fusion protein) attachment protein] receptor) proteins are required for many fusion processes, and recent studies of isolated SNARE proteins reveal that they are inherently capable of fusing lipid bilayers. Cis-SNARE complexes (formed when vesicle SNAREs [v-SNAREs] and target membrane SNAREs [t-SNAREs] combine in the same membrane) are disrupted by the action of the abundant cytoplasmic ATPase NSF, which is necessary to maintain a supply of uncombined v- and t-SNAREs for fusion in cells. Fusion is mediated by these same SNARE proteins, forming trans-SNARE complexes between membranes. This raises an important question: why doesn't NSF disrupt these SNARE complexes as well, preventing fusion from occurring at all? Here, we report several lines of evidence that demonstrate that SNAREpins (trans-SNARE complexes) are in fact functionally resistant to NSF, and they become so at the moment they form and commit to fusion. This elegant design allows fusion to proceed locally in the face of an overall environment that massively favors SNARE disruption.

Indexed as

Vesicular Transport ProteinsAdenosine TriphosphateAnimalsCarrier ProteinsCells, CulturedGene ExpressionIntracellular MembranesLipid BilayersLiposomesMembrane FusionMembrane ProteinsMiceMutagenesisN-Ethylmaleimide-Sensitive ProteinsProtein Structure, TertiaryQa-SNARE ProteinsAdenosine TriphosphateCarrier ProteinsLipid BilayersLiposomesMembrane ProteinsN-Ethylmaleimide-Sensitive ProteinsNsf protein, mouseNsf protein, ratQa-SNARE ProteinsR-SNARE ProteinsSNARE ProteinsSoluble N-Ethylmaleimide-Sensitive Factor Attachment ProteinsVesicular Transport Proteins

Identifiers

PMID10831610
PMCPMC2174819
OpenAlexW2136687453

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.