ArticleMolecular biology of the cell2024
After their membrane assembly, Sec18 (NSF) and Sec17 (SNAP) promote membrane fusion.
Article in Molecular biology of the cell, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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.
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.
Who cites it
4 citing papers in PubMed.
- A pathogenic mutation in α-SNAP impairs membrane lipid binding by concealing a critical hydrophobic loop.Communications biology · 2026Article
- Functional assembly of the Qc-SNARE with Sec18 and Sec17 on membranes.Molecular biology of the cell · 2026Article
- Sec18 ATP hydrolysis selectively releases Sec17 fromMolecular biology of the cell · 2025Article
- Membrane fusion reactions limited by defective SNARE zippering or stiff lipid fatty acyl composition have distinct requirements for Sec17, Sec18, and adenine nucleotide.bioRxiv : the preprint server for biology · 2024Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
The energy that drives membrane fusion can come from either complete SNARE zippering, from Sec17 and Sec18, or both. Sec17 and Sec18 initially form a complex which binds membranes. Sec17, Sec18, and the apolarity of a loop on the N-domain of Sec17 are required for their interdependent membrane association. To determine whether Sec18 and the Sec17 loop apolarity are still required for fusion after their membrane arrival, a hydrophobic transmembrane (TM) anchor was affixed to the N-terminus of Sec17, forming TM-Sec17. Fusion without energy from complete SNARE zippering requires Sec18 as well as either Sec17 or TM-Sec17. Even without the need for membrane targeting, the TM-Sec17 apolar loop strongly stimulates Sec17/18-driven fusion. Thus, Sec18 and the Sec17 apolar loop are first required for membrane targeting, and once bound, drive rapid fusion. Each of these variables-the absence or presence of Sec17, its N-loop apolarity, addition or omission of Sec18, and unimpeded or diminished energy from SNARE zippering-has almost no effect on the amount of
Indexed as
Identifiers
What Socratic holds
Registered trials
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 Socratic graph.