Evidence map›Paper›PMID 30317497›Full record

ReviewMethods in molecular biology (Clifton, N.J.)2019

EPR Lineshape Analysis to Investigate the SNARE Folding Intermediates.

Ryan Khounlo, Brenden J D Hawk, Yeon-Kyun Shin

Abstract readReview
In one paragraph

Review in Methods in molecular biology (Clifton, N.J.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing papers in PubMed
–field-weighted citation impact
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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

3 authors.

Ryan KhounloRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, USA.
Brenden J D HawkRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, USA.
Yeon-Kyun ShinRoy J. Carver Department of Biochemistry, Biophysics and Molecular Biology, Iowa State University, Ames, IA, USA. colishin@iastate.edu.

Funding

Regulations of SNARE-dependent membrane fusionR01GM051290 · NIGMS · UNIVERSITY OF CALIFORNIA BERKELEY · PI SHIN, YEON-KYUN · 1999 to 2019
$5.0M
NIGMS NIH HHS R01 GM051290
6 · The paper itself

Abstract

SNARE complex formation, which is believed to drive intracellular membrane fusion, transits through multiple conformational states along the membrane fusion pathway. The SNARE intermediates are biologically important because they serve as targets for fusion regulators and clostridial neurotoxins. Spin-labeling EPR has contributed significantly to the understanding of the structures and the dynamics of SNARE intermediates. In particular, the EPR lineshape analysis, which is highly sensitive to protein conformational changes such as the local coil-to-helix transition, has revealed the sequential compacting steps leading to formation of the highly stable four-helix bundle.

Indexed as

Membrane FusionProtein FoldingCysteineElectron Spin Resonance SpectroscopyMutagenesis, Site-DirectedProtein Conformation, alpha-HelicalSNARE ProteinsCysteineSNARE ProteinsEPRExocytosisMembrane fusionNanodiscsNeurotransmitter releaseSNAREsSpin labels

Identifiers

PMID30317497
PMCPMC6429964

What OpenQuestion holds

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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.