Evidence map›Paper›PMID 27591900›Full record

ArticleBiochemical and biophysical research communications2016

A mechanism for propagated SOD1 misfolding from frustration analysis of a G85R mutant protein assembly.

Eamonn F Healy

Abstract read
In one paragraph

Article in Biochemical and biophysical research communications, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. 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

1 author.

Eamonn F HealyDepartment of Chemistry, St. Edward's University, Austin, TX 78704, USA. Electronic address: healy@stedwards.edu.

Funding

IRACDA Postdoctoral Program: Collaborative Opportunities for Research EducatorsK12GM102745 · NIGMS · UNIVERSITY OF TEXAS AT AUSTIN · PI BRODBELT, JENNIFER S. · 2013 to 2017
$2.2M
NIGMS NIH HHS K12 GM102745
6 · The paper itself

Abstract

Application of landscape theory and the dehydron hypothesis to a crystal structure of a G85R mutant superoxide dismutase (SOD1) tetrameric complex allows for the description of a prion-like hypothesis that serves to explain propagated SOD1 misfolding. We have developed two conformational-change scenarios, one local to the ESL at the complex interface, and a second displacement at the ESL of the otherdimeric subunit. When taken together these provide for a prion-like mechanism that can serve to explain the observed conversion of wtSOD1 to a misfolded form by the G85R mutant.

Indexed as

Mutation, MissenseProtein FoldingAmyotrophic Lateral SclerosisCrystallography, X-RayHumansHydrogen BondingMolecular Dynamics SimulationMutant ProteinsPrionsProtein ConformationProtein MultimerizationProtein SubunitsStatic ElectricitySuperoxide Dismutase-1Mutant ProteinsPrionsProtein SubunitsSOD1 protein, humanSuperoxide Dismutase-1Amyotrophic lateral sclerosisDehydronsElectrostatic loopFrustration contactsG85R SOD1 mutantSuperoxide dismutase

Identifiers

PMID27591900
PMCPMC5030186

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.