Evidence map›Paper›PMID 30777305›Full record

ArticleBiophysical journal2019

A Cholesterol Analog Induces an Oligomeric Reorganization of VDAC.

Fraser G Ferens, Trushar R Patel, George Oriss, Deborah A Court, Jörg Stetefeld

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.

0numbers the graph read from it
0cells of the map it votes in
8citing papers in PubMed
0.4field-weighted citation impact, top 39% 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

8 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. A C-Terminally Truncated Variant ofFrontiers in physiology · 2021
    Article
  7. Human DDX17 Unwinds Rift Valley Fever Virus Non-Coding RNAs.International journal of molecular sciences · 2020
    Article
  8. 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

5 authors at 2 institutions in 1 country.

Fraser G FerensDepartments of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada; Microbiology, University of Manitoba, Winnipeg, Manitoba, Canada.
Trushar R PatelAlberta RNA Research and Training Institute, Department of Chemistry and Biochemistry, University of Lethbridge, Lethbridge, Alberta, Canada; Li Ka Shing Institute of Virology and Discovery Lab, University of Alberta, Edmonton, Alberta, Canada; Department of Microbiology, Immunology & Infectious Diseases, Cumming School of Medicine, University of Calgary, Calgary, Alberta, Canada.
George OrissDepartments of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada.
Deborah A CourtMicrobiology, University of Manitoba, Winnipeg, Manitoba, Canada.
Jörg StetefeldDepartments of Chemistry, University of Manitoba, Winnipeg, Manitoba, Canada; Biochemistry and Medical Genetics, University of Manitoba, Winnipeg, Manitoba, Canada. Electronic address: jorg.stetefeld@umanitoba.ca.
University of Manitoba · CAUniversity of Lethbridge · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The oligomeric organization of the voltage-dependent anion-selective channel (VDAC) and its interactions with hexokinase play integral roles in mitochondrially mediated apoptotic signaling. Various small to large assemblies of VDAC are observed in mitochondrial outer membranes, but they do not predominate in detergent-solubilized VDAC samples. In this study, a cholesterol analog, cholesteryl-hemisuccinate (CHS), was shown to induce the formation of detergent-soluble VDAC multimers. The various oligomeric states of VDAC induced by the addition of CHS were deciphered through an integrated biophysics approach using microscale thermophoresis, analytical ultracentrifugation, and size-exclusion chromatography small angle x-ray scattering. Furthermore, CHS stabilizes the interaction between VDAC and hexokinase (K

Indexed as

Cholesterol EstersFungal ProteinsHexokinaseNeurospora crassaProtein MultimerizationProtein Structure, QuaternaryProtein Structure, SecondaryVoltage-Dependent Anion ChannelsCholesterol Esterscholesteryl succinateFungal ProteinsHexokinaseVoltage-Dependent Anion Channels

Identifiers

PMID30777305
PMCPMC6400861
OpenAlexW2913467948

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.