Evidence map›Paper›PMID 31407201›Full record

ArticleJournal of biomolecular NMR2019

Structural characterization of the human membrane protein VDAC2 in lipid bilayers by MAS NMR.

Matthew T Eddy, Tsyr-Yan Yu, Gerhard Wagner, Robert G Griffin

Open access · greenAbstract read
In one paragraph

Article in Journal of biomolecular NMR, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.2field-weighted citation impact, top 24% 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

14 citing papers in PubMed, 19 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Structural characterization of E22G AβPhysical chemistry chemical physics : PCCP · 2024
    Article
  7. Review
  8. Diamond rotors.Journal of magnetic resonance (San Diego, Calif. : 1997) · 2023
    Article
  9. Article
  10. Article
  11. Review
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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

4 authors at 3 institutions in 2 countries.

Matthew T EddyDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, 02139, USA.
Tsyr-Yan YuDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, 02115, USA.
Gerhard WagnerDepartment of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA, 02115, USA.
Robert G GriffinDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, 02139, USA. rgg@mit.edu.ORCID http://orcid.org/0000-0003-1589-832X
Harvard University · USMassachusetts Institute of Technology · USUniversity of Florida · US

Funding

OverallP41EB002026 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$17.9M
Acquisition of a 900 MHz NMR SpectrometerP41GM066360 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2002 to 2006
$6.7M
Solid State NMR Studies of Membrane ProteinsR01EB001960 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2017
$6.5M
High Field DNP and EPR in Biological SystemsR01GM132997 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2019 to 2025
$4.6M
TR&D 4 -- Advanced Magic Angle Spinning NMR methodsP41GM132079 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2019 to 2021
$3.6M
New RF Electronics Console and Probes for 900 Mhz NMR SpectrometerS10OD023513 · OD · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2018 to 2018
$1.0M
NIBIB NIH HHS EB001960NIBIB NIH HHS EB002026NIBIB NIH HHS P41 EB002026NIBIB NIH HHS R01 EB001960NIGMS NIH HHS P41 GM066360NIGMS NIH HHS P41 GM132079NIGMS NIH HHS R01 GM132997NIH HHS S10 OD023513
6 · The paper itself

Abstract

The second isoform of the human voltage dependent anion channel (VDAC2) is a mitochondrial porin that translocates calcium and other metabolites across the outer mitochondrial membrane. VDAC2 has been implicated in cardioprotection and plays a critical role in a unique apoptotic pathway in tumor cells. Despite its medical importance, there have been few biophysical studies of VDAC2 in large part due to the difficulty of obtaining homogeneous preparations of the protein for spectroscopic characterization. Here we present high resolution magic angle spinning nuclear magnetic resonance (NMR) data obtained from homogeneous preparation of human VDAC2 in 2D crystalline lipid bilayers. The excellent resolution in the spectra permit several sequence-specific assignments of the signals for a large portion of the VDAC2 N-terminus and several other residues in two- and three-dimensional heteronuclear correlation experiments. The first 12 residues appear to be dynamic, are not visible in cross polarization experiments, and they are not sufficiently mobile on very fast timescales to be visible in

Indexed as

Lipid BilayersHumansMolecular Dynamics SimulationNuclear Magnetic Resonance, BiomolecularProtein ConformationVoltage-Dependent Anion Channel 1Voltage-Dependent Anion Channel 2Lipid BilayersVDAC1 protein, humanVDAC2 protein, humanVoltage-Dependent Anion Channel 1Voltage-Dependent Anion Channel 22D lipid crystalsMagic angle spinning NMRMembrane proteinVoltage dependent anion channel

Identifiers

PMID31407201
PMCPMC6819253
OpenAlexW2967785000

What OpenQuestion holds

Textmetadata
LicenceTDM
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.