Evidence map›Paper›PMID 22435461›Full record

ArticleJournal of the American Chemical Society2012

Lipid dynamics and protein-lipid interactions in 2D crystals formed with the β-barrel integral membrane protein VDAC1.

Matthew T Eddy, Ta-Chung Ong, Lindsay Clark, Oscar Teijido, Patrick C A van der Wel, Robert Garces, Gerhard Wagner, Tatiana K Rostovtseva, Robert G Griffin

Abstract read
In one paragraph

Article in Journal of the American Chemical Society, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing 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

49 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Specific Lipid Studies in Complex Membranes by Solid-State NMR Spectroscopy.Chemistry (Weinheim an der Bergstrasse, Germany) · 2022
    Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Review
  17. Article
  18. Alpha protons as NMR probes in deuterated proteins.Journal of biomolecular NMR · 2019
    Article
  19. Article
  20. 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

9 authors.

Matthew T EddyDepartment of Chemistry, Massachusetts Institute of Technology, Cambridge, Massachusetts 02139, USA.
Ta-Chung Ong
Lindsay Clark
Oscar Teijido
Patrick C A van der Wel
Robert Garces
Gerhard Wagner
Tatiana K Rostovtseva
Robert G Griffin

Funding

Systems Biology of Cell Decision ProcessesP50GM068762 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI SORGER, PETER KARL · 2003 to 2012
$32.3M
OverallP41EB002026 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2018
$17.9M
Solid State NMR Studies of Membrane ProteinsR01EB001960 · NIBIB · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GRIFFIN, ROBERT GUY · 2003 to 2017
$6.5M
Structure and interactions of the Voltage-Dependent Anion Channel(VDAC)R01GM075879 · NIGMS · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI WAGNER, GERHARD · 2005 to 2013
$2.3M
Intramural NIH HHS Z99 HD999999NIBIB NIH HHS EB001960NIBIB NIH HHS EB002026NIBIB NIH HHS P41 EB002026NIBIB NIH HHS R01 EB001960NIGMS NIH HHS GM075879NIGMS NIH HHS GM68762NIGMS NIH HHS P50 GM068762NIGMS NIH HHS R01 GM075879
6 · The paper itself

Abstract

We employ a combination of (13)C/(15)N magic angle spinning (MAS) NMR and (2)H NMR to study the structural and functional consequences of different membrane environments on VDAC1 and, conversely, the effect of VDAC1 on the structure of the lipid bilayer. MAS spectra reveal a well-structured VDAC1 in 2D crystals of dimyristoylphosphatidylcholine (DMPC) and diphytanoylphosphatidylcholine (DPhPC), and their temperature dependence suggests that the VDAC structure does not change conformation above and below the lipid phase transition temperature. The same data show that the N-terminus remains structured at both low and high temperatures. Importantly, functional studies based on electrophysiological measurements on these same samples show fully functional channels, even without the presence of Triton X-100 that has been found necessary for in vitro-refolded channels. (2)H solid-state NMR and differential scanning calorimetry were used to investigate the dynamics and phase behavior of the lipids within the VDAC1 2D crystals. (2)H NMR spectra indicate that the presence of protein in DMPC results in a broad lipid phase transition that is shifted from 19 to ~27 °C and show the existence of different lipid populations, consistent with the presence of both annular and bulk lipids in the functionally and structurally homogeneous samples.

Indexed as

Calorimetry, Differential ScanningCrystallizationDimyristoylphosphatidylcholineElectrophysiologyHumansLipid BilayersLipidsMagnetic Resonance SpectroscopyMembrane ProteinsOctoxynolPhosphatidylcholinesProtein DenaturationProtein FoldingProtein Structure, SecondaryVoltage-Dependent Anion Channel 11,2-diphytanoylphosphatidylcholineDimyristoylphosphatidylcholineLipid BilayersLipidsMembrane ProteinsOctoxynolPhosphatidylcholinesVDAC1 protein, humanVoltage-Dependent Anion Channel 1

Identifiers

PMID22435461
PMCPMC3333839

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Registered trials

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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.