Evidence map›Paper›PMID 19616505›Full record

ArticleBiochimica et biophysica acta2010

Nuclear magnetic resonance evidence for retention of a lamellar membrane phase with curvature in the presence of large quantities of the HIV fusion peptide.

Charles M Gabrys, Rong Yang, Christopher M Wasniewski, Jun Yang, Christian G Canlas, Wei Qiang, Yan Sun, David P Weliky

Open access · greenAbstract read
In one paragraph

Article in Biochimica et biophysica acta, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
0.9field-weighted citation impact, top 26% 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

16 citing papers in PubMed, 22 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. RapidBiochemistry · 2021
    Article
  6. Biochimica et biophysica acta. Biomembranes · 2020
    Article
  7. Article
  8. Article
  9. Magic angle spinning NMR of viruses.Progress in nuclear magnetic resonance spectroscopy · 2015
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. 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

8 authors at 1 institution in 1 country.

Charles M GabrysDepartment of Chemistry, Michigan State University, East Lansing, MI 48824, USA.
Rong Yang
Christopher M Wasniewski
Jun Yang
Christian G Canlas
Wei Qiang
Yan Sun
David P Weliky
Michigan State University · US

Funding

Solid State NMR Studies of the HIV-1 Fusion PeptideR01AI047153 · NIAID · MICHIGAN STATE UNIVERSITY · PI WELIKY, DAVID P · 2001 to 2021
$5.6M
Solid-State NMR of Viral Fusion Peptides and ProteinsR56AI047153 · NIAID · MICHIGAN STATE UNIVERSITY · PI David P Weliky · 2017 to 2026
$661k
SOLID STATE NMR STUDIES OF THE HIV-1 FUSION PEPTIDER21AI047153 · NIAID · MICHIGAN STATE UNIVERSITY · PI WELIKY, DAVID PAUL · 2000 to 2000
$226k
NIAID NIH HHS AI47153NIAID NIH HHS R01 AI047153NIAID NIH HHS R21 AI047153NIAID NIH HHS R56 AI047153
6 · The paper itself

Abstract

The HIV fusion peptide (HFP) is a biologically relevant model system to understand virus/host cell fusion. (2)H and (31)P NMR spectroscopies were applied to probe the structure and motion of membranes with bound HFP and with a lipid headgroup and cholesterol composition comparable to that of membranes of host cells of HIV. The lamellar phase was retained for a variety of highly fusogenic HFP constructs as well as a non-fusogenic HFP construct and for the influenza virus fusion peptide. The lamellar phase is therefore a reasonable structure for modeling the location of HFP in lipid/cholesterol dispersions. Relative to no HFP, membrane dispersions with HFP had faster (31)P transverse relaxation and faster transverse relaxation of acyl chain (2)H nuclei closest to the lipid headgroups. Relative to no HFP, mechanically aligned membrane samples with HFP had broader (31)P signals with a larger fraction of unoriented membrane. The relaxation and aligned sample data are consistent with bilayer curvature induced by the HFP which may be related to its fusion catalytic function. In some contrast to the subtle effects of HFP on a host-cell-like membrane composition, an isotropic phase was observed in dispersions rich in phosphatidylethanolamine lipids and with bound HFP.

Indexed as

CholesterolHIVHIV Envelope Protein gp41Lipid BilayersNuclear Magnetic Resonance, BiomolecularPeptidesPhosphatidylethanolaminesCholesterolHIV Envelope Protein gp41Lipid BilayersPeptidesphosphatidylethanolaminePhosphatidylethanolamines

Identifiers

PMID19616505
PMCPMC2812645
OpenAlexW2017813255

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.