Evidence map›Paper›PMID 19093835›Full record

ArticleBiochemistry2009

HIV fusion peptide and its cross-linked oligomers: efficient syntheses, significance of the trimer in fusion activity, correlation of beta strand conformation with membrane cholesterol, and proximity to lipid headgroups.

Wei Qiang, David P Weliky

Open access · greenAbstract read
In one paragraph

Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.

0numbers the graph read from it
0cells of the map it votes in
36citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

36 citing papers in PubMed, 54 citations in OpenAlex.

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

2 authors at 1 institution in 1 country.

Wei QiangDepartment of Chemistry, Michigan State University, East Lansing, Michigan 48824, USA.
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

For enveloped viruses such as HIV, an approximately 20-residue N-terminal fusion peptide domain in the envelope protein binds to target cell membranes and plays a key role in fusion between the viral and cellular membranes during infection. The chemically synthesized HIV fusion peptide (HFP) catalyzes fusion between membrane vesicles and is a useful model system for understanding some aspects of HIV fusion. Previous studies have shown a common trimeric state for the envelope protein from several different viruses, including HIV, and in this study, practical high-yield syntheses are reported for HFP monomer (HFPmn) and chemically cross-linked HFP dimer (HFPdm), trimer (HFPtr), and tetramer (HFPte). The vesicle fusion rates per strand were ordered as follows: HFPmn < HFPdm < HFPtr approximately HFPte. This suggested that HFPtr is the smallest catalytically efficient oligomer. Solid-state NMR measurements of (13)CO chemical shifts were carried out in constructs labeled at either Ala-6 or Ala-15. For all constructs associated with cholesterol-containing membranes, the chemical shifts of both residues correlated with beta strand conformation while association with membranes without cholesterol resulted in a mixture of helical and beta strand conformations. The dependence of fusion rate on oligomer size is independent of membrane cholesterol content, so one interpretation of the data is fusion activity of both helical and beta strand conformations. Membrane location may be a determinant of fusion activity, and for all constructs in both conformations, a large fraction of the Ala-15 (13)CO groups were 5-6 A from the (31)P atoms in the lipid headgroups, while the Ala-6 (13)CO groups were more distant.

Indexed as

Amino Acid SequenceCell MembraneCholesterolComputer SimulationCross-Linking ReagentsHIVHIV Envelope Protein gp41KineticsLipidsMolecular Sequence DataNuclear Magnetic Resonance, BiomolecularPeptidesProtein BindingProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryCholesterolCross-Linking ReagentsHIV Envelope Protein gp41LipidsPeptides

Identifiers

PMID19093835
PMCPMC2680607
OpenAlexW2117778515

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.