Evidence map›Paper›PMID 14695269›Full record

ArticleBiophysical journal2004

Oligomerization of fusogenic peptides promotes membrane fusion by enhancing membrane destabilization.

Wai Leung Lau, David S Ege, James D Lear, Daniel A Hammer, William F DeGrado

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
1.4field-weighted citation impact, top 20% 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

32 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. Article
  6. Review
  7. Membranotropic peptides mediating viral entry.Peptide science (Hoboken, N.J.) · 2018
    Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. The three lives of viral fusion peptides.Chemistry and physics of lipids · 2014
    Review
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. 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

5 authors at 1 institution in 1 country.

Wai Leung LauDepartment of Biochemistry and Molecular Biophysics, School of Medicine, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.
David S Ege
James D Lear
Daniel A Hammer
William F DeGrado
Philadelphia University · US

Funding

De novo design of alpha-helical bundlesR37GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 2004 to 2013
$3.6M
DE NOVO DESIGN OF ALPHA HELICAL BUNDLESR01GM054616 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI DEGRADO, WILLIAM · 1996 to 2016
$2.4M
NIGMS NIH HHS GM-54616NIGMS NIH HHS R01 GM054616NIGMS NIH HHS R37 GM054616
6 · The paper itself

Abstract

A key element of membrane fusion reactions in biology is the involvement of specific fusion proteins. In many viruses, the proteins that mediate membrane fusion usually exist as homotrimers. Furthermore, they contain extended triple-helical coiled-coil domains and fusogenic peptides. It has been suggested that the coiled-coil domains present the fusogenic peptide in a conformation or geometry favorable for membrane fusion. To test the hypothesis that trimerization of fusogenic peptide is related to optimal fusion, we have designed and synthesized a triple-stranded coiled-coil X31 peptide, also known as the ccX31, which mimics the influenza virus hemagglutinin fusion peptide in the fusion-active state. We compared the membrane interactive properties of ccX31 versus the monomeric X31 fusogenic peptide. Our data show that trimerization enhances peptide-induced leakage of liposomal contents and lipid mixing. Furthermore, studies using micropipette aspiration of single vesicles reveal that ccX31 decreases lysis tension, tau(lysis), but not area expansion modulus, Ka, of phospholipid bilayers, whereas monomeric X31 peptide lowers both tau(lysis) and Ka. Our results are consistent with the hypothesis that oligomerization of fusogenic peptide promotes membrane fusion, possibly by enhancing localized destabilization of lipid bilayers.

Indexed as

Membrane FluidityMembrane FusionDimerizationHemagglutinin Glycoproteins, Influenza VirusLiposomesMacromolecular SubstancesMembrane LipidsMembranes, ArtificialMolecular ConformationPermeabilityPhospholipidsProtein BindingProtein Structure, TertiaryViral Fusion ProteinsHemagglutinin Glycoproteins, Influenza VirusLiposomesMacromolecular SubstancesMembrane LipidsMembranes, ArtificialPhospholipidsViral Fusion Proteins

Identifiers

PMID14695269
PMCPMC1303790
OpenAlexW2153540006

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.