Evidence map›Paper›PMID 10653801›Full record

ArticleBiophysical journal2000

Membrane fusion mediated by coiled coils: a hypothesis.

J Bentz

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
6.5field-weighted citation impact, top 3% 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

44 citing papers in PubMed, 114 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Order and disorder control the functional rearrangement of influenza hemagglutinin.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  6. Structural characterization of a fusion glycoprotein from a retrovirus that undergoes a hybrid 2-step entry mechanism.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2013
    Article
  7. Cell entry of enveloped viruses.Current opinion in virology · 2011
    Review
  8. Article
  9. Article
  10. Addition of a cholesterol group to an HIV-1 peptide fusion inhibitor dramatically increases its antiviral potency.Proceedings of the National Academy of Sciences of the United States of America · 2009
    Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Crystallization and preliminary X-ray diffraction analysis of central structure domains from mumps virus F protein.Acta crystallographica. Section F, Structural biology and crystallization communications · 2005
    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

1 author at 1 institution in 1 country.

J BentzDepartment of Bioscience and Biotechnology, Drexel University, Philadelphia, Pennsylvania 19104-2875, USA. bentzj@drexel.edu
Drexel University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

A molecular model of the low-pH-induced membrane fusion by influenza hemagglutinin (HA) is proposed based upon the hypothesis that the conformational change to the extended coiled coil creates a high-energy hydrophobic membrane defect in the viral envelope or HA expressing cell. It is known that 1) an aggregate of at least eight HAs is required at the fusion site, yet only two or three of these HAs need to undergo the "essential" conformational change for the first fusion pore to form (Bentz, J. 2000. Biophys. J. 78:000-000); 2) the formation of the first fusion pore signifies a stage of restricted lipid flow into the nascent fusion site; and 3) some HAs can partially insert their fusion peptides into their own viral envelopes at low pH. This suggests that the committed step for HA-mediated fusion begins with a tightly packed aggregate of HAs whose fusion peptides are inserted into their own viral envelope, which causes restricted lateral lipid flow within the HA aggregate. The transition of two or three HAs in the center of the aggregate to the extended coiled coil extracts the fusion peptide and creates a hydrophobic defect in the outer monolayer of the virion, which is stabilized by the closely packed HAs. These HAs are inhibited from diffusing away from the site to admit lateral lipid flow, in part because that would initially increase the surface area of hydrophobic exposure. The other obvious pathway to heal this hydrophobic defect, or some descendent, is recruitment of lipids from the outer monolayer of the apposed target membrane, i.e., fusion. Other viral fusion proteins and the SNARE fusion protein complex appear to fit within this hypothesis.

Indexed as

Membrane FusionVesicular Transport ProteinsHemagglutinins, ViralHydrogen-Ion ConcentrationMembrane LipidsMembrane ProteinsModels, MolecularOrthomyxoviridaeProtein ConformationProtein Structure, SecondarySNARE ProteinsViral Fusion ProteinsHemagglutinins, ViralMembrane LipidsMembrane ProteinsSNARE ProteinsVesicular Transport ProteinsViral Fusion Proteins

Identifiers

PMID10653801
PMCPMC1300691
OpenAlexW2035543619

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.