Evidence map›Paper›PMID 11038187›Full record

ArticleThe Journal of cell biology2000

Evidence that the transition of HIV-1 gp41 into a six-helix bundle, not the bundle configuration, induces membrane fusion.

G B Melikyan, R M Markosyan, H Hemmati, M K Delmedico, D M Lambert, F S Cohen

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 334 papers.

0numbers the graph read from it
0cells of the map it votes in
334citing papers in PubMed
9.1field-weighted citation impact, top 1% 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

334 citing papers in PubMed, 583 citations in OpenAlex.

  1. Trial
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  3. FromImmune network · 2026
    Review
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  9. Macropinosomes are a site of HIV-1 entry into primary CD4Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
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274 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

G B MelikyanDepartment of Molecular Biophysics and Physiology, Rush Medical College, Chicago, Illinois 60612, USA.
R M Markosyan
H Hemmati
M K Delmedico
D M Lambert
F S Cohen
Rush University Medical Center · US

Funding

BIOPHYSICS OF PROTEIN-MEDIATED MEMBRANE FUSIONR01GM054787 · NIGMS · UNIVERSITY OF MD BIOTECHNOLOGY INSTITUTE · PI MELIKIAN, GREGORY B · 2000 to 2018
$6.5M
MODEL SYSTEM FOR PHYSIOLOGICAL EXOCYTOSISR01GM027367 · NIGMS · RUSH UNIVERSITY MEDICAL CENTER · PI COHEN, FREDRIC S · 1985 to 2009
$4.2M
BIOPHYSICS OF PROTEIN MEDIATED MEMBRANE FUSIONR29GM054787 · NIGMS · RUSH UNIVERSITY MEDICAL CENTER · PI MELIKIAN, GREGORY B · 1996 to 1999
–
NIGMS NIH HHS GM27367NIGMS NIH HHS GM54787NIGMS NIH HHS R01 GM027367NIGMS NIH HHS R01 GM054787NIGMS NIH HHS R29 GM054787
6 · The paper itself

Abstract

Many viral fusion proteins exhibit a six-helix bundle as a core structure. HIV Env-induced fusion was studied to resolve whether membrane merger was due to the transition into the bundle configuration or occurred after bundle formation. Suboptimal temperature was used to arrest fusion at an intermediate stage. When bundle formation was prevented by adding inhibitory peptides at this stage, membranes did not merge upon raising temperature. Inversely, when membrane merger was prevented by incorporating lysophosphatidylcholine (LPC) into cell membranes at the intermediate, the bundle did not form upon optimizing temperature. In the absence of LPC, the six-helix bundle did not form when the temperature of the intermediate was raised for times too short to promote fusion. Kinetic measures showed that after the temperature pulse, cells had not advanced further toward fusion. The latter results indicate that bundle formation is the rate-limiting step between the arrested intermediate and fusion. Electrical measures showed that the HIV Env-induced pore is initially large and grows rapidly. It is proposed that bundle formation and fusion are each contingent on the other and that movement of Env during its transition into the six-helix bundle directly induces the lipid rearrangements of membrane fusion. Because peptide inhibition showed that, at the intermediate stage, the heptad repeats of gp41 have become stably exposed, creation of the intermediate could be of importance in drug and/or vaccine development.

Indexed as

HIV-1Membrane FusionCD4-Positive T-LymphocytesHIV Envelope Protein gp41LysophosphatidylcholinesModels, BiologicalMotionProtein ConformationReceptors, CXCR4TemperatureThermodynamicsHIV Envelope Protein gp41LysophosphatidylcholinesReceptors, CXCR4

Identifiers

PMID11038187
PMCPMC2192659
OpenAlexW2168357995

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.