Evidence map›Paper›PMID 14722295›Full record

ArticleJournal of virology2004

The mature avian leukosis virus subgroup A envelope glycoprotein is metastable, and refolding induced by the synergistic effects of receptor binding and low pH is coupled to infection.

Jason G Smith, Walther Mothes, Stephen C Blacklow, James M Cunningham

Open access · greenAbstract read
In one paragraph

Article in Journal of virology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

43 citing papers in PubMed, 59 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. The metastable states of proteins.Protein science : a publication of the Protein Society · 2020
    Review
  5. Article
  6. Review
  7. Article
  8. Retroviral host range extension is coupled with Env-activating mutations resulting in receptor-independent entry.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. 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
  14. Article
  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

4 authors at 1 institution in 1 country.

Jason G SmithDepartment of Medicine. Department of Pathology, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts 02115, USA.
Walther Mothes
Stephen C Blacklow
James M Cunningham
Brigham and Women's Hospital · US

Funding

TRAINING PROGRAM IN MOLECULAR HEMATOLOGYT32HL007623 · NHLBI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI HANDIN, ROBERT I · 1985 to 2010
$7.0M
PHD PROGRAM IN IMMUNOBIOLOGYT32AI007498 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI CARROLL, MICHAEL CRAIG · 1995 to 2011
$2.0M
NHLBI NIH HHS T32 HL007623NHLBI NIH HHS T32-HL07623NIAID NIH HHS T32 AI007498NIAID NIH HHS T32-AI07498
6 · The paper itself

Abstract

The spring-loaded model stipulates that influenza virus infection is coupled to the transition of the virus hemagglutinin (HA) from a metastable conformation to a highly stable conformation at low pH. The properties of retrovirus envelope glycoproteins indicate that infection is coupled to an analogous conformational change. As a test of this hypothesis, the requirements for avian leukosis virus A (ALV-A) infection were examined. These studies indicate that, like HA, the conformation of the mature ALV-A envelope glycoprotein is metastable and that infection is linked to refolding at low pH. However, unlike HA, low-pH activation is only observed after priming by receptor. Therefore, ALV-A infection is dependent on the synergistic effects of receptor binding and low pH, suggesting that receptor binding superimposes an additional constraint on activation of ALV-A fusion that proceeds by a mechanism comparable to that of influenza virus.

Indexed as

Protein FoldingAnimalsAvian Leukosis VirusAvian ProteinsCell LineCell MembraneHumansHydrogen-Ion ConcentrationMembrane FusionProtein ConformationReceptors, VirusSolubilityViral Envelope ProteinsAvian ProteinsReceptors, VirusRous sarcoma virus envelope protein gp37Tva receptorViral Envelope Proteins

Identifiers

PMID14722295
PMCPMC321377
OpenAlexW2146488069

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.