Evidence map›Paper›PMID 11274436›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

Modular organization of the Friend murine leukemia virus envelope protein underlies the mechanism of infection.

A L Barnett, R A Davey, J M Cunningham

Open access · bronzeAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
2.9field-weighted citation impact, top 8% 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

45 citing papers in PubMed, 74 citations in OpenAlex.

  1. Article
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  8. Sequential activation of the three protomers in the Moloney murine leukemia virus Env.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  9. Article
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  11. Furin cleavage of the Moloney murine leukemia virus Env precursor reorganizes the spike structure.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  12. 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

3 authors at 3 institutions in 1 country.

A L BarnettDepartment of Medicine and Howard Hughes Medical Institute, Brigham and Women's Hospital, Boston, MA 02115, USA.
R A Davey
J M Cunningham
Brigham and Women's Hospital · USHarvard University · USHoward Hughes Medical Institute · US

Funding

DNA Minor Groove-binding Drugs and Food-borne PathogensU01AI061246 · NIAID · BRIGHAM AND WOMEN'S HOSPITAL · PI PERRELLA, MARK A · 2005 to 2009
$2.1M
ROLE OF ARGININE TRANSPORT IN NITRIC OXIDE PRODUCTIONR01CA061246 · NCI · BRIGHAM AND WOMEN'S HOSPITAL · PI CUNNINGHAM, JAMES M · 1993 to 2001
$354k
NCI NIH HHS 2RO1CA/AI61246-06NIAID NIH HHS U01 AI061246
6 · The paper itself

Abstract

Retrovirus infection is initiated by receptor-dependent fusion of the envelope to the cell membrane. The modular organization of the envelope protein of C type retroviruses has been exploited to investigate how binding of the surface subunit (SU) to receptor triggers fusion mediated by the transmembrane (TM) subunit. We show that deletion of the receptor-binding domain (RBD) from SU of Friend murine leukemia virus (Fr-MLV) abolishes infection that is restored by supplying RBD as a soluble protein. Infection by this mechanism remains dependent on receptor expression. When membrane attachment of the virus lacking RBD is reestablished by inserting the hormone erythropoietin, infection remains dependent on the RBD/receptor complex. However, infection increases 50-fold to 5 x 10(5) units/ml on cells that also express the erythropoietin receptor. Soluble RBD from Fr-MLV also restores infection by amphotropic and xenotropic MLVs in which RBD is deleted. These experiments demonstrate that RBD has two functions: mediating virus attachment and activating the fusion mechanism. In addition, they indicate that receptor engagement triggers fusion by promoting a subgroup-independent functional interaction between RBD and the remainder of SU and/or TM.

Indexed as

Cell Line, TransformedHumansLeukemia Virus, MurineModels, MolecularPlasmidsProtein Structure, TertiaryViral Envelope ProteinsViral Envelope Proteins

Identifiers

PMID11274436
PMCPMC31188
OpenAlexW2134280467

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.