Evidence map›Paper›PMID 11832217›Full record

ArticleCell2002

Structure of the reovirus membrane-penetration protein, Mu1, in a complex with is protector protein, Sigma3.

Susanne Liemann, Kartik Chandran, Timothy S Baker, Max L Nibert, Stephen C Harrison

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.

0numbers the graph read from it
0cells of the map it votes in
123citing papers in PubMed
7.9field-weighted citation impact, top 2% 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

123 citing papers in PubMed, 230 citations in OpenAlex.

  1. Review
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  3. Article
  4. Article
  5. Article
  6. In situ structures of polymerase complex of mammalian reovirus illuminate RdRp activation and transcription regulation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
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  8. Review
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  11. Article
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  16. Article
  17. Article
  18. Review
  19. Review
  20. Article

63 more citing papers are in PubMed but not listed here.

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 3 institutions in 1 country.

Susanne LiemannHoward Hughes Medical Institute, Children's Hospital, Harvard Medical School, 320 Longwood Avenue, Boston, MA 02115, USA.
Kartik Chandran
Timothy S Baker
Max L Nibert
Stephen C Harrison
Harvard University · USHoward Hughes Medical Institute · USPurdue University West Lafayette · US

Funding

VIRUS ASSEMBLY AND TRANSMISSIONP01AI045976 · NIAID · PURDUE UNIVERSITY WEST LAFAYETTE · PI ROSSMANN, MICHAEL G · 1999 to 2008
$8.8M
Microscopy &Image Analysis of Unstained MacromoleculesR37GM033050 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BAKER, TIMOTHY S · 2004 to 2013
$5.6M
STRUCTURE AND ASSEMBLY OF VIRUSES AND OF COATED VESICLESR01CA013202 · NCI · HARVARD UNIVERSITY · PI HARRISON, STEPHEN COPLAN · 1985 to 2024
$4.9M
MICROSCOPY &IMAGE ANALYSIS OF UNSTAINED MACROMOLECULESR01GM033050 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI BAKER, TIMOTHY S · 1985 to 2017
$4.3M
Structure and Assembly of VirusesR37CA013202 · NCI · CHILDREN'S HOSPITAL BOSTON · PI HARRISON, STEPHEN COPLAN · 2003 to 2012
$3.7M
REOVIRUS OUTER-CAPSID ASSEMBLY &FUNCTIONS IN CELL ENTRYR01AI046440 · NIAID · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI NIBERT, MAX L. · 2001 to 2005
$1.7M
NCI NIH HHS CA-13202NCI NIH HHS R01 CA013202NCI NIH HHS R37 CA013202NIAID NIH HHS AI-46440NIAID NIH HHS P01 AI045976NIAID NIH HHS R01 AI046440NIGMS NIH HHS GM-33050NIGMS NIH HHS R01 GM033050NIGMS NIH HHS R37 GM033050
6 · The paper itself

Abstract

Cell entry by nonenveloped animal viruses requires membrane penetration without membrane fusion. The reovirus penetration agent is the outer-capsid protein, Mu1. The structure of Mu1, complexed with its "protector" protein, Sigma3, and the fit of this Mu1(3)Sigma3(3) heterohexameric complex into the cryoEM image of an intact virion, reveal molecular events essential for viral penetration. Autolytic cleavage divides Mu1 into myristoylated Mu1N and Mu1C. A long hydrophobic pocket can receive the myristoyl group. Dissociation of Mu1N, linked to a major conformational change of the entire Mu1 trimer, must precede myristoyl-group insertion into the cellular membrane. A myristoyl switch, coupling exposure of the fatty acid chain, autolytic cleavage of Mu1N, and long-range molecular rearrangement of Mu1C, thus appears to be part of the penetration mechanism.

Indexed as

Capsid ProteinsProtein Structure, TertiaryAmino Acid SequenceAnimalsBinding SitesCapsidCrystallography, X-RayHumansModels, MolecularMolecular Sequence DataProtein SubunitsReoviridaeRNA-Binding ProteinsSequence AlignmentViral ProteinsVirionCapsid Proteinsmu1 protein, ReovirusProtein SubunitsRNA-Binding Proteinssigma protein 3, ReovirusViral Proteins

Identifiers

PMID11832217
PMCPMC4152834
OpenAlexW2092199562

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.