Evidence map›Paper›PMID 16407066›Full record

ArticleStructure (London, England : 1993)2006

Mapping the structure and function of the E1 and E2 glycoproteins in alphaviruses.

Suchetana Mukhopadhyay, Wei Zhang, Stefan Gabler, Paul R Chipman, Ellen G Strauss, James H Strauss, Timothy S Baker, Richard J Kuhn, Michael G Rossmann

Open access · bronzeAbstract read
In one paragraph

Article in Structure (London, England : 1993), 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 117 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
117citing papers in PubMed, 1 pooled it
10.9field-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

117 citing papers in PubMed, 1 synthesis or guideline pooled it, 218 citations in OpenAlex.

  1. Pooled it
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  3. Review
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  15. From transmission to adaptive evolution: genomic surveillance of Getah virus.Frontiers in cellular and infection microbiology · 2025
    Article
  16. Article
  17. Article
  18. Maturation of Viruses.Sub-cellular biochemistry · 2024
    Review
  19. Article
  20. Review

57 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

9 authors at 2 institutions in 1 country.

Suchetana MukhopadhyayDepartment of Biological Sciences, Purdue University, West Lafayette, Indiana 47907, USA. sumukhop@indiana.edu
Wei Zhang
Stefan Gabler
Paul R Chipman
Ellen G Strauss
James H Strauss
Timothy S Baker
Richard J Kuhn
Michael G Rossmann
California Institute of Technology · USPurdue University West Lafayette · US

Funding

Structure-function studies of alpha-and flavivirusesP01AI055672 · NIAID · PURDUE UNIVERSITY WEST LAFAYETTE · PI KUHN, RICHARD J. · 2003 to 2010
$18.4M
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
MOLECULAR BASIS OF ALPHAVIRUS ASSEMBLYR01GM056279 · NIGMS · PURDUE UNIVERSITY WEST LAFAYETTE · PI KUHN, RICHARD J. · 1997 to 2014
$3.7M
TOGAVIRUS REPLICATION STRATEGIES &EVOLUTIONR01AI020612 · NIAID · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI STRAUSS, JAMES · 1989 to 2004
$1.2M
TOGAVIRUS REPLICATION STRATEGIES &EVOLUTIONR22AI020612 · NIAID · CALIFORNIA INSTITUTE OF TECHNOLOGY · PI STRAUSS, JAMES · 1985 to 1991
–
NIAID NIH HHS AI20612NIAID NIH HHS AI55672NIAID NIH HHS P01 AI045976NIAID NIH HHS P01 AI055672NIAID NIH HHS R01 AI020612NIGMS NIH HHS GM56279NIGMS NIH HHS GM R37-033050NIGMS NIH HHS R01 GM056279
6 · The paper itself

Abstract

The 9 A resolution cryo-electron microscopy map of Sindbis virus presented here provides structural information on the polypeptide topology of the E2 protein, on the interactions between the E1 and E2 glycoproteins in the formation of a heterodimer, on the difference in conformation of the two types of trimeric spikes, on the interaction between the transmembrane helices of the E1 and E2 proteins, and on the conformational changes that occur when fusing with a host cell. The positions of various markers on the E2 protein established the approximate topology of the E2 structure. The largest conformational differences between the icosahedral surface spikes at icosahedral 3-fold and quasi-3-fold positions are associated with the monomers closest to the 5-fold axes. The long E2 monomers, containing the cell receptor recognition motif at their extremities, are shown to rotate by about 180 degrees and to move away from the center of the spikes during fusion.

Indexed as

Cryoelectron MicroscopyCrystallography, X-RayMembrane GlycoproteinsNucleocapsid ProteinsProtein Interaction MappingProtein Structure, TertiarySindbis VirusViral Envelope ProteinsViral Fusion Proteinsglycoprotein E1, Sindbis virusglycoprotein E2, Sindbis virusMembrane GlycoproteinsNucleocapsid ProteinsViral Envelope ProteinsViral Fusion Proteins

Identifiers

PMID16407066
PMCPMC2757649
OpenAlexW2105291981

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.