Evidence map›Paper›PMID 19523676›Full record

ArticleCell2009

X-ray structures of the hexameric building block of the HIV capsid.

Owen Pornillos, Barbie K Ganser-Pornillos, Brian N Kelly, Yuanzi Hua, Frank G Whitby, C David Stout, Wesley I Sundquist, Christopher P Hill, Mark Yeager

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 365 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
365citing papers in PubMed, 2 pooled it
19.1field-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

365 citing papers in PubMed, 2 syntheses or guidelines pooled it, 539 citations in OpenAlex.

  1. Pooled it
  2. HIV Genome-Wide Protein Associations: a Review of 30 Years of Research.Microbiology and molecular biology reviews : MMBR · 2016
    Pooled it
  3. Trial
  4. Article
  5. Lenacapavir binding to immature Gag induces giant virions and causes protease-dependent inhibition of viral release.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Exploring the Structural Divergence of HIV and SRLV Lentiviral Capsids.Journal of the American Chemical Society · 2025
    Article
  20. Article

305 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 3 institutions in 1 country.

Owen PornillosDepartment of Cell Biology, The Scripps Research Institute, La Jolla, CA 92037, USA.
Barbie K Ganser-Pornillos
Brian N Kelly
Yuanzi Hua
Frank G Whitby
C David Stout
Wesley I Sundquist
Christopher P Hill
Mark Yeager
Scripps Research Institute · USUniversity of Utah · USUniversity of Virginia Health System · US

Funding

X-ray Cryst. CoreP50GM082545 · NIGMS · UNIVERSITY OF UTAH · PI HOPE, THOMAS · 2007 to 2018
$51.1M
Structure Analysis of Viral Assembly MechanismsR01GM066087 · NIGMS · UNIVERSITY OF VIRGINIA · PI YEAGER, MARK JAY · 2003 to 2014
$4.4M
NIGMS NIH HHS P50 GM082545NIGMS NIH HHS P50GM082545-NIGMS NIH HHS R01 GM066087NIGMS NIH HHS R01-GM066087
6 · The paper itself

Abstract

The mature capsids of HIV and other retroviruses organize and package the viral genome and its associated enzymes for delivery into host cells. The HIV capsid is a fullerene cone: a variably curved, closed shell composed of approximately 250 hexamers and exactly 12 pentamers of the viral CA protein. We devised methods for isolating soluble, assembly-competent CA hexamers and derived four crystallographically independent models that define the structure of this capsid assembly unit at atomic resolution. A ring of six CA N-terminal domains form an apparently rigid core, surrounded by an outer ring of C-terminal domains. Mobility of the outer ring appears to be an underlying mechanism for generating the variably curved lattice in authentic capsids. Hexamer-stabilizing interfaces are highly hydrated, and this property may be key to the formation of quasi-equivalent interactions within hexamers and pentamers. The structures also clarify the molecular basis for capsid assembly inhibition and should facilitate structure-based drug design strategies.

Indexed as

Capsid ProteinsCrystallography, X-RayHIV-1Models, MolecularPolymersProtein Structure, TertiaryCapsid ProteinsPolymers

Identifiers

PMID19523676
PMCPMC2840706
OpenAlexW2117091532

What OpenQuestion holds

Textmetadata
LicenceTDM
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.