Evidence map›Paper›PMID 19327811›Full record

ArticleVirology2009

HIV-1 matrix organizes as a hexamer of trimers on membranes containing phosphatidylinositol-(4,5)-bisphosphate.

Ayna Alfadhli, Robin Lid Barklis, Eric Barklis

Open access · greenAbstract read
In one paragraph

Article in Virology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
3.3field-weighted citation impact, top 7% 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

88 citing papers in PubMed, 130 citations in OpenAlex.

  1. Mechanisms of HIV-1 assembly, release and maturation.Nature reviews. Microbiology · 2026
    Review
  2. Review
  3. Article
  4. Article
  5. PIPScience advances · 2025
    Article
  6. The conserved HIV-1 spacer peptide 2 triggers matrix lattice maturation.bioRxiv : the preprint server for biology · 2024
    Article
  7. Review
  8. Review
  9. Cooperative Membrane Binding of HIV-1 Matrix Proteins.The journal of physical chemistry. B · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Atomic view of the HIV-1 matrix lattice; implications on virus assembly and envelope incorporation.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Review
  16. Review
  17. Article
  18. Article
  19. Review
  20. Review

28 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

3 authors at 2 institutions in 1 country.

Ayna AlfadhliVollum Institute and Department of Microbiology, Oregon Health & Science University, Portland, 97201-3098, USA.
Robin Lid Barklis
Eric Barklis
Oregon Health & Science University · USVollum Institute · US

Funding

In Vitro Analysis of HIV Gag Protein InteractionsR01GM060170 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI BARKLIS, ERIC W · 1999 to 2019
$5.9M
HIV-1 Gag Precursor Protein InteractionsR01AI152579 · NIAID · OREGON HEALTH & SCIENCE UNIVERSITY · PI BARKLIS, ERIC W · 2020 to 2024
$2.5M
Development of a high throughput HIV assembly screenR01AI071798 · NIAID · OREGON HEALTH & SCIENCE UNIVERSITY · PI BARKLIS, ERIC W · 2007 to 2010
$1.5M
NIAID NIH HHS AI071798NIAID NIH HHS R01 AI071798NIAID NIH HHS R01 AI152579NIGMS NIH HHS GM060170NIGMS NIH HHS R01 GM060170
6 · The paper itself

Abstract

The human immunodeficiency virus type 1 (HIV-1) matrix (MA) protein represents the N-terminal domain of the HIV-1 precursor Gag (PrGag) protein and carries an N-terminal myristate (Myr) group. HIV-1 MA fosters PrGag membrane binding, as well as assembly of envelope (Env) proteins into virus particles, and recent studies have shown that HIV-1 MA preferentially directs virus assembly at plasma membrane sites enriched in cholesterol and phosphatidylinositol-(4,5)-bisphosphate (PI[4,5]P(2)). To characterize the membrane binding of MA and PrGag proteins, we have examined how Myr-MA proteins, and proteins composed of Myr-MA and its neighbor Gag capsid (CA) protein associate on membranes containing cholesterol and PI[4,5]P(2). Our results indicate that Myr-MA assembles as a hexamer of trimers on such membranes, and imply that MA trimers interconnect CA hexamer rings in immature virus particles. Our observations suggest a model for the organization of PrGag proteins, and for MA-Env protein interactions.

Indexed as

Cell MembraneCholesterolCrystallizationgag Gene Products, Human Immunodeficiency VirusHIV-1Human Immunodeficiency Virus ProteinsMicroscopy, Electron, TransmissionModels, MolecularMyristic AcidPhosphatidylinositol 4,5-DiphosphateProtein MultimerizationProtein PrecursorsProtein Structure, TertiaryRecombinant ProteinsViral Matrix ProteinsCholesterolgag Gene Products, Human Immunodeficiency VirusHuman Immunodeficiency Virus ProteinsMyristic AcidPhosphatidylinositol 4,5-DiphosphateProtein PrecursorsRecombinant ProteinsViral Matrix Proteins

Identifiers

PMID19327811
PMCPMC2680355
OpenAlexW2010313133

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.