Evidence map›Paper›PMID 24917853›Full record

ReviewFrontiers in microbiology2014

The roles of lipids and nucleic acids in HIV-1 assembly.

Ayna Alfadhli, Eric Barklis

Open access · goldAbstract readReview
In one paragraph

Review in Frontiers in microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.0field-weighted citation impact, top 13% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

  1. Article
  2. PI(4,5)PBiochimica et biophysica acta. Molecular and cell biology of lipids · 2025
    Review
  3. Review
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Methods to Study Determinants for Membrane Targeting of HIV-1 Gag In Vitro.Methods in molecular biology (Clifton, N.J.) · 2016
    Article
  14. Article
  15. Review
  16. Conformation and dynamics of the Gag polyprotein of the human immunodeficiency virus 1 studied by NMR spectroscopy.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  17. Editorial: Role of lipids in virus assembly.Frontiers in microbiology · 2015
    Article
  18. Article
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

2 authors at 1 institution in 1 country.

Ayna AlfadhliDepartment of Molecular Microbiology and Immunology, Oregon Health & Sciences University Portland, OR, USA.
Eric BarklisDepartment of Molecular Microbiology and Immunology, Oregon Health & Sciences University Portland, OR, USA.
Oregon Health & Science University · 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
Analysis of HIV-1 core assembly and inhibitionR01GM101983 · NIGMS · OREGON HEALTH & SCIENCE UNIVERSITY · PI BARKLIS, ERIC W · 2012 to 2015
$1.2M
NIAID NIH HHS R01 AI152579NIGMS NIH HHS R01 GM060170NIGMS NIH HHS R01 GM101983
6 · The paper itself

Abstract

During HIV-1 assembly, precursor Gag (PrGag) proteins are delivered to plasma membrane (PM) assembly sites, where they are triggered to oligomerize and bud from cells as immature virus particles. The delivery and triggering processes are coordinated by the PrGag matrix (MA) and nucleocapsid (NC) domains. Targeting of PrGag proteins to membranes enriched in cholesterol and phosphatidylinositol-4,5-bisphosphate (PI[4,5]P2) is mediated by the MA domain, which also has been shown to bind both RNA and DNA. Evidence suggests that the nucleic-acid-binding function of MA serves to inhibit PrGag binding to inappropriate intracellular membranes, prior to delivery to the PM. At the PM, MA domains putatively trade RNA ligands for PI(4,5)P2 ligands, fostering high-affinity membrane binding. Triggering of oligomerization, budding, and virus particle release results when NC domains on adjacent PrGag proteins bind to viral RNA, leading to capsid (CA) domain oligomerization. This process leads to the assembly of immature virus shells in which hexamers of membrane-bound MA trimers appear to organize above interlinked CA hexamers. Here, we review the functions of retroviral MA proteins, with an emphasis on the nucleic-acid-binding capability of the HIV-1 MA protein, and its effects on membrane binding.

Indexed as

GaglipidmatrixPI(4.5)P2RNA

Identifiers

PMID24917853
PMCPMC4042026
OpenAlexW2150717831

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.