Evidence map›Paper›PMID 33572761›Full record

ReviewLife (Basel, Switzerland)2021

Structure, Function, and Interactions of the HIV-1 Capsid Protein.

Eric Rossi, Megan E Meuser, Camille J Cunanan, Simon Cocklin

Open access · goldAbstract readReview
In one paragraph

Review in Life (Basel, Switzerland), 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
7.7field-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

44 citing papers in PubMed, 74 citations in OpenAlex.

  1. FoldaVirus, a knowledge-based icosahedral capsid prediction tool using AlphaFold.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. Review
  3. Article
  4. Review
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  6. Article
  7. Bee products as alternatives in the treatment of viral infections.Journal of the science of food and agriculture · 2026
    Review
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  14. Lenacapavir: Playing the Long Game in the New Era of Antiretrovirals.Clinical pharmacology and therapeutics · 2025
    Review
  15. Article
  16. Cyclophilin A Regulates Tripartite Motif 5 Alpha Restriction of HIV-1.International journal of molecular sciences · 2025
    Review
  17. Review
  18. Review
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  20. 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

4 authors at 2 institutions in 1 country.

Eric RossiAngle North America, 1500 1st Avenue, Suite 1010, King of Prussia, PA 19462, USA.
Megan E MeuserDepartment of Biochemistry & Molecular Biology, Drexel University College of Medicine, Rooms 10307, 10309, and 10315, 245 North 15th Street, Philadelphia, PA 19102, USA.ORCID 0000-0002-1544-606X
Camille J CunananDepartment of Biochemistry & Molecular Biology, Drexel University College of Medicine, Rooms 10307, 10309, and 10315, 245 North 15th Street, Philadelphia, PA 19102, USA.ORCID 0000-0003-0022-6117
Simon CocklinDepartment of Biochemistry & Molecular Biology, Drexel University College of Medicine, Rooms 10307, 10309, and 10315, 245 North 15th Street, Philadelphia, PA 19102, USA.ORCID 0000-0002-9074-741X
Drexel University · USAlliant Techsystems (United States) · US

Funding

Novel anti-HIV compounds targeting the HIV-1 matrix proteinR01AI150491 · NIAID · DREXEL UNIVERSITY · PI LOLL, PATRICK J · 2020 to 2022
$1.7M
National Institute of Allergy and Infectious Diseases AI150491NIAID NIH HHS R01 AI150491
6 · The paper itself

Abstract

The capsid (CA) protein of the human immunodeficiency virus type 1 (HIV-1) is an essential structural component of a virion and facilitates many crucial life cycle steps through interactions with host cell factors. Capsid shields the reverse transcription complex from restriction factors while it enables trafficking to the nucleus by hijacking various adaptor proteins, such as FEZ1 and BICD2. In addition, the capsid facilitates the import and localization of the viral complex in the nucleus through interaction with NUP153, NUP358, TNPO3, and CPSF-6. In the later stages of the HIV-1 life cycle, CA plays an essential role in the maturation step as a constituent of the Gag polyprotein. In the final phase of maturation, Gag is cleaved, and CA is released, allowing for the assembly of CA into a fullerene cone, known as the capsid core. The fullerene cone consists of ~250 CA hexamers and 12 CA pentamers and encloses the viral genome and other essential viral proteins for the next round of infection. As research continues to elucidate the role of CA in the HIV-1 life cycle and the importance of the capsid protein becomes more apparent, CA displays potential as a therapeutic target for the development of HIV-1 inhibitors.

Indexed as

assemblycapsidHIV-1/AIDShost proteinspost-entry eventsrestriction factorsvirus-host interactions

Identifiers

PMID33572761
PMCPMC7910843
OpenAlexW3126707646

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.