ReviewInternational journal of molecular sciences2022
The HIV-1 Gag Protein Displays Extensive Functional and Structural Roles in Virus Replication and Infectivity.
Review in International journal of molecular sciences, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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.
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.
Who cites it
13 citing papers in PubMed, 26 citations in OpenAlex.
- Mechanisms of APOBEC3 Packaging into HIV-1.Viruses · 2026Review
- Functional roles, mechanistic insights, and therapeutic potential of the IGF2BP family in viral infections and virus-associated cancers.Journal of molecular histology · 2026Review
- Article
- MicroRNAs in HIV infection: dual regulators of viral replication and host immunity.Naunyn-Schmiedeberg's archives of pharmacology · 2025Review
- Subtype-Specific HIV-1 Protease and the Role of Hinge and Flap Dynamics in Drug Resistance: A Subtype C Narrative.Viruses · 2025Review
- Article
- CCR5 gene editing and HIV immunotherapy: current understandings, challenges, and future directions.Frontiers in immunology · 2025Article
- Determinants in the HTLV-1 Capsid Major Homology Region that are Critical for Virus Particle Assembly.Journal of molecular biology · 2024Article
- Review
- Conformational transitions of the HIV-1 Gag polyprotein upon multimerization and gRNA binding.Biophysical journal · 2024Article
- Article
- Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Once merely thought of as the protein responsible for the overall physical nature of the human immunodeficiency virus type 1 (HIV-1), the Gag polyprotein has since been elucidated to have several roles in viral replication and functionality. Over the years, extensive research into the polyproteins' structure has revealed that Gag can mediate its own trafficking to the plasma membrane, it can interact with several host factors and can even aid in viral genome packaging. Not surprisingly, Gag has also been associated with HIV-1 drug resistance and even treatment failure. Therefore, this review provides an extensive overview of the structural and functional roles of the HIV-1 Gag domains in virion integrity, functionality and infectivity.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.