ArticleMolecular biology international2012
Dynamic Association between HIV-1 Gag and Membrane Domains.
Article in Molecular biology international, 2012. 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
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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, 20 citations in OpenAlex.
- Repurposing Amphotericin B and Its Liposomal Formulation for the Treatment of Human Mpox.International journal of molecular sciences · 2023Article
- Post-Translational Modifications of Retroviral HIV-1 Gag Precursors: An Overview of Their Biological Role.International journal of molecular sciences · 2021Review
- Coronavirus Interplay With Lipid Rafts and Autophagy Unveils Promising Therapeutic Targets.Frontiers in microbiology · 2020Review
- Article
- The C-terminal p6 domain of the HIV-1 Pr55RNA biology · 2018Article
- Structural and molecular determinants of HIV-1 Gag binding to the plasma membrane.Frontiers in microbiology · 2015Article
- Basic motifs target PSGL-1, CD43, and CD44 to plasma membrane sites where HIV-1 assembles.Journal of virology · 2015Article
- Editorial: Role of lipids in virus assembly.Frontiers in microbiology · 2015Article
- Could the Ebola virus matrix protein VP40 be a drug target?Expert opinion on therapeutic targets · 2014Article
- HIV-1 Nef promotes the localization of Gag to the cell membrane and facilitates viral cell-to-cell transfer.Retrovirology · 2013Article
- HIV-1 Gag associates with specific uropod-directed microdomains in a manner dependent on its MA highly basic region.Journal of virology · 2013Article
- Super-resolution microscopy reveals specific recruitment of HIV-1 envelope proteins to viral assembly sites dependent on the envelope C-terminal tail.PLoS pathogens · 2013Article
- The cytosolic N-terminus of CD317/tetherin is a membrane microdomain exclusion motif.Biology open · 2013Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 3 institutions in 1 country.
Funding
Abstract
HIV-1 particle assembly is driven by the structural protein Gag. Gag binds to and multimerizes on the inner leaflet of the plasma membrane, eventually resulting in formation of spherical particles. During virus spread among T cells, Gag accumulates to the plasma membrane domain that, together with target cell membrane, forms a cell junction known as the virological synapse. While Gag association with plasma membrane microdomains has been implicated in virus assembly and cell-to-cell transmission, recent studies suggest that, rather than merely accumulating to pre-existing microdomains, Gag plays an active role in reorganizing the microdomains via its multimerization activity. In this paper, we will discuss this emerging view of Gag microdomain interactions. Relationships between Gag multimerization and microdomain association will be further discussed in the context of Gag localization to T-cell uropods and virological synapses.
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.