ArticlePloS one2013
Large-scale functional purification of recombinant HIV-1 capsid.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 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
23 citing papers in PubMed, 31 citations in OpenAlex.
- Trial
- MX2 Mediates Collapse of the HIV-1 Capsid.bioRxiv : the preprint server for biology · 2026Article
- Structural and mechanistic bases for resistance of the M66I capsid variant to lenacapavir.mBio · 2025Article
- Article
- The primary mechanism for highly potent inhibition of HIV-1 maturation by lenacapavir.PLoS pathogens · 2025Article
- A new class of capsid-targeting inhibitors that specifically block HIV-1 nuclear import.EMBO molecular medicine · 2024Article
- Virus specificity and nucleoporin requirements for MX2 activity are affected by GTPase function and capsid-CypA interactions.PLoS pathogens · 2024Article
- Virus specificity and nucleoporin requirements for MX2 activity are affected by GTPase function and capsid-CypA interactions.bioRxiv : the preprint server for biology · 2023Article
- A Tripartite Complex HIV-1 Tat-Cyclophilin A-Capsid Protein Enables Tat Encapsidation That Is Required for HIV-1 Infectivity.Journal of virology · 2023Article
- A Broad-Spectrum Antiviral Molecule, Protoporphyrin IX, Acts as a Moderator of HIV-1 Capsid Assembly by Targeting the Capsid Hexamer.Microbiology spectrum · 2023Article
- Prion-like low complexity regions enable avid virus-host interactions during HIV-1 infection.Nature communications · 2022Article
- Sec24C is an HIV-1 host dependency factor crucial for virus replication.Nature microbiology · 2021Article
- New insight into the significance of KLF4 PARylation in genome stability, carcinogenesis, and therapy.EMBO molecular medicine · 2020Article
- Structural and mechanistic bases for a potent HIV-1 capsid inhibitor.Science (New York, N.Y.) · 2020Article
- MxB Restricts HIV-1 by Targeting the Tri-hexamer Interface of the Viral Capsid.Structure (London, England : 1993) · 2019Article
- Functional analysis of the secondary HIV-1 capsid binding site in the host protein cyclophilin A.Retrovirology · 2019Article
- Recent Developments in Bioprocessing of Recombinant Proteins: Expression Hosts and Process Development.Frontiers in bioengineering and biotechnology · 2019Review
- Article
- Downstream process development strategies for effective bioprocesses: Trends, progress, and combinatorial approaches.Engineering in life sciences · 2017Article
- Thermodynamic instability of viral proteins is a pathogen-associated molecular pattern targeted by human defensins.Scientific reports · 2016Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
During human immunodeficiency virus type-1 (HIV-1) virion maturation, capsid proteins undergo a major rearrangement to form a conical core that protects the viral nucleoprotein complexes. Mutations in the capsid sequence that alter the stability of the capsid core are deleterious to viral infectivity and replication. Recently, capsid assembly has become an attractive target for the development of a new generation of anti-retroviral agents. Drug screening efforts and subsequent structural and mechanistic studies require gram quantities of active, homogeneous and pure protein. Conventional means of laboratory purification of Escherichia coli expressed recombinant capsid protein rely on column chromatography steps that are not amenable to large-scale production. Here we present a function-based purification of wild-type and quadruple mutant capsid proteins, which relies on the inherent propensity of capsid protein to polymerize and depolymerize. This method does not require the packing of sizable chromatography columns and can generate double-digit gram quantities of functionally and biochemically well-behaved proteins with greater than 98% purity. We have used the purified capsid protein to characterize two known assembly inhibitors in our in-house developed polymerization assay and to measure their binding affinities. Our capsid purification procedure provides a robust method for purifying large quantities of a key protein in the HIV-1 life cycle, facilitating identification of the next generation anti-HIV agents.
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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.