ArticleJournal of molecular biology2011
On the solution conformation and dynamics of the HIV-1 viral infectivity factor.
Article in Journal of molecular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers, 1 of them a synthesis that pooled it.
What it found
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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.
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Who cites it
19 citing papers in PubMed, 1 synthesis or guideline pooled it, 30 citations in OpenAlex.
- HIV Genome-Wide Protein Associations: a Review of 30 Years of Research.Microbiology and molecular biology reviews : MMBR · 2016Pooled it
- Mapping the structural dynamics of red- and blue-emitting beetle luciferases revealed by HDX-MS.Life science alliance · 2026Article
- Advances in Hydrogen/Deuterium Exchange Mass Spectrometry and the Pursuit of Challenging Biological Systems.Chemical reviews · 2022Review
- HDX-MS: An Analytical Tool to Capture Protein Motion in Action.Biomedicines · 2020Review
- Article
- Proteomics in the investigation of HIV-1 interactions with host proteins.Proteomics. Clinical applications · 2015Review
- Structural insights for HIV-1 therapeutic strategies targeting Vif.Trends in biochemical sciences · 2014Review
- Multiple APOBEC3 restriction factors for HIV-1 and one Vif to rule them all.Journal of molecular biology · 2014Review
- Characterization of RNA binding and chaperoning activities of HIV-1 Vif protein. Importance of the C-terminal unstructured tail.RNA biology · 2014Article
- Structural analysis of viral infectivity factor of HIV type 1 and its interaction with A3G, EloC and EloB.PloS one · 2014Article
- Active-site inhibitors modulate the dynamic properties of human monoacylglycerol lipase: a hydrogen exchange mass spectrometry study.Biochemistry · 2013Article
- Membrane phospholipid bilayer as a determinant of monoacylglycerol lipase kinetic profile and conformational repertoire.Protein science : a publication of the Protein Society · 2013Article
- Epitope-distal effects accompany the binding of two distinct antibodies to hepatitis B virus capsids.Journal of the American Chemical Society · 2013Article
- Codon pairs of the HIV-1 vif gene correlate with CD4+ T cell count.BMC infectious diseases · 2013Article
- CBFβ stabilizes HIV Vif to counteract APOBEC3 at the expense of RUNX1 target gene expression.Molecular cell · 2013Article
- Partial cooperative unfolding in proteins as observed by hydrogen exchange mass spectrometry.International reviews in physical chemistry · 2013Article
- Integrating mass spectrometry of intact protein complexes into structural proteomics.Proteomics · 2012Review
- The activity spectrum of Vif from multiple HIV-1 subtypes against APOBEC3G, APOBEC3F, and APOBEC3H.Journal of virology · 2012Article
- 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
6 authors at 2 institutions in 1 country.
Funding
Abstract
Human immunodeficiency virus-1 (HIV-1) has evolved a cunning mechanism to circumvent the antiviral activity of the APOBEC3 family of host cell enzymes. HIV-1 Vif [viral (also called virion) infectivity factor], one of several HIV accessory proteins, targets APOBEC3 proteins for proteasomal degradation and downregulates their expression at the mRNA level. Despite the importance of Vif for HIV-1 infection, there is little conformational data on Vif alone or in complex with other cellular factors due to incompatibilities with many structural techniques and difficulties in producing suitable quantities of the protein for biophysical analysis. As an alternative, we have turned to hydrogen exchange mass spectrometry (HX MS), a conformational analysis method that is well suited for proteins that are difficult to study using X-ray crystallography and/or NMR. HX MS was used to probe the solution conformation of recombinant full-length HIV-1 Vif. Vif specifically interacted with the previously identified binding partner Hck and was able to cause kinase activation, suggesting that the Vif studied by HX MS retained a biochemically competent conformation relevant to Hck interaction. HX MS analysis of Vif alone revealed low deuteration levels in the N-terminal portion, indicating that this region contained structured or otherwise protected elements. In contrast, high deuteration levels in the C-terminal portion of Vif indicated that this region was likely unstructured in the absence of cellular interacting proteins. Several regions within Vif displayed conformational heterogeneity in solution, including the APOBEC3G/F binding site and the HCCH zinc finger. Taken together, these HX MS results provide new insights into the solution conformation of Vif.
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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.