Evidence map›Paper›PMID 24185281›Full record

ArticleNature communications2013

Structural determinants of HIV-1 Vif susceptibility and DNA binding in APOBEC3F.

Karen K Siu, Azmiri Sultana, Farshad C Azimi, Jeffrey E Lee

Open access · bronzeAbstract read
In one paragraph

Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
58citing papers in PubMed, 1 pooled it
4.6field-weighted citation impact, top 4% 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

58 citing papers in PubMed, 1 synthesis or guideline pooled it, 80 citations in OpenAlex.

  1. HIV Genome-Wide Protein Associations: a Review of 30 Years of Research.Microbiology and molecular biology reviews : MMBR · 2016
    Pooled it
  2. Review
  3. Article
  4. Article
  5. Article
  6. The current toolbox for APOBEC drug discovery.Trends in pharmacological sciences · 2022
    Review
  7. Article
  8. Article
  9. Review
  10. Review
  11. Structural perspectives on HIV-1 Vif and APOBEC3 restriction factor interactions.Protein science : a publication of the Protein Society · 2020
    Review
  12. Review
  13. Structural basis of antagonism of human APOBEC3F by HIV-1 Vif.Nature structural & molecular biology · 2019
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Hydrogen bonds are a primary driving force for de novo protein folding.Acta crystallographica. Section D, Structural biology · 2017
    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.

Karen K SiuDepartment of Laboratory Medicine and Pathobiology, Faculty of Medicine, University of Toronto, 1 King's College Circle, Room 6316 Toronto, Ontario, Canada M5S 1A8.
Azmiri Sultana
Farshad C Azimi
Jeffrey E Lee
Canada Research Chairs · CAUniversity of Toronto · CA

Funding

Y-FAMILY POLYMERASES AND CO-FACTORS IN TRANSLESION REPLICATIONP41RR015301 · NCRR · CORNELL UNIVERSITY ITHACA · PI EISENBERG, DAVID · 2001 to 2011
$28.2M
CIHR 113554-1CIHR MSH-113554NCRR NIH HHS P41 RR015301NCRR NIH HHS RR-15301
6 · The paper itself

Abstract

The human APOBEC3 family of DNA cytosine deaminases serves as a front-line intrinsic immune response to inhibit the replication of diverse retroviruses. APOBEC3F and APOBEC3G are the most potent factors against HIV-1. As a countermeasure, HIV-1 viral infectivity factor (Vif) targets APOBEC3s for proteasomal degradation. Here we report the crystal structure of the Vif-binding domain in APOBEC3F and a novel assay to assess Vif-APOBEC3 binding. Our results point to an amphipathic surface that is conserved in APOBEC3s as critical for Vif susceptibility in APOBEC3F. Electrostatic interactions likely mediate Vif binding. Moreover, structure-guided mutagenesis reveals a straight ssDNA-binding groove distinct from the Vif-binding site, and an 'aromatic switch' is proposed to explain DNA substrate specificities across the APOBEC3 family. This study opens new lines of inquiry that will further our understanding of APOBEC3-mediated retroviral restriction and provides an accurate template for structure-guided development of inhibitors targeting the APOBEC3-Vif axis.

Indexed as

Amino Acid SequenceAPOBEC DeaminasesBinding SitesCrystallography, X-RayCytidine DeaminaseCytosine DeaminaseDNA, Single-StrandedEscherichia coliGene ExpressionHIV-1Host-Pathogen InteractionsHumansModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedProtein BindingAPOBEC3 proteins, humanAPOBEC DeaminasesCytidine DeaminaseCytosine DeaminaseDNA, Single-StrandedProtein IsoformsRecombinant Proteinsvif Gene Products, Human Immunodeficiency Virusvif protein, Human immunodeficiency virus 1

Identifiers

PMID24185281
PMCPMC4956467
OpenAlexW2043557765

What OpenQuestion holds

Textmetadata
LicenceTDM
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.