Evidence map›Paper›PMID 24345943›Full record

ArticleNature chemistry2014

Oligomerization transforms human APOBEC3G from an efficient enzyme to a slowly dissociating nucleic acid-binding protein.

Kathy R Chaurasiya, Micah J McCauley, Wei Wang, Dominic F Qualley, Tiyun Wu, Shingo Kitamura, Hylkje Geertsema, Denise S B Chan, Amber Hertz, Yasumasa Iwatani and 4 more

Open access · greenAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Nature chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

48 citing papers in PubMed, 72 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Article
  6. Review
  7. Review
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 5 institutions in 2 countries.

Kathy R ChaurasiyaDepartment of Physics, Northeastern University, Boston, Massachusetts 02115, USA.
Micah J McCauleyDepartment of Physics, Northeastern University, Boston, Massachusetts 02115, USA.
Wei WangDepartment of Chemistry and Biochemistry, Center for Retrovirus Research, and Center for RNA Biology, The Ohio State University, Columbus, Ohio 43210, USA.
Dominic F QualleyDepartment of Chemistry and Biochemistry, Center for Retrovirus Research, and Center for RNA Biology, The Ohio State University, Columbus, Ohio 43210, USA.
Tiyun WuSection on Viral Gene Regulation, Program on Genomics of Differentiation, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA.
Shingo KitamuraClinical Research Center, National Hospital Organization Nagoya Medical Center, Nagoya, Aichi 460-0001, Japan.
Hylkje GeertsemaDepartment of Physics, Northeastern University, Boston, Massachusetts 02115, USA.
Denise S B ChanDepartment of Structural Biology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15260, USA.
Amber HertzSection on Viral Gene Regulation, Program on Genomics of Differentiation, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA.
Yasumasa Iwatani1] Section on Viral Gene Regulation, Program on Genomics of Differentiation, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA [2] Clinical Research Center, National Hospital Organization Nagoya Medical Center, Nagoya, Aichi 460-0001, Japan.
Judith G LevinSection on Viral Gene Regulation, Program on Genomics of Differentiation, Eunice Kennedy Shriver National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, Maryland 20892, USA.
Karin Musier-ForsythDepartment of Chemistry and Biochemistry, Center for Retrovirus Research, and Center for RNA Biology, The Ohio State University, Columbus, Ohio 43210, USA.
Ioulia RouzinaDepartment of Biochemistry, Molecular Biology and Biophysics, University of Minnesota, Minneapolis, Minnesota 55455, USA.
Mark C WilliamsDepartment of Physics, Northeastern University, Boston, Massachusetts 02115, USA.
Northeastern University · USThe Ohio State University · USNagoya Medical Center · JPUniversity of Minnesota · USUniversity of Pittsburgh · US

Funding

Molecular Genetics Of Mammalian Retrovirus ReplicationZIAHD000069 · NICHD · EUNICE KENNEDY SHRIVER NATIONAL INSTITUTE OF CHILD HEALTH & HUMAN DEVELOPMENT · PI LEVIN, JUDITH G · 2009 to 2015
$7.2M
RNA Binding and Packaging By Retroviral Gag ProteinsR01GM065056 · NIGMS · UNIVERSITY OF MINNESOTA TWIN CITIES · PI MUSIER-FORSYTH, KARIN M · 2002 to 2018
$4.9M
Single Molecule HIV-1 Replication InteractionsR01GM072462 · NIGMS · NORTHEASTERN UNIVERSITY · PI WILLIAMS, MARK C · 2004 to 2018
$3.9M
Intramural NIH HHSNIGMS NIH HHS GM065056NIGMS NIH HHS GM072462NIGMS NIH HHS R01 GM065056NIGMS NIH HHS R01 GM072462
6 · The paper itself

Abstract

The human APOBEC3 proteins are a family of DNA-editing enzymes that play an important role in the innate immune response against retroviruses and retrotransposons. APOBEC3G is a member of this family that inhibits HIV-1 replication in the absence of the viral infectivity factor Vif. Inhibition of HIV replication occurs by both deamination of viral single-stranded DNA and a deamination-independent mechanism. Efficient deamination requires rapid binding to and dissociation from ssDNA. However, a relatively slow dissociation rate is required for the proposed deaminase-independent roadblock mechanism in which APOBEC3G binds the viral template strand and blocks reverse transcriptase-catalysed DNA elongation. Here, we show that APOBEC3G initially binds ssDNA with rapid on-off rates and subsequently converts to a slowly dissociating mode. In contrast, an oligomerization-deficient APOBEC3G mutant did not exhibit a slow off rate. We propose that catalytically active monomers or dimers slowly oligomerize on the viral genome and inhibit reverse transcription.

Indexed as

APOBEC-3G DeaminaseBiopolymersCytidine DeaminaseDeaminationHIV-1HumansRNA-Directed DNA PolymeraseVirus ReplicationAPOBEC-3G DeaminaseAPOBEC3G protein, humanBiopolymersCytidine DeaminaseRNA-Directed DNA Polymerase

Identifiers

PMID24345943
PMCPMC3950479
OpenAlexW2007861318

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.