Evidence map›Paper›PMID 20212048›Full record

ArticleThe Journal of biological chemistry2010

Structural model for deoxycytidine deamination mechanisms of the HIV-1 inactivation enzyme APOBEC3G.

Linda Chelico, Courtney Prochnow, Dorothy A Erie, Xiaojiang S Chen, Myron F Goodman

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

84 citing papers in PubMed, 117 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Review
  9. Interactions of APOBEC3s with DNA and RNA.Current opinion in structural biology · 2021
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Article
  17. Article
  18. Article
  19. Structural Determinants of the APOBEC3G N-Terminal Domain for HIV-1 RNA Association.Frontiers in cellular and infection microbiology · 2019
    Article
  20. Article

24 more citing papers are in PubMed but not listed here.

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

5 authors at 1 institution in 1 country.

Linda ChelicoDepartment of Biological Sciences, University of Southern California, Los Angeles, California 90089-2910, USA.
Courtney Prochnow
Dorothy A Erie
Xiaojiang S Chen
Myron F Goodman
University of Southern California · US

Funding

ERROR CORRECTION IN DNA SYNTHESIS--A BIOCHEMICAL STUDYR37GM021422 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI GOODMAN, MYRON · 2000 to 2009
$3.5M
Structure Function Studies of DNA Mismatch RepairR01GM079480 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ERIE, DOROTHY A · 2007 to 2017
$2.7M
Understanding The Structural Basis of APOBEC FunctionsR01GM087986 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI CHEN, XIAOJIANG S · 2009 to 2018
$2.5M
Mechanistic studies of DNA repair and damage responseR01GM080294 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI ERIE, DOROTHY A · 2009 to 2010
$565k
NIGMS NIH HHS GM079480NIGMS NIH HHS GM080294NIGMS NIH HHS GM087986NIGMS NIH HHS R01 GM079480NIGMS NIH HHS R01 GM080294NIGMS NIH HHS R01 GM087986NIGMS NIH HHS R37 GM021422NIGMS NIH HHS R37GM21422PHS HHS ESO13192
6 · The paper itself

Abstract

APOBEC3G (Apo3G) is a single-stranded DNA-dependent deoxycytidine deaminase, which, in the absence of the human immunodeficiency virus (HIV) viral infectivity factor, is encapsulated into HIV virions. Subsequently, Apo3G triggers viral inactivation by processively deaminating C-->U, with 3'-->5' polarity, on nascent minus-strand cDNA. Apo3G has a catalytically inactive N-terminal CD1 domain and an active C-terminal CD2 domain. Apo3G exists as monomers, dimers, tetramers, and higher order oligomers whose distributions depend on DNA substrate and salt. Here we use multiangle light scattering and atomic force microscopy to identify oligomerization states of Apo3G. A double mutant (F126A/W127A), designed to disrupt dimerization at the predicted CD1-CD1 dimer interface, predominantly converts Apo3G to a monomer that binds single-stranded DNA, Alu RNA, and catalyzes processive C-->U deaminations with 3'-->5' deamination polarity, similar to native Apo3G. The CD1 domain is essential for both processivity and polarity. We propose a structure-based model to explain the scanning and catalytic behavior of Apo3G.

Indexed as

HIV-1Models, MolecularVirionAlu ElementsAPOBEC-3G DeaminaseCytidine DeaminaseDeaminationDNA, ComplementaryHumansMicroscopy, Atomic ForceProtein MultimerizationProtein Structure, TertiaryRNAStructure-Activity RelationshipAPOBEC-3G DeaminaseAPOBEC3G protein, humanCytidine DeaminaseDNA, ComplementaryRNA

Identifiers

PMID20212048
PMCPMC2871487
OpenAlexW1982475481

What OpenQuestion holds

Textmetadata
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.