Evidence map›Paper›PMID 26195824›Full record

ArticleThe Biochemical journal2015

DNA cytosine and methylcytosine deamination by APOBEC3B: enhancing methylcytosine deamination by engineering APOBEC3B.

Yang Fu, Fumiaki Ito, Gewen Zhang, Braulio Fernandez, Hanjing Yang, Xiaojiang S Chen

Open access · bronzeAbstract read
In one paragraph

Article in The Biochemical journal, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
4.1field-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

40 citing papers in PubMed, 48 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. The current toolbox for APOBEC drug discovery.Trends in pharmacological sciences · 2022
    Review
  11. Review
  12. Specific hypomethylation programs underpin B cell activation in early multiple sclerosis.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Determinants of Oligonucleotide Selectivity of APOBEC3B.Journal of chemical information and modeling · 2019
    Article
  18. Article
  19. Article
  20. 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

6 authors at 1 institution in 1 country.

Yang FuMolecular and Computational Biology Program, Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089, U.S.A.
Fumiaki ItoMolecular and Computational Biology Program, Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089, U.S.A.
Gewen ZhangMolecular and Computational Biology Program, Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089, U.S.A.
Braulio FernandezMolecular and Computational Biology Program, Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089, U.S.A.
Hanjing YangMolecular and Computational Biology Program, Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089, U.S.A.
Xiaojiang S ChenMolecular and Computational Biology Program, Department of Biological Sciences, University of Southern California, Los Angeles, CA 90089, U.S.A. Department of Chemistry, Center of Excellence in NanoBiophysics, Norris Comprehensive Cancer Center, University of Southern California, Los Angeles, CA 90089, U.S.A.
University of Southern California · US

Funding

Understanding The Structural Basis of APOBEC FunctionsR01GM087986 · NIGMS · UNIVERSITY OF SOUTHERN CALIFORNIA · PI CHEN, XIAOJIANG S · 2009 to 2018
$2.5M
NIGMS NIH HHS R01 GM087986NIGMS NIH HHS R01GM087986
6 · The paper itself

Abstract

APOBEC (apolipoprotein B mRNA-editing enzyme catalytic polypeptide-like) is a family of enzymes that deaminates cytosine (C) to uracil (U) on nucleic acid. APOBEC3B (A3B) functions in innate immunity against intrinsic and invading retroelements and viruses. A3B can also induce genomic DNA mutations to cause cancer. A3B contains two cytosine deaminase domains (CD1, CD2), and there are conflicting reports about whether both domains are active. Here we demonstrate that only CD2 of A3B (A3BCD2) has C deamination activity. We also reveal that both A3B and A3BCD2 can deaminate methylcytosine (mC). Guided by structural and functional analysis, we successfully engineered A3BCD2 to gain over two orders of magnitude higher activity for mC deamination. Important determinants that contribute to the activity and selectivity for mC deamination have been identified, which reveals that multiple elements, rather than single ones, contribute to the mC deamination activity and selectivity in A3BCD2 and possibly other APOBECs.

Indexed as

Protein EngineeringCytidine DeaminaseCytosineHumansMinor Histocompatibility AntigensProtein Structure, TertiaryAPOBEC3B protein, humanCytidine DeaminaseCytosineMinor Histocompatibility Antigenscytosine/methylcytosine (C/mC) selectivityenzyme engineeringmultiple determinants for mC specificitysubstrate specificity alterationzinc (Zn) deaminase

Identifiers

PMID26195824
PMCPMC4613526
OpenAlexW2109410065

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.