Evidence map›Paper›PMID 32683309›Full record

ArticleDNA repair2020

Molecular basis for the MacroD1-mediated hydrolysis of ADP-ribosylation.

Xiaoyun Yang, Yinliang Ma, Yimiao Li, Yating Dong, Lily L Yu, Hong Wang, Lulin Guo, Chen Wu, Xiaochun Yu, Xiuhua Liu

Open access · greenAbstract read
In one paragraph

Article in DNA repair, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.

0numbers the graph read from it
0cells of the map it votes in
14citing papers in PubMed
1.3field-weighted citation impact, top 18% 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

14 citing papers in PubMed, 20 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. PARP14 is a writer, reader, and eraser of mono-ADP-ribosylation.The Journal of biological chemistry · 2023
    Article
  7. Review
  8. Article
  9. Pre-Conceptional Exposure to Glyphosate Affects the Maternal Hepatic and Ovarian Proteome.Toxicological sciences : an official journal of the Society of Toxicology · 2022
    Article
  10. Article
  11. Review
  12. Reversible modification of mitochondrial ADP/ATP translocases by pairedProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  13. ADP-ribosylhydrolases: from DNA damage repair to COVID-19.Journal of Zhejiang University. Science. B · 2021
    Review
  14. ADP-ribosylation systems in bacteria and viruses.Computational and structural biotechnology journal · 2021
    Review
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

10 authors at 2 institutions in 1 country.

Xiaoyun YangCollege of Life Science, Institute of Life Science and Green Development, Hebei University, Baoding, 071000, Hebei, PR China.
Yinliang MaCollege of Life Science, Institute of Life Science and Green Development, Hebei University, Baoding, 071000, Hebei, PR China.
Yimiao LiCollege of Life Science, Institute of Life Science and Green Development, Hebei University, Baoding, 071000, Hebei, PR China.
Yating DongCollege of Life Science, Institute of Life Science and Green Development, Hebei University, Baoding, 071000, Hebei, PR China.
Lily L YuWestridge School, 324 Madeline Dr., Pasadena, CA, 91105, USA.
Hong WangCollege of Life Science, Institute of Life Science and Green Development, Hebei University, Baoding, 071000, Hebei, PR China.
Lulin GuoCollege of Life Science, Institute of Life Science and Green Development, Hebei University, Baoding, 071000, Hebei, PR China.
Chen WuCollege of Life Science, Institute of Life Science and Green Development, Hebei University, Baoding, 071000, Hebei, PR China. Electronic address: dawnwuchen@163.com.
Xiaochun YuLife Science Institute, Westlake University, Hangzhou, Zhejiang, PR China. Electronic address: yuxiaochun@westlake.edu.cn.
Xiuhua LiuCollege of Life Science, Institute of Life Science and Green Development, Hebei University, Baoding, 071000, Hebei, PR China. Electronic address: liuxiuhua_2004@163.com.
Hebei University · CNWestlake University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

MacroD1 is an enzyme that hydrolyzes protein mono-ADP-ribosylation. However, the key catalytic residues of MacroD1 in these biochemical reactions remain elusive. Here, we present the crystal structure of MacroD1 in a complex with ADP-ribose (ADPR). The β5-α10-loop functions as a switch loop to mediate substrate recognition and right orientation. The conserved Phe

Indexed as

Catalytic DomainDNA RepairModels, MolecularAdenosine Diphosphate RiboseAmino Acid SequenceCarboxylic Ester HydrolasesCrystallography, X-RayDNA DamageHumansHydrogen BondingHydrolysisProtein ConformationSequence AlignmentAdenosine Diphosphate RiboseCarboxylic Ester HydrolasesMACROD1 protein, humanADPRADP-ribosylationCrystal structureDNA damage repairMacroD1

Identifiers

PMID32683309
PMCPMC7313891
OpenAlexW3037578277

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.