Evidence map›Paper›PMID 25938242›Full record

ReviewCurrent protein & peptide science2015

ADP-ribosyltransferases and poly ADP-ribosylation.

Chao Liu, Xiaochun Yu

Abstract readReview
In one paragraph

Review in Current protein & peptide science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
–field-weighted citation impact
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

56 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. PARG Protein Regulation Roles inInternational journal of molecular sciences · 2024
    Article
  9. A ribose-functionalized NADChemical communications (Cambridge, England) · 2023
    Article
  10. Article
  11. Article
  12. Characterization of anPathogens (Basel, Switzerland) · 2023
    Article
  13. Evolution of the Development of PARP Inhibitors.Cancer treatment and research · 2023
    Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Article
  20. Functional roles of ADP-ribosylation writers, readers and erasers.Frontiers in cell and developmental biology · 2022
    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

2 authors.

Chao Liu
Xiaochun YuDepartment of Internal Medicine, University of Michigan Medical School, Ann Arbor, MI 48109, USA. xiayu@umich.edu.

Funding

Regulation of Ionizing Radiation-Induced DNA Damage ResponseR01CA130899 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI LIU, YILUN · 2009 to 2023
$5.5M
Molecular Mechanisms of BRCA1-Dependent DNA Damage Response and TumorogenesisR01CA132755 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI SHEN, BINGHUI · 2008 to 2019
$3.5M
Functional analysis of BRCA1 in DNA damage response and tumor suppressionR01CA187209 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI YU, XIAOCHUN · 2014 to 2018
$1.7M
Functional analysis of the TET2/OGT complex in epigenetic modificationsR01GM108647 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI YU, XIAOCHUN · 2015 to 2018
$1.3M
NCI NIH HHS CA130899NCI NIH HHS CA132755NCI NIH HHS CA187209NCI NIH HHS R01 CA130899NCI NIH HHS R01 CA132755NCI NIH HHS R01 CA187209NIGMS NIH HHS R01 GM108647
6 · The paper itself

Abstract

Protein ADP-ribosylation is an important posttranslational modification that plays versatile roles in multiple biological processes. ADP-ribosylation is catalyzed by a group of enzymes known as ADP-ribosyltransferases (ARTs). Using nicotinamide adenine dinucleotide (NAD(+)) as the donor, ARTs covalently link single or multiple ADP-ribose moieties from NAD(+) to the substrates, forming mono ADP-ribosylation or poly ADP-ribosylation (PARylation). Novel functions of ARTs and ADPribosylation have been revealed over the past few years. Here we summarize the current knowledge on ARTs and PARylation.

Indexed as

Protein Processing, Post-TranslationalADP Ribose TransferasesAnimalsCatalysisChromatin Assembly and DisassemblyDNA DamageHumansNADPoly(ADP-ribose) PolymerasesProtein BindingProtein Interaction Domains and MotifsADP Ribose TransferasesNADPoly(ADP-ribose) Polymerases

Identifiers

PMID25938242
PMCPMC4725697

What OpenQuestion holds

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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.