Evidence map›Paper›PMID 31077644›Full record

ReviewBiochemical pharmacology2019

Poly(ADP-ribose)-dependent ubiquitination and its clinical implications.

Christina A Vivelo, Vinay Ayyappan, Anthony K L Leung

Open access · greenAbstract readReview
In one paragraph

Review in Biochemical pharmacology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
1.6field-weighted citation impact, top 15% 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

33 citing papers in PubMed, 53 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Covalent Probes To CaptureJournal of the American Chemical Society · 2024
    Article
  12. Article
  13. Article
  14. Review
  15. Article
  16. Decoding Ubiquitin Modifications by Mass Spectrometry.Advances in experimental medicine and biology · 2024
    Review
  17. 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

3 authors at 1 institution in 1 country.

Christina A ViveloDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD, USA.
Vinay AyyappanDepartment of Biomedical Engineering, Johns Hopkins University, Baltimore, MD, USA.
Anthony K L LeungDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD, USA; Department of Molecular Biology and Genetics, School of Medicine, Johns Hopkins University, Baltimore, MD, USA; Department of Oncology, School of Medicine, Johns Hopkins University, Baltimore, MD, USA. Electronic address: anthony.leung@jhu.edu.
Johns Hopkins University · US

Funding

TRAINING IN AREAS FUNDAMENTAL TO CANCER RESEARCHT32CA009110 · NCI · JOHNS HOPKINS UNIVERSITY · PI MATUNIS, MICHAEL J., WEERARATNA, ASHANI T · 1985 to 2025
$13.1M
Networks, Pathways and Dynamics of Lysine ModificationU54GM103520 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BADER, JOEL S. · 2012 to 2013
$7.0M
Role of ADP-Ribosylation in Stress Granules-Equipment SupplementR01GM104135 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Anthony K L Leung · 2015 to 2026
$4.2M
NCI NIH HHS T32 CA009110NIGMS NIH HHS R01 GM104135NIGMS NIH HHS U54 GM103520
6 · The paper itself

Abstract

ADP-ribosylation-the addition of one or multiple ADP-ribose units onto proteins-is a therapeutically important post-translational modification implicated in cancer, neurodegeneration, and infectious diseases. The protein modification regulates a broad range of biological processes, including DNA repair, transcription, RNA metabolism, and the structural integrity of nonmembranous structures. The polymeric form of ADP-ribose, poly(ADP-ribose), was recently identified as a signal for triggering protein degradation through the ubiquitin-proteasome system. Using informatics analyses, we found that these ubiquitinated substrates tend to be low abundance proteins, which may serve as rate-limiting factors within signaling networks or metabolic processes. In this review, we summarize the current literature on poly(ADP-ribose)-dependent ubiquitination (PARdU) regarding its biological mechanisms, substrates, and relevance to diseases.

Indexed as

AnimalsDNA RepairHumansPoly Adenosine Diphosphate RiboseProtein Structure, SecondaryUbiquitinationPoly Adenosine Diphosphate RiboseADP-ribosylationPoly(ADP-ribose)Poly(ADP-ribose)-dependent ubiquitinationProtein degradationRate-limiting factorsTankyraseUbiquitin-proteasome system

Identifiers

PMID31077644
PMCPMC6702056
OpenAlexW2944132034

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.