Evidence map›Paper›PMID 29327913›Full record

ReviewBiochemistry2018

Proteomic Analysis of the Downstream Signaling Network of PARP1.

Yuanli Zhen, Yonghao Yu

Abstract readReview
In one paragraph

Review in Biochemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing 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

26 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. The multifaceted role of PARP1 in RNA biogenesis.Wiley interdisciplinary reviews. RNA · 2021
    Review
  14. A Bifunctional NADACS chemical biology · 2021
    Article
  15. Article
  16. ADPriboDB v2.0: An Updated Database of ADP-ribosylated Proteins.bioRxiv : the preprint server for biology · 2020
    Article
  17. Article
  18. Review
  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

2 authors.

Yuanli ZhenDepartment of Biochemistry, University of Texas Southwestern Medical Center , Dallas, Texas 75390, United States.
Yonghao YuDepartment of Biochemistry, University of Texas Southwestern Medical Center , Dallas, Texas 75390, United States.ORCID 0000-0001-8414-4666

Funding

Mass spectrometric approaches to protein ADP-ribosylationR01GM122932 · NIGMS · UT SOUTHWESTERN MEDICAL CENTER · PI YU, YONGHAO · 2017 to 2019
$1.1M
NIGMS NIH HHS R01 GM122932
6 · The paper itself

Abstract

Poly-ADP-ribosylation (PARylation) is a protein posttranslational modification (PTM) that is critically involved in many biological processes that are linked to cell stress responses. It is catalyzed by a class of enzymes known as poly-ADP-ribose polymerases (PARPs). In particular, PARP1 is a nuclear protein that is activated upon sensing nicked DNA. Once activated, PARP1 is responsible for the synthesis of a large number of PARylated proteins and initiation of the DNA damage response mechanisms. This observation provided the rationale for developing PARP1 inhibitors for the treatment of human malignancies. Indeed, three PARP1 inhibitors (Olaparib, Rucaparib, and Niraparib) have recently been approved by the Food and Drug Administration for the treatment of ovarian cancer. Moreover, in 2017, both Olaparib and Niraparib have also been approved for the treatment of fallopian tube cancer and primary peritoneal cancer. Despite this very exciting progress in the clinic, the basic signaling mechanism that connects PARP1 to a diverse array of biological processes is still poorly understood. This is, in large part, due to the inherent technical difficulty associated with the analysis of protein PARylation, which is a low-abundance, labile, and heterogeneous PTM. The study of PARylation has been greatly facilitated by the recent advances in mass spectrometry-based proteomic technologies tailored to the analysis of this modification. In this Perspective, we discuss these breakthroughs, including their technical development, and applications that provide a global view of the many biological processes regulated by this important protein modification.

Indexed as

Poly ADP RibosylationProteomicsSignal TransductionAntineoplastic AgentsClinical Trials as TopicDrug DesignEnzyme ActivationFemaleHumansMaleMass SpectrometryMolecular Targeted TherapyNeoplasm ProteinsNeoplasmsPoly Adenosine Diphosphate RibosePoly (ADP-Ribose) Polymerase-1Antineoplastic AgentsNeoplasm ProteinsPoly Adenosine Diphosphate RibosePoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) Polymerase Inhibitors

Identifiers

PMID29327913
PMCPMC5790594

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.