Evidence map›Paper›PMID 37626888›Full record

ArticleCells2023

Poly(ADP-Ribose) Polymerase-1 Lacking Enzymatic Activity Is Not Compatible with Mouse Development.

Tatiana Kamaletdinova, Wen Zong, Pavel Urbánek, Sijia Wang, Mara Sannai, Paulius Grigaravičius, Wenli Sun, Zahra Fanaei-Kahrani, Aswin Mangerich, Michael O Hottiger and 2 more

Open access · goldAbstract read
In one paragraph

Article in Cells, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
1.8field-weighted citation impact, top 13% 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

3 citing papers in PubMed, 8 citations in OpenAlex.

  1. Article
  2. Article
  3. PARP1 UFMylation ensures the stability of stalled replication forks.Proceedings of the National Academy of Sciences of the United States of America · 2024
    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

12 authors at 4 institutions in 3 countries.

Tatiana KamaletdinovaLeibniz Institute on Aging-Fritz Lipmann Institute (FLI), 07745 Jena, Germany.
Wen ZongState Key Laboratory of Microbial Technology, Shandong University, 72 Binhai Road, Qingdao 266237, China.ORCID 0000-0001-7800-128X
Pavel UrbánekLeibniz Institute on Aging-Fritz Lipmann Institute (FLI), 07745 Jena, Germany.
Sijia WangState Key Laboratory of Microbial Technology, Shandong University, 72 Binhai Road, Qingdao 266237, China.
Mara SannaiLeibniz Institute on Aging-Fritz Lipmann Institute (FLI), 07745 Jena, Germany.ORCID 0000-0001-9634-004X
Paulius GrigaravičiusLeibniz Institute on Aging-Fritz Lipmann Institute (FLI), 07745 Jena, Germany.
Wenli SunState Key Laboratory of Microbial Technology, Shandong University, 72 Binhai Road, Qingdao 266237, China.
Zahra Fanaei-KahraniLeibniz Institute on Aging-Fritz Lipmann Institute (FLI), 07745 Jena, Germany.
Aswin MangerichMolecular Toxicology, Department of Biology, University of Konstanz, 78464 Konstanz, Germany.ORCID 0000-0001-9742-2338
Michael O HottigerDepartment of Molecular Mechanisms of Disease, University of Zürich, 8057 Zürich, Switzerland.ORCID 0000-0002-7323-2270
Tangliang LiState Key Laboratory of Microbial Technology, Shandong University, 72 Binhai Road, Qingdao 266237, China.ORCID 0000-0003-0671-9166
Zhao-Qi WangLeibniz Institute on Aging-Fritz Lipmann Institute (FLI), 07745 Jena, Germany.ORCID 0000-0002-8336-3485
Leibniz Institute on Aging - Fritz Lipmann Institute (FLI) · DEShandong University · CNUniversity of Potsdam · DEUniversity of Zurich · CH

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Poly(ADP-ribose) polymerase-1 (PARP1) binds DNA lesions to catalyse poly(ADP-ribosyl)ation (PARylation) using NAD+ as a substrate. PARP1 plays multiple roles in cellular activities, including DNA repair, transcription, cell death, and chromatin remodelling. However, whether these functions are governed by the enzymatic activity or scaffolding function of PARP1 remains elusive. In this study, we inactivated in mice the enzymatic activity of PARP1 by truncating its C-terminus that is essential for ART catalysis (PARP1

Indexed as

ChromatinPoly(ADP-ribose) PolymerasesAnimalsBlastocystCatalysisMicePoly (ADP-Ribose) Polymerase-1ChromatinPoly (ADP-Ribose) Polymerase-1Poly(ADP-ribose) Polymerasescatalytic activitydevelopmentES cell differentiationgenotoxic stressPARP1PARP2

Identifiers

PMID37626888
PMCPMC10453916
OpenAlexW4385873338

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.