Evidence map›Paper›PMID 32029451›Full record

ReviewGenes & development2020

(ADP-ribosyl)hydrolases: structure, function, and biology.

Johannes Gregor Matthias Rack, Luca Palazzo, Ivan Ahel

Abstract readReview
In one paragraph

Review in Genes & development, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 123 papers.

0numbers the graph read from it
0cells of the map it votes in
123citing 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

123 citing papers in PubMed.

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63 more citing papers are in PubMed but not listed here.

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.

Johannes Gregor Matthias Rack *Sir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom.
Luca Palazzo *Institute for the Experimental Endocrinology and Oncology, National Research Council of Italy, 80145 Naples, Italy.
Ivan AhelSir William Dunn School of Pathology, University of Oxford, Oxford OX1 3RE, United Kingdom.

Funding

Biotechnology and Biological Sciences Research Council BB/R007195/1Cancer Research UK 22284Cancer Research UK C35050/A22284Wellcome Trust 101794Wellcome Trust 210634
6 · The paper itself

Abstract

ADP-ribosylation is an intricate and versatile posttranslational modification involved in the regulation of a vast variety of cellular processes in all kingdoms of life. Its complexity derives from the varied range of different chemical linkages, including to several amino acid side chains as well as nucleic acids termini and bases, it can adopt. In this review, we provide an overview of the different families of (ADP-ribosyl)hydrolases. We discuss their molecular functions, physiological roles, and influence on human health and disease. Together, the accumulated data support the increasingly compelling view that (ADP-ribosyl)hydrolases are a vital element within ADP-ribosyl signaling pathways and they hold the potential for novel therapeutic approaches as well as a deeper understanding of ADP-ribosylation as a whole.

Indexed as

Adenosine DiphosphateADP-RibosylationHumansHydrolasesProtein DomainsStructure-Activity RelationshipAdenosine DiphosphateHydrolasesADP-riboseADP-ribosylationARH3catalytic mechanismDNA damageDraGgenome stabilitymacrodomainPARGPARPstructural biology

Identifiers

PMID32029451
PMCPMC7050489

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.