Evidence map›Paper›PMID 22673905›Full record

ArticleNature communications2012

Structure and mechanism of a canonical poly(ADP-ribose) glycohydrolase.

Mark S Dunstan, Eva Barkauskaite, Pierre Lafite, Claire E Knezevic, Amy Brassington, Marijan Ahel, Paul J Hergenrother, David Leys, Ivan Ahel

Open access · bronzeAbstract read
PubMed Publisher
In one paragraph

Article in Nature communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

55 citing papers in PubMed, 90 citations in OpenAlex.

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  18. ADP-ribosylation systems in bacteria and viruses.Computational and structural biotechnology journal · 2021
    Review
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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

9 authors at 5 institutions in 4 countries.

Mark S DunstanManchester Interdisciplinary Biocentre, Princess Street 131, M1 7DN, Manchester, UK.
Eva Barkauskaite
Pierre Lafite
Claire E Knezevic
Amy Brassington
Marijan Ahel
Paul J Hergenrother
David Leys
Ivan Ahel
University of Illinois Urbana-Champaign · USCancer Research UK Manchester Institute · GBCentre National de la Recherche Scientifique · FRRudjer Boskovic Institute · HRUniversity of Manchester · GB

Funding

Cancer Research UK
6 · The paper itself

Abstract

Poly(ADP-ribosyl)ation is a reversible post-translational protein modification involved in the regulation of a number of cellular processes including DNA repair, chromatin structure, mitosis, transcription, checkpoint activation, apoptosis and asexual development. The reversion of poly(ADP-ribosyl)ation is catalysed by poly(ADP-ribose) (PAR) glycohydrolase (PARG), which specifically targets the unique PAR (1''-2') ribose-ribose bonds. Here we report the structure and mechanism of the first canonical PARG from the protozoan Tetrahymena thermophila. In addition, we reveal the structure of T. thermophila PARG in a complex with a novel rhodanine-containing mammalian PARG inhibitor RBPI-3. Our data demonstrate that the protozoan PARG represents a good model for human PARG and is therefore likely to prove useful in guiding structure-based discovery of new classes of PARG inhibitors.

Indexed as

Glycoside HydrolasesHumansPhylogenyProtein Structure, SecondaryProtein Structure, TertiaryTetrahymena thermophilaGlycoside Hydrolasespoly ADP-ribose glycohydrolase

Identifiers

PMID22673905
OpenAlexW2070855001

What OpenQuestion holds

Textmetadata
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.