Evidence map›Paper›PMID 29410655›Full record

ArticleFrontiers in microbiology2018

MacroD1 Is a Promiscuous ADP-Ribosyl Hydrolase Localized to Mitochondria.

Thomas Agnew, Deeksha Munnur, Kerryanne Crawford, Luca Palazzo, Andreja Mikoč, Ivan Ahel

Open access · goldAbstract read
In one paragraph

Article in Frontiers in microbiology, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.3field-weighted citation impact, top 6% 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

38 citing papers in PubMed, 57 citations in OpenAlex.

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  14. Computational and structural biotechnology journal · 2022
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  17. Role of mono-ADP-ribosylation histone modification (Review).Experimental and therapeutic medicine · 2021
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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

6 authors at 2 institutions in 2 countries.

Thomas AgnewSir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.
Deeksha MunnurSir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.
Kerryanne CrawfordSir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.
Luca PalazzoSir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.
Andreja MikočDivision of Molecular Biology, Ruđer Bošković Institute, Zagreb, Croatia.
Ivan AhelSir William Dunn School of Pathology, University of Oxford, Oxford, United Kingdom.
University of Oxford · GBRudjer Boskovic Institute · HR

Funding

Cancer Research UK 22284Wellcome Trust 101794
6 · The paper itself

Abstract

MacroD1 is a macrodomain containing protein that has mono-ADP-ribose hydrolase enzymatic activity toward several ADP-ribose adducts. Dysregulation of MacroD1 expression has been shown to be associated with the pathogenesis of several forms of cancer. To date, the physiological functions and sub-cellular localization of MacroD1 are unclear. Previous studies have described nuclear and cytosolic functions of MacroD1. However, in this study we show that endogenous MacroD1 protein is highly enriched within mitochondria. We also show that MacroD1 is highly expressed in human and mouse skeletal muscle. Furthermore, we show that MacroD1 can efficiently remove ADP-ribose from 5' and 3'-phosphorylated double stranded DNA adducts

Indexed as

ADP-riboseADP-ribosylationDNA damage repairhydrolasemacrodomainmitochondriaPARP

Identifiers

PMID29410655
PMCPMC5787345
OpenAlexW2789782564

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.