Evidence map›Paper›PMID 32966781›Full record

ArticleCell reports2020

Mapping Physiological ADP-Ribosylation Using Activated Ion Electron Transfer Dissociation.

Sara C Buch-Larsen, Ivo A Hendriks, Jean M Lodge, Martin Rykær, Benjamin Furtwängler, Evgenia Shishkova, Michael S Westphall, Joshua J Coon, Michael L Nielsen

Abstract read
In one paragraph

Article in Cell reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing 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

81 citing papers in PubMed.

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  14. Unleashing viral mimicry: A combinatorial strategy to enhance the efficacy of PARP7 inhibitors.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
  15. Article
  16. Article
  17. POLD3 as Controller of Replicative DNA Repair.International journal of molecular sciences · 2024
    Review
  18. Article
  19. Review
  20. Review

21 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

9 authors.

Sara C Buch-LarsenProteomics Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.
Ivo A HendriksProteomics Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.
Jean M LodgeUniversity of Wisconsin-Madison, Madison, WI 53706, USA.
Martin RykærProteomics Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.
Benjamin FurtwänglerProteomics Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark.
Evgenia ShishkovaUniversity of Wisconsin-Madison, Madison, WI 53706, USA.
Michael S WestphallUniversity of Wisconsin-Madison, Madison, WI 53706, USA.
Joshua J CoonUniversity of Wisconsin-Madison, Madison, WI 53706, USA.
Michael L NielsenProteomics Program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark. Electronic address: michael.lund.nielsen@cpr.ku.dk.

Funding

TR&D 2 Metabolic Labels for Ultraplexed Protein Quantification p. 453P41GM108538 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI COON, JOSHUA J · 2016 to 2025
$13.1M
NIGMS NIH HHS P41 GM108538
6 · The paper itself

Abstract

ADP-ribosylation (ADPr) is a post-translational modification that plays pivotal roles in a wide range of cellular processes. Mass spectrometry (MS)-based analysis of ADPr under physiological conditions, without relying on genetic or chemical perturbation, has been hindered by technical limitations. Here, we describe the applicability of activated ion electron transfer dissociation (AI-ETD) for MS-based proteomics analysis of physiological ADPr using our unbiased Af1521 enrichment strategy. To benchmark AI-ETD, we profile 9,000 ADPr peptides mapping to >5,000 unique ADPr sites from a limited number of cells exposed to oxidative stress and identify 120% and 28% more ADPr peptides compared to contemporary strategies using ETD and electron-transfer higher-energy collisional dissociation (EThcD), respectively. Under physiological conditions, AI-ETD identifies 450 ADPr sites on low-abundant proteins, including in vivo cysteine modifications on poly(ADP-ribosyl)polymerase (PARP) 8 and tyrosine modifications on PARP14, hinting at specialist enzymatic functions for these enzymes. Collectively, our data provide insights into the physiological regulation of ADPr.

Indexed as

ElectronsAdenosine Diphosphate RiboseADP-RibosylationHeLa CellsHumansIonsPoly (ADP-Ribose) Polymerase-1Adenosine Diphosphate RiboseIonsPoly (ADP-Ribose) Polymerase-1ADP-ribosylationAI-ETDendoplasmic reticulumglycosylationGolgi apparatusmass spectrometryPARP14PARP8physiological ADPrproteomics

Identifiers

PMID32966781
PMCPMC7508052

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.