Evidence map›Paper›PMID 30712989›Full record

ArticleMolecular cell2019

ELTA: Enzymatic Labeling of Terminal ADP-Ribose.

Yoshinari Ando, Elad Elkayam, Robert Lyle McPherson, Morgan Dasovich, Shang-Jung Cheng, Jim Voorneveld, Dmitri V Filippov, Shao-En Ong, Leemor Joshua-Tor, Anthony K L Leung

Abstract read
In one paragraph

Article in Molecular cell, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing 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

48 citing papers in PubMed.

  1. Article
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  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Article
  11. Poly-ADP-ribosylation dynamics, signaling, and analysis.Environmental and molecular mutagenesis · 2024
    Review
  12. Poly ADP-ribose signaling is dysregulated in Huntington disease.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
  18. Review
  19. Switch-like compaction of poly(ADP-ribose) upon cation binding.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  20. 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

10 authors.

Yoshinari AndoDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA.
Elad ElkayamKeck Structural Biology Laboratory, Howard Hughes Medical Institute, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.
Robert Lyle McPhersonDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA.
Morgan DasovichDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA.
Shang-Jung ChengDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA.
Jim VoorneveldGorlaeus Laboratories, Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333 CC Leiden, the Netherlands.
Dmitri V FilippovGorlaeus Laboratories, Leiden Institute of Chemistry, Leiden University, Einsteinweg 55, 2333 CC Leiden, the Netherlands.
Shao-En OngDepartment of Pharmacology, University of Washington, Seattle, WA 98195, USA.
Leemor Joshua-TorKeck Structural Biology Laboratory, Howard Hughes Medical Institute, Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.
Anthony K L LeungDepartment of Biochemistry and Molecular Biology, Bloomberg School of Public Health, Johns Hopkins University, Baltimore, MD 21205, USA; Department of Molecular Biology and Genetics, School of Medicine, Johns Hopkins University, Baltimore, MD 21205, USA; Department of Oncology, School of Medicine, Johns Hopkins University, Baltimore, MD 21205, USA. Electronic address: anthony.leung@jhu.edu.

Funding

Single-Cell Biology Shared ResourceP30CA045508 · NCI · COLD SPRING HARBOR LABORATORY · PI John Edward Moses · 1987 to 2026
$118.9M
TRAINING IN AREAS FUNDAMENTAL TO CANCER RESEARCHT32CA009110 · NCI · JOHNS HOPKINS UNIVERSITY · PI MATUNIS, MICHAEL J., WEERARATNA, ASHANI T · 1985 to 2025
$13.1M
Role of ADP-Ribosylation in Stress Granules-Equipment SupplementR01GM104135 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI Anthony K L Leung · 2015 to 2026
$4.2M
The Chemistry-Biology Interface Program at Johns Hopkins UniversityT32GM080189 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI ROKITA, STEVEN E · 2008 to 2022
$3.5M
Characterizing Muscle Regulatory Elements with Mass Spectrometry-Based ProteomicsR01AR065459 · NIAMS · UNIVERSITY OF WASHINGTON · PI ONG, SHAO-EN · 2013 to 2017
$1.6M
A NanoLC-Orbitrap Tribrid Instrument for Comprehensive Proteomics AnalysesS10OD021502 · OD · UNIVERSITY OF WASHINGTON · PI ONG, SHAO-EN · 2017 to 2017
$906k
NCI NIH HHS P30 CA045508NCI NIH HHS T32 CA009110NIAMS NIH HHS R01 AR065459NIGMS NIH HHS R01 GM104135NIGMS NIH HHS T32 GM080189NIH HHS S10 OD021502
6 · The paper itself

Abstract

ADP-ribosylation refers to the addition of one or more ADP-ribose groups onto proteins. The attached ADP-ribose monomers or polymers, commonly known as poly(ADP-ribose) (PAR), modulate the activities of the modified substrates or their binding affinities to other proteins. However, progress in this area is hindered by a lack of tools to investigate this protein modification. Here, we describe a new method named ELTA (enzymatic labeling of terminal ADP-ribose) for labeling free or protein-conjugated ADP-ribose monomers and polymers at their 2'-OH termini using the enzyme OAS1 and dATP. When coupled with various dATP analogs (e.g., radioactive, fluorescent, affinity tags), ELTA can be used to explore PAR biology with techniques routinely used to investigate DNA or RNA function. We demonstrate that ELTA enables the biophysical measurements of protein binding to PAR of a defined length, detection of PAR length from proteins and cells, and enrichment of sub-femtomole amounts of ADP-ribosylated peptides from cell lysates.

Indexed as

ADP-Ribosylation2',5'-Oligoadenylate SynthetaseAdenosine Diphosphate RiboseAnimalsDeoxyadenine NucleotidesHeLa CellsHumansPoly(ADP-ribose) PolymerasesProtein BindingProtein DomainsSf9 CellsUbiquitin-Protein Ligases2',5'-Oligoadenylate Synthetase2'-deoxy-5'-adenosine monophosphate2'-deoxyadenosine triphosphateAdenosine Diphosphate RiboseDeoxyadenine NucleotidesOAS1 protein, humanPoly(ADP-ribose) PolymerasesRNF146 protein, humanUbiquitin-Protein LigasesADP-riboseADP-ribosylated proteinADP-ribosylationADP-ribosyltransferaseenzymatic labelingmono(ADP-ribosyl)ated proteinoligoadenylate synthetasepoly(ADP-ribose)poly(ADP-ribose) polymerasepoly(ADP-ribosyl)ated protein

Identifiers

PMID30712989
PMCPMC6629254

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Registered trials

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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.