Evidence map›Paper›PMID 26344237›Full record

ArticleCurrent protocols in chemical biology2015

Identifying Direct Protein Targets of Poly-ADP-Ribose Polymerases (PARPs) Using Engineered PARP Variants-Orthogonal Nicotinamide Adenine Dinucleotide (NAD+) Analog Pairs.

Ian Carter-O'Connell, Michael S Cohen

Open access · greenAbstract read
In one paragraph

Article in Current protocols in chemical biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.4field-weighted citation impact, top 17% 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

13 citing papers in PubMed, 18 citations in OpenAlex.

  1. NADRSC chemical biology · 2026
    Review
  2. Review
  3. Review
  4. Article
  5. Role of mono-ADP-ribosylation histone modification (Review).Experimental and therapeutic medicine · 2021
    Review
  6. Review
  7. Article
  8. Forced Self-Modification Assays as a Strategy to Screen MonoPARP Enzymes.SLAS discovery : advancing life sciences R & D · 2020
    Article
  9. Article
  10. Review
  11. Detecting Protein ADP-Ribosylation Using a Clickable Aminooxy Probe.Methods in molecular biology (Clifton, N.J.) · 2017
    Article
  12. Article
  13. Review
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

2 authors at 1 institution in 1 country.

Ian Carter-O'ConnellProgram in Chemical Biology, Department of Physiology and Pharmacology, Oregon Health & Science University, Portland, Oregon.
Michael S CohenProgram in Chemical Biology, Department of Physiology and Pharmacology, Oregon Health & Science University, Portland, Oregon.
Oregon Health & Science University · US

Funding

Decoding protein MARylation networks in astrocytes using chemical biology approachesR01NS088629 · NINDS · OREGON HEALTH & SCIENCE UNIVERSITY · PI COHEN, MICHAEL S · 2014 to 2024
$4.2M
NINDS NIH HHS 1R01NS088629NINDS NIH HHS R01 NS088629
6 · The paper itself

Abstract

Poly-ADP-ribose polymerases (PARPs) comprise a family of 17 distinct enzymes that catalyze the transfer of ADP-ribose from nicotinamide adenine dinucleotide (NAD+) to acceptor sites on protein targets. PARPs have been implicated in a number of essential signaling pathways regulating both normal cell function and pathophysiology. To understand the physiological role of each PARP family member in the cell we need to identify the direct targets for each unique PARP in a cellular context. PARP-family member-specific target identification is challenging because of their shared catalytic mechanism and functional redundancy. To address this challenge, we have engineered a PARP variant that efficiently uses an orthogonal NAD+ analog, an analog that endogenous PARPs cannot use, as a substrate for ADP-ribosylation. The protocols in this unit describe a general procedure for using engineered PARP variants-orthogonal NAD+ analog pairs for labeling and identifying the direct targets of the poly-subfamily of PARPs (PARPs 1-3, 5, and 6).

Indexed as

HEK293 CellsHumansNADPoly(ADP-ribose) PolymerasesProtein EngineeringProtein IsoformsNADPoly(ADP-ribose) PolymerasesProtein IsoformsADPrADP-riboseADP-ribosylationclick chemistryPARPpoly-ADP-ribose polymerasepost-translational modificationproteins

Identifiers

PMID26344237
PMCPMC4562056
OpenAlexW1551109800

What OpenQuestion holds

Textmetadata
LicenceTDM
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.