Evidence map›Paper›PMID 28382184›Full record

ArticleBeilstein journal of organic chemistry2017

Investigation of the action of poly(ADP-ribose)-synthesising enzymes on NAD

Sarah Wallrodt, Edward L Simpson, Andreas Marx

Open access · diamondAbstract read
In one paragraph

Article in Beilstein journal of organic chemistry, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
0.4field-weighted citation impact, top 38% 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

9 citing papers in PubMed, 12 citations in OpenAlex.

  1. NADRSC chemical biology · 2026
    Review
  2. Article
  3. Article
  4. Review
  5. Profiling of the ADP-Ribosylome in Living Cells.Angewandte Chemie (International ed. in English) · 2022
    Article
  6. Review
  7. Article
  8. Article
  9. 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

3 authors at 1 institution in 1 country.

Sarah WallrodtDepartment of Chemistry, University of Konstanz, Universitätsstraße 10, 78457 Konstanz, Germany.
Edward L SimpsonDepartment of Chemistry, University of Konstanz, Universitätsstraße 10, 78457 Konstanz, Germany.
Andreas MarxDepartment of Chemistry, University of Konstanz, Universitätsstraße 10, 78457 Konstanz, Germany.
University of Konstanz · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ADP-ribosyl transferases with diphtheria toxin homology (ARTDs) catalyse the covalent addition of ADP-ribose onto different acceptors forming mono- or poly(ADP-ribos)ylated proteins. Out of the 18 members identified, only four are known to synthesise the complex poly(ADP-ribose) biopolymer. The investigation of this posttranslational modification is important due to its involvement in cancer and other diseases. Lately, metabolic labelling approaches comprising different reporter-modified NAD

Indexed as

ARTDclick chemistryNAD+poly(ADP-ribose)posttranslational modification

Identifiers

PMID28382184
PMCPMC5355910
OpenAlexW2593513826

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.