Evidence map›Paper›PMID 39057953›Full record

ReviewToxins2024

General ADP-Ribosylation Mechanism Based on the Structure of ADP-Ribosyltransferase-Substrate Complexes.

Hideaki Tsuge, Noriyuki Habuka, Toru Yoshida

Abstract readReview
In one paragraph

Review in Toxins, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

0numbers the graph read from it
0cells of the map it votes in
1citing 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

1 citing paper in PubMed.

  1. 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.

Hideaki TsugeFaculty of Life Sciences, Kyoto Sangyo University, Kyoto 6038555, Japan.ORCID 0000-0003-0166-9163
Noriyuki HabukaFaculty of Life Sciences, Kyoto Sangyo University, Kyoto 6038555, Japan.
Toru YoshidaFaculty of Sciences, Japan Women's University, Tokyo 1120015, Japan.ORCID 0000-0002-1384-2210

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ADP-ribosylation is a ubiquitous modification of proteins and other targets, such as nucleic acids, that regulates various cellular functions in all kingdoms of life. Furthermore, these ADP-ribosyltransferases (ARTs) modify a variety of substrates and atoms. It has been almost 60 years since ADP-ribosylation was discovered. Various ART structures have been revealed with cofactors (NAD

Indexed as

ADP Ribose TransferasesADP-RibosylationAnimalsHumansNADSubstrate SpecificityADP Ribose TransferasesNADADP-ribosylationADP-ribosyltransferasecomplexsubstrate recognition

Identifiers

PMID39057953
PMCPMC11281641

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.