Evidence map›Paper›PMID 33430384›Full record

ReviewToxins2021

Common Mechanism for Target Specificity of Protein- and DNA-Targeting ADP-Ribosyltransferases.

Toru Yoshida, Hideaki Tsuge

Open access · goldAbstract readReview
In one paragraph

Review in Toxins, 2021. 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
0.9field-weighted citation impact, top 24% 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, 13 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. ADP-ribosylation systems in bacteria and viruses.Computational and structural biotechnology journal · 2021
    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 2 institutions in 1 country.

Toru YoshidaFaculty of Science, Japan Women's University, 2-8-1 Mejirodai, Bunkyo-ku, Tokyo 112-8681, Japan.ORCID 0000-0002-1384-2210
Hideaki TsugeFaculty of Life Sciences, Kyoto Sangyo University, Kamigamo-motoyama, Kita-ku, Kyoto 603-8555, Japan.ORCID 0000-0003-0166-9163
Japan Women's University · JPKyoto Sangyo University · JP

Funding

Japan Society for the Promotion of Science 15K08289Japan Society for the Promotion of Science 17K15095Ministry of Education, Culture, Sports, Science and Technology 23121529Ministry of Education, Culture, Sports, Science and Technology 25121733
6 · The paper itself

Abstract

Many bacterial pathogens utilize ADP-ribosyltransferases (ARTs) as virulence factors. The critical aspect of ARTs is their target specificity. Each individual ART modifies a specific residue of its substrates, which could be proteins, DNA, or antibiotics. However, the mechanism underlying this specificity is poorly understood. Here, we review the substrate recognition mechanism and target residue specificity based on the available complex structures of ARTs and their substrates. We show that there are common mechanisms of target residue specificity among protein- and DNA-targeting ARTs.

Indexed as

ADP Ribose TransferasesBacteriaGene Expression Regulation, BacterialGene Expression Regulation, EnzymologicProtein ConformationSubstrate SpecificityADP Ribose TransferasesADP-ribosyltransferasecomplex structure of enzyme and substratesubstrate recognitiontarget residue specificity

Identifiers

PMID33430384
PMCPMC7827354
OpenAlexW3119417530

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.