Evidence map›Paper›PMID 31176616›Full record

ReviewBiochemical pharmacology2019

Targeting ADP-ribosylation as an antimicrobial strategy.

Giuliana Catara, Annunziata Corteggio, Carmen Valente, Giovanna Grimaldi, Luca Palazzo

Open access · bronzeAbstract readReview
In one paragraph

Review in Biochemical pharmacology, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
1.5field-weighted citation impact, top 16% 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

7 citing papers in PubMed, 28 citations in OpenAlex.

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

5 authors at 2 institutions in 1 country.

Giuliana CataraInstitute of Protein Biochemistry, National Research Council of Italy, Via Pietro Castellino 111, Naples 80131, Italy.
Annunziata CorteggioInstitute of Protein Biochemistry, National Research Council of Italy, Via Pietro Castellino 111, Naples 80131, Italy.
Carmen ValenteInstitute of Protein Biochemistry, National Research Council of Italy, Via Pietro Castellino 111, Naples 80131, Italy.
Giovanna GrimaldiInstitute of Protein Biochemistry, National Research Council of Italy, Via Pietro Castellino 111, Naples 80131, Italy.
Luca PalazzoInstitute of Protein Biochemistry, National Research Council of Italy, Via Pietro Castellino 111, Naples 80131, Italy. Electronic address: l.palazzo@ibp.cnr.it.
National Research Council · ITInstitute of Protein Biochemistry · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

ADP-ribosylation (ADPr) is an ancient reversible modification of cellular macromolecules controlling major biological processes as diverse as DNA damage repair, transcriptional regulation, intracellular transport, immune and stress responses, cell survival and proliferation. Furthermore, enzymatic reactions of ADPr are central in the pathogenesis of many human diseases, including infectious conditions. By providing a review of ADPr signalling in bacterial systems, we highlight the relevance of this chemical modification in the pathogenesis of human diseases depending on host-pathogen interactions. The post-antibiotic era has raised the need to find alternative approaches to antibiotic administration, as major pathogens becoming resistant to antibiotics. An in-depth understanding of ADPr reactions provides the rationale for designing novel antimicrobial strategies for treatment of infectious diseases. In addition, the understanding of mechanisms of ADPr by bacterial virulence factors offers important hints to improve our knowledge on cellular processes regulated by eukaryotic homologous enzymes, which are often involved in the pathogenesis of human diseases.

Indexed as

ADP-RibosylationAnimalsAnti-Infective AgentsDrug Delivery SystemsEndotoxinsHumansSignal TransductionAnti-Infective AgentsEndotoxinsADP-ribosylationADP-ribosyl transferase (ART)Antimicrobial strategiesART bacterial toxinsPoly(ADP-ribose) polymerase (PARP)

Identifiers

PMID31176616
PMCPMC7172630
OpenAlexW2953215807

What OpenQuestion holds

Textmetadata
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.