Evidence map›Paper›PMID 32817098›Full record

ArticleJournal of bacteriology2020

Molecular Structure and Functional Analysis of Pyocin S8 from Pseudomonas aeruginosa Reveals the Essential Requirement of a Glutamate Residue in the H-N-H Motif for DNase Activity.

Helena Turano, Fernando Gomes, Renato M Domingos, Maximilia F S Degenhardt, Cristiano L P Oliveira, Richard C Garratt, Nilton Lincopan, Luis E S Netto

Open access · greenAbstract read
In one paragraph

Article in Journal of bacteriology, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.

0numbers the graph read from it
0cells of the map it votes in
6citing papers in PubMed
0.2field-weighted citation impact, top 50% 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

6 citing papers in PubMed, 7 citations in OpenAlex.

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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

8 authors at 2 institutions in 2 countries.

Helena TuranoDepartamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, São Paulo, Brazil.
Fernando GomesDepartamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, São Paulo, Brazil.
Renato M DomingosInstituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa, Oeiras, Portugal.
Maximilia F S DegenhardtDepartamento de Física Experimental, Instituto de Física, Universidade de São Paulo, São Paulo, Brazil.
Cristiano L P OliveiraDepartamento de Física Experimental, Instituto de Física, Universidade de São Paulo, São Paulo, Brazil.
Richard C GarrattDepartamento de Física e Ciência Interdisciplinar, Instituto de Física de São Carlos, Universidade de São Paulo, São Carlos, Brazil.
Nilton LincopanDepartamento de Microbiologia, Instituto de Ciências Biomédicas, Universidade de São Paulo, São Paulo, Brazil.ORCID 0000-0003-0161-5800
Luis E S NettoDepartamento de Genética e Biologia Evolutiva, Instituto de Biociências, Universidade de São Paulo, São Paulo, Brazil nettoles@ib.usp.br.ORCID 0000-0002-4250-9177
Universidade de São Paulo · BRUniversidade Nova de Lisboa · PT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Multidrug resistance (MDR) is a serious threat to public health, making the development of new antimicrobials an urgent necessity. Pyocins are protein antibiotics produced by

Indexed as

Amino Acid MotifsAnti-Bacterial AgentsDeoxyribonuclease IGlutamic AcidPseudomonas aeruginosaPyocinsStructure-Activity RelationshipAnti-Bacterial AgentsDeoxyribonuclease IGlutamic AcidPyocinsH-N-H motifMDRmetalsmultidrug resistanceprotein structureprotein structure-functionPseudomonas aeruginosapyocin

Identifiers

PMID32817098
PMCPMC7549359
OpenAlexW3049197602

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.