Evidence map›Paper›PMID 29255163›Full record

ArticleScientific reports2017

Computational and biological profile of boronic acids for the detection of bacterial serine- and metallo-β-lactamases.

Matteo Santucci, Francesca Spyrakis, Simon Cross, Antonio Quotadamo, Davide Farina, Donatella Tondi, Filomena De Luca, Jean-Denis Docquier, Ana Isabel Prieto, Claudia Ibacache and 4 more

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.8field-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

19 citing papers in PubMed, 39 citations in OpenAlex.

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  5. Molecules (Basel, Switzerland) · 2022
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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

14 authors at 7 institutions in 3 countries.

Matteo SantucciDepartment of Life Sciences, University of Modena and Reggio Emilia, Via Campi 103, 41125, Modena, Italy.
Francesca SpyrakisDepartment of Life Sciences, University of Modena and Reggio Emilia, Via Campi 103, 41125, Modena, Italy.
Simon CrossMolecular Discovery Limited, 215 Marsh Road, Pinner Middlesex, London, HA5-5NE, United Kingdom.
Antonio QuotadamoDepartment of Life Sciences, University of Modena and Reggio Emilia, Via Campi 103, 41125, Modena, Italy.
Davide FarinaDepartment of Life Sciences, University of Modena and Reggio Emilia, Via Campi 103, 41125, Modena, Italy.
Donatella TondiDepartment of Life Sciences, University of Modena and Reggio Emilia, Via Campi 103, 41125, Modena, Italy.
Filomena De LucaDipartimento di Biotecnologie Mediche, University of Siena, Viale Bracci 16, 53100, Siena, Italy.
Jean-Denis DocquierDipartimento di Biotecnologie Mediche, University of Siena, Viale Bracci 16, 53100, Siena, Italy.
Ana Isabel PrietoBiomedicine Institute of Sevilla (IBIS)-CSIC, Avda. Manuel Siurot, sn., Sevilla, Spain.
Claudia IbacacheNational Center of Biotechnology-CSIC, Calle Darwin, 3, 28049, Madrid, Spain.
Jesús BlázquezBiomedicine Institute of Sevilla (IBIS)-CSIC, Avda. Manuel Siurot, sn., Sevilla, Spain.
Alberto VenturelliDepartment of Life Sciences, University of Modena and Reggio Emilia, Via Campi 103, 41125, Modena, Italy. a.venturelli@tydockpharma.com.
Gabriele CrucianiDepartment of Chemistry, Biology and Biotechnology, University of Perugia, Via Elce di Sotto 8, 06123, Perugia, Italy. gabri@chemiome.chm.unipg.it.
Maria Paola CostiDepartment of Life Sciences, University of Modena and Reggio Emilia, Via Campi 103, 41125, Modena, Italy. mariapaola.costi@unimore.it.
University of Modena and Reggio Emilia · ITInstituto de Biomedicina de Sevilla · ESUniversity of Siena · ITCentro Nacional de Biotecnología · ESMolecular Discovery (United Kingdom) · GBTydock Pharma (Italy) · ITUniversity of Perugia · IT

Funding

Structure, Function and Inhibition of Beta-LactamasesR01GM063815 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI SHOICHET, BRIAN K · 2001 to 2013
$2.9M
NIGMS NIH HHS R01 GM063815
6 · The paper itself

Abstract

β-Lactamases (BLs) able to hydrolyze β-lactam antibiotics and more importantly the last resort carbapenems, represent a major mechanism of resistance in Gram-negative bacteria showing multi-drug or extensively drug resistant phenotypes. The early detection of BLs responsible of resistant infections is challenging: approaches aiming at the identification of new BLs inhibitors (BLI) can thus serve as the basis for the development of highly needed diagnostic tools. Starting from benzo-[b]-thiophene-2-boronic acid (BZB), a nanomolar inhibitor of AmpC β-lactamase (K

Indexed as

Anti-Bacterial AgentsBacteriaBacterial Proteinsbeta-Lactamase Inhibitorsbeta-LactamasesBoronic AcidsCefotaximeCeftazidimeComputational BiologyDrug Resistance, BacterialEnterobacteriaceae InfectionsMicrobial Sensitivity TestsAmpC beta-lactamasesAnti-Bacterial AgentsBacterial Proteinsbeta-Lactamase Inhibitorsbeta-LactamasesBoronic AcidscarbapenemaseCefotaximeCeftazidime

Identifiers

PMID29255163
PMCPMC5735191
OpenAlexW2771721896

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.