Evidence map›Paper›PMID 21858024›Full record

ArticlePloS one2011

Permeation through the cell membrane of a boron-based β-lactamase inhibitor.

Manuela Minozzi, Gianluca Lattanzi, Roland Benz, Maria P Costi, Alberto Venturelli, Paolo Carloni

Abstract read
In one paragraph

Article in PloS one, 2011. 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
–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

7 citing papers in PubMed.

  1. Review
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  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

6 authors.

Manuela MinozziModeling & Simulation Lab Department of Studies on Structures, University Roma Tre, Roma, Italy.
Gianluca Lattanzi
Roland Benz
Maria P Costi
Alberto Venturelli
Paolo Carloni

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 GM63815NIGMS NIH HHS R01 GM063815
6 · The paper itself

Abstract

Bacteria express beta-lactamases to counteract the beneficial action of antibiotics. Benzo[b]-thiophene-2-boronic acid (BZB) derivatives are β-lactamase inhibitors and, as such, promising compounds to be associated with β-lactam antibacterial therapies. The uncharged form of BZB, in particular, is suggested to diffuse through the outer membrane of gram negative bacteria. In this study, through the combination of electrophysiological experiments across reconstituted PC/n-decane bilayers and metadynamics-based free energy calculations, we investigate the permeation mechanism of boronic compounds. Our experimental data establish that BZB passes through the membrane, while computer simulations provide hints for the existence of an aqueous, water-filled monomolecular channel. These findings provide new perspectives for the design of boronic acid derivatives with high membrane permeability.

Indexed as

beta-Lactamase InhibitorsBacterial Proteinsbeta-Lactam ResistanceBoronic AcidsCell MembraneCell Membrane PermeabilityComputer SimulationDrug DesignElectrophysiologyEnzyme InhibitorsGram-Negative BacteriaKineticsLipid BilayersMolecular StructurePhosphatidylcholinesThiophenes1-palmitoyl-2-oleoylphosphatidylcholineBacterial Proteinsbenzo(b)thiophene-2-boronic acidbeta-Lactamase InhibitorsBoronic AcidsEnzyme InhibitorsLipid BilayersPhosphatidylcholinesThiophenes

Identifiers

PMID21858024
PMCPMC3157353

What OpenQuestion holds

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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.