Evidence map›Paper›PMID 38963480›Full record

ArticleSub-cellular biochemistry2024

Structures and Efflux Mechanisms of the AcrAB-TolC Pump.

Zhili Yu, Xiaodong Shi, Zhao Wang

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Article in Sub-cellular biochemistry, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

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0citing papers in PubMed
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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

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3 · Its place in the literature

Who cites it

0 citing papers in PubMed.

No citing paper in PubMed yet.

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

3 authors.

Zhili YuVerna and Marrs McLean Department of Biochemistry and Molecular Pharmacology, Baylor College of Medicine, Houston, TX, USA.
Xiaodong ShiJiangsu Province Key Laboratory of Anesthesiology and Jiangsu Province Key Laboratory of Anesthesia and Analgesia Application, Xuzhou Medical University, Xuzhou, Jiangsu, China.
Zhao WangVerna and Marrs McLean Department of Biochemistry and Molecular Pharmacology, Baylor College of Medicine, Houston, TX, USA. zhaow@bcm.edu.

Funding

Molecular Assembly of Bacterial Tripartite Multidrug Efflux PumpsR01AI179879 · NIAID · BAYLOR COLLEGE OF MEDICINE · PI Zhao Wang · 2024 to 2026
$1.9M
NIAID NIH HHS R01 AI179879
6 · The paper itself

Abstract

The global emergence of multidrug resistance (MDR) in gram-negative bacteria has become a matter of worldwide concern. MDR in these pathogens is closely linked to the overexpression of certain efflux pumps, particularly the resistance-nodulation-cell division (RND) efflux pumps. Inhibition of these pumps presents an attractive and promising strategy to combat antibiotic resistance, as the efflux pump inhibitors can effectively restore the potency of existing antibiotics. AcrAB-TolC is one well-studied RND efflux pump, which transports a variety of substrates, therefore providing resistance to a broad spectrum of antibiotics. To develop effective pump inhibitors, a comprehensive understanding of the structural aspect of the AcrAB-TolC efflux pump is imperative. Previous studies on this pump's structure have been limited to individual components or in vitro determination of fully assembled pumps. Recent advancements in cellular cryo-electron tomography (cryo-ET) have provided novel insights into this pump's assembly and functional mechanism within its native cell membrane environment. Here, we present a summary of the structural data regarding the AcrAB-TolC efflux pump, shedding light on its assembly pathway and operational mechanism.

Indexed as

Bacterial Outer Membrane ProteinsGram-Negative BacteriaMembrane Transport ProteinsAnti-Bacterial AgentsBacterial Outer MembraneDrug Resistance, Multiple, BacterialGene Expression Regulation, BacterialGram-Negative Bacterial InfectionsHumansMultiprotein ComplexesProtein MultimerizationAnti-Bacterial AgentsBacterial Outer Membrane ProteinsMembrane Transport ProteinsMultiprotein ComplexesAcrAB-TolCCryo-EMCryo-ETMultidrug resistanceRND efflux pump

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Registered trials

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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.