Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Labeling of Specific Residues of the Multidrug Transporter AcrB with Its Fluorescent Substrate.

Methods in molecular biology (Clifton, N.J.) - 1 Jan 2026

Kobayashi Naoki

Abstract excerpt

Gram-negative bacteria possess resistance nodulation cell division (RND)-type drug efflux transporters in the inner membrane that confer a high degree of intrinsic resistance to various drugs. Escherichia coli expresses the most powerful RND-type drug efflux transporter, AcrB, which extrudes various chemical compounds, including antibiotics, by forming a complex with the periplasmic membrane fusion protein AcrA...

Read the complete abstract on PubMed

Topics

Escherichia coli Proteins
ATP-Binding Cassette, Sub-Family C Proteins
Escherichia coli
Fluorescent Dyes
Binding Sites
Rhodamines

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Cysteine

Iodoacetamide

Bacterial Outer Membrane Proteins

Substrate Specificity

Staining and Labeling

Membrane Transport Proteins

Mutation

Lipoproteins

Source

Identifiers

PMID: 42681246
DOI: 10.1007/978-1-0716-5316-6_5

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 25 Oct 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Labeling of Specific Residues of the Multidrug Transporter AcrB with Its Fluorescent Substrate.PMID 42681246Read ↗

Molecular construction of a multidrug exporter system, AcrAB: molecular interaction between AcrA and AcrB, and cleavage of the N-terminal signal sequence of AcrA.Semantic proximity Read ↗

Evidence of a Substrate-Discriminating Entrance Channel in the Lower Porter Domain of the Multidrug Resistance Efflux Pump AcrB.Semantic proximity Read ↗

Conformational flexibility in the multidrug efflux system protein AcrA.Semantic proximity Read ↗

Functional relevance of AcrB Trimerization in pump assembly and substrate binding.Semantic proximity Read ↗

Structures of the multidrug exporter AcrB reveal a proximal multisite drug-binding pocket.Semantic proximity Read ↗

Role of a conserved residue R780 in Escherichia coli multidrug transporter AcrB.Semantic proximity Read ↗

Allosteric drug transport mechanism of multidrug transporter AcrB.Semantic proximity Read ↗

Reversal of the Drug Binding Pocket Defects of the AcrB Multidrug Efflux Pump Protein of Escherichia coli.Semantic proximity Read ↗

Perturbed structural dynamics underlie inhibition and altered efflux of the multidrug resistance pump AcrB.Semantic proximity Read ↗

Chlorpromazine and Amitriptyline Are Substrates and Inhibitors of the AcrB Multidrug Efflux Pump.Semantic proximity Read ↗

Mechanisms of RND multidrug efflux pumps.Semantic proximity Read ↗

Molecular determinant deciphering of MIC-guided RND efflux substrates in E. coliSemantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.