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

Analysis of AcrB and AcrB/DARPin ligand complexes by LILBID MS.

Biochimica et biophysica acta - 1 Sept 2011

Brandstätter Lorenz, Sokolova Lucie, Eicher Thomas, Seeger Markus A, Briand Christophe, Cha Hi-Jea, Cernescu Mihaela, Bohnert Jürgen, Kern Winfried V, Brutschy Bernd, Pos Klaas M

Abstract excerpt

The AcrA/AcrB/TolC complex is responsible for intrinsic multidrug resistance (MDR) in Escherichia coli. Together with the periplasmic adaptor protein AcrA and the outer membrane channel TolC, the inner membrane component AcrB forms an efflux complex that spans both the inner and outer membrane and bridges the periplasm of the Gram-negative cell. Within the entire tripartite complex, homotrimeric AcrB plays a...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Ankyrin Repeat
Share to Chromatography, Thin Layer

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Crystallization

Share to Detergents

Share to Electrophoresis

Share to Electrophoresis, Capillary

Share to Micelles

Share to Ultracentrifugation

Source

Identifiers

PMID: 21616055
DOI: 10.1016/j.bbamem.2011.05.009

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Analysis of AcrB and AcrB/DARPin ligand complexes by LILBID MS.PMID 21616055Read ↗

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

Crystal structure of AcrB complexed with linezolid at 3.5 Å resolutionSemantic proximity Read ↗

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

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 ↗

Sequential mechanism of assembly of multidrug efflux pump AcrAB-TolC.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 ↗

AcrB trimer stability and efflux activity, insight from mutagenesis studies.Semantic proximity Read ↗

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

A periplasmic coiled-coil interface underlying TolC recruitment and the assembly of bacterial drug efflux pumps.Semantic proximity Read ↗

Identification of Binding Sites for Efflux Pump Inhibitors of the AcrAB-TolC Component AcrA.Semantic proximity Read ↗

Multiple entry pathways within the efflux transporter AcrB contribute to multidrug recognition.Semantic proximity Read ↗

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