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

Negative dominance studies demonstrate the oligomeric structure of EmrE, a multidrug antiporter from Escherichia coli.

The Journal of biological chemistry - 6 Dec 1996

Yerushalmi H, Lebendiker M, Schuldiner S

Abstract excerpt

EmrE, the smallest known ion-coupled transporter, is an Escherichia coli 12-kDa protein 80% helical and soluble in organic solvents. EmrE is a polyspecific antiporter that exchanges hydrogen ions with aromatic toxic cations such as methyl viologen. Since it is many times smaller than the classica...

Read the complete abstract on PubMed

Topics

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

Share to Bacterial Proteins
Share to Carrier Proteins
Share to Escherichia coli

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Escherichia coli Proteins

Share to Membrane Proteins

Share to Mutagenesis, Site-Directed

Share to Phenotype

Share to Protein Conformation

Source

Identifiers

PMID: 8940098
DOI: 10.1074/jbc.271.49.31044

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-8940098-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Negative dominance studies demonstrate the oligomeric structure of EmrE, a multidrug antiporter from Escherichia coli.PMID 8940098Read ↗

Functional Analysis of Novel Multidrug Transporters from Human PathogensSemantic proximity Read ↗

EmrE, a small Escherichia coli multidrug transporter, protects Saccharomyces cerevisiae from toxins by sequestration in the vacuole.Semantic proximity Read ↗

Identification of a glycine motif required for packing in EmrE, a multidrug transporter from Escherichia coli.Semantic proximity Read ↗

Two-component bacterial multidrug transporter, EbrAB: Mutations making each component solely functional.Semantic proximity Read ↗

Specificity determinants in small multidrug transporters.Semantic proximity Read ↗

Functional response of the small multidrug resistance protein EmrE to mutations in transmembrane helix 2.Semantic proximity Read ↗

Transforming a drug/H+ antiporter into a polyamine importer by a single mutation.Semantic proximity Read ↗

Role of sequence bias in the topology of the multidrug transporter EmrE.Semantic proximity Read ↗

Oligomerization of the {gamma}-aminobutyric acid transporter-1 is driven by an interplay of polar and hydrophobic interactions in transmembrane helix II.Semantic proximity Read ↗

Suppressing glucose uptake and acetic acid production increases membrane protein overexpression in Escherichia coli.Semantic proximity Read ↗

The assembly motif of a bacterial small multidrug resistance protein.Semantic proximity Read ↗

The key residue for substrate transport (Glu14) in the EmrE dimer is asymmetric.Semantic proximity Read ↗

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