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

Synergistic substrate binding determines the stoichiometry of transport of a prokaryotic H(+)/Cl(-) exchanger.

Nature structural & molecular biology - 8 Apr 2012

Picollo Alessandra, Xu Yanyan, Johner Niklaus, Bernèche Simon, Accardi Alessio

Abstract excerpt

Active exchangers dissipate the gradient of one substrate to accumulate nutrients, export xenobiotics and maintain cellular homeostasis. Mechanistic studies have suggested that two fundamental properties are shared by all exchangers: substrate binding is antagonistic, and coupling is maintained by preventing shuttling of the empty transporter. The CLC H(+)/Cl(-) exchangers control the homeostasis of cellular...

Read the complete abstract on PubMed

Topics

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

Share to Chloride Channels
Share to Chlorides

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

Share to Chlorine

Share to Escherichia coli

Share to Escherichia coli Proteins

Share to Protons

Share to Substrate Specificity

Share to Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 22484316
DOI: 10.1038/nsmb.2277
PMCID: PMC3348462

Genes

CLC

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 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

Synergistic substrate binding determines the stoichiometry of transport of a prokaryotic H(+)/Cl(-) exchanger.PMID 22484316Read ↗

Separate ion pathways in a Cl-/H+ exchanger.Semantic proximity Read ↗

Substrate recognition and proton coupling by a bacterial member of solute carrier family 17.Semantic proximity Read ↗

Evolutionary analysis reveals the origin of sodium coupling in glutamate transportersSemantic proximity Read ↗

Conformational changes required for H(+)/Cl(-) exchange mediated by a CLC transporter.Semantic proximity Read ↗

Structural elements required for coupling ion and substrate transport in the neurotransmitter transporter homolog LeuT.Semantic proximity Read ↗

A CLC-ec1 mutant reveals global conformational change and suggests a unifying mechanism for the CLC Cl-/H+ transport cycle.Semantic proximity Read ↗

Uncoupling and turnover in a Cl-/H+ exchange transporter.Semantic proximity Read ↗

Neurotransmitter/sodium symporter orthologue LeuT has a single high-affinity substrate site.Semantic proximity Read ↗

A mechanism for the activation of the Na/H exchanger NHE-1 by cytoplasmic acidification and mitogens.Semantic proximity Read ↗

Divergent Cl <sup>−</sup> and H <sup>+</sup> pathways underlie transport coupling and gating in CLC exchangers and channelsSemantic proximity Read ↗

Mechanism of cation binding to the glutamate transporter EAAC1 probed with mutation of the conserved amino acid residue Thr101.Semantic proximity Read ↗

Thallium ions can replace both sodium and potassium ions in the glutamate transporter excitatory amino acid carrier 1.Semantic proximity Read ↗

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