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

Interaction of prestin (SLC26A5) with monovalent intracellular anions.

Novartis Foundation symposium - 1 Jan 2006

Oliver Dominik, Schächinger Thorsten, Fakler Bernd

Abstract excerpt

Outer hair cells (OHCs) of the mammalian cochlea are equipped with a specific form of cellular motility that is driven by changes of the membrane potential. This electromotility is a membrane-based process generated by the membrane protein prestin (SLC26A5). Current models suggest that prestin undergoes a force-generating conformational transition upon changes of the membrane potential. The voltage dependence of...

Read the complete abstract on PubMed

Topics

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

Share to Anion Transport Proteins
Share to Bicarbonates
Share to Chlorides

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Mutation

Share to Proteins

Share to Structure-Activity Relationship

Share to Sulfate Transporters

Source

Identifiers

PMID: 17120772

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

Interaction of prestin (SLC26A5) with monovalent intracellular anions.PMID 17120772Read ↗

Intracellular anions as the voltage sensor of prestin, the outer hair cell motor protein.Semantic proximity Read ↗

Combinatorial cysteine mutagenesis reveals a critical intramonomer role for cysteines in prestin voltage sensing.Semantic proximity Read ↗

Current carried by the Slc26 family member prestin does not flow through the transporter pathway.Semantic proximity Read ↗

The C-terminus of prestin influences nonlinear capacitance and plasma membrane targeting.Semantic proximity Read ↗

Cysteine mutagenesis reveals transmembrane residues associated with charge translocation in prestin.Semantic proximity Read ↗

Prestin is required for electromotility of the outer hair cell and for the cochlear amplifier.Semantic proximity Read ↗

N-terminal-mediated homomultimerization of prestin, the outer hair cell motor protein.Semantic proximity Read ↗

Cryo-EM structures reveal the electromotility mechanism of prestin, the cochlear amplifierSemantic proximity Read ↗

Effects of cyclic nucleotides on the function of prestin.Semantic proximity Read ↗

The V499G/Y501H mutation impairs fast motor kinetics of prestin and has significance for defining functional independence of individual prestin subunits.Semantic proximity Read ↗

The frequency dependence of prestin-mediated fast electromotility for mammalian cochlear amplificationSemantic proximity Read ↗

A genetically-encoded YFP sensor with enhanced chloride sensitivity, photostability and reduced ph interference demonstrates augmented transmembrane chloride movement by gerbil prestin (SLC26a5).Semantic proximity Read ↗

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