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

N-terminal-mediated homomultimerization of prestin, the outer hair cell motor protein.

Biophysical journal - 1 Nov 2005

Navaratnam Dhasakumar, Bai Jun-Ping, Samaranayake Haresha, Santos-Sacchi Joseph

Abstract excerpt

The outer hair cell lateral membrane motor, prestin, drives the cell's mechanical response that underpins mammalian cochlear amplification. Little is known about the protein's structure-function relations. Here we provide evidence that prestin is a 10-transmembrane domain protein whose membrane topology differs from that of previous models. We also present evidence that both intracellular termini of prestin are...

Read the complete abstract on PubMed

Topics

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

Share to Allosteric Site
Share to Electric Conductivity
Share to Electrophysiology

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Fluorescence Resonance Energy Transfer

Share to Gerbillinae

Share to Hair Cells, Auditory, Outer

Share to Mechanotransduction, Cellular

Share to Molecular Motor Proteins

Source

Open in PubMed Open full text

Identifiers

PMID: 16113116
DOI: 10.1529/biophysj.105.068759
PMCID: PMC1366831

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

N-terminal-mediated homomultimerization of prestin, the outer hair cell motor protein.PMID 16113116Read ↗

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

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

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

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

The R130S mutation significantly affects the function of prestin, the outer hair cell motor protein.Semantic proximity Read ↗

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

Interaction of prestin (SLC26A5) with monovalent intracellular anions.Semantic proximity Read ↗

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

Normal hearing sensitivity at low-to-middle frequencies with 34% prestin-charge density.Semantic proximity Read ↗

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

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