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GoPubMed Proteins lists recent and important papers and reviews for proteins. Page last changed on 19 Dec 2016.

Solute carrier family 26, member 5

prestin, PreS, SLC26A5
This gene encodes a member of the SLC26A/SulP transporter family. The protein functions as a molecular motor in motile outer hair cells (OHCs) of the cochlea, inducing changes in cell length that act to amplify sound levels. The transmembrane protein is an incomplete anion transporter, and does not allow anions to cross the cell membrane but instead undergoes a conformational change in response to changes in intracellular Cl- levels that results in a change in cell length. The protein functions at microsecond rates, which is several orders of magnitude faster than conventional molecular motor proteins. Mutations in this gene are potential candidates for causing neurosensory deafness. Multiple transcript variants encoding different isoforms have been found for this gene.[provided by RefSeq, Nov 2009] (from NCBI)
Top mentioned proteins: HAIR, CAN, ACID, HAD, V1a
Papers on prestin
Development of a more efficient hepatitis B virus vaccine by targeting hepatitis B virus preS to dendritic cells.
Liu et al., Wuhan, China. In Vaccine, Feb 2016
The preS antigen of HBV was fused with the core streptavidin (cSA) moiety (preS-cSA) and highly expressed in Escherichia coli.
Characterization of hepatitis B virus surface antigen variability and impact on HBs antigen clearance under nucleos(t)ide analogue therapy.
Schvoerer et al., Vandœuvre-lès-Nancy, France. In J Viral Hepat, Feb 2016
PreS/S amino acid (aa) sequences were analysed with bioinformatics to predict HBV envelope antigenicity and aa covariance.
Physiological and Histological Evaluations of the Cochlea between 3xTg-AD Mouse Model of Alzheimer's Diseases and R6/2 Mouse Model of Huntington's Diseases.
Wu et al., Taipei, Taiwan. In Chin J Physiol, Jan 2016
Furthermore, the prestin expression in outer hair cells (OHCs) was significantly decreased in HD mice from 2 months of age and thereafter, and the loss of prestin expression was earlier before OHCs death in HD mice.
Posterior Reversible Encephalopathy Syndrome After Transplantation: a Review.
Zhang et al., Hangzhou, China. In Mol Neurobiol, Jan 2016
UNASSIGNED: Posterior reversible encephalopathy syndrome (PRES) is a rare neurological disease.
HBV-specific and global T-cell dysfunction in chronic hepatitis B.
HBRN et al., Philadelphia, United States. In Gastroenterology, Jan 2016
Peripheral blood lymphocytes from these subjects were analyzed for T-cell responses (proliferation and production of interferon-γ and interleukin-10) to overlapping hepatitis B virus (HBV) peptides (preS, S, preC, core, and reverse transcriptase), influenza matrix peptides, and lipopolysaccharide.
Clinical Management of Posterior Reversible Encephalopathy Syndrome after Allogeneic Hematopoietic Stem Cell Transplantation: A Case Series and Review of the Literature.
Sayer et al., Jena, Germany. In Acta Haematol, Dec 2015
BACKGROUND: Posterior reversible encephalopathy syndrome (PRES) is a rare but serious complication after allogeneic hematopoietic stem cell transplantation (alloHSCT).
Posterior reversible encephalopathy syndrome and graft-versus-host disease after liver transplantation: a case report and review of the literature.
Liu et al., In Int J Clin Pharmacol Ther, Sep 2015
Case (description): A 52-year-old male patient presented with seizures on the 16th day post liver transplantation suggesting tacrolimus-associated posterior reversible encephalopathy syndrome (PRES).
Applications of human hepatitis B virus preS domain in bio- and nanotechnology.
Murata et al., Fukuoka, Japan. In World J Gastroenterol, Jul 2015
In HBsAg, the preS domain (preS1 + preS2) plays a key role in the infection of hepatocytic cells by HBV and has several immunogenic epitopes.
Prestin-Dependence of Outer Hair Cell Survival and Partial Rescue of Outer Hair Cell Loss in PrestinV499G/Y501H Knockin Mice.
Zheng et al., Evanston, United States. In Plos One, 2014
A knockin (KI) mouse expressing mutated prestinV499G/Y501H (499 prestin) was created to study cochlear amplification.
Integrating the active process of hair cells with cochlear function.
Hudspeth, New York City, United States. In Nat Rev Neurosci, 2014
Active motility of the mechanoreceptive hair bundles underlies the active process in amphibians and some reptiles; in mammals, this mechanism operates in conjunction with prestin-based somatic motility.
Hepatitis B virus genetic variants: biological properties and clinical implications.
Wen et al., Providence, United States. In Emerg Microbes Infect, 2013
The impact of viral genotypes and mutations/deletions in the precore, core promoter, preS, and S gene on the establishment of chronic infection, development of fulminant hepatitis and liver cancer is discussed.
Prestin in HEK cells is an obligate tetramer.
Nichols et al., Omaha, United States. In J Neurophysiol, 2012
This result implies that in cell membranes prestin oligomerizes to a tetramer.
The roles of conserved and nonconserved cysteinyl residues in the oligomerization and function of mammalian prestin.
Hallworth et al., Omaha, United States. In J Neurophysiol, 2011
Four mutations (C124A, C192A, C260A, and C415A), all in nonconserved cysteinyl residues, significantly differed in their nonlinear capacitance properties compared with wild-type prestin.
Prestin links extrinsic tuning to neural excitation in the mammalian cochlea.
Russell et al., In Curr Biol, 2011
Prestin has a role in harnessing the basilar membrane as the source of cochlear frequency tuning.
Decrease of prestin expression by increased potassium concentration in organotypic cultures of the organ of Corti of newborn rats.
Gross et al., Berlin, Germany. In Neurosci Lett, 2011
Chronic depolarization decreases prestin expression and possibly contributes to hearing loss and tinnitus.
Loss of prestin does not alter the development of auditory cortical dendritic spines.
Majewska et al., Cambridge, United States. In Neural Plast, 2010
prestin knockout mice had increased auditory threshold but no changes in spine density or morphological characteristics on apical dendrites of auditory cortical layer 5 pyramidal neurons.
An ENU-induced mutation of miR-96 associated with progressive hearing loss in mice.
Steel et al., Sanger, United States. In Nat Genet, 2009
Microarray analysis revealed 96 transcripts with significantly altered expression in homozygotes; notably, Slc26a5, Ocm, Gfi1, Ptprq and Pitpnm1 were downregulated.
Cochlear outer hair cell motility.
Ashmore, London, United Kingdom. In Physiol Rev, 2008
This protein, known as prestin, is a member of a transporter superfamily SLC26.
Force generation by mammalian hair bundles supports a role in cochlear amplification.
Fettiplace et al., Madison, United States. In Nature, 2005
The prevailing hypothesis is that this amplification stems from somatic electromotility of the outer hair cells attributable to the motor protein prestin.
Prestin is required for electromotility of the outer hair cell and for the cochlear amplifier.
Zuo et al., Boston, United States. In Nature, 2002
targeted deletion of prestin in mice results in loss of outer hair cell electromotility in vitro and a 40-60 dB loss of cochlear sensitivity in vivo, without disruption of mechano-electrical transduction in outer hair cells
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