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rdf:type |
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lifeskim:mentions |
umls-concept:C0009195,
umls-concept:C0376249,
umls-concept:C0439660,
umls-concept:C0679058,
umls-concept:C1179106,
umls-concept:C1314939,
umls-concept:C1384666,
umls-concept:C1547699,
umls-concept:C1753024,
umls-concept:C1822756,
umls-concept:C2700640,
umls-concept:C2703881
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pubmed:dateCreated |
2005-8-25
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pubmed:abstractText |
Cochlear outer hair cells change their length in response to variations in membrane potential. This capability, called electromotility, is believed to enable the sensitivity and frequency selectivity of the mammalian cochlea. Prestin is a transmembrane protein required for electromotility. Homozygous prestin knockout mice are profoundly hearing impaired. In humans, a single nucleotide change in SLC26A5, encoding prestin, has been reported in association with hearing loss. This DNA sequence variation, IVS2-2A>G, occurs in the exon 3 splice acceptor site and is expected to abolish splicing of exon 3.
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pubmed:grant |
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/16086836-10376574,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16086836-10821263,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16086836-11125015,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16086836-11668644,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16086836-11807148,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16086836-11976921,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16086836-12239568,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16086836-12394346,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16086836-12584604,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16086836-12719379,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16086836-14571368,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16086836-15207913,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16086836-15319415,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16086836-15608272,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16086836-3658675,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16086836-7689389,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16086836-9490575,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16086836-9779807,
http://linkedlifedata.com/resource/pubmed/commentcorrection/16086836-9927480
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Adenine,
http://linkedlifedata.com/resource/pubmed/chemical/Anion Transport Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Mitochondrial,
http://linkedlifedata.com/resource/pubmed/chemical/Guanine,
http://linkedlifedata.com/resource/pubmed/chemical/Molecular Motor Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Pres protein, mouse,
http://linkedlifedata.com/resource/pubmed/chemical/Pres protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Ribosomal,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, ribosomal, 12S,
http://linkedlifedata.com/resource/pubmed/chemical/RNA Splice Sites,
http://linkedlifedata.com/resource/pubmed/chemical/SLC26A5 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Zebrafish Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
1471-2350
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
8
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
30
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:16086836-Adenine,
pubmed-meshheading:16086836-Alleles,
pubmed-meshheading:16086836-Alternative Splicing,
pubmed-meshheading:16086836-Animals,
pubmed-meshheading:16086836-Anion Transport Proteins,
pubmed-meshheading:16086836-Cochlea,
pubmed-meshheading:16086836-DNA, Mitochondrial,
pubmed-meshheading:16086836-Exons,
pubmed-meshheading:16086836-Genetic Variation,
pubmed-meshheading:16086836-Guanine,
pubmed-meshheading:16086836-Hair Cells, Vestibular,
pubmed-meshheading:16086836-Hearing Loss,
pubmed-meshheading:16086836-Humans,
pubmed-meshheading:16086836-Introns,
pubmed-meshheading:16086836-Mice,
pubmed-meshheading:16086836-Molecular Motor Proteins,
pubmed-meshheading:16086836-Pan troglodytes,
pubmed-meshheading:16086836-Proteins,
pubmed-meshheading:16086836-RNA, Ribosomal,
pubmed-meshheading:16086836-RNA Splice Sites,
pubmed-meshheading:16086836-Rats,
pubmed-meshheading:16086836-Sequence Alignment,
pubmed-meshheading:16086836-Sequence Analysis, DNA,
pubmed-meshheading:16086836-Zebrafish,
pubmed-meshheading:16086836-Zebrafish Proteins
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pubmed:year |
2005
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pubmed:articleTitle |
High frequency of the IVS2-2A>G DNA sequence variation in SLC26A5, encoding the cochlear motor protein prestin, precludes its involvement in hereditary hearing loss.
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pubmed:affiliation |
The Bobby R. Alford Department of Otorhinolaryngology and Communicative Sciences, Baylor College of Medicine, One Baylor Plaza, NA102, Houston, TX 77030, USA. tang@bmc.tmc.edu
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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