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Fishing out proteins that bind to titin

Another giant protein has been detected in cross-striated muscle cells. Given the name obscurin, it was discovered in a yeast two-hybrid screen in which the bait was a small region of titin that is localized near the Z-band. Obscurin is about 720 kD, similar in molecular weight to nebulin, but prese...

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Detalles Bibliográficos
Autores principales: Sanger, Joseph W., Sanger, Jean M.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2001
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2196855/
https://www.ncbi.nlm.nih.gov/pubmed/11448986
http://dx.doi.org/10.1083/jcb.200106072
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author Sanger, Joseph W.
Sanger, Jean M.
author_facet Sanger, Joseph W.
Sanger, Jean M.
author_sort Sanger, Joseph W.
collection PubMed
description Another giant protein has been detected in cross-striated muscle cells. Given the name obscurin, it was discovered in a yeast two-hybrid screen in which the bait was a small region of titin that is localized near the Z-band. Obscurin is about 720 kD, similar in molecular weight to nebulin, but present at about one tenth the level (Young et al., 2001). Like titin, obscurin contains multiple immunoglobulin-like domains linked in tandem, but in contrast to titin it contains just two fibronectin-like domains. It also contains sequences that suggest obscurin may have roles in signal transduction. During embryonic development, its localization changes from the Z-band to the M-band. With these intriguing properties, obscurin may not remain obscure for long.
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spelling pubmed-21968552008-05-01 Fishing out proteins that bind to titin Sanger, Joseph W. Sanger, Jean M. J Cell Biol Reviews Another giant protein has been detected in cross-striated muscle cells. Given the name obscurin, it was discovered in a yeast two-hybrid screen in which the bait was a small region of titin that is localized near the Z-band. Obscurin is about 720 kD, similar in molecular weight to nebulin, but present at about one tenth the level (Young et al., 2001). Like titin, obscurin contains multiple immunoglobulin-like domains linked in tandem, but in contrast to titin it contains just two fibronectin-like domains. It also contains sequences that suggest obscurin may have roles in signal transduction. During embryonic development, its localization changes from the Z-band to the M-band. With these intriguing properties, obscurin may not remain obscure for long. The Rockefeller University Press 2001-07-09 /pmc/articles/PMC2196855/ /pubmed/11448986 http://dx.doi.org/10.1083/jcb.200106072 Text en Copyright © 2001, The Rockefeller University Press This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/).
spellingShingle Reviews
Sanger, Joseph W.
Sanger, Jean M.
Fishing out proteins that bind to titin
title Fishing out proteins that bind to titin
title_full Fishing out proteins that bind to titin
title_fullStr Fishing out proteins that bind to titin
title_full_unstemmed Fishing out proteins that bind to titin
title_short Fishing out proteins that bind to titin
title_sort fishing out proteins that bind to titin
topic Reviews
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2196855/
https://www.ncbi.nlm.nih.gov/pubmed/11448986
http://dx.doi.org/10.1083/jcb.200106072
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