Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin

Myosin, a motor protein essential for intracellular transport to muscle contraction, requires a chaperone UNC-45 for folding and assembly. Here authors use in vitro reconstitution and structural biology to characterize the interplay between UNC-45 and muscle myosin MHC-B.

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Autores principales:	Doris Hellerschmied, Anita Lehner, Nina Franicevic, Renato Arnese, Chloe Johnson, Antonia Vogel, Anton Meinhart, Robert Kurzbauer, Luiza Deszcz, Linn Gazda, Michael Geeves, Tim Clausen
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/988d6ef9a9a34ef79788fa29755892f7
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spelling	oai:doaj.org-article:988d6ef9a9a34ef79788fa29755892f72021-12-02T17:01:26ZMolecular features of the UNC-45 chaperone critical for binding and folding muscle myosin10.1038/s41467-019-12667-82041-1723https://doaj.org/article/988d6ef9a9a34ef79788fa29755892f72019-10-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-12667-8https://doaj.org/toc/2041-1723Myosin, a motor protein essential for intracellular transport to muscle contraction, requires a chaperone UNC-45 for folding and assembly. Here authors use in vitro reconstitution and structural biology to characterize the interplay between UNC-45 and muscle myosin MHC-B.Doris HellerschmiedAnita LehnerNina FranicevicRenato ArneseChloe JohnsonAntonia VogelAnton MeinhartRobert KurzbauerLuiza DeszczLinn GazdaMichael GeevesTim ClausenNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Doris Hellerschmied Anita Lehner Nina Franicevic Renato Arnese Chloe Johnson Antonia Vogel Anton Meinhart Robert Kurzbauer Luiza Deszcz Linn Gazda Michael Geeves Tim Clausen Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin
description	Myosin, a motor protein essential for intracellular transport to muscle contraction, requires a chaperone UNC-45 for folding and assembly. Here authors use in vitro reconstitution and structural biology to characterize the interplay between UNC-45 and muscle myosin MHC-B.
format	article
author	Doris Hellerschmied Anita Lehner Nina Franicevic Renato Arnese Chloe Johnson Antonia Vogel Anton Meinhart Robert Kurzbauer Luiza Deszcz Linn Gazda Michael Geeves Tim Clausen
author_facet	Doris Hellerschmied Anita Lehner Nina Franicevic Renato Arnese Chloe Johnson Antonia Vogel Anton Meinhart Robert Kurzbauer Luiza Deszcz Linn Gazda Michael Geeves Tim Clausen
author_sort	Doris Hellerschmied
title	Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin
title_short	Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin
title_full	Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin
title_fullStr	Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin
title_full_unstemmed	Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin
title_sort	molecular features of the unc-45 chaperone critical for binding and folding muscle myosin
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/988d6ef9a9a34ef79788fa29755892f7
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Molecular features of the UNC-45 chaperone critical for binding and folding muscle myosin

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