Lamin A molecular compression and sliding as mechanisms behind nucleoskeleton elasticity

Lamin A is critical for nuclear architecture but its structure and assembly are not fully understood. Here, the authors use quantitative cross-linking mass spectrometry to map intra- and intermolecular interactions within lamin homomers, providing insights into the molecular basis for lamin’s mechan...

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Autores principales:	Alex A. Makarov, Juan Zou, Douglas R. Houston, Christos Spanos, Alexandra S. Solovyova, Cristina Cardenal-Peralta, Juri Rappsilber, Eric C. Schirmer
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/caf6c534ab4f4275b1626a524f801501
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spelling	oai:doaj.org-article:caf6c534ab4f4275b1626a524f8015012021-12-02T17:01:32ZLamin A molecular compression and sliding as mechanisms behind nucleoskeleton elasticity10.1038/s41467-019-11063-62041-1723https://doaj.org/article/caf6c534ab4f4275b1626a524f8015012019-07-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-11063-6https://doaj.org/toc/2041-1723Lamin A is critical for nuclear architecture but its structure and assembly are not fully understood. Here, the authors use quantitative cross-linking mass spectrometry to map intra- and intermolecular interactions within lamin homomers, providing insights into the molecular basis for lamin’s mechanical properties.Alex A. MakarovJuan ZouDouglas R. HoustonChristos SpanosAlexandra S. SolovyovaCristina Cardenal-PeraltaJuri RappsilberEric C. SchirmerNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-17 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Alex A. Makarov Juan Zou Douglas R. Houston Christos Spanos Alexandra S. Solovyova Cristina Cardenal-Peralta Juri Rappsilber Eric C. Schirmer Lamin A molecular compression and sliding as mechanisms behind nucleoskeleton elasticity
description	Lamin A is critical for nuclear architecture but its structure and assembly are not fully understood. Here, the authors use quantitative cross-linking mass spectrometry to map intra- and intermolecular interactions within lamin homomers, providing insights into the molecular basis for lamin’s mechanical properties.
format	article
author	Alex A. Makarov Juan Zou Douglas R. Houston Christos Spanos Alexandra S. Solovyova Cristina Cardenal-Peralta Juri Rappsilber Eric C. Schirmer
author_facet	Alex A. Makarov Juan Zou Douglas R. Houston Christos Spanos Alexandra S. Solovyova Cristina Cardenal-Peralta Juri Rappsilber Eric C. Schirmer
author_sort	Alex A. Makarov
title	Lamin A molecular compression and sliding as mechanisms behind nucleoskeleton elasticity
title_short	Lamin A molecular compression and sliding as mechanisms behind nucleoskeleton elasticity
title_full	Lamin A molecular compression and sliding as mechanisms behind nucleoskeleton elasticity
title_fullStr	Lamin A molecular compression and sliding as mechanisms behind nucleoskeleton elasticity
title_full_unstemmed	Lamin A molecular compression and sliding as mechanisms behind nucleoskeleton elasticity
title_sort	lamin a molecular compression and sliding as mechanisms behind nucleoskeleton elasticity
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/caf6c534ab4f4275b1626a524f801501
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Lamin A molecular compression and sliding as mechanisms behind nucleoskeleton elasticity

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