The FANCM-BLM-TOP3A-RMI complex suppresses alternative lengthening of telomeres (ALT)

ALT telomeres experience DNA damage that may drive recombination-based telomere elongation. Here, the authors reveal that FANCM plays a critical role in the suppression of ALT activity through its interaction with the BTR (BLM-TOP3A-RMI) complex.

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Autores principales:	Robert Lu, Julienne J. O’Rourke, Alexander P. Sobinoff, Joshua A. M. Allen, Christopher B. Nelson, Christopher G. Tomlinson, Michael Lee, Roger R. Reddel, Andrew J. Deans, Hilda A. Pickett
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2019
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/ec5006d7bd3c48149838ce39d9f207f5
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spelling	oai:doaj.org-article:ec5006d7bd3c48149838ce39d9f207f52021-12-02T17:02:01ZThe FANCM-BLM-TOP3A-RMI complex suppresses alternative lengthening of telomeres (ALT)10.1038/s41467-019-10180-62041-1723https://doaj.org/article/ec5006d7bd3c48149838ce39d9f207f52019-05-01T00:00:00Zhttps://doi.org/10.1038/s41467-019-10180-6https://doaj.org/toc/2041-1723ALT telomeres experience DNA damage that may drive recombination-based telomere elongation. Here, the authors reveal that FANCM plays a critical role in the suppression of ALT activity through its interaction with the BTR (BLM-TOP3A-RMI) complex.Robert LuJulienne J. O’RourkeAlexander P. SobinoffJoshua A. M. AllenChristopher B. NelsonChristopher G. TomlinsonMichael LeeRoger R. ReddelAndrew J. DeansHilda A. PickettNature PortfolioarticleScienceQENNature Communications, Vol 10, Iss 1, Pp 1-14 (2019)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Robert Lu Julienne J. O’Rourke Alexander P. Sobinoff Joshua A. M. Allen Christopher B. Nelson Christopher G. Tomlinson Michael Lee Roger R. Reddel Andrew J. Deans Hilda A. Pickett The FANCM-BLM-TOP3A-RMI complex suppresses alternative lengthening of telomeres (ALT)
description	ALT telomeres experience DNA damage that may drive recombination-based telomere elongation. Here, the authors reveal that FANCM plays a critical role in the suppression of ALT activity through its interaction with the BTR (BLM-TOP3A-RMI) complex.
format	article
author	Robert Lu Julienne J. O’Rourke Alexander P. Sobinoff Joshua A. M. Allen Christopher B. Nelson Christopher G. Tomlinson Michael Lee Roger R. Reddel Andrew J. Deans Hilda A. Pickett
author_facet	Robert Lu Julienne J. O’Rourke Alexander P. Sobinoff Joshua A. M. Allen Christopher B. Nelson Christopher G. Tomlinson Michael Lee Roger R. Reddel Andrew J. Deans Hilda A. Pickett
author_sort	Robert Lu
title	The FANCM-BLM-TOP3A-RMI complex suppresses alternative lengthening of telomeres (ALT)
title_short	The FANCM-BLM-TOP3A-RMI complex suppresses alternative lengthening of telomeres (ALT)
title_full	The FANCM-BLM-TOP3A-RMI complex suppresses alternative lengthening of telomeres (ALT)
title_fullStr	The FANCM-BLM-TOP3A-RMI complex suppresses alternative lengthening of telomeres (ALT)
title_full_unstemmed	The FANCM-BLM-TOP3A-RMI complex suppresses alternative lengthening of telomeres (ALT)
title_sort	fancm-blm-top3a-rmi complex suppresses alternative lengthening of telomeres (alt)
publisher	Nature Portfolio
publishDate	2019
url	https://doaj.org/article/ec5006d7bd3c48149838ce39d9f207f5
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The FANCM-BLM-TOP3A-RMI complex suppresses alternative lengthening of telomeres (ALT)

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