The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core

The pro-apoptotic BAX protein is a monomer under homeostatic conditions and, in response to stress, transforms into oligomers that induce apoptosis. Here, the authors characterize structural features of BAX that individually stabilize the monomer while collectively contributing to oligomerization.

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Autores principales:	Noah B. Bloch, Thomas E. Wales, Michelle S. Prew, Hannah R. Levy, John R. Engen, Loren D. Walensky
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2021
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/6094840e65e043afbdbb1d1b24daacd6
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spelling	oai:doaj.org-article:6094840e65e043afbdbb1d1b24daacd62021-12-02T15:07:56ZThe conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core10.1038/s41467-021-25200-72041-1723https://doaj.org/article/6094840e65e043afbdbb1d1b24daacd62021-08-01T00:00:00Zhttps://doi.org/10.1038/s41467-021-25200-7https://doaj.org/toc/2041-1723The pro-apoptotic BAX protein is a monomer under homeostatic conditions and, in response to stress, transforms into oligomers that induce apoptosis. Here, the authors characterize structural features of BAX that individually stabilize the monomer while collectively contributing to oligomerization.Noah B. BlochThomas E. WalesMichelle S. PrewHannah R. LevyJohn R. EngenLoren D. WalenskyNature PortfolioarticleScienceQENNature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Noah B. Bloch Thomas E. Wales Michelle S. Prew Hannah R. Levy John R. Engen Loren D. Walensky The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core
description	The pro-apoptotic BAX protein is a monomer under homeostatic conditions and, in response to stress, transforms into oligomers that induce apoptosis. Here, the authors characterize structural features of BAX that individually stabilize the monomer while collectively contributing to oligomerization.
format	article
author	Noah B. Bloch Thomas E. Wales Michelle S. Prew Hannah R. Levy John R. Engen Loren D. Walensky
author_facet	Noah B. Bloch Thomas E. Wales Michelle S. Prew Hannah R. Levy John R. Engen Loren D. Walensky
author_sort	Noah B. Bloch
title	The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core
title_short	The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core
title_full	The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core
title_fullStr	The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core
title_full_unstemmed	The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core
title_sort	conformational stability of pro-apoptotic bax is dictated by discrete residues of the protein core
publisher	Nature Portfolio
publishDate	2021
url	https://doaj.org/article/6094840e65e043afbdbb1d1b24daacd6
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The conformational stability of pro-apoptotic BAX is dictated by discrete residues of the protein core

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