Disordered clusters of Bak dimers rupture mitochondria during apoptosis

During apoptosis, Bak and Bax undergo major conformational change and form symmetric dimers that coalesce to perforate the mitochondrial outer membrane via an unknown mechanism. We have employed cysteine labelling and linkage analysis to the full length of Bak in mitochondria. This comprehensive sur...

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Detalles Bibliográficos
Autores principales: Uren, Rachel T, O’Hely, Martin, Iyer, Sweta, Bartolo, Ray, Shi, Melissa X, Brouwer, Jason M, Alsop, Amber E, Dewson, Grant, Kluck, Ruth M
Formato: Online Artículo Texto
Lenguaje:English
Publicado: eLife Sciences Publications, Ltd 2017
Materias:
Biophysics and Structural Biology
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5302884/
https://www.ncbi.nlm.nih.gov/pubmed/28182867
http://dx.doi.org/10.7554/eLife.19944

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5302884/
https://www.ncbi.nlm.nih.gov/pubmed/28182867
http://dx.doi.org/10.7554/eLife.19944

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