Lifetime imaging of a fluorescent protein sensor reveals surprising stability of ER thiol redox

Interfering with disulfide bond formation impedes protein folding and promotes endoplasmic reticulum (ER) stress. Due to limitations in measurement techniques, the relationships of altered thiol redox and ER stress have been difficult to assess. We report that fluorescent lifetime measurements circu...

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Detalles Bibliográficos
Autores principales: Avezov, Edward, Cross, Benedict C.S., Kaminski Schierle, Gabriele S., Winters, Mikael, Harding, Heather P., Melo, Eduardo Pinho, Kaminski, Clemens F., Ron, David
Formato: Online Artículo Texto
Lenguaje:English
Publicado: The Rockefeller University Press 2013
Materias:
Research Articles
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3628511/
https://www.ncbi.nlm.nih.gov/pubmed/23589496
http://dx.doi.org/10.1083/jcb.201211155

Internet

https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3628511/
https://www.ncbi.nlm.nih.gov/pubmed/23589496
http://dx.doi.org/10.1083/jcb.201211155

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