@article{b616ad51780f4f969221cda83e6dcd0d,
title = "Chaperone-mediated autophagy in protein quality control",
abstract = "Chaperone-mediated autophagy is a selective mechanism for degradation of soluble cytosolic proteins in lysosomes that distinguishes itself from other autophagic pathways by the selectivity with which CMA substrates are targeted for degradation. The recent molecular dissection of this autophagic pathway and the development of experimental models with compromised CMA have unveiled the important contribution of this pathway to protein quality control. In fact, CMA activation seems to be a common mechanism of cellular defense against proteotoxicity.",
author = "Esperanza Arias and Cuervo, {Ana Maria}",
note = "Funding Information: The authors want to express their profound appreciation for the late Fred Dice ({\textquoteleft}Paulo{\textquoteright}) for his pioneering work on this pathway and for the great influence that he and his work have always had, and will continue to have, in this field. We thank Ms. Samantha Orenstein for critically reading the manuscript. Work in our laboratory is supported by NIH grants from NIA ( AG021904 , AG031782 ), NIDKK ( DK041918 ), NINDS ( NS038370 ), a Glenn Foundation Award and a Hirsch/Weill-Caulier Career Scientist Award. E.A. is a Fullbright Fellow. ",
year = "2011",
month = apr,
doi = "10.1016/j.ceb.2010.10.009",
language = "English (US)",
volume = "23",
pages = "184--189",
journal = "Current Opinion in Cell Biology",
issn = "0955-0674",
publisher = "Elsevier Limited",
number = "2",
}