Chaperone-mediated autophagy: roles in disease and aging

By A. Cuervo, Esther Wong. Cell Research, 2013

829 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Geriatrics and Gerontology

View Paper: https://www.semanticscholar.org/paper/109fd911b8e0720ed6cb55496add3fc6cd69ac8d

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In Cell Biology

In Epidemiology

In Geriatrics and Gerontology

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Citations in the corpus

Oxidative Stress in Aging Human Skin (2015, background): “In addition to macroautophagy, microautophagy [252] as well as chaperone-mediated autophagy [253,254] are possible candidates for the removal of oxidized”
Neuronal Cell Death. (2018, neutral): “Another type of autophagy that has been especially implicated in Parkinson’s and Huntington’s disease is chaperone-mediated autophagy, where proteins are delivered to lysosomes by binding via a KFERQ motif to the Hsp70-cognate protein Hsc70, and imported into the lysosomes via Lamp2a (140).”
Selective Autophagy: ATG8 Family Proteins, LIR Motifs and Cargo Receptors. (2020, background): “Chaperone-mediated autophagy is in principle a selective process where single polypeptides are recognized as unfolded/ misfolded when exposing binding sites (degenerate KFERQ-like pentapeptide motifs) for heat shockcognate protein of 70 kDa (Hsc70) [2].”
Inflammaging and 'Garb-aging'. (2017, background): “Actually, autophagy is reported to decrease with ageing [36,37], further supporting the idea that inflammaging is fuelled by accumulation of cellular components that are not appropriately disposed.”
Monitoring and Measuring Autophagy (2017, background): “CMA was observed only in mammalian cells; in CMA, proteins are unfolded and directly translocated into lysosomes dependently on the Lys-Phe-Glu-Arg-Gln (KFERQ)-like motif of the substrate, and on cytosolic heat shock-cognate chaperone of 70 kDa (HSC70), lysosome-associated membrane protein type-2A (”
Molecular definitions of autophagy and related processes (2017, neutral): “…at baseline levels, hence contributing to the preservation of cellular homeostasis as they avoid the accumulation of potentially cytotoxic entities that may accumulate as a result of normal cellular functions (e.g., damaged mitochondria) (Li et al , 2012; Cuervo & Wong, 2014; Sica et al , 2015).”