Chaperone-mediated autophagy is one of several lysosomal pathways of proteolysis. This
pathway is activated by physiological stresses such as prolonged starvation. Cytosolic …

Chaperone-mediated autophagy (CMA) is a lysosomal pathway of proteolysis that is
responsible for the degradation of 30% of cytosolic proteins under conditions of prolonged …

The selective degradation of cytosolic proteins in lysosomes by chaperone‐mediated
autophagy depends, at least in part, on the levels of a substrate receptor at the lysosomal …

Chaperone-mediated autophagy (CMA) is a selective type of autophagy by which specific
cytosolic proteins are sent to lysosomes for degradation. Substrate proteins bind to the …

Chaperone-mediated autophagy (CMA) is a selective pathway for the degradation of
cytosolic proteins in lysosomes. CMA declines with age because of a decrease in the levels …

Rates of autophagy, the mechanism responsible for lysosomal clearance of cellular
components, decrease with age. We have previously described an age-related decline in …

Chaperone-mediated autophagy (CMA) is a highly regulated cellular process that mediates
the degradation of a selective subset of cytosolic proteins in lysosomes. Increasing CMA …

Chaperone-mediated autophagy (CMA) is a selective form of autophagy in which cytosolic
proteins bearing a pentapeptide motif biochemically related to the KFERQ sequence, are …

Autophagy is a process involved in the proteolytic degradation of cellular macromolecules in
lysosomes, which requires the activity of proteases, enzymes that hydrolyse peptide bonds …

All cellular proteins undergo continuous synthesis and degradation. This permanent
renewal is necessary to maintain a functional proteome and to allow rapid changes in levels …