path(MESH:"Protein Aggregation, Pathological") decreases act(p(HGNC:HSPA8))

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PubMed:24706768

Here, we show that diverse disease-associated aggregates se- quester the highly abundant major chaperone heat shock cognate protein 70 (HSC70) to the point of functional collapse of an essential cellular process, clathrin-mediated endocytosis (CME).

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• path(MESH:"Protein Aggregation, Pathological") decreases bp(GO:"clathrin-dependent endocytosis")

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