Heat shock 70 kDa proteins (HSP70s) are ubiquitous molecular chaperones that function in
a myriad of biological processes, modulating polypeptide folding, degradation and …

Heat shock proteins (Hsps) are overexpressed in a wide range of human cancers and are
implicated in tumor cell proliferation, differentiation, invasion, metastasis, death, and …

Cysteine cathepsin protease activity is frequently dysregulated in the context of neoplastic
transformation. Increased activity and aberrant localization of proteases within the tumour …

Lysosomal hydrolases participate in the digestion of endocytosed and autophagocytosed
material inside the lysosomal/autolysosomal compartment in acute cell death when released …

The human heat shock protein 70 (Hsp70) family contains at least eight homologous
chaperone proteins. Endoplasmatic reticulum and mitochondria have their specific Hsp70 …

The HSP70 family of heat shock proteins consists of molecular chaperones of approximately
70kDa in size that serve critical roles in protein homeostasis. These adenosine …

Adverse outcome pathways (AOPs) are a recent toxicological construct that connects, in a
formalized, transparent and quality-controlled way, mechanistic information to apical …

Heat shock protein 70 (Hsp70) is a potent survival protein whose depletion triggers massive
caspase-independent tumor cell death. Here, we show that Hsp70 exerts its prosurvival …

Interest in the lysosome's potential role in anticancer therapies has recently been
appreciated in the field of immuno-oncology. Targeting lysosomes triggers apoptotic …

The multifunctional, stress-inducible molecular chaperone HSP70 has important roles in
aiding protein folding and maintaining protein homeostasis. HSP70 expression is elevated …