Cooperation between Hsp90 and mortalin/GRP75 in resistance to cell death induced by complement C5b-9 (original) (raw)

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Selective depletion of heat shock protein 70 (Hsp70) activates a tumor-specific death program that is independent of caspases and bypasses Bcl-2

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Heat Shock Protein 70 Is Required for the Survival of Cancer Cells

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Annals of the New York Academy of Sciences, 2006

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Heat shock protein 70 is a potent activator of the human complement system

Emese Kiss

Cell stress & …, 2002

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Heat shock protein 90 as a molecular target for cancer therapeutics

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Complement C5b-9 and Cancer: Mechanisms of Cell Damage, Cancer Counteractions, and Approaches for Intervention

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Frontiers in Immunology, 2019

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Heat shock proteins in the regulation of apoptosis: new strategies in tumor therapy: a comprehensive review

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Targeting of multiple signalling pathways by heat shock protein 90 molecular chaperone inhibitors

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The Role of Heat Shock Proteins in Cancer

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Caspase-dependent, geldanamycin-enhanced cleavage of co-chaperone p23 in leukemic apoptosis

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Heat-shock protein 60 translocates to the surface of apoptotic cells and differentiated megakaryocytes and stimulates phagocytosis

James Ross

Cellular and Molecular Life Sciences, 2011

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CacyBP/SIP, a Hsp90 binding chaperone, in cellular stress response

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Proteotoxicity is not the reason for the dependence of cancer cells on the major chaperone Hsp70

Michael Sherman

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Hsp90 Inhibition Accelerates Cell Lysis: ANTI-Hsp90 RIBOZYME REVEALS A COMPLEX MECHANISM OF Hsp90 INHIBITORS INVOLVING BOTH SUPEROXIDE- AND Hsp90-DEPENDENT EVENTS

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Mitochondrial heat shock protein (HSP) 70 synergizes with HSP60 in transducing endothelial cell apoptosis induced by anti-HSP60 autoantibody

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Cell Surface-bound Heat Shock Protein 70 (Hsp70) Mediates Perforin-independent Apoptosis by Specific Binding and Uptake of Granzyme B

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Targeting heat shock protein 72 enhances Hsp90 inhibitor-induced apoptosis in myeloma

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Leukemia, 2010

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