Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1823, Issue 3, Pages 767-773Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2011.08.007
Keywords
Mitochondria; Apoptosis; Permeability transition pore; Chaperone; Tumor growth
Categories
Funding
- NIH [CA140043, CA78810, CA118005]
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Protein folding quality control does not occur randomly in cells, but requires the action of specialized molecular chaperones compartmentalized in subcellular microenvironments and organelles. Fresh experimental evidence has now linked a mitochondrial-specific Heat Shock Protein-90 (Hsp90) homolog, Tumor Necrosis Factor Receptor-Associated Protein-1 (TRAP-1) to pleiotropic signaling circuitries of organelle integrity and cellular homeostasis. TRAP-1-directed compartmentalized protein folding is broadly exploited in cancer and neurodegenerative diseases, presenting new opportunities for therapeutic intervention in humans. This article is part of a Special Issue entitled: Heat Shock Protein 90 (Hsp90). (C) 2011 Elsevier B.V. All rights reserved.
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