Regulation of Tumor Cell Mitochondrial Homeostasis by an Organelle-Specific Hsp90 Chaperone Network

[1]  J. Olzmann,et al.  PINK1 Protects against Oxidative Stress by Phosphorylating Mitochondrial Chaperone TRAP1 , 2007, PLoS biology.

[2]  Ian Collins,et al.  New approaches to molecular cancer therapeutics , 2006, Nature chemical biology.

[3]  R. Baron,et al.  Hsp90 inhibition transiently activates Src kinase and promotes Src-dependent Akt and Erk activation. , 2006, Proceedings of the National Academy of Sciences of the United States of America.

[4]  Vladimir P Torchilin,et al.  Recent approaches to intracellular delivery of drugs and DNA and organelle targeting. , 2006, Annual review of biomedical engineering.

[5]  M. Drysdale,et al.  Targeting Hsp90 for the treatment of cancer. , 2006, Current opinion in drug discovery & development.

[6]  L. Pearl,et al.  Structure and mechanism of the Hsp90 molecular chaperone machinery. , 2006, Annual review of biochemistry.

[7]  W. Craigen,et al.  Properties of the permeability transition in VDAC1(-/-) mitochondria. , 2006, Biochimica et biophysica acta.

[8]  S. Lindquist,et al.  HSP90 and the chaperoning of cancer , 2005, Nature Reviews Cancer.

[9]  S. Lindquist,et al.  Hsp90 Potentiates the Rapid Evolution of New Traits: Drug Resistance in Diverse Fungi , 2005, Science.

[10]  M. Waltham,et al.  The heat shock protein 90 inhibitor, 17-allylamino-17-demethoxygeldanamycin, enhances osteoclast formation and potentiates bone metastasis of a human breast cancer cell line. , 2005, Cancer research.

[11]  G. Colombo,et al.  Rational design of shepherdin, a novel anticancer agent. , 2005, Cancer cell.

[12]  Jeffrey Robbins,et al.  Loss of cyclophilin D reveals a critical role for mitochondrial permeability transition in cell death , 2005, Nature.

[13]  Tetsuya Watanabe,et al.  Cyclophilin D-dependent mitochondrial permeability transition regulates some necrotic but not apoptotic cell death , 2005, Nature.

[14]  D. Altieri,et al.  Mitochondrial survivin inhibits apoptosis and promotes tumorigenesis. , 2004, The Journal of clinical investigation.

[15]  Jason C. Young,et al.  Pathways of chaperone-mediated protein folding in the cytosol , 2004, Nature Reviews Molecular Cell Biology.

[16]  D. Green,et al.  The Pathophysiology of Mitochondrial Cell Death , 2004, Science.

[17]  H. Beere `The stress of dying': the role of heat shock proteins in the regulation of apoptosis , 2004, Journal of Cell Science.

[18]  Dean P. Jones,et al.  The ADP/ATP translocator is not essential for the mitochondrial permeability transition pore , 2004, Nature.

[19]  R. Jope,et al.  Rapid accumulation of Akt in mitochondria following phosphatidylinositol 3‐kinase activation , 2003, Journal of neurochemistry.

[20]  Marjan S. Bolouri,et al.  Integrated Analysis of Protein Composition, Tissue Diversity, and Gene Regulation in Mouse Mitochondria , 2003, Cell.

[21]  W. Sessa,et al.  Regulation of survivin function by Hsp90 , 2003, Proceedings of the National Academy of Sciences of the United States of America.

[22]  L. Neckers,et al.  Heat shock protein 90 , 2003, Current opinion in oncology.

[23]  L. Fritz,et al.  A high-affinity conformation of Hsp90 confers tumour selectivity on Hsp90 inhibitors , 2003, Nature.

[24]  L. Neckers,et al.  Heat shock protein 90 as a molecular target for cancer therapeutics. , 2003, Cancer cell.

[25]  Nicholas J. Hoogenraad,et al.  Molecular Chaperones Hsp90 and Hsp70 Deliver Preproteins to the Mitochondrial Import Receptor Tom70 , 2003, Cell.

[26]  Paul Workman,et al.  Activation of the ATPase activity of hsp90 by the stress-regulated cochaperone aha1. , 2002, Molecular cell.

[27]  K. Yamamoto,et al.  Disassembly of Transcriptional Regulatory Complexes by Molecular Chaperones , 2002, Science.

[28]  Lihua He,et al.  Regulated and unregulated mitochondrial permeability transition pores: a new paradigm of pore structure and function? , 2002, FEBS letters.

[29]  F. Hartl,et al.  Role of the Myosin Assembly Protein UNC-45 as a Molecular Chaperone for Myosin , 2002, Science.

[30]  Scott W. Lowe,et al.  Apoptosis A Link between Cancer Genetics and Chemotherapy , 2002, Cell.

[31]  Jason C. Young,et al.  Hsp90: a specialized but essential protein-folding tool. , 2001, The Journal of cell biology.

[32]  J. Cechetto,et al.  Immunoelectron microscopy provides evidence that tumor necrosis factor receptor-associated protein 1 (TRAP-1) is a mitochondrial protein which also localizes at specific extramitochondrial sites. , 2000, Experimental cell research.

[33]  T. Tsuruo,et al.  Modulation of Akt kinase activity by binding to Hsp90. , 2000, Proceedings of the National Academy of Sciences of the United States of America.

[34]  S. Srinivasula,et al.  Negative regulation of cytochrome c‐mediated oligomerization of Apaf‐1 and activation of procaspase‐9 by heat shock protein 90 , 2000, The EMBO journal.

[35]  D. Donner,et al.  The hsp90-related Protein TRAP1 Is a Mitochondrial Protein with Distinct Functional Properties* , 2000, The Journal of Biological Chemistry.

[36]  J. Riordan,et al.  Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome , 1998, The EMBO journal.

[37]  Roger Fan,et al.  Dynamic activation of endothelial nitric oxide synthase by Hsp90 , 1998, Nature.

[38]  Y. Chen,et al.  A new member of the hsp90 family of molecular chaperones interacts with the retinoblastoma protein during mitosis and after heat shock , 1996, Molecular and cellular biology.

[39]  B. de Kruijff,et al.  Improved methods to isolate and subfractionate rat liver mitochondria. Lipid composition of the inner and outer membrane. , 1990, Biochimica et biophysica acta.

[40]  Luca Scorrano,et al.  A distinct pathway remodels mitochondrial cristae and mobilizes cytochrome c during apoptosis. , 2002, Developmental cell.