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Saturday August 24 |
Afternoon |
Arrival and registration |
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18.30 |
Dinner |
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19.45 |
Opening remarks |
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20.00 |
Key note lecture |
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21.00 - 21.45 |
Chaperone machine #1 |
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Sunday August 25 |
08.30 - 12.15 |
Chaperone machine #2 |
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Structure |
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Co-chaperones #1 |
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12.15 |
Photo session and lunch |
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15.30 - 18.00 |
Poster session #1 (B - J) |
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18.30 |
Dinner |
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19.30 - 22.00 |
Co-chaperones #2 |
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Hsp90 in quality control |
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Hsp90 regulators |
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Monday August 26 |
Early morning to early afternoon |
Excursions |
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15.30 - 17.45 |
Poster session #2 (K - RE) |
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17.45 18.30 |
Welcome drink / speech, Mayor of Evolene Dinner |
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19.30 - 22.00 |
Hsp90 clients in disease |
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Hsp90 clients in the cell cycle |
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Tuesday August 27 |
08.30 - 12.15 |
Hsp90 and signal transduction |
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Hsp90s in evolution and development |
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12.30 |
Lunch |
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15.00 - 17.00 |
Poster session #3 (RI - Z) |
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17.15 - 19.30 |
Hsp90 relatives |
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Hsp90 family members as drug targets and therapeutics |
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20.00 |
Banquet, surprise, party |
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Wednesday August 28 |
Before or after breakfast |
Departure |
Session details
Evening session (19.45 - 21. 45) (chaired by Didier Picard)
19.45 Opening remarks by Didier Picard (Universite de Geneve, Geneve, Switzerland)
20.00 Key note lecture: David F. Smith (Mayo Clinic, Scottsdale, USA). Regulation of steroid signaling in vivo by the immunophilins and other Hsp90 co-chaperones.
21.00 Chaperone machine #1
Johannes Buchner (Technische Unversitaet Muenchen, Garching, Germany). Regulation of the Hsp90 chaperone machinery.
Chris Prodromou (Institute of Cancer Research, London, UK). Activation of the ATPase activity of Hsp90 by a novel heat shock-regulated co-chaperone, Aha1.
Morning sessions (08.30 - 12.15) (chaired by Johannes Buchner)
Chaperone machine #2
Sophie E. Jackson (Cambridge University, Cambridge, UK). Stimulation of the weak ATPase activity of human Hsp90 by a client protein.
Jason C. Young (Max-Planck-Institut, Martinsried, Germany). Regulation of the Hsp90/Hsp70 machinery by co-chaperones.
Maciej Zylicz (International Institute of Molecular and Cell Biology, Warszawa, Poland). Hsp90 interaction with the p53 tumour suppressor protein.
Klaus Richter (Technische Universität München, Garching, Germany). The Hsp90 ATPase.
Structure
Philippe Meyer (Institute of Cancer Research, London, UK). Crystal structure of the middle region of Hsp90 molecular chaperone.
Reza M. Salek (University College, London, UK). NMR studies of the solution structure and function of the Hsp90 N-terminal ATPase domain.
Malcolm D. Walkinshaw (University of Edinburgh, Edinburgh, UK). The interaction of Hsp90 with large immunophilins.
Co-chaperones #1
Thomas Ratajczak (University of Western Australia, Nedlands, Australia). An Hsp90 C-terminal motif targeted by the Hsp90 antagonist novobiocin contains specific leucine residues essential for Hsp90 dimerisation and interaction with steroid receptor-associated immunophilins.
Odutayo Odunuga (Rhodes University, Grahamstown, South Africa). Discrimination between the TPR-mediated interactions of mSTI1 with Hsp90 and Hsc70.
Evening sessions (19.30 - 22.00) (chaired by F. Ulrich Hartl)
Co-chaperones #2
Avrom Caplan (Mount Sinai School of Medicine, New York, USA). Role of Cdc37 in protein kinase folding and androgen receptor activation.
Wolfgang M. J. Obermann (Unversitaet Bonn, Bonn, Germany). Elucidating the role of novel organizers of the Hsp90/Hsp70 chaperone system.
Hsp90 in quality control
Joerg Hoehfeld (Unversitaet Bonn, Bonn, Germany). Cooperation of molecular chaperones with the ubiquitin / proteasome system.
Judith Frydman (Stanford University, Stanford, USA). The von Hippel-Lindau tumor suppressor as a model substrate for the degradation of misfolded cytosolic proteins.
Ami Citri (Weizmann Institute, Rehovot, Israel). The ubiquitin-ligase CHIP and the Hsp90 co-chaperone CDC37 mediate triage decisions relating to ErbB receptor tyrosine kinases.
Hsp90 regulators
Kevin A. Morano (University of Texas, Houston, USA). Sch9 and Sse1: two regulators of Hsp90 function in yeast.
Evening sessions (19.30 - 22.00) (chaired by Olivier Donzé)
Hsp90 clients in disease
Jianming Hu (Boston University, Boston, USA). Role of the Hsp90 complex in the assembly and reverse transcription of hepadnaviruses.
Lorenz Poellinger (Karolinska Institutet, Stockholm, Sweden). Regulation of dioxin and hypoxia signaling by hsp90 and co-chaperones.
Hsp90 clients in the cell cycle
Cayetano Gonzalez (EMBL, Heidelberg, Germany). Hsp90 and cell cycle control.
Juan Jimenez (Universidad Pablo de Olavide, Sevilla, Spain). The role of the Cdc2/Hsp90 complex in the switch from mitosis to apoptosis in the fission yeast.
Morning sessions (08.30 - 12.15) (chaired by Richard I. Morimoto)
Hsp90 and signal transduction
Didier Picard (Universite de Geneve, Geneve, Switzerland). In vivo functions of the Hsp90 chaperone system.
Robert Matts (Oklahoma State University, Stillwater, USA). Roles of Hsp90 and its associated co-chaperones in modulating protein kinase maturation and activation.
Brian C. Freeman (University of California, San Francisco, USA). Disassembly of transcriptional regulatory complexes by molecular chaperones.
Hsp90s in evolution and development
Christine Queitsch (University of Chicago & Harvard University, Cambridge, USA). Hsp90 as a capacitor of phenotypic variation.
Adina Breiman (Tel Aviv University, Tel Aviv, Israel). The involvement of plant FKBPs in development.
Joachim Clos (Bernhard Nocht Institute for Tropical Medicine, Hamburg, Germany). HSP90 homeostasis controls Leishmania donovanilife cycle stage differentiation.
Yair Argon (University of Chicago, Chicago, USA). GRP94 is essential for selective protein secretion by B lymphocytes and for progression of gastrulation in mouse embryogenesis.
Late afternoon sessions (17.15 - 19.30) (chaired by Yair Argon)
Hsp90 relatives
Christopher Nicchitta (Duke University Medical School, Durham, USA). Hsp90 - (poly)peptide interactions: immunobiology as a tool to identify the mechanism of substrate binding to GRP94.
Richard I. Morimoto (Northwestern University, Evanston, USA). Chaperone networks as stress sensors and protein misfolding diseases.
Hsp90 family members as drug targets and therapeutics
Sreyashi Basu (University of Connecticut School of Medicine, Farmington, USA). Hsp90 family members as key mediators of mammalian immune response.
Len Neckers (NCI-NIH, Rockville, USA). Hsp90 regulates multiple signaling pathways important for cancer cell survival.
Luke Whitesell (University of Arizona, Tucson, USA). Targeting Hsp90 function: identification of a novel small molecule inhibitor of tyrosine kinase activity in tumor cells.
Neal Rosen (Memorial Sloan-Kettering Cancer Center, New York, USA). Inhibitors of Hsp90 as potential anti-cancer therapeutics.