Protein misfolding and assembly in ageing and disease
Roscoff (Brittany), France, June 5-9, 2010
Registration closed
Chairperson: Ronald Melki
CNRS – UPR 3082, Laboratoire d'enzymologie et de biochimie structurales, Bât.34,
91198 Gif-sur-Yvette, France
Phone: 33 169823503 – Fax: 33 169823129
Mail : melki@lebs.cnrs-gif.fr
Vice-Chairperson: Louise Serpell
Department of Biochemistry, University of Sussex, John Maynard Smith Building,
Falmer BN1 9QG, UK
Phone: 44 1273 877363 – Fax: 44 1273 679433
Mail : L.C.Serpell@sussex.ac.uk
Protein misfolding and assembly is associated with at least 30 human diseases collectively known as “conformational” or misfolding diseases. Abnormal protein assembly and aggregation is also associated with ageing. The deposition of polypeptides such as α-synuclein, huntingtin, amyloid-ß and Tau in the human brain lead to Parkinson's, Huntington's and Alzheimer's diseases respectively. Other protein deposits lead to the development of a “gain of toxic function” and are at the origin diabetes type 2 (amylin) and haemodialysis-related amyloidosis (β2-microglobulin).
It is clear that transmissible diseases are linked to the aggregation of a protein belonging to a group that includes Creutzfeldt-Jacob disease (CJD), scrapie and Bovine Spongiform Encephalopathy (BSE) and there is now compelling evidence that Tau, α-synuclein and huntingtin aggregates have infectious properties. One of the issues that remains poorly understood is what makes aggregated proteins infectious? Another issue critical for the rational design of therapeutics for these diseases, is the understanding of the role of cellular factors such as molecular chaperones that modulate protein aggregation and the clearance of protein aggregates. This meeting, intends to explore the relationship between protein misfolding and disease, the relationship between the genetic background and disease appearance, the specific signaling pathways at the origin of cell degeneration, in particular neuronal degeneration, that are triggered by protein aggregation, the effect of protein aggregation on neuronal plasticity and the consequences of the inflammatory response triggered by protein aggregation.
- Molecular events associated with protein aggregation
- Molecular basis of protein assembly into toxic oligomeric and fibrillar structures
- Disease implications of protein aggregation
- Cellular factors important for the regulation of protein folding & aggregation
- Cellular responses to protein aggregation and clearance of protein aggregates
- Signaling, neurodegeneration and brain plasticity
- Genetic and therapeutic approaches to protein misfolding disorders
Invited speakers
(provisional titles)
BELLOTTI Vittorio (Pavia, Italy)
Amyloidoses
BERTOLOTTI Anne (Paris, France)
Protein misfolding in neurodegenerative diseases
BLONDEL Marc (Roscoff, France)
Screening for anti-prion drugs using yeast cells
BOCKMANN Anja (Lyon, France)
Structural studies of protein fibrils by high-resolution solid-state NMR
BRUNDIN Patrik (Lund, Sweden)
Parkinson's disease pathology
BUEE Luc (Lille, France)
Tautopathies
BUXBAUM Joël (San Diego, USA)
Can an amyloid precursor be an amyloid inhibitor? Transthyretin as an example
CROWTHER Damian (Cambridge, UK)
Modulating protein aggregation and assessing the toxicity using animal model systems
DERREUMAUX Philippe (Paris, France)
Molecular simulation of protein aggregation
DILLIN Andrew (La Jolla, USA)
Aging is an event of proteostasis decline
DOBSON Christopher (Cambridge, UK)
Generic aspects of protein aggregation disease
GOLDBERG Alfred (Boston, USA)
Clearance of toxic protein aggregates
HARTL Ulrich (Martinsreid, Germany)
Characterizing aberrant protein interactions in amyloidogenic aggregation
HIRSCH Etienne (Paris, France)
Brain plasticity in Parkinson's disease
KOPITO Ron (Stanford, USA)
Protein aggregates clearance /infectivity of protein aggregates
LOEFFLER Jean-Philippe (Strasbourg, France)
Molecular signaling and neurodegeneration
LOMAS David (Cambridge, UK)
Serpin polymers and disease
MANDELKOW Eva Maria (Hamburg, Germany)
Modelling tau pathology in Alzheimer's disease: From beta structure to transgenic mice
MEZGER Valérie (Paris, France)
Heat shock factors in normal and pathological brain development
MORIMOTO Richard (Evanston, USA)
Stress, ageing and neurodegenerative diseases
NOLLEN Ellen (Groningen, The Netherlands)
Genetic modifiers of protein aggregation
RADFORD Sheena (Leeds, UK)
Switching amyloid aggregation on and off: atomistic studies of beta-2-microglobulin
ROUSSEAU Frédéric (Bruxelles, BE)
Evolutionary pressure and protein aggregation
SCHULDINER Maya (Revohot, Israel)
A systematic approach to study protein folding in the endoplasmic reticulum
SERIO Tricia (Providence, USA)
Cellular effect of Sup35 yeast prion
STANIFORTH Rosemary (Sheffield, UK)
Assembly, folding and domain swapping in cystatins
STEFANI Massimo (Firenze, Italy)
Oligomer and membrane biophysical features both contribute to amyloid cytotoxicity
TEPLOW David (Los Angeles, USA)
Early conformational changes in polypeptides leading to nucleation and amyloid formation
TRILLER Antoine (Paris, France)
Synaptic plasticity and receptor binding
TUITE Mick (Canterbury, UK)
The control of de novo prion formation in yeast
WALTER Peter (San Francisco, USA)
The unfolded protein response in health and disease
WEISSMAN Jonathan (San Francisco, USA)
Molecular basis of prion strains
Registration closed
Registration fee (including board and lodging)
370 € for PhD students
540 € for other participants
Application for registration
The total number of participants is limited to about 115 and all participants are expected to attend for the whole duration of the conference. Selection is made on the basis of the affinity of potential participants with the topics of the conference. Scientists and PhD Students interested in the meeting should send:
- their curriculum vitae
- the list of their main publications for the 3 last years
- the abstract of their presentation
to the Chairperson of the conference before the deadline. After it, the chairman will select the participants. Except in some particular cases approved by the Chairperson, it is recommended that all selected participants present their work during the conference, either in poster form or by a brief in- session talk. The organizers choose the form in which the presentations are made. No payment will be sent with application. Information on how and when to pay will be mailed in due time to those selected.