Protein misfolding and aggregation in ageing and disease

Roscoff (Brittany), France, April 11-15, 2007

 

Deadline for application: January 20, 2007

President : Mick TUITE

University of Kent, Department of Biosciences, CANTERBURY, Kent CT2 7NJ, United Kingdom
Phone: +44 1227 823 699 - Fax: +44 1227 763 912
E-mail: m.f.tuite@kent.ac.uk

Vice-Président : Ronald MELKI

Centre National de la Recherche Scientifique, Laboratoire d'Enzymologie et Biochimie Structurales,
Bâtiment 34, Avenue de la Terrasse, F-91198 GIF-sur-YVETTE, France
Phone: 01 69 82 35 03 - Fax: 01 69 82 31 29
E-mail: melki@lebs.cnrs-gif.fr

The conference will focus on the role of protein misfolding and aggregation in disease and ageing. In all species, proteins that do not remain correctly folded or that have failed to fold correctly are usually destroyed. In higher organisms, including humans, when this quality control process fails to remove the incorrectly folded proteins, a wide range of diseases can result. We already know that protein misfolding and subsequent aggregation is at the origin of over 20 different human diseases and in some cases these ‘conformational diseases’ are also associated with ageing. Neurodegenerative diseases such as Alzheimer’s disease and Creutzfeldt - Jakob disease perfectly illustrate the debilitating consequences of misfolding diseases; they are associated with high societal costs and result in an extensive loss of life expectancy and a dramatic reduction in the quality of life.

This conference will bring together 30 leading scientists working at the forefront of research into the structural and molecular basis for protein misfolding and aggregation in a variety of cellular systems and contexts. Although actively studied, the fundamental mechanism of the misfolding of a variety of polypeptides leading to their aggregation and associated diseases is far from being understood. The speakers will provide a comprehensive description, at the molecular level, of what we currently know about the early steps of aggregation, the high-resolution structures of prefibrillar and fibrillar amyloid states, and our ability to predict the aggregation propensity of polypeptides, all of which are crucial for the rational design of therapeutics preventing diseases associated with protein deposits. The scientific programme has been developed to ensure that an integrated view of this important field is provided and set into a wider clinical framework.

 

Invited Speakers

(provisional titles)

BLONDEL Marc (Roscoff, France) Mechanism of action of various unrelated antiprion drugs revealed by systematic reverse screening analysis

BRAAKMAN Ineke (Utrecht, The Netherlands) Protein folding and disulfide bond formation in the ER

BUEE Luc (Lille, France) Mechanisms of Tau aggregation in degenerating neurons: phosphorylation and peptide bond isomerization

CHITI Fabrizio (Firenze, Italy) The sequence and structural determinants of protein aggregation

DERREUMAUX Philippe (Paris, France) Computer simulations of amyloid-fibril formation

DJIAN Philippe (Paris, France) Protein aggregation in Huntington disease

DOBSON Chris (Cambridge, United Kingdom) Generic aspects of protein misfolding and aggregation disorders

EISENBERG David (Los Angeles, USA) Structural studies of aggregating proteins

GARRIDO Carmen (Dijon, France) Role of the chaperone HSP70 in apoptosis and erythropietic cells differentiation

GAZIT Ehud (Tel Aviv, Israel) Formation of amyloid fibrils and soluble amyloidal oligomers: Mechanism of association and novel directions for inhibition

GOLDBERG Michel (Paris, France) From Jacques Monod's interest in a folding code, to folding, misfolding and prions

GRATEAU Gilles (Paris, France) The changing face of amyloidosis

HARTL Ulrich (Martinsried, Germany) Modulation of polyQ proteotoxicity by molecular chaperones

JACKSON Graham (London, United Kingdom) Templated protein aggregation is the key event in the transmission of prion disease

KELLY Jeff (La Jolla, USA) Understanding and ameliorating protein misfolding diseases

KOPITO Ron (Stanford, USA) Cellular proteolytic strategies to suppress aggregate toxicity

LIPPENS Guy (Lille, France) Tau aggregation and Alzheimer's disease: a study by NMR

LOMAS, David (Cambridge, USA) Serpinopathies and Alzheimer’s disease’

MADDELEIN Marie-Lise (Bordeaux, France)Infectivity of the prion HET-s and amyloid formation in Podospora anserina

MELKI Ronald (Gif-sur-Yvette, France) Molecular chaperones and the aggregation of the Asn- and Gln-rich yeast prions

MUCHOWSKI Paul (San Francisco, USA) Genetic and biochemical analyses of mutant huntingtin

PEPYS Mark (London, United Kingdom) Amyloidosis: disease caused by amyloid

RADFORD Sheena (University of Leeds, United Kingdom) Insights into the molecular mechanism of amyloid assembly

SERIO Tricia (Providence, USA) Prion dynamics and protein-only inheritance

SERPELL Louise (Falmer, United Kingdom) The structural architecture of fibrils involved in protein misfolding diseases

SERRANO Luis (Heidelberg, Germany) Sequence determinants of amyloid toxicity

TEPLOW Dave (Los Angeles, USA) Multidisciplinary studies of amyloid beta-protein folding and assembly

TROTTIER Yvon (Strasbourg, France) Structural properties of polyglutamines

TUITE Mick (Canterbury, United Kingdom) Transmissible amyloids in yeast

WANKER Erich (Berlin-Buch, Germany) Identification and characterization of small molecules that modulate amyloid oligomerization

WEISSMAN Jonathan (San Francisco, USA) From conformation to phenotype: the physical basis of prion strain diversity

 

Deadline for application: January 20, 2007

 

Registration fee (including board and lodging)

350 € for PhD students
650 € 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 chairman 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.