Home Programme

Preliminary Programme

For this advanced course, six highly relevant and related topics have been selected:

  1. Amyloid structures: Recent structural analysis suggests a molecular basis for amyloid polymorphism and alternative concepts for amyloid formation.
  2. Chaperones in amyloid formation: Molecular chaperones are an important cellular target to control pathogenic amyloid formation and possibly amyloid clearance. 
  3. Membrane-less organelles: Membrane-less compartments in cells (LLPS) may promote protein fibrilization in neurodegenerative and related diseases.
  4. Lipids and membranes in amyloid formation: Lipids/lipid membranes provide a hydrophobic surface which can catalyze the formation of amyloid(like) structures.  
  5. Functional amyloids: Functional amyloids reinforce the emerging concept that the amyloid fold is capable of carrying out a diversity of (biological) functions.
  6. Pathology of amyloids: Amyloids are observed in neurodegenerative and age-related diseases. The molecular basis for toxicity of amyloids is poorly understood.

Schedule

 

Morning 

Afternoon 

Friday September 1

Arrival & Welcome 

Saturday September 2 

Amyloid Structures 

Poster session A 

Keynote Evening lecture

Sunday September 3 

Chaperones 

Poster session A 

Keynote Evening lecture

Monday September 4 

Membrane-less organelles 

Excursion with

‘meet-the-Expert session’

on the beach 

Tuesday September 5 

Lipids and Membranes 

Poster session B 

Keynote Evening lecture

Wednesday September 6 

Functional amyloids 

Poster session B 

Keynote Evening lecture

Thursday September 7 

Pathology of amyloids 

Conference dinner 

Friday September 8  

Departure


Speakers Lecturers

Bernd Bukau

  • Chaperone action on amyloids

Assaf Friedler

  • Intrinsically disordered proteins as drug targets
  • Interactions and regulation of disordered proteins

Monika Fuxreiter

  • Context-dependent interactions within higher-order protein assemblies
  • Computational approaches to protein droplets and aggregation

Céline Galvagnion

  • Amyloid proteins–membrane interactions: The influence of lipids
  • Strategies to prevent alpha-synuclein aggregation and toxicity

Bernd Helms

  • Regulation of autophagy by lipid-mediated protein oligomerization

Sebastian Hiller

  • Biophysical principles of chaperone-client interactions resolved at the atomic level
  • Regulation of dynamic chaperone interactions networks and functional cycles
Zoya Leonenko
  • Biophysical approaches to study molecular mechanisms of Alzheimer’s disease that involve lipids
  • Molecular mechanism of Alzheimer’s disease: towards drug development

Sara Linse

  •  Cooperative biniding of α-synuclein to membranes. Mechanism of membrane-induced α-synuclein aggregation and the associated protein-lipid co-aggregation

Aline Miller

  • Engineering the self-assembly of functional amyloids; from the molecule to hydrogel for healthcare applications

Rick Morimoto

  •  Proteostasis Collapse in Aging and Neurodegenerative Disease

Daniel Otzen

  • Functional amyloids in bacteria: mechanisms and microbiology
  • Pathological protein oligomers in conformational diseases

Sheena Radford

  • Seeing amyloid: beautiful structures and toxic mechanisms

Frederic Rousseau and Joost Schymkowitz

  • Prediction of aggregation-prone and amyloidogenic sequences
  • Exploiting the sequence-specificity of protein aggregation as a platform technology for protein knockdown

Stefan Rüdiger

  • The cellular protein folding machinery
  • Chaperone control of Tau fibrils

Helen Sibil

  • Machinery for protein disaggregation
  • Huntington exon 1 aggregation via a reversible, liquid phase intermediate

Sjors Scheres

  • Structure determination of amyloids by helical reconstruction of cryo-EM images
  • Cryo-EM structures of tau filaments in neurodegenerative disease

Patricija van Oosten-Hawle

  • Protein Folding 2.0: How molecular chaperones reverse and protect against amyloid aggregation
  • The diverse nature of functional amyloids: from bacteria to humans.

Simon Alberti

  • Biomolecular condensates at the nexus of stress, disease and ageing







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