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.



Afternoon & Evening

September 1

Arrival and Welcome

September 2

Amyloid structures
Technology lecture

Poster session A
Keynote lecture

September 3

Technology lecture

Poster session B
Keynote lecture

September 4

Technology lecture


September 5

Lipids & Membranes
Technology lecture

Poster session C
Keynote lecture

September 6

Functional Amyloids
Technology lecture

Poster session D
Keynote lecture

September 7

Amyloid Pathology
Technology lecture

Poster session A
Student short talks Conference diner

September 8


Speakers Lecturers

Simon Alberti
  • Biomolecular condensates at the nexus of stress, disease and ageing
Bernd Bukau
  • Chaperone action on amyloids
Mireille Claessens
  • Alpha-Synuclein fibril strains: ​​​​​​​Decoding Strain Transformations and their possible role in Parkinson's disease.
  • (Dis)functional membrane interactions of the intrinsically disordered protein alpha-synuclein.
Assaf Friedler
  • Intrinsically disordered proteins as drug targets
  • Interactions and regulation of disordered proteins
Monika Fuxreiter
  • Cellular landscapes of protein interactions.
  • Sequence-based determinants of aggregation within protein condensates.
Céline Galvagnion
  • Lipid changes associated with alpha-synuclein and Parkinson’s Disease pathology
  • Strategies to prevent and revert apha-synuclein aggregation and lipid changes associated with Parkinson’s Disease
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
  • Heterotypic Amyloid interactions and their effect on amyloid assembly
  • Evolutionary imprints of protein aggregation on protein structure and chaperone interactions
Stefan Rüdiger
  • The cellular protein folding machinery
  • Chaperone control of Tau fibrils
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.

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