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

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

• 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