1. Early aggregation of Amyloid-β (1-42) studied by Fluorescence Correlation Spectroscopy
Mercedes Novo, Cibrán Pérez-González, Sonia Freire, and Wajih Al-Soufi
2. Preparation and investigation of crucial oligomers in the early stages of Aβ40 and Aβ42 aggregation
Bertrand Morel and Francisco Conejero-Lara
3. Preparation and fractionation of heterogeneous Aβ42 oligomers with different aggregation properties
Erica W. Chen and Zhefeng Guo
4. An efficient method of expression and purification of amyloid beta (Aβ1-42) peptide from E.coli
Dhiman Ghosh, Marielle Aulikki Wälti, and Roland Riek
5. Solid-state NMR structure of amyloid-β fibrils
Beat H. Meier and Anja Böckmann
6. Time-resolved in situ AFM measurement of growth rates of Aβ40 fibrils
Peter G. Vekilov and Peter G. Wolynes
7. Monitoring kinetics of pH-dependent aggregation and disaggregation of the Pmel17 repeat domain
Dexter N. Dean and Jennifer C. Lee
8.Analysis of Tau: nucleoporin interactions by Surface Plasmon Resonance Spectroscopy
Lisa Diez, Larisa E. Kapinos, Roderick Y. H. Lim, and Susanne Wegmann
9. Microfluidic chamber technology to study missorting and spreading of Tau protein in Alzheimer disease
Senthilvelrajan Kaniyappan, Varun Balaji, Yipeng Wang, and Eckhard Mandelkow
10. Using FRET-based biosensor cells to study the seeding activity of tau and α-synuclein Katherine N. Maina, Caroline Smet-Nocca, and Gal Bitan
11. Functional applications of stable tau oligomers in cell biology and electrophysiology studies Emily Hill, Kevin G. Moffat, Mark J. Wall, Henrik Zetterberg, Kaj Blennow, and Thomas K. Karikari
12. An additive-free model for tau self-assembly
Youssra K Al-Hilaly, Karen E Marshall, Liisa Lutter, Luca Biasetti, Kurtis Mengham, Charles R Harrington, Wei-Feng Xue, Claude M Wischik, and Louise C Serpell
13. Cross-linking mass spectrometry analysis of metastable compact structures in intrinsically disordered proteins
Dailu Chen and Lukasz A. Joachimiak
14. A validated method to prepare stable tau oligomers
Emily Hill, Kevin G. Moffat, Mark J. Wall, Henrik Zetterberg, Kaj Blennow, and Thomas K. Karikari
15. Light microscopy and dynamic light scattering to study liquid-liquid phase separation of Tau proteins in vitro
Janine Hochmair, Christian Exner, Christian Betzel, Eckhard Mandelkow, and Susanne Wegmann
16. Study of tau liquid-liquid phase separation in vitro
Solomiia Boyko and Witold K. Surewicz
17. Liquid-Liquid Phase Separation to study the association of proteins in solution
Irving Vega and Andrew Umstead
18. Mapping phase diagram of tau-RNA LLPS under live cell coculturing conditions
Yanxian Lin, Yann Fichou, Jennifer N. Rauch, Xuemei Zhang, Kenneth S. Kosik, and Songi Han
19. The role of buffers in wild-type HEWL amyloid fibril formation mechanism - a methodological approach Sandi Brudar and Barbara Hribar-Lee
20. Reproducible formation of insulin superstructures: amyloid-like fibrils, spherulites and particulates
Camilla Thorlaksen, Martin Busch Neergaard, Minna Groenning, and Vito Foderà
21. CD and solid-state NMR studies of low-order oligomers of transthyretin
Anvesh K. R. Dasar
Table of Contents:
Early aggregation of Amyloid-β (1-42) studied by Fluorescence Correlation Spectroscopy.- Preparation and investigation of crucial oligomers in the early stages of Aβ40 and Aβ42 aggregation.- Preparation and fractionation of heterogeneous Aβ42 oligomers with different aggregation properties.- An efficient method of expression and purification of amyloid beta (Aβ1-42) peptide from E.coli.- Solid-state NMR structure of amyloid-β fibrils.- Time-resolved in situ AFM measurement of growth rates of Aβ40 fibrils.- Monitoring kinetics of pH-dependent aggregation and disaggregation of the Pmel17 repeat domain.- Analysis of Tau:nucleoporin interactions by Surface Plasmon Resonance Spectroscopy.- Microfluidic chamber technology to study missorting and spreading of Tau protein in Alzheimer disease.- Using FRET-based biosensor cells to study the seeding activity of tau and α-synuclein.- Functional applications of stable tau oligomers in cell biology and electrophysiology studies.- An additive-free model for tau self-assembly.- Cross-linking mass spectrometry analysis of metastable compact structures in intrinsically disordered proteins.- A validated method to prepare stable tau oligomers.- Light microscopy and dynamic light scattering to study liquid-liquid phase separation of Tau proteins in vitro.- Study of tau liquid-liquid phase separation in vitro.- Liquid-Liquid Phase Separation to study the association of proteins in solution.- Mapping phase diagram of tau-RNA LLPS under live cell coculturing conditions.- The role of buffers in wild-type HEWL amyloid fibril formation mechanism - a methodological approach.- Reproducible formation of insulin superstructures: amyloid-like fibrils, spherulites and particulates.- CD and solid-state NMR studies of low-order oligomers of transthyretin.- Identifying biological and biophysical features of different maturation states of α-synuclein amyloid fibrils.- Preparation of α-synuclein fibril, ribbon and fibril-91 amyloid polymorphs for structural studies.- Propagation of distinct alpha-synuclein strains within human reconstructed neuronal network and associated neuronal dysfunctions.- Single-particle analysis of the interaction between molecules and protein aggregated species by Dual-Color Time-Resolved Fluorescence Spectroscopy.- FRAP & FRET investigation of α-synuclein fibrillization via liquid-liquid phase separation in vitro and in HeLa cells.- Spectrally-resolved FRET microscopy of -synuclein phase-separated liquid droplets.- Combined H-N cross polarization and carbonyl detection NMR spectroscopy allows to record high-resolution, high-sensitivity spectra of alpha-synuclein in bacterial cells.- Identification of distinct soluble states during fibril formation using multilinear analysis of NMR diffusiondata.- Structural analysis of SOD1 fibrils with mass spectrometry, limited proteolysis and atomic force microscopy (AFM).- Biophysical studies of LLPS and aggregation of TDP-43 LCD.- A spectrophotometric turbidity assay to study Liquid-Liquid Phase Separation of UBQLN2 in vitro.- An optimized SG detection method: Investigation of UBQLN2 effect on RNA-FUS interaction and SG formation.- Neuronal puncta/aggregate formation by wild-type and mutant UBQLN2.- In vivo analysis of a biomolecular condensate in the nervous system of C. elegans.- FLIM-FRET investigation of heterogeneous huntingtin aggregation in HeLa cells.- In vitro characterization of protein:nucleic acid liquid-liquid phase separation by microscopy methods and nanoparticle tracking analysis.- Cross-seeding assay in the investigation of the amyloid core of prion fibrils.- Mapping the domain structure and aggregation propensity of proteins using a Gateway plasmid vector system.
