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Protein Aggregation

Protein Aggregation

Methods and Protocols

by Andrzej Stanisław Cieplak
Hardback
Publication Date: 31/10/2022

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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
ISBN:
9781071625965
9781071625965
Category:
Chemistry
Format:
Hardback
Publication Date:
31-10-2022
Language:
English
Publisher:
Springer
Country of origin:
United States
Dimensions (mm):
254x178mm
Weight:
1.5kg

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