Bio-nanoimaging protein misfolding & aggregation / edited by Vladimir N. Uversky, Yuri L. Lyubchenko.

• 1. Molecular Mechanisms of Protein Misfolding / Leonid Breydo, Vladimir N. Uversky -- Part I: Nanoimaging and Nanotechnology of Aggregating Proteins: A. In Vitro Approaches -- 2. Amyloid Fibril Length Quantification by Atomic Force Microscopy / Wei-Feng Xue -- 3. Imaging Nucleation, Growth and Heterogeneity in Self-Assembled Amyloid Phases / Neil R. Anthony, Keith M. Berland, Anil K. Mehta, David G. Lynn, W. Seth Childers -- 4. Molecular-Level Insights into Amyloid Polymorphism from Solid-State Nuclear Magnetic Resonance / Robert Tycko -- 5. Single-Molecule Imaging of Amyloid-β Protein (Aβ) of Alzheimer’s Disease: From Single-Molecule Structures to Aggregation Mechanisms and Membrane Interactions / Marie-Isabel Aguilar, Xu Hou, Dusan Losic, Adam I. Mechler, Lisandra L. Martin, David H. Small -- 6. Nanomechanics of Neurotoxic Proteins: Insights at the Start of the Neurodegeneration Cascade / Rubén Hervás, María del, Carmen Fernández-Ramírez, Laura Esther Abelleira, Douglas V. Laurents, Mariano Carrión-Vázquez -- 7. Reporters of Amyloid Structural Polymorphism / Harry LeVine III, K. Peter, R. Nilsson, Per Hammarström -- 8. Conformation-Dependent Antibodies as Tools for Characterization of Amyloid Protein Aggregates / Jessica W. Wu, Leonid Breydo -- Part II: Nanoimaging and Nanotechnology of Aggregating Proteins: B. In Vivo Approaches -- 9. Analyzing Alzheimer’s Disease-Related Protein Deposition In Vivo By Multiphoton Laser Scanning Microscopy / Nikita Rudinskiy, Tara L. Spires-Jones -- 10. Probing Amyloid Aggregation and Morphology In Situ by Multiparameter Imaging and Super-Resolution Fluorescence Microscopy / Gabriele S. Kaminski Schierle, Markus Sauer, Clemens F. Kaminski -- 11. Imaging of Amyloid-β Aggregation Using a Novel Quantum dot Nanoprobe and its Advanced Applications / Kiyotaka Tokuraku, Tsuneya Ikezu -- 12. Studying the Molecular Determinants of Protein Oligomerization in Neurodegenerative Disorders by Bimolecular Fluorescence Complementation / Federico Herrera, Susana Gonçalves, Joana Branco dos Santos, Tiago Fleming Outeiro -- 13. Structure-Specific Intrinsic Fluorescence of Protein Amyloids Used to Study their Kinetics of Aggregation / Fiona T.S. Chan, Dorothea Pinotsi, S. Gabriele, Kaminski Schierle, Clemens F. Kaminski -- 14. Real-Time Monitoring of Inclusion Formation in Living Zebrafish / Sophie Rothhämel, Katrin Strecker, Christian Haass, Bettina Schmid -- 15. Scanning for Intensely Fluorescent Targets (SIFT) in the Study of Protein Aggregation at the Single-Particle Level / Georg Nübling, Armin Giese. 
• Part III: Polymorphism of Protein Misfolding and Aggregated Species -- 16. The Molecular Basis For TGFBIp-Related Corneal Dystrophies / Marcel Stenvang, Maria Andreasen, Jan Johannes Enghild, Daniel E. Otzen -- 17. Aβ Fibril Polymorphism and Alzheimer’s Disease / Magdalena Bereza, Marcus Fändrich -- 18. Structural Heterogeneity and Bioimaging of S100 Amyloid Assemblies / Sofia B. Carvalho, Isabel Cardoso, Hugo M. Botelho, Kiran Yanamandra, Günter Fritz, Cláudio M. Gomes, Ludmilla A. Morozova-Roche -- 19. Polymorphism of Tau Fibrils / Yoshiaki Furukawa -- 20. Amyloid-Like Protofibrils with Different Physical Properties / Annalisa Relini -- 21. Insulin Oligomers: Detection, Characterization and Quantification Using Different Analytical Methods / Mirco Sorci, Georges Belfort -- 22. Imaging the Morphology and Structure of Apolipoprotein Amyloid Fibrils / Yee-Foong Mok, Chai Lean Teoh, Geoffrey J. Howlett, Michael D.W. Griffin -- 23. Polymorphism of Amyloid Fibrils and their Complexes with Catalase / Nathaniel G.N. Milton, J. Robin Harris -- 24. On Possible Function and Toxicity of Multiple Oligomeric/Conformational States of a Globular Protein – Human Stefin B / Eva Žerovnik -- 25. Fibrillar Structures of Yeast Prion Sup35 In Vivo / Hideki Taguchi, Shigeko Kawai-Noma -- 26. Glycosaminoglycans and Fibrillar Polymorphism / G. Malmos, Daniel E. Otzen -- 27. Dopamine-Induced α-Synuclein Oligomers / Agata Rekas, Roberto Cappai, Cyril Curtain, Chi Le Lan Pham -- 28. The Formation of Amyloid-Like Superstructures: On the Growth of Amyloid Spherulites / Vito Foderà, Athene M. Donald -- 29. Characterizing Nanoscale Morphologic and Mechanical Properties of α-Synuclein Amyloid Fibrils with Atomic Force Microscopy / Kim K.M. Sweers, Martin Stöckl, Martin L. Bennink, Vinod Subramaniam -- 30. Polymorphism in Casein Protein Aggregation and Amyloid Fibril Formation /David C. Thorn, Heath Ecroyd, John A. Carver -- 31. Structural Basis for the Polymorphism of β-Lactoglobulin Amyloid-Like Fibrils / Corianne C. van den Akker, Michael Schleeger, Mischa Bonn, Gijsje H. Koenderink -- 32. Fibrillation and Polymorphism of Human Serum Albumin /, Silvia Barbosa, Pablo Taboada, Víctor Mosquera -- 33. Formation of α-Helix-Based Twisted Ribbon-Like Fibrils from Ionic-Complementary Peptides /, Meng Qin, Dawei Zou, Yi Cao, Wei Wang -- 34. Polymorphism, Metastable Species and Interconversion: The Many States of Glucagon Fibrils / Shirin D. Ghodke, Grethe V. Jensen, Anna S.P. Svane, Katrin Weise, Anne Søndergaard, Manja A. Behrens, Jan Skov Pedersen, Niels Chr Nielsen, Jesper Søndergaard Pedersen, Roland Winter, Daniel E. Otzen. 
• Part IV: Polymorphism of Protein Misfolding and Aggregation Processes -- 35. Multiple Pathways of Lysozyme Aggregation / Martin Muschol, Shannon E. Hill, Mentor Mulaj -- 36. Structure–Function Studies of Amyloid Pores in Alzheimer’s Disease as a Case Example of Neurodegenerative Diseases / Fernando Teran Arce, Hyunbum Jang, Laura Connelly, Srinivasan Ramachandran, Bruce L. Kagan, Ruth Nussinov, Ratnesh Lal -- 37. Nanoscale Optical Imaging of Protein Amyloids / Samrat Mukhopadhyay, Vijit Dalal, Shruti Arya -- 38. Assembly of Amyloid β-Protein Variants Containing Familial Alzheimer’s Disease-Linked Amino Acid Substitutions / Aida Attar, Derya Meral, Brigita Urbanc, Gal Bitan -- 39. Role of Aberrant α-Synuclein–Membrane Interactions in Parkinson’s Disease / Amy M. Griggs, Daniel Ysselstein, Jean-Christophe Rochet -- 40. ELOA – Equine Lysozyme Complexes with Oleic Acid: Structure and Cytotoxicity Studied by Bio-Imaging Techniques / Vladana Vukojević, Alexei Klechikov, Ludmilla A. Morozova-Roche -- 41. Structure of a Misfolded Intermediate of a PDZ Domain / Alfonso De Simone, Stefano Gianni, Michele Vendruscolo -- 42. Intranuclear Amyloid – Local and Quantitative Analysis of Protein Fibrillation in the Cell Nucleus / Florian Arnhold, Anna von Mikecz -- 43. Conversion of α-Helical Proteins into an Alternative β-Amyloid Fibril Conformation / Jason C. Collins, Lesley H. Greene -- 44. The Effect of Shear Flow on Amyloid Fibril Formation and Morphology / Innocent B. Bekard, Dave E. Dunstan. 

• Bio-Nanoimaging: Protein Misfolding & Aggregation provides a unique introduction to both novel and established nanoimaging techniques for visualization and characterization of misfolded and aggregated protein species. The book is divided into three sections covering: - Nanotechnology and nanoimaging technology, including cryoelectron microscopy of beta(2)-microglobulin, studying amyloidogensis by FRET; and scanning tunneling microscopy of protein deposits - Polymorphisms of protein misfolded and aggregated species, including fibrillar polymorphism, amyloid-like protofibrils, and insulin oligomers - Polymorphisms of misfolding and aggregation processes, including multiple pathways of lysozyme aggregation, misfolded intermediate of a PDZ domain, and micelle formation by human islet amyloid polypeptide. Protein misfolding and aggregation is a fast-growing frontier in molecular medicine and protein chemistry. Related disorders include cataracts, arthritis, cystic fibrosis, late-onset diabetes mellitus, and numerous neurodegenerative diseases like Alzheimers and Parkinsons. Nanoimaging technology has proved crucial in understanding protein-misfolding pathologies and in potential drug design aimed at the inhibition or reversal of protein aggregation. Using these technologies, researchers can monitor the aggregation process, visualize protein aggregates and analyze their properties.

Ämnesord

Imaging systems.  (LCSH)

Nanotechnology.  (LCSH)

Protein folding  -- Computer simulation. (LCSH)

Publikations- och innehållstyp

572.6 (DDC)

Ue.04823 (kssb/8 (machine generated))