Protein Chaperones and Protection from Neurodegenerative Diseases. Wiley Series in Protein and Peptide Science

  • ID: 2170955
  • Book
  • 444 Pages
  • John Wiley and Sons Ltd
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How protein chaperones protect cells from neurodegenerative diseases

Including contributions from leading experts, Protein Chaperones and Protection from Neurodegenerative Diseases provides an in–depth exploration of how protein chaperones are involved in shielding cells from toxic aggregated or misfolded protein states that cause ALS, Parkinson′s, and related diseases.

Examining how different protein chaperones ameliorate the toxicity of proteins that are known to cause neurodegenerative damage, the book addresses both research and clinical perspectives on chaperone and anti–chaperone properties. The intersection of molecular chaperones and neurodegeneration is an intensely studied area, partly because of the potential for manipulating the expression of molecular chaperones to thwart the progression of debilitating diseases, and partly because of the ever–aging global population.

Discussing the potential to harness the power of protein chaperones, and future directions for research, discovery, and therapeutics, this book is essential reading for scientists working in the fields of biochemistry, molecular medicine, pharmacology and drug discovery, biotechnology and pharmaceutical companies, advanced students, and anyone interested in this cutting–edge topic.

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1 Intrinsically Disordered Chaperones and Neurodegeneration (Vladimir N. Uversky).

2 Redox Regulation of Protein Misfolding, Synaptic Damage, and Neuronal Loss in Neurodegenerative Diseases (Tomohiro Nakamura and Stuart A. Lipton).

3 Chaperone–Mediated Autophagy and Parkinson s Disease (Marta Martinez–Vicente and Ester Wong).

4 Chaperone and Anti–Chaperone Properties of Synuclein: Implications for Development, Aging, and Neurodegenerative Disease (Makoto Hashimoto, Kazuanri Sekiyama, Akio Sekigawa, and Masayo Fujita).

5 The Ubiquitin Proteasome System in Neurodegenerative Diseases: More than the Usual Suspects (Anne Bertolotti).

6 Regulation of the Polyglutamine Androgen Receptor by the Hsp90/Hsp70–Based Chaperone Machinery (Andrew P. Lieberman and William B. Pratt).

7 Amyloid Remodeling by Hsp104 (James Shorter).

8 Chaperone–Dependent Amyloid Assembly and Prion Toxicity (Daniel W. Summers, Katie J. Wolfe, and Douglas M. Cyr).

9 Modulation of Amyloid Propagation in Yeast by Hsp70 and its Regulators and Chaperone Partners (Daniel C. Masison).

10 ALS and the Copper Chaperone CCS (Marjatta Son and Jeffrey L. Elliott).

11 Emerging Area: TorsinA, a Novel ATP–Dependent Factor Linked to Dystonia (Michal Zolkiewski and Hui–Chuan Wu).

12 Therapeutics: Harnessing the Power of Molecular and Pharmacological Chaperones (David S. Gross, Ronald L. Klein and Stephan N. Witt).


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Stephan N. Witt is a Professor in the Department of Biochemistry and Molecular Biology at the Louisiana State University Health Sciences Center in Shreveport, Louisiana. He obtained his PhD in biophysical chemistry from the California Institute of Technology.??Dr. Witt is a member of the editorial board of Cell Stress and Chaperones. He has served on numerous NIH study sections, has authored over forty scientific publications, and edited a book on using yeast as a model for human disease. His research focuses on identifying genes and small molecules that can be used against Parkinson′s disease.

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