1.

Record Nr.

UNINA9910139612003321

Titolo

Protein chaperones and protection from neurodegenerative diseases / / edited by Stephan Witt

Pubbl/distr/stampa

Hoboken, : John Wiley & Sons, c2011

ISBN

1-283-25775-0

9786613257758

1-118-06389-9

1-118-06390-2

1-118-06388-0

Descrizione fisica

1 online resource (448 p.)

Collana

Wiley series on protein and peptide science

Altri autori (Persone)

WittStephan N

Disciplina

612.8

Soggetti

Molecular chaperones

Nervous system - Degeneration

Lingua di pubblicazione

Inglese

Formato

Materiale a stampa

Livello bibliografico

Monografia

Note generali

Description based upon print version of record.

Nota di bibliografia

Includes bibliographical references and index.

Nota di contenuto

PROTEIN CHAPERONES AND PROTECTION FROM NEURODEGENERATIVE DISEASES; CONTENTS; Preface; Introduction; Contributors; 1 Intrinsically Disordered Chaperones and Neurodegeneration; 2 Redox Regulation of Protein Misfolding, Synaptic Damage, and Neuronal Loss in Neurodegenerative Diseases; 3 Chaperone-Mediated Autophagy and Parkinson's Disease; 4 Chaperone and Anti-Chaperone Properties of Synuclein: Implications for Development, Aging, and Neurodegenerative Disease; 5 The Ubiquitin-Proteasome System in Neurodegenerative Diseases: More than the Usual Suspects

6 Regulation of the Polyglutamine Androgen Receptor by the Hsp90/Hsp70-Based Chaperone Machinery7 Amyloid Remodeling by Hsp104; 8 Chaperone-Dependent Amyloid Assembly and Prion Toxicity; 9 Modulation of Amyloid Propagation in Yeast by Hsp70 and its Regulators and Chaperone Partners; 10 ALS and the Copper Chaperone CCS; 11 Emerging Area: TorsinA, a Novel ATP-Dependent Factor Linked to Dystonia; 12 Therapeutics: Harnessing the Power of Molecular and Pharmacological Chaperones; Index

Sommario/riassunto

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