1.

Record Nr.

UNINA9910437835403321

Titolo

Protein quality control in neurodegenerative diseases / / Richard I. Morimoto, Yves Christen, editors

Pubbl/distr/stampa

New York, : Springer, 2013

ISBN

1-283-93490-6

3-642-27928-7

Edizione

[1st ed. 2013.]

Descrizione fisica

1 online resource (144 p.)

Collana

Research and perspectives in Alzheimer's disease, , 0945-6066

Altri autori (Persone)

MorimotoRichard I

ChristenYves

Disciplina

616.8

616.80471

Soggetti

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

The Regulation and Function of the Heat Shock Response by Eric Guisbert and Richard I. Morimoto -- The Endoplasmic Reticulum Unfolded Protein Response and Neurodegeneration by David Ron -- Proteostasis and the aging pathways by Ian Nicastro and Andrew Dillin -- The Membrane Sources of Macroautophagy by Daniel J. Klionsky, Melinda A. Lynch-Day, Jiefei Geng, and Wei-Lien Yen -- Selective Autophagy in Cellular Quality Control by Susmita Kaushik and Ana Maria Cuervo -- Quality Control of Proteins and Organelles by Autophagy by Noboru Mizushima -- The Role of the Co-Chaperone BAG3 in Selective Macroautophagy: Implications for Aging and Disease by Christian Behl -- Predicting Fates in Models of Neurodegenerative Disease: Longitudinal Measures of Protein Homeostasis in Live Neurons by Steven Finkbeiner -- Therapeutic Potential of Longevity Modulators as Neuroprotective Targets in Neurodegenerative Disease by Rafael Vazquez-Manrique, Cendrine Tourette and Christian Neri -- Subject code.

Sommario/riassunto

The health of the proteome depends upon protein quality control to regulate the proper synthesis, folding., translocation, and clearance of proteins. The cell is challenged constantyl by environmental and physiological stress, aging, and the chronic expressions of disease



associated misfolded proteins. Substantial evidence supports the hypothesis that the expression of damaged proteins initiates a cascade of molecular events that leads to Alzheimer's disease, Parkinson's disease, amyotrophic lateral sclerosis, Huntington's disease, and other diseases of protein conformation.