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Protein Aggregation as a Cause for Disease

Title data

Buchner, Johannes ; Scheibel, Thomas:
Protein Aggregation as a Cause for Disease.
In: Starke, Br. K. ; Gaestel, Matthias (ed.): Molecular chaperones in Health and Disease. - Berlin : Springer , 2006 . - pp. 199-219 . - (Handbook of Experimental Pharmacology ; 172 )
ISBN 978-3-540-25875-9
DOI: https://doi.org/10.1007/3-540-29717-0_9

Abstract in another language

The ability of proteins to fold into a defined and functional conformation is one of the most fundamental processes in biology. Certain conditions, however, initiate misfolding or unfolding of proteins. This leads to the loss of functional protein or it can result in a wide range of diseases. One group of diseases, which includes Alzheimer’s, Parkinson’s, Huntington’s disease, and the transmissible spongiformencephalopathies (prion diseases),
involves deposition of aggregated proteins. Normally, such protein aggregates are not found in properly functioning biological systems, because a variety of mechanisms inhibit their formation. Understanding the nature of these protective mechanisms together with the understanding of factors reducing or deactivating the natural protection machinery will be crucial for developing strategies to prevent and treat these disastrous diseases.

Further data

Item Type: Article in a book
Refereed: Yes
Keywords: Alzheimer; Amyloid; Huntington; Parkinson; Prion; Protein deposits;Quality control; Toxic species
Institutions of the University: Faculties
Faculties > Faculty of Engineering Science
Faculties > Faculty of Engineering Science > Chair Biomaterials
Faculties > Faculty of Engineering Science > Chair Biomaterials > Chair Biomaterials - Univ.-Prof. Dr. Thomas Scheibel
Profile Fields > Advanced Fields > Advanced Materials
Profile Fields > Advanced Fields > Molecular Biosciences
Profile Fields > Advanced Fields > Polymer and Colloid Science
Profile Fields > Emerging Fields > Food and Health Sciences
Profile Fields
Profile Fields > Advanced Fields
Profile Fields > Emerging Fields
Result of work at the UBT: Yes
DDC Subjects: 600 Technology, medicine, applied sciences
600 Technology, medicine, applied sciences > 620 Engineering
Date Deposited: 13 Oct 2015 10:08
Last Modified: 26 Nov 2015 10:51
URI: https://eref.uni-bayreuth.de/id/eprint/20330