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Mammalian versus yeast prions : biophysical insights in structure and assembly mechanisms

Title data

Vendrely, Charlotte ; Scheibel, Thomas:
Mammalian versus yeast prions : biophysical insights in structure and assembly mechanisms.
In: Doupher, Bridgette V. (ed.): Prions : New Research. - New York : Nova Science Publishers , 2006 . - pp. 251-284
ISBN 1-60021-019-8

Abstract in another language

Recently, an increasing number of studies have been focused on elucidating the secrets of prion proteins from mammals and yeasts. The most frequently asked question raised by
prion proteins concerns the mechanism of their conformational conversion starting from a soluble protein state into distinct supramolecular entities. So far it appears that soluble prion proteins originating from different organisms show different cellular localizations
and functions. However, certain common structural characteristics can be found, such as one intrinsically unstructured region. Such intrinsically unstructured region could explain the propensity of a soluble protein to assemble into supramolecular structures upon external triggers without complete denaturation of the involved protein. Based on conformational conversion studies, several assembly models have been developed. Since all of the assembly modes depend on the starting and the final structures of the underlying proteins, structural properties of both states have been investigated. While for
most of the proteins good structural data of the soluble form exist, little is known about the assembled structures. Several methods including X-Ray diffraction and microscopy
techniques have given certain insights into the structure of assembled prion proteins.
However, further work is necessary to resolve all of the structural features of prion proteins. In this review, we summarize work on both mammalian and yeast prion Proteins concerning their soluble structure, their assembly mechanisms, analysis of fibril stability and fibril structure.

Further data

Item Type: Article in a book
Refereed: Yes
Keywords: Transmissible spongiform encephalopathies; structure; amyloid; fibrils; aggregates; assembly
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 10:01
Last Modified: 26 Nov 2015 10:51
URI: https://eref.uni-bayreuth.de/id/eprint/20327