NDLI: Amyloid fibrils

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Amyloid fibrils

Content Provider	Scilit
Author	Rambaran, Roma N. Serpell, Louise C.
Copyright Year	2008
Description	Journal: Prion Amyloid refers to the abnormal fibrous, extracellular, proteinaceous deposits found in organs and tissues. Amyloid is insoluble and is structurally dominated by beta-sheet structure. Unlike other fibrous proteins it does not commonly have a structural, supportive or motility role but is associated with the pathology seen in a range of diseases known as the amyloidoses. These diseases include Alzheimer's, the spongiform encephalopathies and type II diabetes, all of which are progressive disorders with associated high morbidity and mortality. Not surprisingly, research into the physicochemical properties of amyloid and its formation is currently intensely pursued. In this chapter we will highlight the key scientific findings and discuss how the stability of amyloid fibrils impacts on bionanotechnology.
Related Links	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2634529/pdf https://www.landesbioscience.com/journals/prion/RambaranSerpellPRION2-3.pdf
Ending Page	117
Page Count	6
Starting Page	112
ISSN	19336896
e-ISSN	1933690X
DOI	10.4161/pri.2.3.7488
Journal	Prion
Issue Number	3
Volume Number	2
Language	English
Publisher	Informa UK Limited
Publisher Date	2008-07-01
Access Restriction	Open
Subject Keyword	Journal: Prion Pharmacology and Pharmacy Encephalopathies Structurally
Content Type	Text
Subject	Cell Biology Infectious Diseases Biochemistry Cellular and Molecular Neuroscience

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