Molecular Mechanisms of Amyloid Fibril Formation: The Lysozyme Model

1996 ◽  
Vol 90 (s34) ◽  
pp. 1P-1P
Author(s):  
D R Booth ◽  
V Bellotti ◽  
M Sunde ◽  
C V Robinson ◽  
P E Fraser ◽  
...  
Keyword(s):  
Molecular Mechanisms ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation

Chemical Kinetics for Bridging Molecular Mechanisms and Macroscopic Measurements of Amyloid Fibril Formation

2018 ◽  
Vol 69 (1) ◽  
pp. 273-298 ◽  
Author(s):  
Thomas C.T. Michaels ◽  
Anđela Šarić ◽  
Johnny Habchi ◽  
Sean Chia ◽  
Georg Meisl ◽  
...  
Keyword(s):  
Chemical Kinetics ◽  
Molecular Mechanisms ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation

scholarly journals Sulphur K-edge XANES Spectroscopy of Transthyretin Amyloid Fibres

2002 ◽  
Vol 16 (3-4) ◽  
pp. 281-283
Author(s):  
L. Gales ◽  
I. Cardoso ◽  
B. Fayard ◽  
M.J. Saraiva ◽  
A.M. Damas
Keyword(s):  
Oxidation State ◽  
Molecular Mechanisms ◽  
Amyloid Fibrils ◽  
Amyloid Fibril ◽  
Cellular Level ◽  
Fibril Formation ◽  
The Self ◽  
Xanes Spectroscopy ◽  
Amyloid Fibril Formation ◽  
Self Association

Transthyretin (TTR) amyloidosis results from the self-association of TTR leading to insoluble deposits that occur at the extra cellular level. Sulphur K-edge XANES spectroscopy was used to determine the sulphur oxidation state in transtyretin present in amyloid fibrils. These data is discussed in relation to molecular mechanisms involved in amyloid fibril formation.

Immunocytochemical Localization of Amyloid Protein AA in the “Dense Fibrillar Inclusions” of the Reticuloendothelical Cells

1977 ◽  
Vol 35 ◽  
pp. 438-439
Author(s):  
T. Shirahama ◽  
M. Skinner ◽  
A.S. Cohen
Keyword(s):  
Amyloid Fibril ◽  
Close Association ◽  
Gel Filtration ◽  
Fibril Formation ◽  
Amyloid Protein ◽  
Electron Microscopic ◽  
Amyloid Deposits ◽  
Amyloid Fibril Formation ◽  
Electron Microscopic Technique ◽  
Lysosomal System

A1thought the mechanisms of amyloidogenesis have not been entirely clarified, proteolysis of the parent proteins may be one of the important steps in the amyloid fibril formation. Recently, we reported that "dense fibrillar inclusions" (DFI), which had the characteristics of lysosomes and contained organized fibrillar profiles as well, were observed in the reticuloendothelial cells in close association with the foci of new amyloid deposits. We considered the findings as evidence for the involvement of lysosomal system in amyloid fibril formation (l). In the present study, we attempted to determine the identity of the contents of the DFI by the use of antisera against the amyloid protein (AA) and an immuno-electron microscopic technique.Amyloidosis was induced in CBA/J mice by daily injections of casein (l). AA was isolated from amyloid-laden spleens by gel filtration and antibody to it was produced in rabbits (2). For immunocytochemistry, the unlabeled antibody enzyme method (3) was employed.

Monitoring the prevention of amyloid fibril formation by α-crystallin

FEBS Journal ◽  
2007 ◽  
Vol 274 (24) ◽  
pp. 6290-6304 ◽  
Author(s):  
Agata Rekas ◽  
Lucy Jankova ◽  
David C. Thorn ◽  
Roberto Cappai ◽  
John A. Carver
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation
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