Amyloid Fibril Formation and Seeding by Wild-Type Human Lysozyme and Its Disease-Related Mutational Variants

2000 ◽  
Vol 130 (2-3) ◽  
pp. 339-351 ◽  
Author(s):  
Ludmilla A. Morozova-Roche ◽  
Jesús Zurdo ◽  
Andrew Spencer ◽  
Wim Noppe ◽  
Veronique Receveur ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Wild Type ◽  
Human Lysozyme ◽  
Amyloid Fibril Formation

scholarly journals A Nanobody Binding to Non-Amyloidogenic Regions of the Protein Human Lysozyme Enhances Partial Unfolding but Inhibits Amyloid Fibril Formation

2013 ◽  
Vol 117 (42) ◽  
pp. 13245-13258 ◽  
Author(s):  
Erwin De Genst ◽  
Pak-Ho Chan ◽  
Els Pardon ◽  
Shang-Te D. Hsu ◽  
Janet R. Kumita ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Human Lysozyme ◽  
Amyloid Fibril Formation ◽  
Partial Unfolding

Investigating the inhibitory effects of entacapone on amyloid fibril formation of human lysozyme

2020 ◽  
Vol 161 ◽  
pp. 1393-1404
Author(s):  
Li Jin ◽  
Wen Gao ◽  
Chunhong Liu ◽  
Ning Zhang ◽  
Shruti Mukherjee ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Inhibitory Effects ◽  
Human Lysozyme ◽  
Amyloid Fibril Formation

scholarly journals Does deamidation of islet amyloid polypeptide accelerate amyloid fibril formation?

2018 ◽  
Vol 54 (98) ◽  
pp. 13853-13856 ◽  
Author(s):  
Yuko P. Y. Lam ◽  
Christopher A. Wootton ◽  
Ian Hands-Portman ◽  
Juan Wei ◽  
Cookson K. C. Chiu ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Islet Amyloid Polypeptide ◽  
Fibril Formation ◽  
Wild Type ◽  
Islet Amyloid ◽  
Amyloid Fibril Formation

Deamidation sites of hIAPP were determined and the amount of fibril formed in mutant hIAPPs was higher than in wild-type hIAPP.

scholarly journals Amyloid fibril formation of human lysozyme in vitro

1999 ◽  
Vol 39 (supplement) ◽  
pp. S152
Author(s):  
S. Goda ◽  
K. Takano ◽  
Y. Yamagata ◽  
S. Maki ◽  
K. Namba ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Human Lysozyme ◽  
Amyloid Fibril Formation

scholarly journals Application of Lysine-specific Labeling to Detect Transient Interactions Present During Human Lysozyme Amyloid Fibril Formation

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Minkoo Ahn ◽  
Christopher A. Waudby ◽  
Ana Bernardo-Gancedo ◽  
Erwin De Genst ◽  
Anne Dhulesia ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Human Lysozyme ◽  
Amyloid Fibril Formation ◽  
Transient Interactions

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.

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