Nicking and fragmentation are responsible for α‐lactalbumin amyloid fibril formation at acidic pH and elevated temperature

2021 ◽  
Author(s):  
Rahamtullah ◽  
Rajesh Mishra
Keyword(s):  
Elevated Temperature ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Acidic Ph ◽  
Amyloid Fibril Formation

Synthesis of a Regioregular Zwitterionic Conjugated Oligoelectrolyte, Usable as an Optical Probe for Detection of Amyloid Fibril Formation at Acidic pH

2005 ◽  
Vol 127 (7) ◽  
pp. 2317-2323 ◽  
Author(s):  
Anna Herland ◽  
K. Peter R. Nilsson ◽  
Johan D. M. Olsson ◽  
Per Hammarström ◽  
Peter Konradsson ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Optical Probe ◽  
Fibril Formation ◽  
Acidic Ph ◽  
Amyloid Fibril Formation

Amyloid Fibril Formation of the Mouse VLDomain at Acidic pH

Biochemistry ◽  
2002 ◽  
Vol 41 (10) ◽  
pp. 3389-3395 ◽  
Author(s):  
Sergey P. Martsev ◽  
Anatoly P. Dubnovitsky ◽  
Alexander P. Vlasov ◽  
Masaru Hoshino ◽  
Kazuhiro Hasegawa ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Acidic Ph ◽  
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

scholarly journals Polyphosphates induce amyloid fibril formation of α-synuclein in concentration-dependent distinct manners

2021 ◽  
Vol 296 ◽  
pp. 100510
Author(s):  
Keiichi Yamaguchi ◽  
Masatomo So ◽  
César Aguirre ◽  
Kensuke Ikenaka ◽  
Hideki Mochizuki ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Amyloid Fibril Formation

scholarly journals Investigation of a Peptide Responsible for Amyloid Fibril Formation of β2-Microglobulin byAchromobacterProtease I

2001 ◽  
Vol 277 (2) ◽  
pp. 1310-1315 ◽  
Author(s):  
Gennady V. Kozhukh ◽  
Yoshihisa Hagihara ◽  
Toru Kawakami ◽  
Kazuhiro Hasegawa ◽  
Hironobu Naiki ◽  
...  
Keyword(s):  
Amyloid Fibril ◽  
Fibril Formation ◽  
Β2 Microglobulin ◽  
Amyloid Fibril Formation
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