scholarly journals Appearance of annular ring-like intermediates during amyloid fibril formation from human serum albumin

2015 ◽  
Vol 17 (35) ◽  
pp. 22862-22871 ◽  
Author(s):  
Shruti Arya ◽  
Arpana Kumari ◽  
Vijit Dalal ◽  
Mily Bhattacharya ◽  
Samrat Mukhopadhyay

A profound conformational conversion coupled with the temporal evolution of morphologically-distinct ring-like nanoscopic intermediates were monitored during the amyloid assembly of human serum albumin into β-sheet-rich fibrils.

PLoS ONE ◽  
2014 ◽  
Vol 9 (1) ◽  
pp. e84552 ◽  
Author(s):  
Giuseppe Sancataldo ◽  
Valeria Vetri ◽  
Vito Foderà ◽  
Gianluca Di Cara ◽  
Valeria Militello ◽  
...  

2006 ◽  
Vol 110 (42) ◽  
pp. 20733-20736 ◽  
Author(s):  
Pablo Taboada ◽  
Silvia Barbosa ◽  
Emilio Castro ◽  
Víctor Mosquera

Biochemistry ◽  
2016 ◽  
Vol 55 (24) ◽  
pp. 3345-3348 ◽  
Author(s):  
Bibin G. Anand ◽  
Kriti Dubey ◽  
Dolat Singh Shekhawat ◽  
Karunakar Kar

Amyloid ◽  
2016 ◽  
Vol 23 (2) ◽  
pp. 67-75 ◽  
Author(s):  
Hiroka Takase ◽  
Masafumi Tanaka ◽  
Aki Yamamoto ◽  
Shiori Watanabe ◽  
Sanae Takahashi ◽  
...  

2016 ◽  
Vol 29 (12) ◽  
pp. 611-618 ◽  
Author(s):  
F. Taghavi ◽  
M. Habibi-Rezaei ◽  
M. Bohlooli ◽  
M. Farhadi ◽  
M. Goodarzi ◽  
...  

RSC Advances ◽  
2018 ◽  
Vol 8 (2) ◽  
pp. 980-986 ◽  
Author(s):  
Heloise R. Barros ◽  
Maria Kokkinopoulou ◽  
Izabel C. Riegel-Vidotti ◽  
Katharina Landfester ◽  
Héloïse Thérien-Aubin

Formation of amyloid protein fibrils is associated with degenerative diseases. Here, the interaction mechanism between globular and fibrillar proteins with AuNPs were investigated in order to potentially control and reverse the fibrillation process.


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