Regulation of Amyloid Fibril Formation from Human Islet Amyloid Polypeptide by a Ligand Binding to the Fusion of FK506-binding Protein and the Insertion-in-Flap Domain

2017 ◽  
Vol 38 (11) ◽  
pp. 1293-1298
Author(s):  
Soyoung Yoon ◽  
Soohyun Kim ◽  
Hana Im ◽  
Kyunghee Lee
Keyword(s):  
Ligand Binding ◽  
Amyloid Fibril ◽  
Binding Protein ◽  
Islet Amyloid Polypeptide ◽  
Fibril Formation ◽  
Human Islet ◽  
Islet Amyloid ◽  
Fk506 Binding Protein ◽  
Human Islet Amyloid Polypeptide ◽  
Amyloid Fibril Formation

scholarly journals The flanking peptides issue from the maturation of the human islet amyloid polypeptide (hIAPP) slightly modulate hIAPP-fibril formation but not hIAPP-induced cell death

Biochimie ◽  
2020 ◽  
Vol 170 ◽  
pp. 26-35 ◽  
Author(s):  
Shadai Salazar Vazquez ◽  
Bertrand Blondeau ◽  
Pierre Cattan ◽  
Mathieu Armanet ◽  
Ghislaine Guillemain ◽  
...  
Keyword(s):  
Cell Death ◽  
Islet Amyloid Polypeptide ◽  
Fibril Formation ◽  
Human Islet ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide

Ruthenium complexes as novel inhibitors of human islet amyloid polypeptide fibril formation

Metallomics ◽  
2013 ◽  
Vol 5 (12) ◽  
pp. 1599 ◽  
Author(s):  
Lei He ◽  
Xuesong Wang ◽  
Cong Zhao ◽  
Hongfei Wang ◽  
Weihong Du
Keyword(s):  
Islet Amyloid Polypeptide ◽  
Ruthenium Complexes ◽  
Fibril Formation ◽  
Human Islet ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide

scholarly journals Time dependence of NMR observables reveals salient differences in the accumulation of early aggregated species between human islet amyloid polypeptide and amyloid-β

2018 ◽  
Vol 20 (14) ◽  
pp. 9561-9573 ◽  
Author(s):  
Anaïs R. F. Hoffmann ◽  
Lucie Caillon ◽  
Lilian Shadai Salazar Vazquez ◽  
Pierre-Alexandre Spath ◽  
Ludovic Carlier ◽  
...  
Keyword(s):  
Time Dependence ◽  
Islet Amyloid Polypeptide ◽  
Proton Nmr ◽  
Amyloid Β ◽  
Fibril Formation ◽  
Human Islet ◽  
Islet Amyloid ◽  
Human Islet Amyloid Polypeptide

Proton NMR shows that IAPP fibril formation does not involve the accumulation of early aggregated species, in contrast with Aβ.

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