Opening Amyloid-Windows to the secondary structure of proteins: The amyloidogenecity increases tenfold inside beta-sheets-Reference-Cited by-同舟云学术

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Opening Amyloid-Windows to the secondary structure of proteins: The amyloidogenecity increases tenfold inside beta-sheets

Published:2024-09 Issue: Volume:179 Page:108863
ISSN:0010-4825
Container-title:Computers in Biology and Medicine
language:en
Short-container-title:Computers in Biology and Medicine

Author:

Takács Kristóf,Varga Bálint,Farkas Viktor,Perczel András,Grolmusz Vince

Publisher

Elsevier BV

Reference22 articles.

1. Structure of the cross-β spine of amyloid-like fibrils;Nelson;Nature,2005

2. The amyloid state of proteins in human diseases;Eisenberg;Cell,2012

3. Protein aggregation in a nutshell: The splendid molecular architecture of the dreaded amyloid fibrils;Horvath;Curr. Protein Peptide Sci.,2019

4. The route from the folded to the amyloid state: Exploring the potential energy surface of a drug-like miniprotein;Taricska;Chem A Eur J,2020

5. Amyloidosis:: A clinical overview;Hazenberg;Rheumatic Dis. Clin. North America,2013

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