The Route from the Folded to the Amyloid State: Exploring the Potential Energy Surface of a Drug‐Like Miniprotein-Reference-Cited by-同舟云学术

The Route from the Folded to the Amyloid State: Exploring the Potential Energy Surface of a Drug‐Like Miniprotein

Published:2019-12-27 Issue:9 Volume:26 Page:1968-1978
ISSN:0947-6539
Container-title:Chemistry – A European Journal
language:en
Short-container-title:Chem. Eur. J.

Author:

Taricska Nóra¹,Horváth Dániel¹,Menyhárd Dóra K.¹,Ákontz‐Kiss Hanna¹,Noji Masahiro²,So Masatomo²,Goto Yuji²,Fujiwara Toshimichi²,Perczel András¹^ORCID

Affiliation:

1. Laboratory of Structural Chemistry and Biology & MTA-ELTE Protein Modeling Research Group Eötvös Loránd University Pázmány Péter sétány 1A 1117 Budapest Hungary

2. Institute for Protein Research Osaka University 3-2 Yamadaoka Suita, Osaka 565-0871 Japan

Funder

Magyar Tudományos Akadémia

Publisher

Wiley

Subject

General Chemistry,Catalysis,Organic Chemistry

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/chem.201903826

Reference63 articles.

1. Human LilrB2 Is a β-Amyloid Receptor and Its Murine Homolog PirB Regulates Synaptic Plasticity in an Alzheimer’s Model

2. Natural Oligomers of the Alzheimer Amyloid- Protein Induce Reversible Synapse Loss by Modulating an NMDA-Type Glutamate Receptor-Dependent Signaling Pathway

3. Cellular prion protein mediates impairment of synaptic plasticity by amyloid-β oligomers

4. Alpha-synuclein fibrils recruit TBK1 and OPTN to lysosomal damage sites and induce autophagy in microglial cells

5. Instability, unfolding and aggregation of human lysozyme variants underlying amyloid fibrillogenesis

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