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1.
Regulation of α-synuclein by chaperones in mammalian cells.
Nature
; 577(7788): 127-132, 2020 01.
Article
in English
| MEDLINE | ID: mdl-31802003
2.
ApoE Isoforms Inhibit Amyloid Aggregation of Proinflammatory Protein S100A9.
Int J Mol Sci
; 25(4)2024 Feb 09.
Article
in English
| MEDLINE | ID: mdl-38396791
3.
The Stabilization of S100A9 Structure by Calcium Inhibits the Formation of Amyloid Fibrils.
Int J Mol Sci
; 24(17)2023 Aug 25.
Article
in English
| MEDLINE | ID: mdl-37686007
4.
Formation of Calprotectin Inhibits Amyloid Aggregation of S100A8 and S100A9 Proteins.
ACS Chem Neurosci
; 15(9): 1915-1925, 2024 05 01.
Article
in English
| MEDLINE | ID: mdl-38634811
5.
Formation of amyloid fibrils by the regulatory 14-3-3ζ protein.
Open Biol
; 14(1): 230285, 2024 Jan.
Article
in English
| MEDLINE | ID: mdl-38228169
6.
The seeding barrier between human and Syrian hamster prion protein amyloid fibrils is determined by ß2-α2 loop sequence elements.
Int J Biol Macromol
; 238: 124038, 2023 May 31.
Article
in English
| MEDLINE | ID: mdl-36921824
7.
Structural basis of DegP protease temperature-dependent activation.
Sci Adv
; 7(50): eabj1816, 2021 Dec 10.
Article
in English
| MEDLINE | ID: mdl-34878848
8.
Interaction between Copper Chaperone Atox1 and Parkinson's Disease Protein α-Synuclein Includes Metal-Binding Sites and Occurs in Living Cells.
ACS Chem Neurosci
; 10(11): 4659-4668, 2019 11 20.
Article
in English
| MEDLINE | ID: mdl-31600047
9.
Finke-Watzky Two-Step Nucleation-Autocatalysis Model of S100A9 Amyloid Formation: Protein Misfolding as "Nucleation" Event.
ACS Chem Neurosci
; 8(10): 2152-2158, 2017 10 18.
Article
in English
| MEDLINE | ID: mdl-28759719
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