Detalhe da pesquisa
1.
Direct observation of the interconversion of normal and toxic forms of α-synuclein.
Cell
; 149(5): 1048-59, 2012 May 25.
Artigo
em Inglês
| MEDLINE | ID: mdl-22632969
2.
Characterization of Pairs of Toxic and Nontoxic Misfolded Protein Oligomers Elucidates the Structural Determinants of Oligomer Toxicity in Protein Misfolding Diseases.
Acc Chem Res
; 56(12): 1395-1405, 2023 06 20.
Artigo
em Inglês
| MEDLINE | ID: mdl-37071750
3.
All-or-none amyloid disassembly via chaperone-triggered fibril unzipping favors clearance of α-synuclein toxic species.
Proc Natl Acad Sci U S A
; 118(36)2021 09 07.
Artigo
em Inglês
| MEDLINE | ID: mdl-34462355
4.
Effects of oligomer toxicity, fibril toxicity and fibril spreading in synucleinopathies.
Cell Mol Life Sci
; 79(3): 174, 2022 Mar 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-35244787
5.
The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity.
Molecules
; 27(4)2022 Feb 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-35209093
6.
Defining α-synuclein species responsible for Parkinson's disease phenotypes in mice.
J Biol Chem
; 294(27): 10392-10406, 2019 07 05.
Artigo
em Inglês
| MEDLINE | ID: mdl-31142553
7.
A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity.
Proc Natl Acad Sci U S A
; 114(6): E1009-E1017, 2017 02 07.
Artigo
em Inglês
| MEDLINE | ID: mdl-28096355
8.
Multiplicity of α-Synuclein Aggregated Species and Their Possible Roles in Disease.
Int J Mol Sci
; 21(21)2020 Oct 28.
Artigo
em Inglês
| MEDLINE | ID: mdl-33126694
9.
Kinetic model of the aggregation of alpha-synuclein provides insights into prion-like spreading.
Proc Natl Acad Sci U S A
; 113(9): E1206-15, 2016 Mar 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-26884195
10.
The contribution of biophysical and structural studies of protein self-assembly to the design of therapeutic strategies for amyloid diseases.
Neurobiol Dis
; 109(Pt B): 178-190, 2018 Jan.
Artigo
em Inglês
| MEDLINE | ID: mdl-28709995
11.
Ca2+ is a key factor in α-synuclein-induced neurotoxicity.
J Cell Sci
; 129(9): 1792-801, 2016 05 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-26989132
12.
Structural characterization of toxic oligomers that are kinetically trapped during α-synuclein fibril formation.
Proc Natl Acad Sci U S A
; 112(16): E1994-2003, 2015 Apr 21.
Artigo
em Inglês
| MEDLINE | ID: mdl-25855634
13.
Inhibition of α-Synuclein Fibril Elongation by Hsp70 Is Governed by a Kinetic Binding Competition between α-Synuclein Species.
Biochemistry
; 56(9): 1177-1180, 2017 03 07.
Artigo
em Inglês
| MEDLINE | ID: mdl-28230968
14.
Correction: Defining α-synuclein species responsible for Parkinson's disease phenotypes in mice.
J Biol Chem
; 295(4): 1142, 2020 Jan 24.
Artigo
em Inglês
| MEDLINE | ID: mdl-31980482
15.
Amyloid-ß and α-Synuclein Decrease the Level of Metal-Catalyzed Reactive Oxygen Species by Radical Scavenging and Redox Silencing.
J Am Chem Soc
; 138(12): 3966-9, 2016 Mar 30.
Artigo
em Inglês
| MEDLINE | ID: mdl-26967463
16.
Fast flow microfluidics and single-molecule fluorescence for the rapid characterization of α-synuclein oligomers.
Anal Chem
; 87(17): 8818-26, 2015 Sep 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-26258431
17.
Single-Particle Analysis of the Interaction Between Molecules and Protein Aggregated Species by Dual-Color Time-Resolved Fluorescence Spectroscopy.
Methods Mol Biol
; 2551: 379-394, 2023.
Artigo
em Inglês
| MEDLINE | ID: mdl-36310216
18.
Molecular mechanism for the synchronized electrostatic coacervation and co-aggregation of alpha-synuclein and tau.
Nat Commun
; 13(1): 4586, 2022 08 06.
Artigo
em Inglês
| MEDLINE | ID: mdl-35933508
19.
Population of nonnative states of lysozyme variants drives amyloid fibril formation.
J Am Chem Soc
; 133(20): 7737-7743, 2011 May 25.
Artigo
em Inglês
| MEDLINE | ID: mdl-21528861
20.
Identification of pharmacological chaperones as potential therapeutic agents to treat phenylketonuria.
J Clin Invest
; 118(8): 2858-67, 2008 Aug.
Artigo
em Inglês
| MEDLINE | ID: mdl-18596920