Detalhe da pesquisa
1.
The C-terminal domain of the antiamyloid chaperone DNAJB6 binds to amyloid-ß peptide fibrils and inhibits secondary nucleation.
J Biol Chem
; 299(11): 105317, 2023 11.
Artigo
Inglês
| MEDLINE | ID: mdl-37797698
2.
Mass Spectrometry and Machine Learning Reveal Determinants of Client Recognition by Antiamyloid Chaperones.
Mol Cell Proteomics
; 21(10): 100413, 2022 10.
Artigo
Inglês
| MEDLINE | ID: mdl-36115577
3.
A Hairpin Motif in the Amyloid-ß Peptide Is Important for Formation of Disease-Related Oligomers.
J Am Chem Soc
; 145(33): 18340-18354, 2023 08 23.
Artigo
Inglês
| MEDLINE | ID: mdl-37555670
4.
Oligomer Dynamics of LL-37 Truncated Fragments Probed by α-Hemolysin Pore and Molecular Simulations.
Small
; 19(37): e2206232, 2023 09.
Artigo
Inglês
| MEDLINE | ID: mdl-37170734
5.
Structural Basis for Dityrosine-Mediated Inhibition of α-Synuclein Fibrillization.
J Am Chem Soc
; 144(27): 11949-11954, 2022 07 13.
Artigo
Inglês
| MEDLINE | ID: mdl-35749730
6.
Amyloid-ß oligomers are captured by the DNAJB6 chaperone: Direct detection of interactions that can prevent primary nucleation.
J Biol Chem
; 295(24): 8135-8144, 2020 06 12.
Artigo
Inglês
| MEDLINE | ID: mdl-32350108
7.
Native Ion Mobility-Mass Spectrometry Reveals the Formation of ß-Barrel Shaped Amyloid-ß Hexamers in a Membrane-Mimicking Environment.
J Am Chem Soc
; 141(26): 10440-10450, 2019 07 03.
Artigo
Inglês
| MEDLINE | ID: mdl-31141355
8.
Metal binding to the amyloid-ß peptides in the presence of biomembranes: potential mechanisms of cell toxicity.
J Biol Inorg Chem
; 24(8): 1189-1196, 2019 12.
Artigo
Inglês
| MEDLINE | ID: mdl-31562546
9.
Erratum: The amyloid-inhibiting NCAM-PrP peptide targets Aß peptide aggregation in membrane-mimetic environments.
iScience
; 26(4): 106576, 2023 Apr 21.
Artigo
Inglês
| MEDLINE | ID: mdl-37091237
10.
Cell-Penetrating Peptides with Unexpected Anti-Amyloid Properties.
Pharmaceutics
; 14(4)2022 Apr 09.
Artigo
Inglês
| MEDLINE | ID: mdl-35456657
11.
A "spindle and thread" mechanism unblocks p53 translation by modulating N-terminal disorder.
Structure
; 30(5): 733-742.e7, 2022 05 05.
Artigo
Inglês
| MEDLINE | ID: mdl-35290795
12.
The amyloid-inhibiting NCAM-PrP peptide targets Aß peptide aggregation in membrane-mimetic environments.
iScience
; 24(8): 102852, 2021 Aug 20.
Artigo
Inglês
| MEDLINE | ID: mdl-34381976
13.
Ion mobility-mass spectrometry shows stepwise protein unfolding under alkaline conditions.
Chem Commun (Camb)
; 57(12): 1450-1453, 2021 Feb 15.
Artigo
Inglês
| MEDLINE | ID: mdl-33439171
14.
Charge Engineering Reveals the Roles of Ionizable Side Chains in Electrospray Ionization Mass Spectrometry.
JACS Au
; 1(12): 2385-2393, 2021 Dec 27.
Artigo
Inglês
| MEDLINE | ID: mdl-34977906
15.
Role of hydrophobic residues for the gaseous formation of helical motifs.
Chem Commun (Camb)
; 55(35): 5147-5150, 2019 Apr 25.
Artigo
Inglês
| MEDLINE | ID: mdl-30977489
16.
Membrane-mimetic systems for biophysical studies of the amyloid-ß peptide.
Biochim Biophys Acta Proteins Proteom
; 1867(5): 492-501, 2019 05.
Artigo
Inglês
| MEDLINE | ID: mdl-30468884
17.
Solvent-Assisted Paper Spray Ionization Mass Spectrometry (SAPSI-MS) for the Analysis of Biomolecules and Biofluids.
Sci Rep
; 9(1): 10296, 2019 07 16.
Artigo
Inglês
| MEDLINE | ID: mdl-31311939
18.
Gas-Phase Collisions with Trimethylamine-N-Oxide Enable Activation-Controlled Protein Ion Charge Reduction.
J Am Soc Mass Spectrom
; 30(8): 1385-1388, 2019 Aug.
Artigo
Inglês
| MEDLINE | ID: mdl-31286443
19.
Amyloid-ß Peptide Interactions with Amphiphilic Surfactants: Electrostatic and Hydrophobic Effects.
ACS Chem Neurosci
; 9(7): 1680-1692, 2018 07 18.
Artigo
Inglês
| MEDLINE | ID: mdl-29683649
20.
Alzheimer's disease and cigarette smoke components: effects of nicotine, PAHs, and Cd(II), Cr(III), Pb(II), Pb(IV) ions on amyloid-ß peptide aggregation.
Sci Rep
; 7(1): 14423, 2017 10 31.
Artigo
Inglês
| MEDLINE | ID: mdl-29089568