Detalhe da pesquisa
1.
p53 amyloid pathology is correlated with higher cancer grade irrespective of the mutant or wild-type form.
J Cell Sci
; 136(17)2023 09 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-37622400
2.
Benzimidazole-based fluorophores for the detection of amyloid fibrils with higher sensitivity than Thioflavin-T.
J Neurochem
; 156(6): 1003-1019, 2021 03.
Artigo
em Inglês
| MEDLINE | ID: mdl-32750740
3.
Biocompatible Fluorescent Probe for Selective Detection of Amyloid Fibrils.
Anal Chem
; 92(15): 10336-10341, 2020 08 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-32635722
4.
Glycosaminoglycans have variable effects on α-synuclein aggregation and differentially affect the activities of the resulting amyloid fibrils.
J Biol Chem
; 293(34): 12975-12991, 2018 08 24.
Artigo
em Inglês
| MEDLINE | ID: mdl-29959225
5.
The Familial α-Synuclein A53E Mutation Enhances Cell Death in Response to Environmental Toxins Due to a Larger Population of Oligomers.
Biochemistry
; 57(33): 5014-5028, 2018 08 21.
Artigo
em Inglês
| MEDLINE | ID: mdl-30025458
6.
Comparison of Kinetics, Toxicity, Oligomer Formation, and Membrane Binding Capacity of α-Synuclein Familial Mutations at the A53 Site, Including the Newly Discovered A53V Mutation.
Biochemistry
; 57(35): 5183-5187, 2018 09 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-29771508
7.
Sensitized Emission Imaging Allows Nanoscale Surface Polarity Mapping of α-Synuclein Amyloid Fibrils.
ACS Chem Neurosci
; 15(1): 108-118, 2024 01 03.
Artigo
em Inglês
| MEDLINE | ID: mdl-38099928
8.
Liquid-liquid Phase Separation of α-Synuclein: A New Mechanistic Insight for α-Synuclein Aggregation Associated with Parkinson's Disease Pathogenesis.
J Mol Biol
; 435(1): 167713, 2023 01 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-35787838
9.
Intermolecular interactions underlie protein/peptide phase separation irrespective of sequence and structure at crowded milieu.
Nat Commun
; 14(1): 6199, 2023 10 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-37794023
10.
Phase separation and other forms of α-Synuclein self-assemblies.
Essays Biochem
; 66(7): 987-1000, 2022 12 16.
Artigo
em Inglês
| MEDLINE | ID: mdl-36373662
11.
Charge and hydrophobicity of amyloidogenic protein/peptide templates regulate the growth and morphology of gold nanoparticles.
Nanoscale
; 14(40): 15021-15033, 2022 Oct 21.
Artigo
em Inglês
| MEDLINE | ID: mdl-36194184
12.
Intermediates of α-synuclein aggregation: Implications in Parkinson's disease pathogenesis.
Biophys Chem
; 281: 106736, 2022 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-34923391
13.
Direct Demonstration of Seed Size-Dependent α-Synuclein Amyloid Amplification.
J Phys Chem Lett
; 13(28): 6427-6438, 2022 Jul 21.
Artigo
em Inglês
| MEDLINE | ID: mdl-35816132
14.
Co-aggregation and secondary nucleation in the life cycle of human prolactin/galanin functional amyloids.
Elife
; 112022 03 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-35257659
15.
α-Synuclein Aggregation Intermediates form Fibril Polymorphs with Distinct Prion-like Properties.
J Mol Biol
; 434(19): 167761, 2022 10 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-35907572
16.
Structural and Functional Insights into α-Synuclein Fibril Polymorphism.
Biomolecules
; 11(10)2021 09 28.
Artigo
em Inglês
| MEDLINE | ID: mdl-34680054
17.
Machine-Free Polymerase Chain Reaction with Triangular Gold and Silver Nanoparticles.
J Phys Chem Lett
; 11(24): 10489-10496, 2020 Dec 17.
Artigo
em Inglês
| MEDLINE | ID: mdl-33275439
18.
α-Synuclein aggregation nucleates through liquid-liquid phase separation.
Nat Chem
; 12(8): 705-716, 2020 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-32514159