Detalhe da pesquisa
1.
Mechanistic basis for receptor-mediated pathological α-synuclein fibril cell-to-cell transmission in Parkinson's disease.
Proc Natl Acad Sci U S A
; 118(26)2021 06 29.
Artigo
em Inglês
| MEDLINE | ID: mdl-34172566
2.
A Hydroxylamine-Mediated Amidination of Lysine Residues That Retains the Protein's Positive Charge.
Angew Chem Int Ed Engl
; : e202402880, 2024 May 17.
Artigo
em Inglês
| MEDLINE | ID: mdl-38758629
3.
Parkinson's disease-related phosphorylation at Tyr39 rearranges α-synuclein amyloid fibril structure revealed by cryo-EM.
Proc Natl Acad Sci U S A
; 117(33): 20305-20315, 2020 08 18.
Artigo
em Inglês
| MEDLINE | ID: mdl-32737160
4.
Rational Design of a Cocktail of Inhibitors against Aß Aggregation.
Chemistry
; 26(16): 3499-3503, 2020 Mar 18.
Artigo
em Inglês
| MEDLINE | ID: mdl-32011042
5.
Phosphorylation and O-GlcNAcylation at the same α-synuclein site generate distinct fibril structures.
Nat Commun
; 15(1): 2677, 2024 Mar 27.
Artigo
em Inglês
| MEDLINE | ID: mdl-38538591
6.
Late-stage peptide and protein modifications through phospha-Michael addition reaction.
Chem Commun (Camb)
; 56(83): 12632-12635, 2020 Oct 25.
Artigo
em Inglês
| MEDLINE | ID: mdl-32960198