Detalhe da pesquisa
1.
A Targetable N-Terminal Motif Orchestrates α-Synuclein Oligomer-to-Fibril Conversion.
J Am Chem Soc
; 146(18): 12702-12711, 2024 May 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-38683963
2.
DisProt in 2022: improved quality and accessibility of protein intrinsic disorder annotation.
Nucleic Acids Res
; 50(D1): D480-D487, 2022 01 07.
Artigo
em Inglês
| MEDLINE | ID: mdl-34850135
3.
The small aromatic compound SynuClean-D inhibits the aggregation and seeded polymerization of multiple α-synuclein strains.
J Biol Chem
; 298(5): 101902, 2022 05.
Artigo
em Inglês
| MEDLINE | ID: mdl-35390347
4.
A3D database: structure-based predictions of protein aggregation for the human proteome.
Bioinformatics
; 38(11): 3121-3123, 2022 05 26.
Artigo
em Inglês
| MEDLINE | ID: mdl-35445695
5.
DisProt: intrinsic protein disorder annotation in 2020.
Nucleic Acids Res
; 48(D1): D269-D276, 2020 01 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-31713636
6.
Design, synthesis and structure-activity evaluation of novel 2-pyridone-based inhibitors of α-synuclein aggregation with potentially improved BBB permeability.
Bioorg Chem
; 117: 105472, 2021 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-34775206
7.
Aggrescan3D (A3D) 2.0: prediction and engineering of protein solubility.
Nucleic Acids Res
; 47(W1): W300-W307, 2019 07 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-31049593
8.
Small molecule inhibits α-synuclein aggregation, disrupts amyloid fibrils, and prevents degeneration of dopaminergic neurons.
Proc Natl Acad Sci U S A
; 115(41): 10481-10486, 2018 10 09.
Artigo
em Inglês
| MEDLINE | ID: mdl-30249646
9.
Dual Binding Mode of Metallacarborane Produces a Robust Shield on Proteins.
Chemistry
; 25(55): 12820-12829, 2019 Oct 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-31411775
10.
DisProt 7.0: a major update of the database of disordered proteins.
Nucleic Acids Res
; 45(D1): D219-D227, 2017 01 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-27899601
11.
The Disordered C-Terminus of Yeast Hsf1 Contains a Cryptic Low-Complexity Amyloidogenic Region.
Int J Mol Sci
; 19(5)2018 May 06.
Artigo
em Inglês
| MEDLINE | ID: mdl-29734798
12.
AGGRESCAN3D (A3D): server for prediction of aggregation properties of protein structures.
Nucleic Acids Res
; 43(W1): W306-13, 2015 Jul 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-25883144
13.
High-Throughput Screening Methodology to Identify Alpha-Synuclein Aggregation Inhibitors.
Int J Mol Sci
; 18(3)2017 Mar 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-28257086
14.
Corrigendum: DisProt 7.0: a major update of the database of disordered proteins.
Nucleic Acids Res
; 45(D1): D1123-D1124, 2017 01 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-27965415
15.
A3D 2.0 Update for the Prediction and Optimization of Protein Solubility.
Methods Mol Biol
; 2406: 65-84, 2022.
Artigo
em Inglês
| MEDLINE | ID: mdl-35089550
16.
Protocols for Rational Design of Protein Solubility and Aggregation Properties Using Aggrescan3D Standalone.
Methods Mol Biol
; 2340: 17-40, 2022.
Artigo
em Inglês
| MEDLINE | ID: mdl-35167068
17.
α-Helical peptidic scaffolds to target α-synuclein toxic species with nanomolar affinity.
Nat Commun
; 12(1): 3752, 2021 06 18.
Artigo
em Inglês
| MEDLINE | ID: mdl-34145261
18.
Chemical Chaperones as Novel Drugs for Parkinson's Disease.
Trends Mol Med
; 26(4): 408-421, 2020 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-32277934
19.
Computational prediction of protein aggregation: Advances in proteomics, conformation-specific algorithms and biotechnological applications.
Comput Struct Biotechnol J
; 18: 1403-1413, 2020.
Artigo
em Inglês
| MEDLINE | ID: mdl-32637039
20.
Inhibition of α-Synuclein Aggregation and Mature Fibril Disassembling With a Minimalistic Compound, ZPDm.
Front Bioeng Biotechnol
; 8: 588947, 2020.
Artigo
em Inglês
| MEDLINE | ID: mdl-33178678