Detalhe da pesquisa
1.
The expanding amyloid family: Structure, stability, function, and pathogenesis.
Cell
; 184(19): 4857-4873, 2021 09 16.
Artigo
em Inglês
| MEDLINE | ID: mdl-34534463
2.
Structural Studies of Amyloid Proteins at the Molecular Level.
Annu Rev Biochem
; 86: 69-95, 2017 06 20.
Artigo
em Inglês
| MEDLINE | ID: mdl-28125289
3.
How Hard It Is Seeing What Is in Front of Your Eyes.
Cell
; 174(1): 8-11, 2018 06 28.
Artigo
em Inglês
| MEDLINE | ID: mdl-29958112
4.
Amyloid fibrils in FTLD-TDP are composed of TMEM106B and not TDP-43.
Nature
; 605(7909): 304-309, 2022 05.
Artigo
em Inglês
| MEDLINE | ID: mdl-35344984
5.
Small molecules disaggregate alpha-synuclein and prevent seeding from patient brain-derived fibrils.
Proc Natl Acad Sci U S A
; 120(7): e2217835120, 2023 02 14.
Artigo
em Inglês
| MEDLINE | ID: mdl-36757890
6.
Structure-based design of nanobodies that inhibit seeding of Alzheimer's patient-extracted tau fibrils.
Proc Natl Acad Sci U S A
; 120(41): e2300258120, 2023 10 10.
Artigo
em Inglês
| MEDLINE | ID: mdl-37801475
7.
Cryo-EM structures of the D290V mutant of the hnRNPA2 low-complexity domain suggests how D290V affects phase separation and aggregation.
J Biol Chem
; 300(2): 105531, 2024 Feb.
Artigo
em Inglês
| MEDLINE | ID: mdl-38072051
8.
Propagation of Tau Aggregates and Neurodegeneration.
Annu Rev Neurosci
; 40: 189-210, 2017 07 25.
Artigo
em Inglês
| MEDLINE | ID: mdl-28772101
9.
Cryo-EM structure of RNA-induced tau fibrils reveals a small C-terminal core that may nucleate fibril formation.
Proc Natl Acad Sci U S A
; 119(15): e2119952119, 2022 04 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-35377792
10.
De novo designed protein inhibitors of amyloid aggregation and seeding.
Proc Natl Acad Sci U S A
; 119(34): e2206240119, 2022 08 23.
Artigo
em Inglês
| MEDLINE | ID: mdl-35969734
11.
TDP-43 and RNA form amyloid-like myo-granules in regenerating muscle.
Nature
; 563(7732): 508-513, 2018 11.
Artigo
em Inglês
| MEDLINE | ID: mdl-30464263
12.
Micro-electron diffraction structure of the aggregation-driving N terminus of Drosophila neuronal protein Orb2A reveals amyloid-like ß-sheets.
J Biol Chem
; 298(10): 102396, 2022 10.
Artigo
em Inglês
| MEDLINE | ID: mdl-35988647
13.
Bioinformatic identification of previously unrecognized amyloidogenic proteins.
J Biol Chem
; 298(5): 101920, 2022 05.
Artigo
em Inglês
| MEDLINE | ID: mdl-35405097
14.
Toxicity of eosinophil MBP is repressed by intracellular crystallization and promoted by extracellular aggregation.
Mol Cell
; 57(6): 1011-1021, 2015 Mar 19.
Artigo
em Inglês
| MEDLINE | ID: mdl-25728769
15.
The α-synuclein hereditary mutation E46K unlocks a more stable, pathogenic fibril structure.
Proc Natl Acad Sci U S A
; 117(7): 3592-3602, 2020 02 18.
Artigo
em Inglês
| MEDLINE | ID: mdl-32015135
16.
Prevalence and species distribution of the low-complexity, amyloid-like, reversible, kinked segment structural motif in amyloid-like fibrils.
J Biol Chem
; 297(4): 101194, 2021 10.
Artigo
em Inglês
| MEDLINE | ID: mdl-34537246
17.
The activities of amyloids from a structural perspective.
Nature
; 539(7628): 227-235, 2016 11 10.
Artigo
em Inglês
| MEDLINE | ID: mdl-27830791
18.
De novo phasing with X-ray laser reveals mosquito larvicide BinAB structure.
Nature
; 539(7627): 43-47, 2016 11 03.
Artigo
em Inglês
| MEDLINE | ID: mdl-27680699
19.
Crystal structure of a conformational antibody that binds tau oligomers and inhibits pathological seeding by extracts from donors with Alzheimer's disease.
J Biol Chem
; 295(31): 10662-10676, 2020 07 31.
Artigo
em Inglês
| MEDLINE | ID: mdl-32493775
20.
Structure of the toxic core of α-synuclein from invisible crystals.
Nature
; 525(7570): 486-90, 2015 Sep 24.
Artigo
em Inglês
| MEDLINE | ID: mdl-26352473