Detalhe da pesquisa
1.
Maximum entropy determination of mammalian proteome dynamics.
Proc Natl Acad Sci U S A
; 121(18): e2313107121, 2024 Apr 30.
Artigo
em Inglês
| MEDLINE | ID: mdl-38652742
2.
Self-replication of Aß42 aggregates occurs on small and isolated fibril sites.
Proc Natl Acad Sci U S A
; 121(7): e2220075121, 2024 Feb 13.
Artigo
em Inglês
| MEDLINE | ID: mdl-38335256
3.
Design of amyloidogenic peptide traps.
Nat Chem Biol
; 2024 Mar 19.
Artigo
em Inglês
| MEDLINE | ID: mdl-38503834
4.
Kinetic analysis reveals that independent nucleation events determine the progression of polyglutamine aggregation in C. elegans.
Proc Natl Acad Sci U S A
; 118(11)2021 03 16.
Artigo
em Inglês
| MEDLINE | ID: mdl-33836595
5.
The binding of the small heat-shock protein αB-crystallin to fibrils of α-synuclein is driven by entropic forces.
Proc Natl Acad Sci U S A
; 118(38)2021 09 21.
Artigo
em Inglês
| MEDLINE | ID: mdl-34518228
6.
Phase Separation and Fibrillization of Human Annexin A7 Are Mediated by Its Proline-Rich Domain.
Biochemistry
; 62(21): 3036-3040, 2023 11 07.
Artigo
em Inglês
| MEDLINE | ID: mdl-37788367
7.
The role of fibril structure and surface hydrophobicity in secondary nucleation of amyloid fibrils.
Proc Natl Acad Sci U S A
; 117(41): 25272-25283, 2020 10 13.
Artigo
em Inglês
| MEDLINE | ID: mdl-33004626
8.
Kinetic diversity of amyloid oligomers.
Proc Natl Acad Sci U S A
; 117(22): 12087-12094, 2020 06 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-32414930
9.
Ultrastructural evidence for self-replication of Alzheimer-associated Aß42 amyloid along the sides of fibrils.
Proc Natl Acad Sci U S A
; 117(21): 11265-11273, 2020 05 26.
Artigo
em Inglês
| MEDLINE | ID: mdl-32439711
10.
Thermodynamic and kinetic design principles for amyloid-aggregation inhibitors.
Proc Natl Acad Sci U S A
; 117(39): 24251-24257, 2020 09 29.
Artigo
em Inglês
| MEDLINE | ID: mdl-32929030
11.
Characterization of full-length p53 aggregates and their kinetics of formation.
Biophys J
; 121(22): 4280-4298, 2022 11 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-36230002
12.
The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity.
Molecules
; 27(4)2022 Feb 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-35209093
13.
Mechanism of Secondary Nucleation at the Single Fibril Level from Direct Observations of Aß42 Aggregation.
J Am Chem Soc
; 143(40): 16621-16629, 2021 10 13.
Artigo
em Inglês
| MEDLINE | ID: mdl-34582216
14.
Alpha Synuclein only Forms Fibrils In Vitro when Larger than its Critical Size of 70 Monomers.
Chembiochem
; 22(19): 2867-2871, 2021 10 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-34383993
15.
On the role of sidechain size and charge in the aggregation of Aß42 with familial mutations.
Proc Natl Acad Sci U S A
; 115(26): E5849-E5858, 2018 06 26.
Artigo
em Inglês
| MEDLINE | ID: mdl-29895690
16.
Transthyretin Inhibits Primary and Secondary Nucleations of Amyloid-ß Peptide Aggregation and Reduces the Toxicity of Its Oligomers.
Biomacromolecules
; 21(3): 1112-1125, 2020 03 09.
Artigo
em Inglês
| MEDLINE | ID: mdl-32011129
17.
The catalytic nature of protein aggregation.
J Chem Phys
; 152(4): 045101, 2020 Jan 31.
Artigo
em Inglês
| MEDLINE | ID: mdl-32007046
18.
Phage display and kinetic selection of antibodies that specifically inhibit amyloid self-replication.
Proc Natl Acad Sci U S A
; 114(25): 6444-6449, 2017 06 20.
Artigo
em Inglês
| MEDLINE | ID: mdl-28584111
19.
A natural product inhibits the initiation of α-synuclein aggregation and suppresses its toxicity.
Proc Natl Acad Sci U S A
; 114(6): E1009-E1017, 2017 02 07.
Artigo
em Inglês
| MEDLINE | ID: mdl-28096355
20.
Secondary nucleation of monomers on fibril surface dominates α-synuclein aggregation and provides autocatalytic amyloid amplification.
Q Rev Biophys
; 50: e6, 2017 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-29233218