Detalhe da pesquisa
1.
Molecular structure of ß-amyloid fibrils in Alzheimer's disease brain tissue.
Cell
; 154(6): 1257-68, 2013 Sep 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-24034249
2.
Assembly of SARS-CoV-2 nucleocapsid protein with nucleic acid.
Nucleic Acids Res
; 2024 Apr 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-38587193
3.
Structures of brain-derived 42-residue amyloid-ß fibril polymorphs with unusual molecular conformations and intermolecular interactions.
Proc Natl Acad Sci U S A
; 120(11): e2218831120, 2023 03 14.
Artigo
em Inglês
| MEDLINE | ID: mdl-36893281
4.
Two structurally defined Aß polymorphs promote different pathological changes in susceptible mice.
EMBO Rep
; 24(8): e57003, 2023 08 03.
Artigo
em Inglês
| MEDLINE | ID: mdl-37424505
5.
Time-resolved DEER EPR and solid-state NMR afford kinetic and structural elucidation of substrate binding to Ca2+-ligated calmodulin.
Proc Natl Acad Sci U S A
; 119(6)2022 02 08.
Artigo
em Inglês
| MEDLINE | ID: mdl-35105816
6.
Experimental Evidence for Millisecond-Timescale Structural Evolution Following the Microsecond-Timescale Folding of a Small Protein.
Phys Rev Lett
; 132(4): 048402, 2024 Jan 26.
Artigo
em Inglês
| MEDLINE | ID: mdl-38335342
7.
Structural differences in amyloid-ß fibrils from brains of nondemented elderly individuals and Alzheimer's disease patients.
Proc Natl Acad Sci U S A
; 118(45)2021 11 09.
Artigo
em Inglês
| MEDLINE | ID: mdl-34725161
8.
Molecular structure of a prevalent amyloid-ß fibril polymorph from Alzheimer's disease brain tissue.
Proc Natl Acad Sci U S A
; 118(4)2021 01 26.
Artigo
em Inglês
| MEDLINE | ID: mdl-33431654
9.
Structural variation in amyloid-ß fibrils from Alzheimer's disease clinical subtypes.
Nature
; 541(7636): 217-221, 2017 01 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-28052060
10.
Application of millisecond time-resolved solid state NMR to the kinetics and mechanism of melittin self-assembly.
Proc Natl Acad Sci U S A
; 116(34): 16717-16722, 2019 08 20.
Artigo
em Inglês
| MEDLINE | ID: mdl-31387974
11.
Constraints on the Structure of Fibrils Formed by a Racemic Mixture of Amyloid-ß Peptides from Solid-State NMR, Electron Microscopy, and Theory.
J Am Chem Soc
; 143(33): 13299-13313, 2021 08 25.
Artigo
em Inglês
| MEDLINE | ID: mdl-34375097
12.
Millisecond Time-Resolved Solid-State NMR Reveals a Two-Stage Molecular Mechanism for Formation of Complexes between Calmodulin and a Target Peptide from Myosin Light Chain Kinase.
J Am Chem Soc
; 142(50): 21220-21232, 2020 12 16.
Artigo
em Inglês
| MEDLINE | ID: mdl-33280387
13.
Oncological Safety and Technical Feasibility of Nipple-Sparing Mastectomy for Breast Cancer: The Hong Kong Experience.
World J Surg
; 42(5): 1375-1383, 2018 05.
Artigo
em Inglês
| MEDLINE | ID: mdl-28894930
14.
Fibrillation of ß amyloid peptides in the presence of phospholipid bilayers and the consequent membrane disruption.
Biochim Biophys Acta
; 1848(1 Pt B): 266-76, 2015 Jan.
Artigo
em Inglês
| MEDLINE | ID: mdl-24769158
15.
Successive Stages of Amyloid-ß Self-Assembly Characterized by Solid-State Nuclear Magnetic Resonance with Dynamic Nuclear Polarization.
J Am Chem Soc
; 137(25): 8294-307, 2015 Jul 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-26068174
16.
Antiparallel ß-sheet architecture in Iowa-mutant ß-amyloid fibrils.
Proc Natl Acad Sci U S A
; 109(12): 4443-8, 2012 Mar 20.
Artigo
em Inglês
| MEDLINE | ID: mdl-22403062
17.
Structure of Amyloid Peptide Ribbons Characterized by Electron Microscopy, Atomic Force Microscopy, and Solid-State Nuclear Magnetic Resonance.
J Phys Chem B
; 128(7): 1711-1723, 2024 Feb 22.
Artigo
em Inglês
| MEDLINE | ID: mdl-38348474
18.
From Milliseconds to Minutes: Melittin Self-Assembly from Concerted Non-Equilibrium Pressure-Jump and Equilibrium Relaxation Nuclear Magnetic Resonance.
J Phys Chem Lett
; 15(7): 1930-1935, 2024 Feb 22.
Artigo
em Inglês
| MEDLINE | ID: mdl-38346015
19.
Early events in amyloid-ß self-assembly probed by time-resolved solid state NMR and light scattering.
Nat Commun
; 14(1): 2964, 2023 05 23.
Artigo
em Inglês
| MEDLINE | ID: mdl-37221174
20.
Assembly reactions of SARS-CoV-2 nucleocapsid protein with nucleic acid.
bioRxiv
; 2023 Nov 23.
Artigo
em Inglês
| MEDLINE | ID: mdl-38045338