Detalhe da pesquisa
1.
Size-Selective Phagocytic Clearance of Fibrillar α-Synuclein through Conformational Activation of Complement Receptor 4.
J Immunol
; 204(5): 1345-1361, 2020 03 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-31969389
2.
Avidity within the N-terminal anchor drives α-synuclein membrane interaction and insertion.
FASEB J
; 34(6): 7462-7482, 2020 06.
Artigo
em Inglês
| MEDLINE | ID: mdl-32277854
3.
Distinct α-Synuclein:Lipid Co-Structure Complexes Affect Amyloid Nucleation through Fibril Mimetic Behavior.
Biochemistry
; 58(50): 5052-5065, 2019 12 17.
Artigo
em Inglês
| MEDLINE | ID: mdl-31747254
4.
Mechanistic study of the inhibitory activity of Geum urbanum extract against α-Synuclein fibrillation.
Biochim Biophys Acta
; 1864(9): 1160-1169, 2016 09.
Artigo
em Inglês
| MEDLINE | ID: mdl-27353564
5.
SAS-Based Studies of Protein Fibrillation.
Adv Exp Med Biol
; 1009: 149-165, 2017.
Artigo
em Inglês
| MEDLINE | ID: mdl-29218558
6.
Analysis of biostructural changes, dynamics, and interactions - Small-angle X-ray scattering to the rescue.
Arch Biochem Biophys
; 602: 69-79, 2016 Jul 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-26945933
7.
Monoclonal Antibodies Follow Distinct Aggregation Pathways During Production-Relevant Acidic Incubation and Neutralization.
Pharm Res
; 33(3): 716-28, 2016 Mar.
Artigo
em Inglês
| MEDLINE | ID: mdl-26563206
8.
The architecture of amyloid-like peptide fibrils revealed by X-ray scattering, diffraction and electron microscopy.
Acta Crystallogr D Biol Crystallogr
; 71(Pt 4): 882-95, 2015 Apr.
Artigo
em Inglês
| MEDLINE | ID: mdl-25849399
9.
A high-affinity, dimeric inhibitor of PSD-95 bivalently interacts with PDZ1-2 and protects against ischemic brain damage.
Proc Natl Acad Sci U S A
; 109(9): 3317-22, 2012 Feb 28.
Artigo
em Inglês
| MEDLINE | ID: mdl-22343531
10.
Protein/lipid coaggregates are formed during α-synuclein-induced disruption of lipid bilayers.
Biomacromolecules
; 15(10): 3643-54, 2014 Oct 13.
Artigo
em Inglês
| MEDLINE | ID: mdl-25210839
11.
Low-resolution structure of a vesicle disrupting α-synuclein oligomer that accumulates during fibrillation.
Proc Natl Acad Sci U S A
; 108(8): 3246-51, 2011 Feb 22.
Artigo
em Inglês
| MEDLINE | ID: mdl-21300904
12.
Small angle X-ray scattering-based elucidation of the self-association mechanism of human insulin analogue lys(B29)(N(ε)ω-carboxyheptadecanoyl) des(B30).
Biochemistry
; 52(2): 282-94, 2013 Jan 15.
Artigo
em Inglês
| MEDLINE | ID: mdl-23256662
13.
Protein fibrillation from another small angle-SAXS data analysis of developing systems.
Methods Enzymol
; 678: 377-409, 2023.
Artigo
em Inglês
| MEDLINE | ID: mdl-36641215
14.
Identifying Biological and Biophysical Features of Different Maturation States of α-Synuclein Amyloid Fibrils.
Methods Mol Biol
; 2551: 321-344, 2023.
Artigo
em Inglês
| MEDLINE | ID: mdl-36310213
15.
High concentration formulation studies of an IgG2 antibody using small angle X-ray scattering.
Pharm Res
; 29(8): 2225-35, 2012 Aug.
Artigo
em Inglês
| MEDLINE | ID: mdl-22477029
16.
Protein fibrillation from another small angle: Sample preparation and SAXS data collection.
Methods Enzymol
; 677: 291-321, 2022.
Artigo
em Inglês
| MEDLINE | ID: mdl-36410953
17.
Structure and thermodynamics of transient protein-protein complexes by chemometric decomposition of SAXS datasets.
Structure
; 29(9): 1074-1090.e4, 2021 09 02.
Artigo
em Inglês
| MEDLINE | ID: mdl-33862013
18.
Extensive small-angle X-ray scattering studies of blood coagulation factor VIIa reveal interdomain flexibility.
Biochemistry
; 49(45): 9739-45, 2010 Nov 16.
Artigo
em Inglês
| MEDLINE | ID: mdl-20873866
19.
Time-resolved SAXS measurements facilitated by online HPLC buffer exchange.
J Synchrotron Radiat
; 17(6): 769-73, 2010 Nov.
Artigo
em Inglês
| MEDLINE | ID: mdl-20975222
20.
A helical structural nucleus is the primary elongating unit of insulin amyloid fibrils.
PLoS Biol
; 5(5): e134, 2007 May.
Artigo
em Inglês
| MEDLINE | ID: mdl-17472440