Detalhe da pesquisa
1.
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
2.
A Platform for Site-Specific DNA-Antibody Bioconjugation by Using Benzoylacrylic-Labelled Oligonucleotides.
Angew Chem Int Ed Engl
; 60(49): 25905-25913, 2021 12 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-34555238
3.
The small heat shock protein Hsp27 binds α-synuclein fibrils, preventing elongation and cytotoxicity.
J Biol Chem
; 293(12): 4486-4497, 2018 03 23.
Artigo
em Inglês
| MEDLINE | ID: mdl-29382725
4.
Nanoscopic Characterisation of Individual Endogenous Protein Aggregates in Human Neuronal Cells.
Chembiochem
; 19(19): 2033-2038, 2018 10 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-30051958
5.
PINK1 signalling in neurodegenerative disease.
Essays Biochem
; 65(7): 913-923, 2021 12 22.
Artigo
em Inglês
| MEDLINE | ID: mdl-34897410
6.
Single cell morphology distinguishes genotype and drug effect in Hereditary Spastic Paraplegia.
Sci Rep
; 11(1): 16635, 2021 08 17.
Artigo
em Inglês
| MEDLINE | ID: mdl-34404843
7.
Neuroserpin and transthyretin are extracellular chaperones that preferentially inhibit amyloid formation.
Sci Adv
; 7(50): eabf7606, 2021 Dec 10.
Artigo
em Inglês
| MEDLINE | ID: mdl-34890220
8.
Tumour necrosis factor induces increased production of extracellular amyloid-ß- and α-synuclein-containing aggregates by human Alzheimer's disease neurons.
Brain Commun
; 2(2): fcaa146, 2020.
Artigo
em Inglês
| MEDLINE | ID: mdl-33543132
9.
Soluble aggregates present in cerebrospinal fluid change in size and mechanism of toxicity during Alzheimer's disease progression.
Acta Neuropathol Commun
; 7(1): 120, 2019 07 26.
Artigo
em Inglês
| MEDLINE | ID: mdl-31349874
10.
Secondary nucleation and elongation occur at different sites on Alzheimer's amyloid-ß aggregates.
Sci Adv
; 5(4): eaau3112, 2019 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-31001578
11.
Different soluble aggregates of Aß42 can give rise to cellular toxicity through different mechanisms.
Nat Commun
; 10(1): 1541, 2019 04 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-30948723
12.
Shedding light on aberrant interactions - a review of modern tools for studying protein aggregates.
FEBS J
; 285(19): 3604-3630, 2018 10.
Artigo
em Inglês
| MEDLINE | ID: mdl-29453901
13.
Single-Molecule Characterization of the Interactions between Extracellular Chaperones and Toxic α-Synuclein Oligomers.
Cell Rep
; 23(12): 3492-3500, 2018 06 19.
Artigo
em Inglês
| MEDLINE | ID: mdl-29924993
14.
Quantifying Co-Oligomer Formation by α-Synuclein.
ACS Nano
; 12(11): 10855-10866, 2018 11 27.
Artigo
em Inglês
| MEDLINE | ID: mdl-30371053
15.
α-synuclein oligomers interact with ATP synthase and open the permeability transition pore in Parkinson's disease.
Nat Commun
; 9(1): 2293, 2018 06 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-29895861
16.
Flow cytometric measurement of the cellular propagation of TDP-43 aggregation.
Prion
; 11(3): 195-204, 2017 05 04.
Artigo
em Inglês
| MEDLINE | ID: mdl-28486039
17.
Clusterin protects neurons against intracellular proteotoxicity.
Acta Neuropathol Commun
; 5(1): 81, 2017 Nov 07.
Artigo
em Inglês
| MEDLINE | ID: mdl-29115989
18.
Inhibiting the Ca2+ Influx Induced by Human CSF.
Cell Rep
; 21(11): 3310-3316, 2017 Dec 12.
Artigo
em Inglês
| MEDLINE | ID: mdl-29241555