Detalhe da pesquisa
1.
Therapeutic Strategies to Reduce the Toxicity of Misfolded Protein Oligomers.
Int J Mol Sci
; 21(22)2020 Nov 17.
Artigo
em Inglês
| MEDLINE | ID: mdl-33212787
2.
Rationally Designed Antibodies as Research Tools to Study the Structure-Toxicity Relationship of Amyloid-ß Oligomers.
Int J Mol Sci
; 21(12)2020 Jun 25.
Artigo
em Inglês
| MEDLINE | ID: mdl-32630615
3.
EGCG inactivates a pore-forming toxin by promoting its oligomerization and decreasing its solvent-exposed hydrophobicity.
Chem Biol Interact
; 371: 110307, 2023 Feb 01.
Artigo
em Inglês
| MEDLINE | ID: mdl-36535315
4.
A Brain-Permeable Aminosterol Regulates Cell Membranes to Mitigate the Toxicity of Diverse Pore-Forming Agents.
ACS Chem Neurosci
; 13(8): 1219-1231, 2022 04 20.
Artigo
em Inglês
| MEDLINE | ID: mdl-35404569
5.
Squalamine and Its Derivatives Modulate the Aggregation of Amyloid-ß and α-Synuclein and Suppress the Toxicity of Their Oligomers.
Front Neurosci
; 15: 680026, 2021.
Artigo
em Inglês
| MEDLINE | ID: mdl-34220435
6.
Trodusquemine displaces protein misfolded oligomers from cell membranes and abrogates their cytotoxicity through a generic mechanism.
Commun Biol
; 3(1): 435, 2020 08 13.
Artigo
em Inglês
| MEDLINE | ID: mdl-32792544