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1.
Early stage ß-amyloid-membrane interactions modulate lipid dynamics and influence structural interfaces and fibrillation.
J Biol Chem
; 298(10): 102491, 2022 10.
Artículo
en Inglés
| MEDLINE | ID: mdl-36115457
2.
Distinct Membrane Disruption Pathways Are Induced by 40-Residue ß-Amyloid Peptides.
J Biol Chem
; 291(23): 12233-44, 2016 Jun 03.
Artículo
en Inglés
| MEDLINE | ID: mdl-27056326
3.
Application of DNP-enhanced solid-state NMR to studies of amyloid-ß peptide interaction with lipid membranes.
Chem Phys Lipids
; 236: 105071, 2021 05.
Artículo
en Inglés
| MEDLINE | ID: mdl-33716023
4.
Fibrillization of 40-Residue ß-Amyloid Peptides in Membrane-Like Environments Leads to Different Fibril Structures and Reduced Molecular Polymorphisms.
Biomolecules
; 10(6)2020 06 08.
Artículo
en Inglés
| MEDLINE | ID: mdl-32521743
5.
The on-fibrillation-pathway membrane content leakage and off-fibrillation-pathway lipid mixing induced by 40-residue ß-amyloid peptides in biologically relevant model liposomes.
Biochim Biophys Acta Biomembr
; 1860(9): 1670-1680, 2018 Sep.
Artículo
en Inglés
| MEDLINE | ID: mdl-29548698
6.
Solid-State-NMR-Structure-Based Inhibitor Design to Achieve Selective Inhibition of the Parallel-in-Register ß-Sheet versus Antiparallel Iowa Mutant ß-Amyloid Fibrils.
J Phys Chem B
; 121(22): 5544-5552, 2017 06 08.
Artículo
en Inglés
| MEDLINE | ID: mdl-28535056
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