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Brain Acetylcholinesterase Promotes Amyloid-B-Peptide Aggregation But Does Not Hydrolyze Amyloid Precursor Protein Peptides

Campos, E.; Inestrosa Cantín, Nibaldo (1998)

Catalytic amyloids as novel synthetic hydrolases

Durán Meza, Eva Lisa; Díaz Espinoza, Rodrigo (MDPI, 2021)

Amyloids are supramolecular assemblies composed of polypeptides stabilized by an intermolecular beta-sheet core. These misfolded conformations have been traditionally associated with pathological conditions such as Alzheimer's ...

Overcoming electrostatic repulsions during amyloid assembly: Effect of pH and interaction with divalent metals using model peptides

Díaz Espinoza, Rodrigo; Nova, Esteban; Monasterio Opazo, Octavio (Academic Press Inc., 2017)

© 2017 Elsevier Inc. Amyloids are polypeptide aggregates involved in many pathologies including Alzheimer's disease. Amyloid assembly is a complex process affected by different interactions including hydrogen bonding, van ...

Charge regulation phenomenon predicted from the modeling of polypeptide electrophoretic mobilities as a relevant mechanism of amyloid-beta peptide oligomerization

Deiber, Julio Alcides; Peirotti, Marta Beatriz; Piaggio, María Virginia (Wiley VCH Verlag, 2016-03)

Electrophoretic mobilities of amyloid-beta (1-40) and (1-42) peptides and their aggregates are modeled to study the amyloidogenic pathway associated with Alzheimer´s Disease. The near molecule pH generated by the intraparticle ...

Amyloid Precursor Protein in Central and Peripheral Cholinergic Synaptopathies

Borroni, Maria Virginia; Barrantes, Francisco Jose (Nova Science Publishers, 2011-05)

Alzheimer´s disease is the most widespread form of dementia in the elderly. One of the characteristics of this disease is the profound functional deficit of the cholinergic system as a consequence of synaptic loss. Amyloid ...

Amyloid-ß-peptide reduces copper(II) to copper(I) independent of its aggregation state

OPAZO,CARLOS; RUIZ,FRANCISCA H; INESTROSA,NIBALDO C (Sociedad de Biología de Chile, 2000)

Molecular Modeling of the Amyloid-B-Peptide Using the Homology to a Fragment of Triosephosphate Isomerase That Forms Amyloid in Vitro

Contreras, C.; Inestrosa Cantín, Nibaldo (1999)

Molecular modeling of the amyloid-beta-peptide using the homology to a fragment of triosephosphate isomerase that forms amyloid in vitro

Autor desconocido (OXFORD UNIVERSITY PRESS, 1999)

The a-Helical to B-Strand Transition in the Amino-Terminal Fragment of the Amyloid B-Peptide Modulates Amyloid Formation

Soto, Claudio.; Inestrosa Cantín, Nibaldo (1995)

Molecular modeling of the amyloid-beta-peptide using the homology to a fragment of triosephosphate isomerase that forms amyloid in vitro

Autor desconocido (OXFORD UNIVERSITY PRESS, 1999)

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Brain Acetylcholinesterase Promotes Amyloid-B-Peptide Aggregation But Does Not Hydrolyze Amyloid Precursor Protein Peptides

Catalytic amyloids as novel synthetic hydrolases

Overcoming electrostatic repulsions during amyloid assembly: Effect of pH and interaction with divalent metals using model peptides

Charge regulation phenomenon predicted from the modeling of polypeptide electrophoretic mobilities as a relevant mechanism of amyloid-beta peptide oligomerization

Amyloid Precursor Protein in Central and Peripheral Cholinergic Synaptopathies

Amyloid-ß-peptide reduces copper(II) to copper(I) independent of its aggregation state

Molecular Modeling of the Amyloid-B-Peptide Using the Homology to a Fragment of Triosephosphate Isomerase That Forms Amyloid in Vitro

Molecular modeling of the amyloid-beta-peptide using the homology to a fragment of triosephosphate isomerase that forms amyloid in vitro

The a-Helical to B-Strand Transition in the Amino-Terminal Fragment of the Amyloid B-Peptide Modulates Amyloid Formation

Molecular modeling of the amyloid-beta-peptide using the homology to a fragment of triosephosphate isomerase that forms amyloid in vitro