about
Insight into a New Binding Site of Zinc Ions in Fibrillar Amylin.Two Distinct Polymorphic Folding States of Self-Assembly of the Non-amyloid-β Component Differ in the Arrangement of the Residues.Mechanistic perspective and functional activity of insulin in amylin aggregation.Study of Molecular Mechanisms of α-Synuclein Assembly: Insight into a Cross-β Structure in the N-Termini of New α-Synuclein Fibrils.Distinct Primary Nucleation of Polymorphic Aβ Dimers Yields to Distinguished Fibrillation PathwaysUnique Inversion Events of Residues around the Backbone in the Turn Domain of β-Arches in Amylin FibrilsZinc Binding Sites Conserved in Short Neuropeptides Containing a Diphenylalanine MotifFibrils of α-Synuclein Abolish the Affinity of Cu2+-Binding Site to His50 and Induce Hopping of Cu2+ Ions in the TerminiInhibitory Activity of Insulin on Aβ Aggregation Is Restricted Due to Binding Selectivity and Specificity to Polymorphic Aβ States
P50
Q48152032-2C12349E-5395-411F-BE0B-511CA08779BEQ48339727-A0547C09-2A8A-4AC5-9335-2E3926BDE147Q55039919-E2C6ACF7-F8D2-4998-AC54-82AD39FBB29CQ55688977-98DC453D-44CE-4E6A-868D-E286136D3D16Q90158300-4C787119-B5FB-4378-A027-FBAB0D08AC1CQ90631899-590215CA-40FF-441B-B2E4-2FF13A798703Q91750816-EEC8958A-7248-4DDE-A393-C37E4D33702DQ92338074-C09DF629-2847-4D45-A49C-3965DA30E633Q92402684-A738ECB9-B31B-41F6-8E25-BD1380E3563D
P50
description
researcher
@en
name
Yifat Miller
@en
type
label
Yifat Miller
@en
prefLabel
Yifat Miller
@en
P31
P496
0000-0002-1163-9745