Conformational Change of Amyloid-β 40 in Association with Binding to GM1-Glycan Cluster
Abstract Aggregates of amyloid-β (Aβ) peptide are well known to be the causative substance of Alzheimer’s disease (AD). Recent studies showed that monosialotetrahexosylganglioside (GM1) clusters induce the pathological aggregation of Aβ peptide responsible for the onset and development of AD. Howeve...
Saved in:
Main Authors: | Yuhei Tachi, Yuko Okamoto, Hisashi Okumura |
---|---|
Format: | article |
Language: | EN |
Published: |
Nature Portfolio
2019
|
Subjects: | |
Online Access: | https://doaj.org/article/dd56961f09d24c21b1d253dd95928a15 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Similar Items
-
Binding, conformational transition and dimerization of amyloid-β peptide on GM1-containing ternary membrane: insights from molecular dynamics simulation.
by: Moutusi Manna, et al.
Published: (2013) -
Cell-based glycan arrays for probing glycan–glycan binding protein interactions
by: Jennie Grace Briard, et al.
Published: (2018) -
Conformational Heterogeneity of the HIV Envelope Glycan Shield
by: Mingjun Yang, et al.
Published: (2017) -
Conformational effects of N-glycan core fucosylation of immunoglobulin G Fc region on its interaction with Fcγ receptor IIIa
by: Yoshitake Sakae, et al.
Published: (2017) -
Characterization of Conformational Ensembles of Protonated N-glycans in the Gas-Phase
by: Suyong Re, et al.
Published: (2018)