Predicting energetically favorable residue interactions between LL-37 and familial alzheimer's disease mutants of Aβ42 using molecular dynamics simulations
Amyloid beta (Aβ) peptides self-aggregate into plaques, which is a hallmark of Alzheimer’s disease (AD) and is thought to cause the deterioration of neurons. Mutations at the E22 of the wildtype Aβ42 are likewise seen in patients with genetic and early-onset familial AD. It was previously shown that...
Saved in:
Main Author: | Miranda, Martin Carlos Y. |
---|---|
Format: | text |
Language: | English |
Published: |
Animo Repository
2024
|
Subjects: | |
Online Access: | https://animorepository.dlsu.edu.ph/etdb_chem/48 https://animorepository.dlsu.edu.ph/context/etdb_chem/article/1056/viewcontent/2024_Miranda_Predicting_energetically_favorable_residue_interactions_between_L.pdf |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Institution: | De La Salle University |
Language: | English |
Similar Items
-
Clinical and biomarker trajectories in sporadic Alzheimer's disease: A longitudinal study
by: Wang, H.-F., et al.
Published: (2021) -
THERAPEUTIC POTENTIAL OF CHIMERIC AMYLOID-BETA PRECURSOR PROTEIN INTRACELLULAR DOMAIN MUTANT IN ALZHEIMER'S DISEASE
by: PAWAN KUMAR
Published: (2020) -
Regulated trafficking of APP by SORLA in Alzheimer's disease
by: Lao, Angelyn R., et al.
Published: (2012) -
Truncated Tau caused by intron retention is enriched in Alzheimer’s disease cortex and exhibits altered biochemical properties
by: Ngian, ZK, et al.
Published: (2023) -
Regulated trafficking of APP by SORLA in Alzheimer’s disease
by: Lao, Angelyn R.
Published: (2012)