2022
DOI: 10.1007/978-1-0716-2597-2_12
|View full text |Cite
|
Sign up to set email alerts
|

An Additive-Free Model for Tau Self-Assembly

Help me understand this report

Search citation statements

Order By: Relevance

Paper Sections

Select...
1

Citation Types

0
1
0

Year Published

2024
2024
2024
2024

Publication Types

Select...
2

Relationship

0
2

Authors

Journals

citations
Cited by 2 publications
(1 citation statement)
references
References 31 publications
0
1
0
Order By: Relevance
“…Under pathological conditions, tau phosphorylation sites may reach saturation, and the highly phosphorylated tau protein in the brain of AD patients may lead to its configuration change and loss of tubulin polymerization ability, resulting in impaired microtubule function [ 31 , 32 ]. A high level of intracellular tau is involved in tau-tau interactions that may form insoluble PHFs and straight filaments (SFs), resulting in the formation of intracranial fibrous deposits, namely NFTs [ 33 ]. NFTs can reduce the number of synapses, produce neurotoxicity, and cause cellular dysfunction [ 34 ].…”
Section: Hypothesis Of Pathogenesis Of Admentioning
confidence: 99%
“…Under pathological conditions, tau phosphorylation sites may reach saturation, and the highly phosphorylated tau protein in the brain of AD patients may lead to its configuration change and loss of tubulin polymerization ability, resulting in impaired microtubule function [ 31 , 32 ]. A high level of intracellular tau is involved in tau-tau interactions that may form insoluble PHFs and straight filaments (SFs), resulting in the formation of intracranial fibrous deposits, namely NFTs [ 33 ]. NFTs can reduce the number of synapses, produce neurotoxicity, and cause cellular dysfunction [ 34 ].…”
Section: Hypothesis Of Pathogenesis Of Admentioning
confidence: 99%