A key region of Tau that is able to drive assembly and modulate inhibition by Hydromethylthionine
1
thomson
10/2022
Journal of Molecular Biology
أ.م.د . يسرى كريم جابر
Dityrosine Cross-links are Present in Alzheimer’s Disease-derived Tau Oligomers and Paired Helical Filaments (PHF) which Promotes the Stability of the PHF-core Tau (297–391) In Vitro
2
thomson
2022
JMB
أ.م.د . يسرى كريم جابر
Structural Identification of Individual Helical Amyloid Filaments by Integration of Cryo-Electron Microscopy-Derived Maps in Comparative Morphometric Atomic Force Microscopy Image Analysis
3
thomson
2021
Frontiers in molecular Biosciences
أ.م.د . يسرى كريم جابر
The Disease Associated Tau35 Fragment has an Increased Propensity to Aggregate Compared to Full-Length Tau
4
local
2020/10/29
Iraqi Journal of Nanotechnology
أ.م.د . يسرى كريم جابر
Dityrosine Crossed-linked Amyloid-like Fibrils as Bionanomaterials
5
thomson
7/8/2020
Journal of Molecular Biology
أ.م.د . يسرى كريم جابر
Paired Helical Filament-Forming Region of Tau (297–391) Influences Endogenous Tau Protein and Accumulates in Acidic Compartments in Human Neuronal Cells
6
thomson
11/12/2020
Frontiers in neurology
أ.م.د . يسرى كريم جابر
Tau Filament Self-Assembly and Structure: Tau as a Therapeutic Target
7
thomson
22/3/2021
Cells
أ.م.د . يسرى كريم جابر
Oxidative Stress Conditions Result in Trapping of PHF-Core Tau (297–391) Intermediates
8
thomson
2020
iScience
أ.م.د . يسرى كريم جابر
Metal- and UV- Catalyzed Oxidation Results in Trapped Amyloid-β Intermediates Revealing that Self-Assembly Is Required for Aβ-Induced Cytotoxicity
9
thomson
2020
FEBS LETTERS
أ.م.د . يسرى كريم جابر
Tau (297-391) forms filaments that structurally mimic the core of paired helical filaments in Alzheimer’s disease brain
10
thomson
06/05/2019
Dalton Transactions
أ.م.د . يسرى كريم جابر
Zinc–dysprosium functionalized amyloid fibrils
11
scopus
2019
Journal of Physics
أ.م.د . يسرى كريم جابر
The involvement of dityrosine crosslinks in lipofuscin accumulation in Alzheimer's disease
12
thomson
03/07/2019
Chemical Science
أ.م.د . يسرى كريم جابر
Using chirality to influence supramolecular gelation
13
thomson
31/05/2019
Journal of Molecular Biology
أ.م.د . يسرى كريم جابر
The Molecular Basis for Apolipoprotein E4 as the Major Risk Factor for Late-Onset Alzheimer's Disease
14
thomson
13/11/2019
FEBS Letter
أ.م.د . يسرى كريم جابر
Tau (297‐391) forms filaments that structurally mimic the core of paired helical filaments in Alzheimer’s disease brain
15
nature
28-02-2019
Scientific Reports
أ.م.د . يسرى كريم جابر
The CDR1 and Other Regions of Immunoglobulin Light Chains are Hot Spots for Amyloid Aggregation
16
thomson
01-03-2019
Acta Neuropathologica Communications
أ.م.د . يسرى كريم جابر
The elusive tau molecular structures: can we translate the recent breakthroughs into new targets for intervention?
17
thomson
10/2018
Methods in Molecular Biology
أ.م.د . يسرى كريم جابر
Methods for Structural Analysis of Amyloid Fibrils in Misfolding Diseases
18
thomson
16/08/2018
Journal of Molecular Biology
أ.م.د . يسرى كريم جابر
Cysteine-Independent Inhibition of Alzheimer's Disease-like Paired Helical Filament Assembly by Leuco-Methylthioninium (LMT).
19
local
2012-05-04
مجلة القادسية للعلوم الصرفة
أ.م.د . يسرى كريم جابر
Separation and Study Isoenzymes of Soluble Acetyl Cholineesterase in Normal Human Brain and Gli
20
thomson
24-11-2017
Journal of Molecular Biology
أ.م.د . يسرى كريم جابر
Alzheimer's Disease-like Paired Helical Filament Assembly from Truncated Tau Protein Is Independent of Disulfide Crosslinking
21
nature
16-12-2016
Scientific Reports
أ.م.د . يسرى كريم جابر
The involvement of dityrosine crosslinking in α-synuclein assembly and deposition in Lewy Bodies in Parkinson’s disease
22
nature
22-07-2016
Scientific reports
أ.م.د . يسرى كريم جابر
A critical role for the self-assembly of Amyloid-β1-42 in neurodegeneration
23
thomson
07/01/2016
Biomolecules
أ.م.د . يسرى كريم جابر
Nuclear Tau and Its Potential Role in Alzheimer’s Disease
24
scopus
2013-12-18
Acta Neuropathologica Communications
أ.م.د . يسرى كريم جابر
A central role for dityrosine crosslinking of Amyloid-β in Alzheimer’s disease