O4-11-04: Identification of novel small molecules as tau protein aggregation inhibitors

2012 ◽  
Vol 8 (4S_Part_17) ◽  
pp. P637-P637
Author(s):  
Judy Cam ◽  
Joel Cummings ◽  
Thomas Lake ◽  
Kelsey Hanson ◽  
Luke Esposito ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Small Molecules ◽  
Tau Protein ◽  
Aggregation Inhibitors

P2-529: Identification of Exebryl-1® and other novel small molecules as tau protein aggregation inhibitors

2011 ◽  
Vol 7 ◽  
pp. S481-S481 ◽  
Author(s):  
Qubai Hu ◽  
Judy Cam ◽  
Thomas Lake ◽  
Joel Cummings ◽  
Luke Esposito ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Small Molecules ◽  
Tau Protein ◽  
Aggregation Inhibitors

Tau Protein Aggregation in Alzheimer's Disease: Recent Advances in the Development of Novel Therapeutic Agents

2020 ◽  
Vol 26 (15) ◽  
pp. 1682-1692
Author(s):  
Kadja L.C. Monteiro ◽  
Marcone G. dos S. Alcântara ◽  
Thiago M. de Aquino ◽  
Edeildo F. da Silva-Júnior
Keyword(s):  
Alzheimer’S Disease ◽  
Alzheimer's Disease ◽  
Protein Aggregation ◽  
Tau Protein ◽  
Therapeutic Agents ◽  
Model Systems ◽  
Aggregation Inhibitors ◽  
Disease Modifying Agents ◽  
Tau Aggregation

: Major research in Alzheimer’s disease (AD) related to disease-modifying agents is concentrated on pharmacological approaches related to diagnostic markers, neurofibrillary tangles and amyloid plaques. Although most studies focus on anti-amyloid strategies, investigations on tau protein have produced significant advances in the modulation of the pathophysiology of several neurodegenerative diseases. Since the discovery of phenothiazines as tau protein aggregation inhibitors (TAGIs), many additional small molecule inhibitors have been discovered and characterized in biological model systems, which exert their interaction effects by covalent and noncovalent means. In this paper, we summarize the latest advances in the discovery and development of tau aggregation inhibitors using a specialized approach in their chemical classes. The design of new TAGIs and their encouraging use in in vivo and clinical trials support their potential therapeutic use in AD.

scholarly journals 3D QSAR CoMFA Study on Phenylthiazolylhydrazide (PTH) Derivataives as Tau Protein Aggregation Inhibitors

2010 ◽  
Vol 31 (12) ◽  
pp. 3838-3841 ◽  
Author(s):  
Hye-Ri Park ◽  
Mi-Kyoung Kim ◽  
Dong-Woon Kim ◽  
Il-Han Choo ◽  
You-Hoon Chong
Keyword(s):  
Protein Aggregation ◽  
Tau Protein ◽  
3D Qsar ◽  
Aggregation Inhibitors ◽  
Comfa Study

scholarly journals Ring-opened aminothienopyridazines as novel tau aggregation inhibitors

MedChemComm ◽  
2017 ◽  
Vol 8 (6) ◽  
pp. 1275-1282 ◽  
Author(s):  
M. Moir ◽  
S. W. Chua ◽  
T. Reekie ◽  
A. D. Martin ◽  
A. Ittner ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Tau Protein ◽  
Aggregation Inhibitors ◽  
Tau Aggregation

Simplified aminothienopyridazine analogues were synthesised and their inhibition of tau protein aggregation assessed.

Tau protein aggregation in the frontal and entorhinal cortices as a function of aging

2005 ◽  
Vol 156 (2) ◽  
pp. 127-138 ◽  
Author(s):  
Wencheng Yang ◽  
Lee Cyn Ang ◽  
Michael J. Strong
Keyword(s):  
Protein Aggregation ◽  
Tau Protein

An in vitro study of the role of docosahexaenoic acid in human tau protein aggregation

2016 ◽  
Vol 35 (14) ◽  
pp. 3176-3181
Author(s):  
Elham Sadat Mostafavi ◽  
Mohammad Ali Nasiri Khalili ◽  
Sirus Khodadadi ◽  
Gholam Hossein Riazi
Keyword(s):  
Docosahexaenoic Acid ◽  
Protein Aggregation ◽  
Tau Protein ◽  
In Vitro Study ◽  
Vitro Study

Chronic lithium treatment decreases mutant tau protein aggregation in a transgenic mouse model

2003 ◽  
Vol 5 (4) ◽  
pp. 301-308 ◽  
Author(s):  
Mar Pérez ◽  
Félix Hernández ◽  
Filip Lim ◽  
Javier Díaz-Nido ◽  
Jesús Avila
Keyword(s):  
Mouse Model ◽  
Protein Aggregation ◽  
Transgenic Mouse ◽  
Tau Protein ◽  
Lithium Treatment ◽  
Transgenic Mouse Model

Beta Amyloid Aggregation Inhibitors: Small Molecules as Candidate Drugs for Therapy of Alzheimers Disease

2010 ◽  
Vol 17 (27) ◽  
pp. 2990-3006 ◽  
Author(s):  
F. Re ◽  
C. Airoldi ◽  
C. Zona ◽  
M. Masserini ◽  
B. La Ferla ◽  
...  
Keyword(s):  
Small Molecules ◽  
Beta Amyloid ◽  
Amyloid Aggregation ◽  
Alzheimers Disease ◽  
Aggregation Inhibitors

scholarly journals Thermodynamic and kinetic design principles for protein aggregation inhibitors

2020 ◽  
Author(s):  
Thomas C. T. Michaels ◽  
Andela Šarić ◽  
Georg Meisl ◽  
Gabriella T. Heller ◽  
Samo Curk ◽  
...  
Keyword(s):  
Protein Aggregation ◽  
Protein Misfolding ◽  
Complex Problem ◽  
Binding Rate ◽  
Potent Inhibition ◽  
Aggregation Inhibitors ◽  
Aggregation Inhibition ◽  
General Physical ◽  
Misfolding Diseases ◽  
Physical Laws

AbstractUnderstanding the mechanism of action of compounds capable of inhibiting protein aggregation is critical to the development of potential ther-apeutics against protein misfolding diseases. A fundamental challenge for progress is the range of possible target species and the disparate timescales involved, since the aggregating proteins are simultaneously the reactants, products, intermediates and catalysts of the reaction. It is a complex problem, therefore, to choose the states of the aggregating proteins that should be bound by the compounds to achieve the most potent inhibition. We present here a comprehensive kinetic theory of protein aggregation inhibition which reveals the fundamental thermodynamic and kinetic signatures characterising effective inhibitors by identifying quantitative relationships between the aggregation and binding rate constants. These results provide general physical laws to guide the design and optimisation of protein aggregation inhibitors.

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