Author(s): M.Vijey Aanandhi, Niventhi.A, Rujaswini.T, Hemalatha C.N, Praveen.D

Email(s): hodpchemistry@velsuniv.ac.in

DOI: 10.5958/0974-360X.2018.00149.X   

Address: M.Vijey Aanandhi*1, Niventhi.A2, Rujaswini.T2, Hemalatha C.N3, Praveen.D4
1Department of Pharmaceutical Chemistry and Analysis, School of Pharmaceutical Sciences, (VISTAS) Vels University, Chennai, India.
2Department of Pharmacy Practice, School of Pharmaceutical Sciences, (VISTAS)Vels University, Chennai, India.
3Research Scholar,Department of Pharmaceutical Chemistry and Analysis, School of Pharmaceutical Sciences, (VISTAS) Vels University, Chennai, India.
4Research Scholar,School of Pharmaceutical Sciences, (VISTAS) Vels University, Chennai, India.
*Corresponding Author

Published In:   Volume - 11,      Issue - 2,     Year - 2018


ABSTRACT:
Tau proteins are the one of the most important causes of neurological diseases like Alzheimer’s disease (AD).Tau proteins are the stabilized form of microtubule associated protein (MAP) of a normal motor neuron.Tau protein is a highly soluble microtubule-associated protein (MAP). In humans, these proteins are found mostly in neurons compared to non-neuronal cells. One of the tau's main functions is to modulate the stability of axonal microtubules.Neurofibrillary tangles are obtained by hyperphosphorylation of a microtubule-associated protein. This article deals with the role of Tau proteins and the methods in which they lead to AD


Cite this article:
M.Vijey Aanandhi, Niventhi.A, Rujaswini.T, Hemalatha C.N, Praveen.D. A Comprehensive Review on the Role of Tau Proteins in Alzheimer’s Pathology. Research J. Pharm. and Tech 2018; 11(2):788-790. doi: 10.5958/0974-360X.2018.00149.X

Cite(Electronic):
M.Vijey Aanandhi, Niventhi.A, Rujaswini.T, Hemalatha C.N, Praveen.D. A Comprehensive Review on the Role of Tau Proteins in Alzheimer’s Pathology. Research J. Pharm. and Tech 2018; 11(2):788-790. doi: 10.5958/0974-360X.2018.00149.X   Available on: https://rjptonline.org/AbstractView.aspx?PID=2018-11-2-71


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RNI: CHHENG00387/33/1/2008-TC                     
DOI: 10.5958/0974-360X 

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