01613nas a2200157   4500008004100000022001500041245007500056210006900131260000800200300001300208490000700221520105700228100002801285700003601313856010601349       2018                        eng d  a 0895-869600aTau protein squired by molecular chaperones during alzheimer's disease0 aTau protein squired by molecular chaperones during alzheimers di  cNOV  a 356-3680 v663 a<p>Alzheimer's disease (AD) is a neurodegenerative disorder characterized by progressive neuronal loss, caused by misfolding and accumulation of tau and Amyloid -42. Cellular mechanisms involving phosphatases, chaperones, ubiquitin proteasome system (UPS) and aggresomes solubilize or remove these toxic aggregates. Chaperones such as Hsp70 and Hsp90 functions in folding tau to its native form or in the downstream degrade and eliminated tau from the cell. Chaperones are involved in lysosomal degradation of tau by a process called chaperone mediated autophagy (CMA). In pathological conditions, chaperones fail to remove the toxic tau species, leading to their accumulation. In this scenario, inhibiting the chaperone activity would aid in overcoming AD. Small molecules inhibitors against chaperone activity are known to be effective in the clearance of aberrant tau from cell. In this review, the aspects of inhibition and prevention of tau aggregates formation are discussed in terms of chaperone activity and their small molecule modulators.</p>1 aGorantla, Nalini, Vijay1 aChinnathambi, Subashchandrabose  uhttps://library.ncl.res.in/content/tau-protein-squired-molecular-chaperones-during-alzheimers-disease