<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Qureshi, Tazeen</style></author><author><style face="normal" font="default" size="100%">Chinnathambi, Subashchandrabose</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Histone deacetylase-6 modulates Tau function in Alzheimer's disease</style></title><secondary-title><style face="normal" font="default" size="100%">Biochimica Et Biophysica Acta-Molecular Cell Research</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Actin</style></keyword><keyword><style  face="normal" font="default" size="100%">Cytoskeleton</style></keyword><keyword><style  face="normal" font="default" size="100%">HDAC6</style></keyword><keyword><style  face="normal" font="default" size="100%">Microtubules</style></keyword><keyword><style  face="normal" font="default" size="100%">Proteostasis</style></keyword><keyword><style  face="normal" font="default" size="100%">Tau</style></keyword><keyword><style  face="normal" font="default" size="100%">ZnF UBP domain</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2022</style></year><pub-dates><date><style  face="normal" font="default" size="100%">AUG</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">1869</style></volume><pages><style face="normal" font="default" size="100%">119275</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p&gt;
	Alzheimer's disease (AD), one of the major tauopathies, is multifactorial with a massive demand for disease modifying treatments rather than symptom management. An AD-affected neuron shows Tau depositions generated due to overload on the proteostasis machinery of the cell and/or abnormal post-translational modifications on Tau protein. Loss of memory or dementia is the most significant concern in AD, occurring due to the loss of neurons and the connections between them. In a healthy brain, neurons interact with the environment and each other through extensions and migratory structures. It can thus be safe to assume that Tau depositions affect these growth structures in neurons. A Histone Deacetylase, HDAC6, has shown elevated levels in AD while also demonstrating direct interaction with the Tau protein. HDAC6 interacts with multiple proteins in the cell and is possibly involved in various signalling pathways. Its deacetylase activity has been a point of controversy in AD; however other functional domains remain unexplored. This review highlights the beneficial potential of HDAC6 in AD in mediating both Tau proteostasis and cytoskeletal rewiring for the neuritic extensions through its Ubiquitin Binding domain (HDAC6 ZnF UBP).&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">8</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">&lt;p&gt;
	Foreign&lt;/p&gt;
</style></custom3><custom4><style face="normal" font="default" size="100%">&lt;p&gt;
	5.011&lt;/p&gt;
</style></custom4></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Abhishek Ankur Balmik</style></author><author><style face="normal" font="default" size="100%">Subashchandrabose Chinnathambi</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Inter-relationship of Histone Deacetylase-6 with Tau-cytoskeletal organization and remodeling</style></title><secondary-title><style face="normal" font="default" size="100%">European Journal of Cell Biology</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Actin</style></keyword><keyword><style  face="normal" font="default" size="100%">Cell migration</style></keyword><keyword><style  face="normal" font="default" size="100%">Cytoskeleton remodeling</style></keyword><keyword><style  face="normal" font="default" size="100%">HDAC6</style></keyword><keyword><style  face="normal" font="default" size="100%">Microtubules</style></keyword><keyword><style  face="normal" font="default" size="100%">Podosomes</style></keyword><keyword><style  face="normal" font="default" size="100%">ZnF UBP</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2022</style></year><pub-dates><date><style  face="normal" font="default" size="100%">APR</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">101</style></volume><pages><style face="normal" font="default" size="100%">151202</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">Cytoskeletal elements are the key players in cellular integrity, structure, signalling and migration. Each cytoskeletal element comprises of properties with respect to its structure and stability, which serve a specific array of functions. These structures are highly dynamic and regulated by modulation via direct interaction or post-translational modifications. HDAC6 is a cytoplasmic deacetylase known to regulate a wide range of cellular functions either through its deacetylase activity or direct interaction via its C-terminal ZnF UBP domain. HDAC6 has been widely studied for its role in aggresome formation, which acts as a protective mechanism upon protein aggregation. HDAC6 is known to play a critical role in the regulation of cytoskeletal elements-microtubules and actin filaments. This review summarizes the regulatory role of HDAC6 in cytoskeletal remodeling and dynamics of neuronal cells and its significance in neurodegenerative diseases.</style></abstract><issue><style face="normal" font="default" size="100%">2</style></issue><work-type><style face="normal" font="default" size="100%">Article</style></work-type><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">4.492</style></custom4></record></records></xml>