<?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%">Chinnathambi, Subashchandrabose</style></author><author><style face="normal" font="default" size="100%">Gorantla, Nalini Vijay</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Implications of valosin-containing protein in promoting autophagy to prevent tau aggregation</style></title><secondary-title><style face="normal" font="default" size="100%">Neuroscience</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Autophagy</style></keyword><keyword><style  face="normal" font="default" size="100%">segregase</style></keyword><keyword><style  face="normal" font="default" size="100%">Tau aggregates</style></keyword><keyword><style  face="normal" font="default" size="100%">Ubiquitin-proteasome system</style></keyword><keyword><style  face="normal" font="default" size="100%">valosin-containing protein</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2021</style></year><pub-dates><date><style  face="normal" font="default" size="100%">NOV</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">476</style></volume><pages><style face="normal" font="default" size="100%">125-134</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">and cellular degradative mechanisms modulate Tau aggregation. During aging and neu-rodegenerative disorders, the cellular proteostasis is disturbed due to impaired protective mechanisms. This results in accumulation of aberrant Tau aggregates in the neuron that leads to microtubule destabilization and neuronal degeneration. The intricate mechanisms to prevent Tau aggregation involve chaperones, autophagy, and proteasomal system have gained main focus about concerning to therapeutic intervention. However, the thor-ough understanding of other key proteins, such as Valosin-containing protein (VCP), is limited. In various neu-rodegenerative diseases, the chaperone-like activity of VCP is involved in preventing protein aggregation and mediating the degradation of aberrant proteins by proteasome and autophagy. In the case of Tau aggregation associated with Alzheimer's disease, the importance of VCP is poorly understood. VCP is known to co-localize with Tau, and alterations in VCP cause aberrant accumulation of Tau. Nevertheless, the direct mechanism of VCP in altering Tau aggregation is not known. Hence, we speculate that VCP might be one of the key modulators in preventing Tau aggregation and can disintegrate Tau aggregates by directing its clearance by autophagy. = 2021 IBRO. Published by Elsevier Ltd. All rights reserved.</style></abstract><work-type><style face="normal" font="default" size="100%">Review</style></work-type><custom3><style face="normal" font="default" size="100%">Foreign</style></custom3><custom4><style face="normal" font="default" size="100%">3.590</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%">Chinnathambi, Subashchandrabose</style></author><author><style face="normal" font="default" size="100%">Das, Rashmi</style></author><author><style face="normal" font="default" size="100%">Desale, Smita Eknath</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Tau aggregates improve the Purinergic receptor P2Y12-associated podosome rearrangements in microglial cells</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%">Alzheimer `s disease</style></keyword><keyword><style  face="normal" font="default" size="100%">Filopodia</style></keyword><keyword><style  face="normal" font="default" size="100%">microglia</style></keyword><keyword><style  face="normal" font="default" size="100%">Podosome</style></keyword><keyword><style  face="normal" font="default" size="100%">Tau aggregates</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2023</style></year><pub-dates><date><style  face="normal" font="default" size="100%">JUN</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">1870</style></volume><pages><style face="normal" font="default" size="100%">119477</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) is a progressive neurodegenerative disease that is associated with protein misfolding, plaque accumulation, neuronal dysfunction, synaptic loss, and cognitive decline. The pathological cascade of AD includes the intracellular Tau hyperphosphorylation and its subsequent aggregation, extracellular Amyloid-&amp;amp; beta; plaque formation and microglia-mediated neuroinflammation. The extracellular release of aggregated Tau is sensed by surveilling microglia through the involvement of various cell surface receptors. Among all, purinergic P2Y12R signaling is involved in microglial chemotaxis towards the damaged neurons. Microglial migration is highly linked with membrane-associated actin remodeling leading to the phagocytosis of extracellular Tau species. Here, we studied the formation of various actin structures such as podosome, lamellipodia and filopodia, in response to extracellular Tau monomers and aggregates. Microglial podosomes are colocalized with actin nucleator protein WASP, Arp2 and TKS5 adaptor protein during Tau-mediated migration. Moreover, the P2Y12 receptors were associated with F-actin-rich podosome structures, which signify the potential of Tau aggregates in microglial chemotaxis through the involvement of actin remodeling.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">5</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;
	5.1&lt;/p&gt;
</style></custom4></record></records></xml>