3.4.22.44	additional information	overexpression of NIa in rat B103 neuroblastoma cells results in a significant reduction in cell death caused by both intracellularly generated and exogenously added Amyloidbeta. Moreover, lentiviral-mediated expression of NIa in APPsw/PS1 transgenic mice significantly reduces the levels of Amyloid-beta and plaques in the brain	718264	
3.4.22.44	additional information	the full-length potyviral genome protease, VPg-Pro, has two domains: an N-terminal viral protein genome-linked, VPg, and a C-terminal protease NIa-Pro. Regulation of nuclear inclusion protein-a protease is crucial for polyprotein processing and hence, for successful infection by potyviruses, mechanisms regulating nuclear inclusion protein-a protease activity. Firstly, the influence of the VPg domain on the proteolytic activity of NIa-Pro increases when the two domains interact each other. Secondly, the protease activity of NIa-Pro can also be modulated by phosphorylation at Ser129. interaction with VPg as well as phosphorylation of Ser129 relays a signal through Trp143 present at the protein surface to the active site pocket by subtle conformational changes, thus modulating protease activity of NIa-Pro, molecular modeling, homology modeling, and molecular dynamics simulations, overview	718449	
3.4.22.44	physiological function	NIa-Pro responds to the presence of the aphid vector during infection by relocalizing to the vacuole. Remarkably, vacuolar localization is required for the ability of NIa-Pro to enhance aphid reproduction on host plants, vacuole localization disappears when aphids are removed	754840	
3.4.22.44	physiological function	oligomeric amyloid beta-induced cytotoxicity and mitochondrial dysfunction are significantly ameliorated by the enzyme. The enzyme prevents mitochondrial deposition of amyloid beta	732794	
3.4.22.44	physiological function	potyviral NIa targets many host elements during infection, establishing a network in which information is efficiently transmitted	753096	
3.4.22.44	physiological function	potyviral protein genome-linked, established as an intrinsically disordered domain, undergoes plausible structural alterations upon interaction with globular nuclear inclusion-a protease which induces the ATPase activity	731247	
3.4.22.44	physiological function	protease NIa not only reduces amyloid-beta pathology, but also improves behavioral deficits in mice	731765	
3.4.22.44	physiological function	the nuclear inclusion a protease of turnip mosaic virus is responsible for the processing of the viral polyprotein into functional proteins. Degradation of Amyloid-beta in the cytoplasm can be a novel strategy to control the levels of Amyloid-beta, plaque formation, and the associated cell death	718264	
3.4.22.44	physiological function	the nuclear inclusion a-protease domain increases Myzus persicae growth and reproduction on both Nicotiana benthamiana and Arabidopsis thaliana	732630	
3.4.22.44	physiological function	the TVMV genome is translated into a single large polyprotein that is subsequently processed by three virally encoded proteases. Seven of the nine cleavage events are carried out by the NIa protease	718366