EC Number |
General Information |
Reference |
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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 | more |
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 | 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 | more |
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 |
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 |