Biosynthetic processing of cathepsins and lysosomal degradation are abolished in asparaginyl endopeptidase-deficient mice
about
Angiostrongylus cantonensis cathepsin B-like protease (Ac-cathB-1) is involved in host gut penetrationNeuroprotective actions of PIKE-L by inhibition of SET proteolytic degradation by asparagine endopeptidaseAsparagine endopeptidase controls anti-influenza virus immune responses through TLR7 activationVacuolar processing enzyme in plant programmed cell deathNucleic acid recognition by Toll-like receptors is coupled to stepwise processing by cathepsins and asparagine endopeptidase.Design of cell-permeable, fluorescent activity-based probes for the lysosomal cysteine protease asparaginyl endopeptidase (AEP)/legumain.Blastocystis legumain is localized on the cell surface, and specific inhibition of its activity implicates a pro-survival role for the enzyme.Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo.Cleavage of tau by asparagine endopeptidase mediates the neurofibrillary pathology in Alzheimer's disease.Asparagine endopeptidase is an innovative therapeutic target for neurodegenerative diseases.Nuclear legumain activity in colorectal cancer.Divergent paths for the selection of immunodominant epitopes from distinct antigenic sources.The asparaginyl endopeptidase legumain is essential for functional recovery after spinal cord injury in adult zebrafish.Development of near-infrared fluorophore (NIRF)-labeled activity-based probes for in vivo imaging of legumainFunctional imaging of legumain in cancer using a new quenched activity-based probeTargeting cell surface alpha(v)beta(3) integrin increases therapeutic efficacies of a legumain protease-activated auristatin prodrugThe exogenous pathway for antigen presentation on major histocompatibility complex class II and CD1 molecules.Dendritic cells: microbial clearance via autophagy and potential immunobiological consequences for periodontal diseaseCounter Selection Substrate Library Strategy for Developing Specific Protease Substrates and Probes.Asparaginyl endopeptidase: case history of a class II MHC compartment protease.Delta-secretase cleaves amyloid precursor protein and regulates the pathogenesis in Alzheimer's diseaseThe protease cathepsin L regulates Th17 cell differentiation.Activation of asparaginyl endopeptidase leads to Tau hyperphosphorylation in Alzheimer disease.Electrochemical Protease Biosensor Based on Enhanced AC Voltammetry Using Carbon Nanofiber Nanoelectrode ArraysMice lacking asparaginyl endopeptidase develop disorders resembling hemophagocytic syndrome.Pathomimetic cancer avatars for live-cell imaging of protease activity.Proteases: essential actors in processing antigens and intracellular toll-like receptors.Asparaginyl endopeptidase cleaves TDP-43 in brainActivity-based probes as a tool for functional proteomic analysis of proteases.Two vacuole-mediated defense strategies in plants.The role of vacuole in plant cell death.Classes of programmed cell death in plants, compared to those in animals.The endosome-lysosome pathway and information generation in the immune system.Proteolysis mediated by cysteine cathepsins and legumain-recent advances and cell biological challenges.Autophagic activity measured in whole rat hepatocytes as the accumulation of a novel BHMT fragment (p10), generated in amphisomes by the asparaginyl proteinase, legumain.Effects of legumain as a potential prognostic factor on gastric cancers.The Other Function: Class II-Restricted Antigen Presentation by B Cells.Association of legumain expression pattern with prostate cancer invasiveness and aggressiveness.Human and mouse perforin are processed in part through cleavage by the lysosomal cysteine proteinase cathepsin L.Internalization of exogenous cystatin F supresses cysteine proteases and induces the accumulation of single-chain cathepsin L by multiple mechanisms.
P2860
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P2860
Biosynthetic processing of cathepsins and lysosomal degradation are abolished in asparaginyl endopeptidase-deficient mice
description
2003 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Journal of Biological Chemistry
@fr
artículu científicu espublizáu en 2003
@ast
im August 2003 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2003/08/29)
@sk
vědecký článek publikovaný v roce 2003
@cs
wetenschappelijk artikel (gepubliceerd op 2003/08/29)
@nl
наукова стаття, опублікована в серпні 2003
@uk
name
Biosynthetic processing of cat ...... l endopeptidase-deficient mice
@ast
Biosynthetic processing of cat ...... l endopeptidase-deficient mice
@en
Biosynthetic processing of cat ...... l endopeptidase-deficient mice
@nl
type
label
Biosynthetic processing of cat ...... l endopeptidase-deficient mice
@ast
Biosynthetic processing of cat ...... l endopeptidase-deficient mice
@en
Biosynthetic processing of cat ...... l endopeptidase-deficient mice
@nl
prefLabel
Biosynthetic processing of cat ...... l endopeptidase-deficient mice
@ast
Biosynthetic processing of cat ...... l endopeptidase-deficient mice
@en
Biosynthetic processing of cat ...... l endopeptidase-deficient mice
@nl
P2093
P2860
P921
P356
P1476
Biosynthetic processing of cat ...... l endopeptidase-deficient mice
@en
P2093
Akitsugu Yamamoto
Ikuko Hara-Nishimura
Kanae Shirahama-Noda
Kazushi Sugihara
Masahide Asano
Mikio Nishimura
Noriyoshi Hashimoto
P2860
P304
33194–33199
P356
10.1074/JBC.M302742200
P407
P577
2003-08-29T00:00:00Z