Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo.
about
Cystatin F is a cathepsin C-directed protease inhibitor regulated by proteolysisNeuroprotective actions of PIKE-L by inhibition of SET proteolytic degradation by asparagine endopeptidaseAsparagine endopeptidase controls anti-influenza virus immune responses through TLR7 activationIrAE – An asparaginyl endopeptidase (legumain) in the gut of the hard tick Ixodes ricinusMechanistic and structural studies on legumain explain its zymogenicity, distinct activation pathways, and regulationStructural analysis of asparaginyl endopeptidase reveals the activation mechanism and a reversible intermediate maturation stageBiochemical, transcriptomic and proteomic analyses of digestion in the scorpion Tityus serrulatus: insights into function and evolution of digestion in an ancient arthropodDesign 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.The biology of human lymphoid malignancies revealed by gene expression profiling.Cleavage of tau by asparagine endopeptidase mediates the neurofibrillary pathology in Alzheimer's disease.Structural basis of reduction-dependent activation of human cystatin F.Asparagine endopeptidase is an innovative therapeutic target for neurodegenerative diseases.Nuclear legumain activity in colorectal cancer.An evolutionary analysis of antigen processing and presentation across different timescales reveals pervasive selection.Local mitochondrial-endolysosomal microfusion cleaves voltage-dependent anion channel 1 to promote survival in hypoxia.Functional 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.Crystal Structure and Activity Studies of the C11 Cysteine Peptidase from Parabacteroides merdae in the Human Gut Microbiome.Asparaginyl endopeptidase: case history of a class II MHC compartment protease.Delta-secretase cleaves amyloid precursor protein and regulates the pathogenesis in Alzheimer's diseaseActivation of asparaginyl endopeptidase leads to Tau hyperphosphorylation in Alzheimer disease.A dyad of lymphoblastic lysosomal cysteine proteases degrades the antileukemic drug L-asparaginaseCathepsin G: roles in antigen presentation and beyond.Microtubule-associated protein tau as a therapeutic target in Alzheimer's disease.Proteolysis mediated by cysteine cathepsins and legumain-recent advances and cell biological challenges.Comparative structural analysis of the caspase family with other clan CD cysteine peptidases.Tau and neurodegenerative disease: the story so far.Functional role of asparaginyl endopeptidase ubiquitination by TRAF6 in tumor invasion and metastasis.Internalization of exogenous cystatin F supresses cysteine proteases and induces the accumulation of single-chain cathepsin L by multiple mechanisms.Delta-Secretase Phosphorylation by SRPK2 Enhances Its Enzymatic Activity, Provoking Pathogenesis in Alzheimer's Disease.The C-terminal region of the proprotein convertase 1/3 (PC1/3) exerts a bimodal regulation of the enzyme activity in vitro.Reconstruction of a pathway of antigen processing and class II MHC peptide capture.Activation of legumain involves proteolytic and conformational events, resulting in a context- and substrate-dependent activity profile.Protease activity of legumain is inhibited by an increase of cystatin E/M in the DJ-1-knockout mouse spleen, cerebrum and heart.Simvastatin inhibits glucose metabolism and legumain activity in human myotubes.GARP: a key receptor controlling FOXP3 in human regulatory T cells.The asparaginyl endopeptidase legumain after experimental stroke.The human G1m1 allotype associates with CD4+ T-cell responsiveness to a highly conserved IgG1 constant region peptide and confers an asparaginyl endopeptidase cleavage site
P2860
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P2860
Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo.
description
2003 nî lūn-bûn
@nan
2003 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo.
@ast
Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo.
@en
Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo.
@nl
type
label
Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo.
@ast
Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo.
@en
Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo.
@nl
prefLabel
Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo.
@ast
Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo.
@en
Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo.
@nl
P2093
P2860
P356
P1476
Multistep autoactivation of asparaginyl endopeptidase in vitro and in vivo.
@en
P2093
Antony N Antoniou
Colin Watts
Daniela Mazzeo
Dongtao Ni Li
Stephen P Matthews
P2860
P304
38980-38990
P356
10.1074/JBC.M305930200
P407
P577
2003-07-14T00:00:00Z