The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH
about
Neuronal ceroid lipofuscinoses are connected at molecular level: interaction of CLN5 protein with CLN2 and CLN3Defective endoplasmic reticulum-resident membrane protein CLN6 affects lysosomal degradation of endocytosed arylsulfatase AA model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidasesStructure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosisCrystal Structure and Autoactivation Pathway of the Precursor Form of Human Tripeptidyl-peptidase 1, the Enzyme Deficient in Late Infantile Ceroid LipofuscinosisInteractions of the proteins of neuronal ceroid lipofuscinosis: clues to functionProduction and characterization of recombinant human CLN2 protein for enzyme-replacement therapy in late infantile neuronal ceroid lipofuscinosisA critical tryptophan and Ca2+ in activation and catalysis of TPPI, the enzyme deficient in classic late-infantile neuronal ceroid lipofuscinosisLoss of Niemann-Pick C1 or C2 protein results in similar biochemical changes suggesting that these proteins function in a common lysosomal pathwayDetermination of the substrate specificity of tripeptidyl-peptidase I using combinatorial peptide libraries and development of improved fluorogenic substrates.The genetic spectrum of human neuronal ceroid-lipofuscinoses.Systemic administration of tripeptidyl peptidase I in a mouse model of late infantile neuronal ceroid lipofuscinosis: effect of glycan modification.Correlations between genotype, ultrastructural morphology and clinical phenotype in the neuronal ceroid lipofuscinoses.Overexpression in colorectal carcinoma of two lysosomal enzymes, CLN2 and CLN1, involved in neuronal ceroid lipofuscinosis.Clarification of the mechanism of acylation reaction and origin of substrate specificity of the serine-carboxyl peptidase sedolisin through QM/MM free energy simulationsThe N-acylethanolamine-hydrolyzing acid amidase (NAAA).Partial genetic suppression of a loss-of-function mutant of the neuronal ceroid lipofuscinosis-associated protease TPP1 in Dictyostelium discoideum.The neuronal ceroid-lipofuscinoses.Beta-endorphin 1-31 biotransformation and cAMP modulation in inflammationThe intracellular location and function of proteins of neuronal ceroid lipofuscinoses.Progress in the Development of Small Molecule Therapeutics for the Treatment of Neuronal Ceroid Lipofuscinoses (NCLs).The QM/MM molecular dynamics and free energy simulations of the acylation reaction catalyzed by the serine-carboxyl peptidase kumamolisin-As.Brain Region-Specific Degeneration with Disease Progression in Late Infantile Neuronal Ceroid Lipofuscinosis (CLN2 Disease).3,4-Dihydroxyphenylalanine Peptides as Nonperturbative Quantum Dot Sensors of Aminopeptidase.Lysosomal serine protease CLN2 regulates tumor necrosis factor-alpha-mediated apoptosis in a Bid-dependent mannerAnalysis of NCL Proteins from an Evolutionary Standpoint.Radioiodinated Capsids Facilitate In Vivo Non-Invasive Tracking of Adeno-Associated Gene Transfer Vectors.N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I.Biosynthesis, glycosylation, and enzymatic processing in vivo of human tripeptidyl-peptidase I.Prosegment of tripeptidyl peptidase I is a potent, slow-binding inhibitor of its cognate enzyme.Mannose 6-phosphorylated proteins are required for tumor necrosis factor-induced apoptosis: defective response in I-cell disease fibroblasts.Late infantile neuronal ceroid lipofuscinosis: quantitative description of the clinical course in patients with CLN2 mutations.Biotransformation of beta-endorphin and possible therapeutic implications.Aorsin, a novel serine proteinase with trypsin-like specificity at acidic pH.Functional consequences and rescue potential of pathogenic missense mutations in tripeptidyl peptidase I.The specificity of lysosomal tripeptidyl peptidase-I determined by its action on angiotensin-II analogues.Maturation of human tripeptidyl-peptidase I in vitro.Glycosaminoglycans modulate activation, activity, and stability of tripeptidyl-peptidase I in vitro and in vivo.Viral-mediated delivery of the late-infantile neuronal ceroid lipofuscinosis gene, TPP-I to the mouse central nervous system.AAV2-mediated CLN2 gene transfer to rodent and non-human primate brain results in long-term TPP-I expression compatible with therapy for LINCL.
P2860
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P2860
The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH
description
2001 nî lūn-bûn
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2001 թուականի Յունուարին հրատարակուած գիտական յօդուած
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2001 թվականի հունվարին հրատարակված գիտական հոդված
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2001年の論文
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2001年論文
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2001年論文
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2001年論文
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2001年論文
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2001年論文
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2001年论文
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name
The human CLN2 protein/tripept ...... hat autoactivates at acidic pH
@ast
The human CLN2 protein/tripept ...... hat autoactivates at acidic pH
@en
The human CLN2 protein/tripept ...... hat autoactivates at acidic pH
@en-gb
The human CLN2 protein/tripept ...... hat autoactivates at acidic pH
@nl
type
label
The human CLN2 protein/tripept ...... hat autoactivates at acidic pH
@ast
The human CLN2 protein/tripept ...... hat autoactivates at acidic pH
@en
The human CLN2 protein/tripept ...... hat autoactivates at acidic pH
@en-gb
The human CLN2 protein/tripept ...... hat autoactivates at acidic pH
@nl
prefLabel
The human CLN2 protein/tripept ...... hat autoactivates at acidic pH
@ast
The human CLN2 protein/tripept ...... hat autoactivates at acidic pH
@en
The human CLN2 protein/tripept ...... hat autoactivates at acidic pH
@en-gb
The human CLN2 protein/tripept ...... hat autoactivates at acidic pH
@nl
P2093
P2860
P356
P1476
The human CLN2 protein/tripept ...... hat autoactivates at acidic pH
@en
P2093
P2860
P304
P356
10.1074/JBC.M008562200
P407
P577
2001-01-19T00:00:00Z