Purification and characterization of a tripeptidyl peptidase I from human osteoclastomas: evidence for its role in bone resorption
about
Classical late infantile neuronal ceroid lipofuscinosis fibroblasts are deficient in lysosomal tripeptidyl peptidase IThe human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pHCrystal Structure and Autoactivation Pathway of the Precursor Form of Human Tripeptidyl-peptidase 1, the Enzyme Deficient in Late Infantile Ceroid LipofuscinosisProduction and characterization of recombinant human CLN2 protein for enzyme-replacement therapy in late infantile neuronal ceroid lipofuscinosisBone-associated gene evolution and the origin of flight in birdsDevelopmental study of tripeptidyl peptidase I activity in the mouse central nervous system and peripheral organs.Tripeptidyl peptidase II promotes maturation of caspase-1 in Shigella flexneri-induced macrophage apoptosisPotential pitfalls and solutions for use of fluorescent fusion proteins to study the lysosomeHistochemical Demonstration of Tripeptidyl Aminopeptidase I.Tripeptidyl-peptidase I in health and disease.Analysis of NCL Proteins from an Evolutionary Standpoint.Human iPSC models of neuronal ceroid lipofuscinosis capture distinct effects of TPP1 and CLN3 mutations on the endocytic pathwayBiosynthesis, glycosylation, and enzymatic processing in vivo of human tripeptidyl-peptidase I.Proteolytic mechanisms of cartilage breakdown: a target for arthritis therapy?A tripeptidyl peptidase 1 is a binding partner of the Golgi pH regulator (GPHR) in Dictyostelium.Distribution of tripeptidyl peptidase I in human tissues under normal and pathological conditions.The specificity of lysosomal tripeptidyl peptidase-I determined by its action on angiotensin-II analogues.Diagnosis of late-infantile neuronal ceroid lipofuscinosis: a new sensitive method to assay lysosomal pepstatin-insensitive proteinase activity in human and animal specimens by capillary electrophoresis.Rat tripeptidyl peptidase I: molecular cloning, functional expression, tissue localization and enzymatic characterization.Cathepsin D is specifically inhibited by deoxyribonucleic acids.Ser475, Glu272, Asp276, Asp327, and Asp360 are involved in catalytic activity of human tripeptidyl-peptidase I.Viral-mediated delivery of the late-infantile neuronal ceroid lipofuscinosis gene, TPP-I to the mouse central nervous system.Characterization and cloning of tripeptidyl peptidase II from the fruit fly, Drosophila melanogaster.Cloning, Purification, and Characterization of Tripeptidyl Peptidase from Streptomyces herbaricolor TY-21.Characterisation of lipofuscin-like lysosomal inclusion bodies from human placenta.
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P2860
Purification and characterization of a tripeptidyl peptidase I from human osteoclastomas: evidence for its role in bone resorption
description
1993 nî lūn-bûn
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1993 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
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1993 թվականի նոյեմբերին հրատարակված գիտական հոդված
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1993年の論文
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1993年論文
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1993年論文
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1993年論文
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1993年論文
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1993年論文
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1993年论文
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Purification and characterizat ...... or its role in bone resorption
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Purification and characterizat ...... or its role in bone resorption
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Purification and characterizat ...... or its role in bone resorption
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Purification and characterizat ...... or its role in bone resorption
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Purification and characterizat ...... or its role in bone resorption
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Purification and characterizat ...... or its role in bone resorption
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Purification and characterizat ...... or its role in bone resorption
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M J Warburton
T J Chambers
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10.1006/ABBI.1993.1523
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P577
1993-11-01T00:00:00Z