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Disease on EC 3.4.14.9 - tripeptidyl-peptidase I

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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Amyotrophic Lateral Sclerosis
Trehalose induces autophagy via lysosomal-mediated TFEB activation in models of motoneuron degeneration.
Arthritis, Rheumatoid
Lysosomal peptidases and glycosidases in rheumatoid arthritis.
Ataxia
Autosomal Recessive Spinocerebellar Ataxia 7 (SCAR7) is Caused by Variants in TPP1, The Gene Involved in Classic Late-Infantile Neuronal Ceroid Lipofuscinosis 2 Disease (CLN2 Disease).
Blindness
Management Strategies for CLN2 Disease.
Bone Resorption
Inhibition of bone resorption by inhibitors of tripeptidyl peptidase-I.
Purification and characterization of a tripeptidyl peptidase I from human osteoclastomas: evidence for its role in bone resorption.
Brain Injuries
[A primary study on the ARP-SRP gene expression profiling of brain injury by cDNA microarray]
Breast Neoplasms
A lysosomal pepstatin-insensitive proteinase as a novel biomarker for breast carcinoma.
Bulbo-Spinal Atrophy, X-Linked
Trehalose induces autophagy via lysosomal-mediated TFEB activation in models of motoneuron degeneration.
Carcinoma
Significance and prognostic value of lysosomal enzyme activities measured in surgically operated adenocarcinomas of the gastroesophageal junction and squamous cell carcinomas of the lower third of esophagus.
Carcinoma, Squamous Cell
Significance and prognostic value of lysosomal enzyme activities measured in surgically operated adenocarcinomas of the gastroesophageal junction and squamous cell carcinomas of the lower third of esophagus.
Cysts
The lysosomal aminopeptidase tripeptidyl peptidase 1 displays increased activity in malignant pancreatic cysts.
Dementia
Study of Intraventricular Cerliponase Alfa for CLN2 Disease.
Validity of a rapid and simple fluorometric tripeptidyl peptidase 1 (TPP1) assay using dried blood specimens to diagnose CLN2 disease.
Epilepsy
Autosomal Recessive Spinocerebellar Ataxia 7 (SCAR7) is Caused by Variants in TPP1, The Gene Involved in Classic Late-Infantile Neuronal Ceroid Lipofuscinosis 2 Disease (CLN2 Disease).
Disease characteristics and progression in patients with late-infantile neuronal ceroid lipofuscinosis type 2 (CLN2) disease: an observational cohort study.
Validity of a rapid and simple fluorometric tripeptidyl peptidase 1 (TPP1) assay using dried blood specimens to diagnose CLN2 disease.
Gangliosidoses, GM2
Tripeptidyl-peptidase I in neuronal ceroid lipofuscinoses and other lysosomal storage disorders.
Genetic Diseases, Inborn
Clinical protocol. Administration of a replication-deficient adeno-associated virus gene transfer vector expressing the human CLN2 cDNA to the brain of children with late infantile neuronal ceroid lipofuscinosis.
Systemic administration of tripeptidyl peptidase I in a mouse model of late infantile neuronal ceroid lipofuscinosis: effect of glycan modification.
Validity of a rapid and simple fluorometric tripeptidyl peptidase 1 (TPP1) assay using dried blood specimens to diagnose CLN2 disease.
Heredodegenerative Disorders, Nervous System
Residual levels of tripeptidyl-peptidase I activity dramatically ameliorate disease in late-infantile neuronal ceroid lipofuscinosis.
The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH.
Huntington Disease
Trehalose induces autophagy via lysosomal-mediated TFEB activation in models of motoneuron degeneration.
Lafora Disease
Advances in the genetics of progressive myoclonus epilepsy.
Language Development Disorders
Management Strategies for CLN2 Disease.
Lysosomal Storage Diseases
Assessment of Disease Severity in Late Infantile Neuronal Ceroid Lipofuscinosis Using Multiparametric MR Imaging.
Central nervous system stem cell transplantation for children with neuronal ceroid lipofuscinosis.
Classical late infantile neuronal ceroid lipofuscinosis fibroblasts are deficient in lysosomal tripeptidyl peptidase I.
Guidelines on the diagnosis, clinical assessments, treatment and management for CLN2 disease patients.
Slowing late infantile Batten disease by direct brain parenchymal administration of a rh.10 adeno-associated virus expressing CLN2.
The lysosomal degradation of neuromedin B is dependent on tripeptidyl peptidase-I: evidence for the impairment of neuropeptide degradation in late-infantile neuronal ceroid lipofuscinosis.
The specificity of lysosomal tripeptidyl peptidase-I determined by its action on angiotensin-II analogues.
Tripeptidyl peptidases: enzymes that count.
Melanoma
Impact of Gln94Glu mutation on the structure and function of protection of telomere 1, a cause of cutaneous familial melanoma.
MERRF Syndrome
Advances in the genetics of progressive myoclonus epilepsy.
Muscular Atrophy
Trehalose induces autophagy via lysosomal-mediated TFEB activation in models of motoneuron degeneration.
Neoplasms
A lysosomal pepstatin-insensitive proteinase as a novel biomarker for breast carcinoma.
Purification and characterization of a tripeptidyl peptidase I from human osteoclastomas: evidence for its role in bone resorption.
Nervous System Diseases
Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
Neuroblastoma
Trehalose induces autophagy via lysosomal-mediated TFEB activation in models of motoneuron degeneration.
Neurodegenerative Diseases
A mouse model of classical late-infantile neuronal ceroid lipofuscinosis based on targeted disruption of the CLN2 gene results in a loss of tripeptidyl-peptidase I activity and progressive neurodegeneration.
A tripeptidyl peptidase 1 is a binding partner of the Golgi pH regulator (GPHR) in Dictyostelium.
A zebrafish model of CLN2 disease is deficient in tripeptidyl peptidase 1 and displays progressive neurodegeneration accompanied by a reduction in proliferation.
AAV gene transfer delays disease onset in a TPP1-deficient canine model of the late infantile form of Batten disease.
Analysis of catalytic properties of tripeptidyl peptidase I (TTP-I), a serine carboxyl lysosomal protease, and its detection in tissue extracts using selective FRET peptide substrate.
Catalytic residues and substrate specificity of recombinant human tripeptidyl peptidase I (CLN2).
Chronic Enzyme Replacement to the Brain of a Late Infantile Neuronal Ceroid Lipofuscinosis Mouse Has Differential Effects on Phenotypes of Disease.
Clinical Pharmacokinetics and Pharmacodynamics of Cerliponase Alfa, Enzyme Replacement Therapy for CLN2 Disease by Intracerebroventricular Administration.
Detection of tripeptidyl peptidase I activity in living cells by fluorogenic substrates.
Determination of the substrate specificity of tripeptidyl-peptidase I using combinatorial peptide libraries and development of improved fluorogenic substrates.
Diagnosis of neuronal ceroid lipofuscinosis type 2 (CLN2 disease): Expert recommendations for early detection and laboratory diagnosis.
Dipeptidyl-peptidase I does not functionally compensate for the loss of tripeptidyl-peptidase I in the neurodegenerative disease late-infantile neuronal ceroid lipofuscinosis.
First-trimester diagnosis of late-infantile neuronal ceroid lipofuscinosis (LINCL) by tripeptidyl peptidase I assay and CLN2 mutation analysis.
Gemfibrozil, food and drug administration-approved lipid-lowering drug, increases longevity in mouse model of late infantile neuronal ceroid lipofuscinosis.
Genetic modulation of apoptotic pathways fails to alter disease course in tripeptidyl-peptidase 1 deficient mice.
Glial fibrillary acidic protein is elevated in the lysosomal storage disease classical late-infantile neuronal ceroid lipofuscinosis but is not a component of the storage material.
Inducible transgenic expression of tripeptidyl peptidase 1 in a mouse model of late-infantile neuronal ceroid lipofuscinosis.
Intraventricular Enzyme Replacement Improves Disease Phenotypes in a Mouse Model of Late Infantile Neuronal Ceroid Lipofuscinosis.
Intraventricular enzyme replacement improves disease phenotypes in a mouse model of late infantile neuronal ceroid lipofuscinosis.
Lysosomal degradation of cholecystokinin-(29-33)-amide in mouse brain is dependent on tripeptidyl peptidase-I: implications for the degradation and storage of peptides in classical late-infantile neuronal ceroid lipofuscinosis.
Specific substrate for CLN2 protease/tripeptidyl-peptidase I assay.
Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
Trehalose induces autophagy via lysosomal-mediated TFEB activation in models of motoneuron degeneration.
Tripeptidyl peptidase-I is essential for the degradation of sulphated cholecystokinin-8 (CCK-8S) by mouse brain lysosomes.
Tripeptidyl-peptidase I in health and disease.
Neuronal Ceroid-Lipofuscinoses
A Basic ApoE-Based Peptide Mediator to Deliver Proteins across the Blood-Brain Barrier: Long-Term Efficacy, Toxicity, and Mechanism.
A mouse model of classical late-infantile neuronal ceroid lipofuscinosis based on targeted disruption of the CLN2 gene results in a loss of tripeptidyl-peptidase I activity and progressive neurodegeneration.
A tripeptidyl peptidase 1 is a binding partner of the Golgi pH regulator (GPHR) in Dictyostelium.
AAV gene transfer delays disease onset in a TPP1-deficient canine model of the late infantile form of Batten disease.
AAV2-mediated CLN2 gene transfer to rodent and non-human primate brain results in long-term TPP-I expression compatible with therapy for LINCL.
Advances in the genetics of progressive myoclonus epilepsy.
An Australasian diagnostic service for the neuronal ceroid lipofuscinoses.
Aorsin, a novel serine proteinase with trypsin-like specificity at acidic pH.
Autism, Epilepsy, and Neuroregression: Photosensitivity on Electroencephalography Solved the Riddle.
Autosomal Recessive Spinocerebellar Ataxia 7 (SCAR7) is Caused by Variants in TPP1, The Gene Involved in Classic Late-Infantile Neuronal Ceroid Lipofuscinosis 2 Disease (CLN2 Disease).
Central nervous system stem cell transplantation for children with neuronal ceroid lipofuscinosis.
Chronic Enzyme Replacement to the Brain of a Late Infantile Neuronal Ceroid Lipofuscinosis Mouse Has Differential Effects on Phenotypes of Disease.
Classical late infantile neuronal ceroid lipofuscinosis fibroblasts are deficient in lysosomal tripeptidyl peptidase I.
Clinical study in Chinese patients with late-infantile form neuronal ceroid lipofuscinoses.
Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
Detection of tripeptidyl peptidase I activity in living cells by fluorogenic substrates.
Determination of the substrate specificity of tripeptidyl-peptidase I using combinatorial peptide libraries and development of improved fluorogenic substrates.
Developmental study of tripeptidyl peptidase I activity in the mouse central nervous system and peripheral organs.
Diagnosis of late-infantile neuronal ceroid lipofuscinosis using dried blood spot-based assay for TPPI enzyme activity: TPPI diagnostic assay from DBS.
Diagnosis of neuronal ceroid lipofuscinosis type 2 (CLN2 disease): Expert recommendations for early detection and laboratory diagnosis.
Dipeptidyl-peptidase I does not functionally compensate for the loss of tripeptidyl-peptidase I in the neurodegenerative disease late-infantile neuronal ceroid lipofuscinosis.
Disease characteristics and progression in patients with late-infantile neuronal ceroid lipofuscinosis type 2 (CLN2) disease: an observational cohort study.
Distribution and development of CLN2 protein, the late-infantile neuronal ceroid lipofuscinosis gene product.
Effective intravenous therapy for neurodegenerative disease with a therapeutic enzyme and a Peptide that mediates delivery to the brain.
Enhanced Survival of the LINCL Mouse Following CLN2 Gene Transfer Using the rh.10 Rhesus Macaque-derived Adeno-associated Virus Vector.
Enzyme replacement therapy with recombinant pro-CTSD (cathepsin D) corrects defective proteolysis and autophagy in neuronal ceroid lipofuscinosis.
Enzyme-based diagnosis of classical late infantile neuronal ceroid lipofuscinosis: comparison of tripeptidyl peptidase I and pepstatin-insensitive protease assays.
Exclusion of late infantile neuronal ceroid lipofuscinosis (LINCL) in a fetus by assay of tripeptidyl peptidase I in chorionic villi.
First-trimester diagnosis of late-infantile neuronal ceroid lipofuscinosis (LINCL) by tripeptidyl peptidase I assay and CLN2 mutation analysis.
Functional consequences and rescue potential of pathogenic missense mutations in tripeptidyl peptidase I.
Gemfibrozil and fenofibrate, FDA-approved lipid-lowering drugs, upregulate tripeptidyl-peptidase 1 in brain cells via peroxisome proliferator-activated receptor-a: implications for late infantile neuronal ceroid lipofuscinosis therapy.
Gemfibrozil, food and drug administration-approved lipid-lowering drug, increases longevity in mouse model of late infantile neuronal ceroid lipofuscinosis.
Genetic modulation of apoptotic pathways fails to alter disease course in tripeptidyl-peptidase 1 deficient mice.
Glial fibrillary acidic protein is elevated in the lysosomal storage disease classical late-infantile neuronal ceroid lipofuscinosis but is not a component of the storage material.
Global Brain Transcriptome Analysis of a Tpp1 Neuronal Ceroid Lipofuscinoses Mouse Model.
Inducible transgenic expression of tripeptidyl peptidase 1 in a mouse model of late-infantile neuronal ceroid lipofuscinosis.
Intracerebroventricular Cerliponase Alfa for Neuronal Ceroid Lipofuscinosis Type 2 Disease: Clinical Practice Considerations From US Clinics.
Intracranial delivery of CLN2 reduces brain pathology in a mouse model of classical late infantile neuronal ceroid lipofuscinosis.
Intrathecal tripeptidyl-peptidase 1 reduces lysosomal storage in a canine model of late infantile neuronal ceroid lipofuscinosis.
Intraventricular Enzyme Replacement Improves Disease Phenotypes in a Mouse Model of Late Infantile Neuronal Ceroid Lipofuscinosis.
Intraventricular enzyme replacement improves disease phenotypes in a mouse model of late infantile neuronal ceroid lipofuscinosis.
Late infantile neuronal ceroid lipofuscinosis: a new mutation in Arabs.
Long Term Expression and Safety of Administration of AAVrh.10hCLN2 to the Brain of Rats and Non-human Primates for the Treatment of Late Infantile Neuronal Lipofuscinosis.
Long-term expression and safety of administration of AAVrh.10hCLN2 to the brain of rats and nonhuman primates for the treatment of late infantile neuronal ceroid lipofuscinosis.
Lysosomal degradation of cholecystokinin-(29-33)-amide in mouse brain is dependent on tripeptidyl peptidase-I: implications for the degradation and storage of peptides in classical late-infantile neuronal ceroid lipofuscinosis.
Lysosomal protein thermal stability does not correlate with cellular half-life: global observations and a case study of tripeptidyl-peptidase 1.
Mutation of the glycosylated asparagine residue 286 in human CLN2 protein results in loss of enzymatic activity.
Mutation update: Review of TPP1 gene variants associated with neuronal ceroid lipofuscinosis CLN2 disease.
Mutations in classical late infantile neuronal ceroid lipofuscinosis disrupt transport of tripeptidyl-peptidase I to lysosomes.
Neurofilament light is a treatment-responsive biomarker in CLN2 disease.
Neuronal ceroid lipofuscinosis type CLN2: a new rationale for the construction of phenotypic subgroups based on a survey of 25 cases in South America.
Palmitoyl Protein Thioesterase1 (PPT1) and Tripeptidyl Peptidase-I (TPP-I) are expressed in the human saliva. A reliable and non-invasive source for the diagnosis of infantile (CLN1) and late infantile (CLN2) neuronal ceroid lipofuscinoses.
Perampanel attenuates myoclonus in a patient with neuronal ceroid lipofuscinoses type 2 disease.
Pre- and postnatal diagnosis of patients with CLN1 and CLN2 by assay of palmitoyl-protein thioesterase and tripeptidyl-peptidase I activities.
Production and characterization of recombinant human CLN2 protein for enzyme-replacement therapy in late infantile neuronal ceroid lipofuscinosis.
Residual levels of tripeptidyl-peptidase I activity dramatically ameliorate disease in late-infantile neuronal ceroid lipofuscinosis.
Revealing the clinical phenotype of atypical neuronal ceroid lipofuscinosis type 2 disease: Insights from the largest cohort in the world.
Safety of Direct Administration of AAV2(CU)hCLN2, a Candidate Treatment for the Central Nervous System Manifestations of Late Infantile Neuronal Ceroid Lipofuscinosis, to the Brain of Rats and Nonhuman Primates.
Safety of direct administration of AAV2(CU)hCLN2, a candidate treatment for the central nervous system manifestations of late infantile neuronal ceroid lipofuscinosis, to the brain of rats and nonhuman primates.
Slowing late infantile Batten disease by direct brain parenchymal administration of a rh.10 adeno-associated virus expressing CLN2.
Specific substrate for CLN2 protease/tripeptidyl-peptidase I assay.
Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
Study of Intraventricular Cerliponase Alfa for CLN2 Disease.
Survival advantage of neonatal CNS gene transfer for late infantile neuronal ceroid lipofuscinosis.
Systemic administration of tripeptidyl peptidase I in a mouse model of late infantile neuronal ceroid lipofuscinosis: effect of glycan modification.
The expression of tripeptidyl peptidase I in various tissues of rats and mice.
The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH.
The lysosomal degradation of neuromedin B is dependent on tripeptidyl peptidase-I: evidence for the impairment of neuropeptide degradation in late-infantile neuronal ceroid lipofuscinosis.
The specificity of lysosomal tripeptidyl peptidase-I determined by its action on angiotensin-II analogues.
The substrate range of tripeptidyl-peptidase I.
Timing of therapeutic intervention determines functional and survival outcomes in a mouse model of late infantile batten disease.
Tripeptidyl peptidase I, the late infantile neuronal ceroid lipofuscinosis gene product, initiates the lysosomal degradation of subunit c of ATP synthase.
Tripeptidyl peptidase-I is essential for the degradation of sulphated cholecystokinin-8 (CCK-8S) by mouse brain lysosomes.
Tripeptidyl peptidases: enzymes that count.
Tripeptidyl-peptidase I deficiency in classical late-infantile neuronal ceroid lipofuscinosis brain tissue. Evidence for defective peptidase rather than proteinase activity.
Tripeptidyl-peptidase I in health and disease.
Tripeptidyl-peptidase I in neuronal ceroid lipofuscinoses and other lysosomal storage disorders.
Tripeptidyl-peptidase I is apparently the CLN2 protein absent in classical late-infantile neuronal ceroid lipofuscinosis.
Upregulation of tripeptidyl-peptidase 1 by 3-hydroxy-(2,2)-dimethyl butyrate, a brain endogenous ligand of PPAR?: Implications for late-infantile Batten disease therapy.
Validity of a rapid and simple fluorometric tripeptidyl peptidase 1 (TPP1) assay using dried blood specimens to diagnose CLN2 disease.
Viral-mediated delivery of the late-infantile neuronal ceroid lipofuscinosis gene, TPP-I to the mouse central nervous system.
[Tripeptidyl peptidase 1 deficiency in neuronal ceroid lipofuscinosis. A novel mutation]
Pancreatic Cyst
The lysosomal aminopeptidase tripeptidyl peptidase 1 displays increased activity in malignant pancreatic cysts.
Parkinson Disease
Trehalose induces autophagy via lysosomal-mediated TFEB activation in models of motoneuron degeneration.
Seizures
Management Strategies for CLN2 Disease.
Viral-mediated delivery of the late-infantile neuronal ceroid lipofuscinosis gene, TPP-I to the mouse central nervous system.
Spinocerebellar Ataxias
Trehalose induces autophagy via lysosomal-mediated TFEB activation in models of motoneuron degeneration.
tripeptidyl-peptidase i deficiency
Detection of tripeptidyl peptidase I activity in living cells by fluorogenic substrates.
First-trimester diagnosis of late-infantile neuronal ceroid lipofuscinosis (LINCL) by tripeptidyl peptidase I assay and CLN2 mutation analysis.
Intracerebroventricular Cerliponase Alfa for Neuronal Ceroid Lipofuscinosis Type 2 Disease: Clinical Practice Considerations From US Clinics.
Pre- and postnatal enzyme analysis for infantile, late infantile and adult neuronal ceroid lipofuscinosis (CLN1 and CLN2).
Tripeptidyl-peptidase I deficiency in classical late-infantile neuronal ceroid lipofuscinosis brain tissue. Evidence for defective peptidase rather than proteinase activity.
[Tripeptidyl peptidase 1 deficiency in neuronal ceroid lipofuscinosis. A novel mutation]
Unverricht-Lundborg Syndrome
Advances in the genetics of progressive myoclonus epilepsy.