Associated Papers
Development of national biobank for lysosomal storage disorders in India- a step towards advancing research and precision medicine.
Sheth J et al.
Orphanet Journal of Rare Diseases, 2026
Universal noninvasive prenatal diagnosis for monogenic disorders using cell-free plasma DNA.
Zhang L et al.
Genome Medicine, 2025
Genetic Spectrum of Negative Electroretinograms in a Predominantly Pediatric Cohort of 177 Patients.
Zaslavsky K et al.
Investigative Ophthalmology & Visual Science, 2025
A needle in a haystack? The impact of a targeted epilepsy gene panel in the identification of a treatable but rapidly progressive metabolic epilepsy: CLN2 disease.
Lourenço CM et al.
Arquivos De Neuro-psiquiatria, 2024
A computational approach to analyzing the functional and structural impacts of Tripeptidyl-Peptidase 1 missense mutations in neuronal ceroid lipofuscinosis.
K P et al.
Metabolic Brain Disease, 2024
Protein domains provide a new layer of information for classifying human variations in rare diseases.
Corcuff M et al.
Frontiers in Bioinformatics, 2023
Neuronal ceroid lipofuscinosis in the South American-Caribbean region: An epidemiological overview.
Guelbert G et al.
Frontiers in Neurology, 2022
Genetic and phenotypic spectrum of Chinese patients with epilepsy and photosensitivity.
Niu Y et al.
Frontiers in Neurology, 2022
Revealing the clinical phenotype of atypical neuronal ceroid lipofuscinosis type 2 disease: Insights from the largest cohort in the world.
Lourenço CM et al.
Journal of Paediatrics and Child Health, 2021
Mutation update: Review of TPP1 gene variants associated with neuronal ceroid lipofuscinosis CLN2 disease.
Gardner E et al.
Human Mutation, 2019
Systematic analysis of the intersection of disease mutations with protein modifications.
Simpson CM et al.
Bmc Medical Genomics, 2019
Homozygous missense TPP1 mutation associated with mild late infantile neuronal ceroid lipofuscinosis and the genotype-phenotype correlation.
Chen ZR et al.
Seizure, 2019
The Clinical and Genetic Features of Co-occurring Epilepsy and Autism Spectrum Disorder in Chinese Children.
Long S et al.
Frontiers in Neurology, 2019
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).
Sun Y et al.
Human Mutation, 2013
Neuronal ceroid lipofuscinosis type CLN2: a new rationale for the construction of phenotypic subgroups based on a survey of 25 cases in South America.
Kohan R et al.
Gene, 2013
Alterations in ROS activity and lysosomal pH account for distinct patterns of macroautophagy in LINCL and JNCL fibroblasts.
Vidal-Donet JM et al.
Plos One, 2013
A critical tryptophan and Ca2+ in activation and catalysis of TPPI, the enzyme deficient in classic late-infantile neuronal ceroid lipofuscinosis.
Kuizon S et al.
Plos One, 2010
Functional consequences and rescue potential of pathogenic missense mutations in tripeptidyl peptidase I.
Walus M et al.
Human Mutation, 2010
Lysosomal serine protease CLN2 regulates tumor necrosis factor-alpha-mediated apoptosis in a Bid-dependent manner.
Autefage H et al.
The Journal of Biological Chemistry, 2009
Structure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosis.
Pal A et al.
The Journal of Biological Chemistry, 2009
Crystal structure and autoactivation pathway of the precursor form of human tripeptidyl-peptidase 1, the enzyme deficient in late infantile ceroid lipofuscinosis.
Guhaniyogi J et al.
The Journal of Biological Chemistry, 2009
Tripeptidyl-peptidase I in health and disease.
Golabek AA et al.
Biological Chemistry, 2006
Correlations between genotype, ultrastructural morphology and clinical phenotype in the neuronal ceroid lipofuscinoses.
Mole SE et al.
Neurogenetics, 2005
Ser475, Glu272, Asp276, Asp327, and Asp360 are involved in catalytic activity of human tripeptidyl-peptidase I.
Walus M et al.
Febs Letters, 2005
Mutations in classical late infantile neuronal ceroid lipofuscinosis disrupt transport of tripeptidyl-peptidase I to lysosomes.
Steinfeld R et al.
Human Molecular Genetics, 2004
Biosynthesis, glycosylation, and enzymatic processing in vivo of human tripeptidyl-peptidase I.
Golabek AA et al.
The Journal of Biological Chemistry, 2003
Two novel CLN2 gene mutations in a Chinese patient with classical late-infantile neuronal ceroid lipofuscinosis.
Lam CW et al.
American Journal of Medical Genetics, 2001
The human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pH.
Lin L et al.
The Journal of Biological Chemistry, 2001
Mutational analysis of the defective protease in classic late-infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder.
Sleat DE et al.
American Journal of Human Genetics, 1999
Molecular basis of the neuronal ceroid lipofuscinoses: mutations in CLN1, CLN2, CLN3, and CLN5.
Mole SE et al.
Human Mutation, 1999