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
Benchmarking Nanopore Sequencing for CLN2 (TPP1) Mutation Detection: Integrating Rapid Genomics and Orthogonal Validation for Precision Diagnostics.
Teker B et al.
International Journal of Molecular Sciences, 2025
Mutation update: Review of TPP1 gene variants associated with neuronal ceroid lipofuscinosis CLN2 disease.
Gardner E et al.
Human Mutation, 2019
Batten disease: biochemical and molecular characterization revealing novel PPT1 and TPP1 gene mutations in Indian patients.
Sheth J et al.
Bmc Neurology, 2018
The population genetics of human disease: The case of recessive, lethal mutations.
Amorim CEG et al.
Plos Genetics, 2017
Progressive conduction defects and cardiac death in late infantile neuronal ceroid lipofuscinosis.
Fukumura S et al.
Developmental Medicine and Child Neurology, 2012
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
PhenoHM: human-mouse comparative phenome-genome server.
Sardana D et al.
Nucleic Acids Research, 2010
Functional consequences and rescue potential of pathogenic missense mutations in tripeptidyl peptidase I.
Walus M et al.
Human Mutation, 2010
Glycosylation- and phosphorylation-dependent intracellular transport of lysosomal hydrolases.
Pohl S et al.
Biological Chemistry, 2009
The effect of individual N-glycans on enzyme activity.
Skropeta D
Bioorganic & Medicinal 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
Analysis of NCL Proteins from an Evolutionary Standpoint.
Muzaffar NE et al.
Current Genomics, 2008
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
Mutations in classical late infantile neuronal ceroid lipofuscinosis disrupt transport of tripeptidyl-peptidase I to lysosomes.
Steinfeld R et al.
Human Molecular Genetics, 2004
Mutation of the glycosylated asparagine residue 286 in human CLN2 protein results in loss of enzymatic activity.
Tsiakas K et al.
Glycobiology, 2004
N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I.
Wujek P et al.
The Journal of Biological Chemistry, 2004
The genetic spectrum of human neuronal ceroid-lipofuscinoses.
Mole SE
Brain Pathology (zurich, Switzerland), 2004
Late infantile neuronal ceroid lipofuscinosis: quantitative description of the clinical course in patients with CLN2 mutations.
Steinfeld R et al.
American Journal of Medical Genetics, 2002