Associated Papers
CLN2 Disease: Current Understandings, Challenges, and Future Directions.
Shock M et al.
Journal of Child Neurology, 2026
Genetic disease risks of under-represented founder populations in New York City.
Isshiki M et al.
Plos Genetics, 2025
Genetic disease risks of under-represented founder populations in New York City.
Isshiki M et al.
Medrxiv : the Preprint Server for Health Sciences, 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
TPP1 Variants in Iranian patients: A Novel Pathogenic Homozygous Variant Causing Neuronal Ceroid Lipofuscinosis 2.
Vafaei N et al.
Molecular Syndromology, 2024
Buffy Coat Score as a Biomarker of Treatment Response in Neuronal Ceroid Lipofuscinosis Type 2.
Sivananthan S et al.
Brain Sciences, 2023
Mutations, Genes, and Phenotypes Related to Movement Disorders and Ataxias.
Martínez-Rubio D et al.
International Journal of Molecular Sciences, 2022
Deep phenotyping and whole-exome sequencing improved the diagnostic yield for nuclear pedigrees with neurodevelopmental disorders.
Wang Q et al.
Molecular Genetics & Genomic Medicine, 2022
Neuronal ceroid lipofuscinosis in the South American-Caribbean region: An epidemiological overview.
Guelbert G et al.
Frontiers in Neurology, 2022
An ERG and OCT study of neuronal ceroid lipofuscinosis CLN2 Battens retinopathy.
Thompson DA et al.
Eye (london, England), 2021
Cerliponase Alfa for the Treatment of Atypical Phenotypes of CLN2 Disease: A Retrospective Case Series.
Wibbeler E et al.
Journal of Child Neurology, 2021
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
Cerebrospinal fluid neurofilament light chain levels in CLN2 disease patients treated with enzyme replacement therapy normalise after two years on treatment.
Iwan K et al.
F1000research, 2021
Slowing late infantile Batten disease by direct brain parenchymal administration of a rh.10 adeno-associated virus expressing CLN2.
Sondhi D et al.
Science Translational Medicine, 2020
Treatable Inherited Movement Disorders in Children: Spotlight on Clinical and Biochemical Features.
Galosi S et al.
Movement Disorders Clinical Practice, 2020
Changing Times for CLN2 Disease: The Era of Enzyme Replacement Therapy.
Specchio N et al.
Therapeutics and Clinical Risk Management, 2020
Mutation update: Review of TPP1 gene variants associated with neuronal ceroid lipofuscinosis CLN2 disease.
Gardner E et al.
Human Mutation, 2019
Optimizing clinical exome design and parallel gene-testing for recessive genetic conditions in preconception carrier screening: Translational research genomic data from 14,125 exomes.
Capalbo A et al.
Plos Genetics, 2019
Upregulation of tripeptidyl-peptidase 1 by 3-hydroxy-(2,2)-dimethyl butyrate, a brain endogenous ligand of PPARα: Implications for late-infantile Batten disease therapy.
Chakrabarti S et al.
Neurobiology of Disease, 2019
Homozygous missense TPP1 mutation associated with mild late infantile neuronal ceroid lipofuscinosis and the genotype-phenotype correlation.
Chen ZR et al.
Seizure, 2019
Protracted late infantile ceroid lipofuscinosis due to TPP1 mutations: Clinical, molecular and biochemical characterization in three sibs.
Di Giacopo R et al.
Journal of the Neurological Sciences, 2015
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
Gemfibrozil and fenofibrate, Food and Drug Administration-approved lipid-lowering drugs, up-regulate tripeptidyl-peptidase 1 in brain cells via peroxisome proliferator-activated receptor α: implications for late infantile Batten disease therapy.
Ghosh A et al.
The Journal of Biological Chemistry, 2012
A novel CLN2/TPP1 mutation in a Chinese patient with late infantile neuronal ceroid lipofuscinosis.
Wang YL et al.
Neurogenetics, 2011
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
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
Atypical CLN2 with later onset and prolonged course: a neuropathologic study showing different sensitivity of neuronal subpopulations to TPP1 deficiency.
Elleder M et al.
Acta Neuropathologica, 2008
Tripeptidyl-peptidase I in health and disease.
Golabek AA et al.
Biological Chemistry, 2006
Mutations in classical late infantile neuronal ceroid lipofuscinosis disrupt transport of tripeptidyl-peptidase I to lysosomes.
Steinfeld R et al.
Human Molecular Genetics, 2004
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.
Sleat DE et al.
The Journal of Neuroscience : the Official Journal of the Society for Neuroscience, 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
Expression and analysis of CLN2 variants in CHO cells: Q100R represents a polymorphism, and G389E and R447H represent loss-of-function mutations.
Lin L et al.
Human Mutation, 2001
Distribution of tripeptidyl peptidase I in human tissues under normal and pathological conditions.
Kida E et al.
Journal of Neuropathology and Experimental Neurology, 2001
Neuronal ceroid lipofuscinoses: research update.
Wisniewski KE et al.
Neurological Sciences : Official Journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology, 2000
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
Heterogeneity of late-infantile neuronal ceroid lipofuscinosis.
Zhong N et al.
Genetics in Medicine : Official Journal of the American College of Medical Genetics, 0