Mutational analysis of the defective protease in classic late-infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder
about
Batten's disease: clues to neuronal protein catabolism in lysosomesThe human CLN2 protein/tripeptidyl-peptidase I is a serine protease that autoactivates at acidic pHA model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidasesMoving towards effective therapeutic strategies for Neuronal Ceroid LipofuscinosisStructure of tripeptidyl-peptidase I provides insight into the molecular basis of late infantile neuronal ceroid lipofuscinosisCrystal Structure and Autoactivation Pathway of the Precursor Form of Human Tripeptidyl-peptidase 1, the Enzyme Deficient in Late Infantile Ceroid LipofuscinosisTwo novel CLN2 gene mutations in a Chinese patient with classical late-infantile neuronal ceroid lipofuscinosisInteractions of the proteins of neuronal ceroid lipofuscinosis: clues to functionProduction and characterization of recombinant human CLN2 protein for enzyme-replacement therapy in late infantile neuronal ceroid lipofuscinosisExtraneuronal pathology in a canine model of CLN2 neuronal ceroid lipofuscinosis after intracerebroventricular gene therapy that delays neurological disease progression.Analysis of large-scale whole exome sequencing data to determine the prevalence of genetically-distinct forms of neuronal ceroid lipofuscinosis.Determination of the substrate specificity of tripeptidyl-peptidase I using combinatorial peptide libraries and development of improved fluorogenic substrates.Prenatal diagnosis of the neuronal ceroid lipofuscinoses.The genetic spectrum of human neuronal ceroid-lipofuscinoses.Advances in the genetics of progressive myoclonus epilepsy.Spectrum of ocular manifestations in CLN2-associated batten (Jansky-Bielschowsky) disease correlate with advancing age and deteriorating neurological functionThe neuronal ceroid-lipofuscinoses.Large-volume intrathecal enzyme delivery increases survival of a mouse model of late infantile neuronal ceroid lipofuscinosis.Progress in the Development of Small Molecule Therapeutics for the Treatment of Neuronal Ceroid Lipofuscinoses (NCLs).Neuron-astrocyte interactions in neurodegenerative diseases: Role of neuroinflammationAstrocytes and lysosomal storage diseases.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.Tripeptidyl-peptidase I in health and disease.Molecular epidemiology of childhood neuronal ceroid-lipofuscinosis in Italy.Lysosomal Storage Diseases-Regulating Neurodegeneration.Residual levels of tripeptidyl-peptidase I activity dramatically ameliorate disease in late-infantile neuronal ceroid lipofuscinosis.Assessment of disease severity in late infantile neuronal ceroid lipofuscinosis using multiparametric MR imaging.Inhibition of a secreted glutamic peptidase prevents growth of the fungus Talaromyces emersoniiLong-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.Neuronal ceroid lipofuscinosis type CLN2: a new rationale for the construction of phenotypic subgroups based on a survey of 25 cases in South America.Update of the mutation spectrum and clinical correlations of over 360 mutations in eight genes that underlie the neuronal ceroid lipofuscinoses.N-glycosylation is crucial for folding, trafficking, and stability of human tripeptidyl-peptidase I.Biosynthesis, glycosylation, and enzymatic processing in vivo of human tripeptidyl-peptidase I.Biochemical characterization of a lysosomal protease deficient in classical late infantile neuronal ceroid lipofuscinosis (LINCL) and development of an enzyme-based assay for diagnosis and exclusion of LINCL in human specimens and animal models.The role of nonsense-mediated decay in neuronal ceroid lipofuscinosis.Late infantile neuronal ceroid lipofuscinosis: quantitative description of the clinical course in patients with CLN2 mutations.The human urine mannose 6-phosphate glycoproteome.Distribution of tripeptidyl peptidase I in human tissues under normal and pathological conditions.Maturation of human tripeptidyl-peptidase I in vitro.Glycosaminoglycans modulate activation, activity, and stability of tripeptidyl-peptidase I in vitro and in vivo.
P2860
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P2860
Mutational analysis of the defective protease in classic late-infantile neuronal ceroid lipofuscinosis, a neurodegenerative lysosomal storage disorder
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունիսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Mutational analysis of the def ...... ive lysosomal storage disorder
@ast
Mutational analysis of the def ...... ive lysosomal storage disorder
@en
Mutational analysis of the def ...... ive lysosomal storage disorder
@nl
type
label
Mutational analysis of the def ...... ive lysosomal storage disorder
@ast
Mutational analysis of the def ...... ive lysosomal storage disorder
@en
Mutational analysis of the def ...... ive lysosomal storage disorder
@nl
prefLabel
Mutational analysis of the def ...... ive lysosomal storage disorder
@ast
Mutational analysis of the def ...... ive lysosomal storage disorder
@en
Mutational analysis of the def ...... ive lysosomal storage disorder
@nl
P2093
P2860
P3181
P356
P1476
Mutational analysis of the def ...... ive lysosomal storage disorder
@en
P2093
A N Siakotos
D N Palmer
K Wisniewski
R J Donnelly
R K Pullarkat
R M Boustany
P2860
P304
P3181
P356
10.1086/302427
P407
P577
1999-06-01T00:00:00Z