Tripeptidyl peptidase I, the late infantile neuronal ceroid lipofuscinosis gene product, initiates the lysosomal degradation of subunit c of ATP synthase
about
A model of tripeptidyl-peptidase I (CLN2), a ubiquitous and highly conserved member of the sedolisin family of serine-carboxyl peptidasesInteractions of the proteins of neuronal ceroid lipofuscinosis: clues to functionLysosomal 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.Determination of the substrate specificity of tripeptidyl-peptidase I using combinatorial peptide libraries and development of improved fluorogenic substrates.A tailored mouse model of CLN2 disease: A nonsense mutant for testing personalized therapies.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.Correlations between genotype, ultrastructural morphology and clinical phenotype in the neuronal ceroid lipofuscinoses.Overexpression in colorectal carcinoma of two lysosomal enzymes, CLN2 and CLN1, involved in neuronal ceroid lipofuscinosis.Dipeptidyl-peptidase I does not functionally compensate for the loss of tripeptidyl-peptidase I in the neurodegenerative disease late-infantile neuronal ceroid lipofuscinosis.Genetics of inherited human epilepsiesThe intracellular location and function of proteins of neuronal ceroid lipofuscinoses.Monitoring autophagy in lysosomal storage disordersLysosomal serine protease CLN2 regulates tumor necrosis factor-alpha-mediated apoptosis in a Bid-dependent mannerPersistence of the mitochondrial permeability transition in the absence of subunit c of human ATP synthase.Late infantile neuronal ceroid lipofuscinosis: quantitative description of the clinical course in patients with CLN2 mutations.The specificity of lysosomal tripeptidyl peptidase-I determined by its action on angiotensin-II analogues.Viral-mediated delivery of the late-infantile neuronal ceroid lipofuscinosis gene, TPP-I to the mouse central nervous system.AAV2-mediated CLN2 gene transfer to rodent and non-human primate brain results in long-term TPP-I expression compatible with therapy for LINCL.Differences in expression patterns of cathepsin C/dipeptidyl peptidase I in normal, pathological and aged mouse central nervous system.A zebrafish model of CLN2 disease is deficient in tripeptidyl peptidase 1 and displays progressive neurodegeneration accompanied by a reduction in proliferation.Neural stem cells for disease modeling and evaluation of therapeutics for infantile (CLN1/PPT1) and late infantile (CLN2/TPP1) neuronal ceroid lipofuscinoses.
P2860
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P2860
Tripeptidyl peptidase I, the late infantile neuronal ceroid lipofuscinosis gene product, initiates the lysosomal degradation of subunit c of ATP synthase
description
2000 nî lūn-bûn
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2000 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
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2000 թվականի սեպտեմբերին հրատարակված գիտական հոդված
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name
Tripeptidyl peptidase I, the l ...... n of subunit c of ATP synthase
@ast
Tripeptidyl peptidase I, the l ...... n of subunit c of ATP synthase
@en
Tripeptidyl peptidase I, the l ...... n of subunit c of ATP synthase
@en-gb
Tripeptidyl peptidase I, the l ...... n of subunit c of ATP synthase
@nl
type
label
Tripeptidyl peptidase I, the l ...... n of subunit c of ATP synthase
@ast
Tripeptidyl peptidase I, the l ...... n of subunit c of ATP synthase
@en
Tripeptidyl peptidase I, the l ...... n of subunit c of ATP synthase
@en-gb
Tripeptidyl peptidase I, the l ...... n of subunit c of ATP synthase
@nl
prefLabel
Tripeptidyl peptidase I, the l ...... n of subunit c of ATP synthase
@ast
Tripeptidyl peptidase I, the l ...... n of subunit c of ATP synthase
@en
Tripeptidyl peptidase I, the l ...... n of subunit c of ATP synthase
@en-gb
Tripeptidyl peptidase I, the l ...... n of subunit c of ATP synthase
@nl
P2093
P921
P1476
Tripeptidyl peptidase I, the l ...... n of subunit c of ATP synthase
@en
P2093
E Kominami
M Takeda-Ezaki
P304
P356
10.1093/OXFORDJOURNALS.JBCHEM.A022781
P407
P577
2000-09-01T00:00:00Z