A lysosomal proteinase, the late infantile neuronal ceroid lipofuscinosis gene (CLN2) product, is essential for degradation of a hydrophobic protein, the subunit c of ATP synthase.
about
Purification and characterization of bovine brain lysosomal pepstatin-insensitive proteinase, the gene product deficient in the human late-infantile neuronal ceroid lipofuscinosisA tailored mouse model of CLN2 disease: A nonsense mutant for testing personalized therapies.The neuronal ceroid-lipofuscinoses.The intracellular location and function of proteins of neuronal ceroid lipofuscinoses.Lysosomal accumulation of SCMAS (subunit c of mitochondrial ATP synthase) in neurons of the mouse model of mucopolysaccharidosis III B.Tripeptidyl-peptidase I in health and disease.Different molecular mechanisms involved in spontaneous and oxidative stress-induced mitochondrial fragmentation in tripeptidyl peptidase-1 (TPP-1)-deficient fibroblasts.Lysosomal membrane permeability stimulates protein aggregate formation in neurons of a lysosomal diseaseNeuronal pigmented autophagic vacuoles: lipofuscin, neuromelanin, and ceroid as macroautophagic responses during aging and disease.Lysosomal serine protease CLN2 regulates tumor necrosis factor-alpha-mediated apoptosis in a Bid-dependent mannerLong-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.Analysis of NCL Proteins from an Evolutionary Standpoint.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.Enhanced expression of manganese-dependent superoxide dismutase in human and sheep CLN6 tissuesDistribution of tripeptidyl peptidase I in human tissues under normal and pathological conditions.Rat tripeptidyl peptidase I: molecular cloning, functional expression, tissue localization and enzymatic characterization.Glycosaminoglycans modulate activation, activity, and stability of tripeptidyl-peptidase I in vitro and in vivo.Ser475, Glu272, Asp276, Asp327, and Asp360 are involved in catalytic activity of human tripeptidyl-peptidase I.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.A zebrafish model of CLN2 disease is deficient in tripeptidyl peptidase 1 and displays progressive neurodegeneration accompanied by a reduction in proliferation.Human and rat brain lipofuscin proteome.CLC-3 deficiency leads to phenotypes similar to human neuronal ceroid lipofuscinosis.Early-onset progressive myoclonic epilepsy with dystonia mapping to 16pter-p13.3.
P2860
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P2860
A lysosomal proteinase, the late infantile neuronal ceroid lipofuscinosis gene (CLN2) product, is essential for degradation of a hydrophobic protein, the subunit c of ATP synthase.
description
1999 nî lūn-bûn
@nan
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
1999年论文
@zh
1999年论文
@zh-cn
name
A lysosomal proteinase, the la ...... the subunit c of ATP synthase.
@en
type
label
A lysosomal proteinase, the la ...... the subunit c of ATP synthase.
@en
prefLabel
A lysosomal proteinase, the la ...... the subunit c of ATP synthase.
@en
P2093
P1476
A lysosomal proteinase, the la ...... the subunit c of ATP synthase
@en
P2093
P304
P356
10.1046/J.1471-4159.1999.0722573.X
P407
P50
P577
1999-06-01T00:00:00Z