about
Purification and structure of human liver aspartylglucosaminidaseHuman leucocyte glycosylasparaginase is an alpha/beta-heterodimer of 19 kDa alpha-subunit and 17 and 18 kDa beta-subunitCharacterization of a human core-specific lysosomal {alpha}1,6-mannosidase involved in N-glycan catabolism.Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the diseaseCharacterization of the cDNA and genomic sequence of a G protein gamma subunit (gamma 5)Crystallographic Snapshot of a Productive Glycosylasparaginase–Substrate ComplexAn HLA-A2-restricted tyrosinase antigen on melanoma cells results from posttranslational modification and suggests a novel pathway for processing of membrane proteinsCerebellar alterations and gait defects as therapeutic outcome measures for enzyme replacement therapy in α-mannosidosis.Phylogenetic analyses suggest multiple changes of substrate specificity within the glycosyl hydrolase 20 family.Impaired lysosomal trimming of N-linked oligosaccharides leads to hyperglycosylation of native lysosomal proteins in mice with alpha-mannosidosis.Aspartylglucosaminuria in northern Norway: a molecular and genealogical study.Distribution and Severity of Neuropathology in β-Mannosidase-Deficient Mice is Strain Dependent.Lysosomal aspartylglucosaminidase is processed to the active subunit complex in the endoplasmic reticulumN-acetylglucosamine: production and applicationsSpectrum of mutations in alpha-mannosidosis.Investigating the interaction of saposin C with POPS and POPC phospholipids: a solid-state NMR spectroscopic study.Crystal structure of glycosylasparaginase from Flavobacterium meningosepticum.Lipopolysaccharide-induced inflammation or unilateral ureteral obstruction yielded multiple types of glycosylated Lipocalin 2Integrated regulatory responses of fimB to N-acetylneuraminic (sialic) acid and GlcNAc in Escherichia coli K-12.Intracellular transport of human lysosomal alpha-mannosidase and alpha-mannosidosis-related mutants.Protein signatures of molecular pathways in non-small cell lung carcinoma (NSCLC): comparison of glycoproteomics and global proteomics.Characterization of three alleles causing aspartylglycosaminuria: two from a British family and one from an American patient.Substrate specificity of the bovine and feline neutral alpha-mannosidasesComparison of liver glycosylasparaginases from six vertebrates.Possible role of α-mannosidase and β-galactosidase in larynx cancer.Keratan sulfate degradationLysosomal oligosaccharide catabolismCrystal structure of a mutant glycosylasparaginase shedding light on aspartylglycosaminuria-causing mechanism as well as on hydrolysis of non-chitobiose substrate.
P2860
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P2860
description
1989 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
artículu científicu espublizáu en 1989
@ast
scientific journal article
@en
vedecký článok (publikovaný 1989/12/01)
@sk
vědecký článek publikovaný v roce 1989
@cs
wetenschappelijk artikel (gepubliceerd op 1989/12/01)
@nl
wissenschaftlicher Artikel
@de
наукова стаття, опублікована в грудні 1989
@uk
مقالة علمية (نشرت في ديسمبر 1989)
@ar
name
Lysosomal degradation of Asn-linked glycoproteins
@ast
Lysosomal degradation of Asn-linked glycoproteins
@en
Lysosomal degradation of Asn-linked glycoproteins
@nl
type
label
Lysosomal degradation of Asn-linked glycoproteins
@ast
Lysosomal degradation of Asn-linked glycoproteins
@en
Lysosomal degradation of Asn-linked glycoproteins
@nl
prefLabel
Lysosomal degradation of Asn-linked glycoproteins
@ast
Lysosomal degradation of Asn-linked glycoproteins
@en
Lysosomal degradation of Asn-linked glycoproteins
@nl
P1433
P1476
Lysosomal degradation of Asn-linked glycoproteins
@en
P2093
M. J. Kuranda
N. N. Aronson
P304
P407
P577
1989-12-01T00:00:00Z