Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease
about
Human aspartylglucosaminidase. A biochemical and immunocytochemical characterization of the enzyme in normal and aspartylglucosaminuria fibroblastsHuman leucocyte glycosylasparaginase is an alpha/beta-heterodimer of 19 kDa alpha-subunit and 17 and 18 kDa beta-subunitHuman leucocyte aspartylglucosaminidase. Evidence for two different subunits in a more complex native structureSeveral cooperating binding sites mediate the interaction of a lysosomal enzyme with phosphotransferaseIdentification of a common mutation in Finnish patients with nonketotic hyperglycinemiaTransglutaminase 1 mutations in autosomal recessive congenital ichthyosis: private and recurrent mutations in an isolated populationInitial insight into the function of the lysosomal 66.3 kDa protein from mouse by means of X-ray crystallographyAspartylglycosaminuria: a reviewCharacterization of the Niemann-Pick C pathway in alveolar type II cells and lamellar bodies of the lungIdentification of Small Molecule Compounds for Pharmacological Chaperone Therapy of AspartylglucosaminuriaA system for specific, high-throughput genotyping by allele-specific primer extension on microarrays.Aspartylglucosaminuria in northern Norway: a molecular and genealogical study.Lysosomal aspartylglucosaminidase is processed to the active subunit complex in the endoplasmic reticulumAssignment of a novel locus for autosomal recessive congenital ichthyosis to chromosome 19p13.1-p13.2.Finnish type of familial amyloidosis: cosegregation of Asp187----Asn mutation of gelsolin with the disease in three large families.Overgrowth of oral mucosa and facial skin, a novel feature of aspartylglucosaminuriaFunctional analyses of active site residues of human lysosomal aspartylglucosaminidase: implications for catalytic mechanism and autocatalytic activation.Structural Characterization of the Loop at the Alpha-Subunit C-Terminus of the Mixed Lineage Leukemia Protein Activating Protease Taspase1.Spectrum of mutations in aspartylglucosaminuria.Functional Analysis of the Ser149/Thr149 Variants of Human Aspartylglucosaminidase and Optimization of the Coding Sequence for Protein Production.Genetics in an isolated population like Finland: a different basis for genomic medicine?Characterization of three alleles causing aspartylglycosaminuria: two from a British family and one from an American patient.Comparison of liver glycosylasparaginases from six vertebrates.
P2860
Q24528082-4D70D4B4-11A1-476F-A0A2-C8BBEE4CAB0CQ24528875-27B51F4C-84E6-4BB7-9AD6-C3F87DB69CA0Q24529577-9C1840CC-1F76-465E-A026-005A5F989AABQ24532839-F5C791C7-A282-4D3C-ADC3-9D44C24CD553Q24564863-0B16BCE9-6478-465C-B8C2-4285959E77AFQ24678416-750BC22A-6FDA-407D-A049-CDAF2E4D9B64Q27657154-CE7BD131-1D1C-4016-A1AD-F26B61A8B044Q28077247-A1A5F7E5-94D7-4916-B97D-E47E97D1BBA4Q28384948-CA294846-31D0-4B1F-B6C1-800A2D7A4A96Q28820747-AE20C70E-04A0-479A-BEAE-6288C98AD6CAQ30651566-CDCF215D-5B8A-44C5-80FF-CF52DC73F0F1Q33674126-10CC1C12-B101-4BC4-8A61-2FDECAF6AA18Q34041841-2D0E54A7-4484-42A3-B24F-EB1583E5DD57Q34145298-EA16A963-1014-431F-B880-32B081C5FB9BQ35196805-50EBC673-513E-4390-9D73-758B0AE338CCQ35432381-10E9596E-17F9-44E3-B4E5-58610F0BA67BQ35851826-567A2C85-FF05-4DCC-92F6-2ED636E658F4Q35956482-CA4B6650-C39E-4E30-80ED-1CF9BFEDA44CQ37643452-64F31B8B-3716-4DE0-999D-E0A69A6158E6Q38874011-AF7EF06E-5F35-4589-BD83-821C634EF4B8Q39449815-4212D401-AA5D-4E0F-B92E-452218ED6AA9Q41565600-6F974CF5-05AC-47A6-844E-96F356F43377Q42793157-A9CE6648-E3C9-42E4-B20D-D773CE0B1CD3
P2860
Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease
description
1991 nî lūn-bûn
@nan
1991 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1991 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1991年の論文
@ja
1991年論文
@yue
1991年論文
@zh-hant
1991年論文
@zh-hk
1991年論文
@zh-mo
1991年論文
@zh-tw
1991年论文
@wuu
name
Aspartylglucosaminuria: cDNA e ...... e mutation causing the disease
@ast
Aspartylglucosaminuria: cDNA e ...... e mutation causing the disease
@en
Aspartylglucosaminuria: cDNA e ...... e mutation causing the disease
@nl
type
label
Aspartylglucosaminuria: cDNA e ...... e mutation causing the disease
@ast
Aspartylglucosaminuria: cDNA e ...... e mutation causing the disease
@en
Aspartylglucosaminuria: cDNA e ...... e mutation causing the disease
@nl
prefLabel
Aspartylglucosaminuria: cDNA e ...... e mutation causing the disease
@ast
Aspartylglucosaminuria: cDNA e ...... e mutation causing the disease
@en
Aspartylglucosaminuria: cDNA e ...... e mutation causing the disease
@nl
P2093
P2860
P1433
P1476
Aspartylglucosaminuria: cDNA e ...... e mutation causing the disease
@en
P2093
A C Syvänen
L Peltonen
P2860
P407
P577
1991-01-01T00:00:00Z