Aspartylglycosaminuria: a review - Test2 - elhamkhani - TriplyDB

Aspartylglycosaminuria: a review

Aspartylglycosaminuria: a review

http://www.wikidata.org/entity/Q28077247

about

Biochemical characterization and comparison of aspartylglucosaminidases secreted in venom of the parasitoid wasps Asobara tabida and Leptopilina heterotoma.

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Aspartylglycosaminuria: a review

http://www.wikidata.org/entity/Q28077247

description

2016 nî lūn-bûn

@nan

2016 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2016 թվականի դեկտեմբերին հրատարակված գիտական հոդված

@hy

2016年の論文

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2016年論文

@yue

2016年論文

@zh-hant

2016年論文

@zh-hk

2016年論文

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2016年論文

@zh-tw

2016年论文

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name

Aspartylglycosaminuria: a review

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Aspartylglycosaminuria: a review

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Aspartylglycosaminuria: a review

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type

label

Aspartylglycosaminuria: a review

@ast

Aspartylglycosaminuria: a review

@en

Aspartylglycosaminuria: a review

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prefLabel

Aspartylglycosaminuria: a review

@ast

Aspartylglycosaminuria: a review

@en

Aspartylglycosaminuria: a review

@nl

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Orphanet Journal of Rare Diseases

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Aspartylglycosaminuria: a review

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Ilkka Mononen

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Creative Commons Attribution 4.0 International

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Characterization of the mutation responsible for aspartylglucosaminuria in three Finnish patients. Amino acid substitution Cys163----Ser abolishes the activity of lysosomal glycosylasparaginase and its conversion into subunits

Aspartylglucosaminuria: cDNA encoding human aspartylglucosaminidase and the missense mutation causing the disease

Aspartylglycosaminuria in the Finnish population: identification of two point mutations in the heavy chain of glycoasparaginase

Aspartylglycosaminuria: protein chemistry and molecular biology of the most common lysosomal storage disorder of glycoprotein degradation

A protein catalytic framework with an N-terminal nucleophile is capable of self-activation

High prevalence of aspartylglycosaminuria among school-age children in eastern Finland

Cloning and sequence analysis of a cDNA for human glycosylasparaginase. A single gene encodes the subunits of this lysosomal amidase

Localization of the disulfide bond involved in post-translational processing of glycosylasparaginase and disrupted by a mutation in the Finnish-type aspartylglycosaminuria

Enzyme replacement therapy in a mouse model of aspartylglycosaminuria

Substrate specificity and reaction mechanism of human glycoasparaginase. The N-glycosidic linkage of various glycoasparagines is cleaved through a reaction mechanism similar to L-asparaginase.

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aspartylglucosaminuria

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