Associated Papers
N-linked glycosylation plays an essential role in the stability and function of tissue-nonspecific alkaline phosphatase.
Atanasova D et al.
The Journal of Biological Chemistry, 2025
The structural pathology for hypophosphatasia caused by malfunctional tissue non-specific alkaline phosphatase.
Yu Y et al.
Nature Communications, 2023
37422472 (PubMed )
Supplement: 41467_2023_39833_MOESM1_ESM.pdf
Large-scale in vitro functional testing and novel variant scoring via protein modeling provide insights into alkaline phosphatase activity in hypophosphatasia.
Del Angel G et al.
Human Mutation, 2020
32160374 (PubMed )
Supplement: HUMU-41-1250-s002.xlsx › Supplemental_table_2
Hypophosphatasia in Japan: ALPL Mutation Analysis in 98 Unrelated Patients.
Michigami T et al.
Calcified Tissue International, 2020
iFish: predicting the pathogenicity of human nonsynonymous variants using gene-specific/family-specific attributes and classifiers.
Wang M et al.
Scientific Reports, 2016
27527004 (PubMed )
Supplement: srep31321-s3.xls › NovelVar
Glycosylation-deficient mutations in tissue-nonspecific alkaline phosphatase impair its structure and function and are linked to infantile hypophosphatasia.
Komaru K et al.
The Febs Journal, 2016
Hypophosphatasia: validation and expansion of the clinical nosology for children from 25 years experience with 173 pediatric patients.
Whyte MP et al.
Bone, 2015
[Molecular basis of hypophosphatasia].
Oda K
Seikagaku. the Journal of Japanese Biochemical Society, 2008
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