Article
A dimerization defect caused by a glycine substitution at position 420 by serine in tissue-nonspecific alkaline phosphatase associated with perinatal hypophosphatasia.
The FEBS journal - 1 Dec 2012
Makita Saori, Al-Shawafi Hiba A, Sultana Sara, Sohda Miwa, Nomura Shuichi, Oda Kimimitsu
Abstract excerpt
Mutations in the tissue-nonspecific alkaline phosphatase (TNSALP) gene cause hypophosphatasia (HPP), an inborn error of metabolism characterized by defects in bone and teeth mineralization accompanying subnormal levels of serum alkaline phosphatase activity. Missense mutations at position 420 of TNSALP (standard nomenclature), which convert glycine to serine [TNSALP (G420S)] or alanine [TNSALP (G420A)], have been...
Read the complete abstract on PubMedTopics
Share this publication in a Topic to start or enrich a Post.