Disulfide bonds are critical for tissue-nonspecific alkaline phosphatase function revealed by analysis of mutant proteins bearing a C 201-Y or C 489-S substitution associated with severe hypophosphatasia

Biochimica et Biophysica Acta - Molecular Basis of Disease

Volumn 1822, Issue 4, 2012, Pages 581-588

  Satou, Yasuhito ^a   Al Shawafi, Hiba A ^a   Sultana, Sara ^a   Makita, Saori ^a   Sohda, Miwa ^a   Oda, Kimimitsu ^a  

^a NIIGATA UNIVERSITY GRADUATE SCHOOL OF MEDICAL AND DENTAL SCIENCES   (Japan)

Author keywords

Degradation; Disulfide bond; Hypophosphatasia; Proteasome; Tissue nonspecific alkaline phosphatase; Ubiquitination

Indexed keywords

ALKALINE PHOSPHATASE; MONOMER; MUTANT PROTEIN; N ACETYL BETA GLUCOSAMINIDASE; PROTEASOME;

ALKALINE PHOSPHATASE BLOOD LEVEL; ANIMAL CELL; ARTICLE; CONTROLLED STUDY; DISULFIDE BOND; ENDOPLASMIC RETICULUM ASSOCIATED DEGRADATION; ENZYME ACTIVITY; HYPOPHOSPHATASIA; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN ASSEMBLY; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN FOLDING; UBIQUITINATION;

ALKALINE PHOSPHATASE; ANIMALS; BLOTTING, WESTERN; CERCOPITHECUS AETHIOPS; COS CELLS; DISULFIDES; HUMANS; HYPOPHOSPHATASIA; MUTATION; UBIQUITINATION;

EID: 84856485352     PISSN: 09254439     EISSN: 1879260X     Source Type: Journal    
DOI: 10.1016/j.bbadis.2012.01.007     Document Type: Article

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