CYP24A1 mutations in idiopathic infantile hypercalcemia

New England Journal of Medicine

Volumn 365, Issue 18, 2011, Pages 1741-1743

  Ji, Hong Fang ^a   Shen, Liang ^a  

^a SHANDONG UNIVERSITY OF TECHNOLOGY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

CALCITRIOL; HEME; OXYGENASE; STEROID 24 HYDROXYLASE; UNCLASSIFIED DRUG; STEROID MONOOXYGENASE; VITAMIN D;

CATABOLISM; CYP24A1 GENE; ENZYME BINDING; GENE; GENE FUNCTION; HUMAN; HYDROGEN BOND; HYPERCALCEMIA; IDIOPATHIC INFANTILE HYPERCALCEMIA; LETTER; MISSENSE MUTATION; PATHOPHYSIOLOGY; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN INTERACTION; ANIMAL; FEMALE; GENETICS; MALE; MUTATION; NOTE;

ANIMALS; FEMALE; HUMANS; HYPERCALCEMIA; MALE; MUTATION; STEROID HYDROXYLASES; VITAMIN D;

EID: 80455173535     PISSN: 00284793     EISSN: 15334406     Source Type: Journal    
DOI: 10.1056/NEJMc1110226     Document Type: Letter

References (5)

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5. Annalora AJ, Goodin DB, Hong WX, Zhang Q, Johnson EF, Stout CD. Crystal structure of CYP24A1, a mitochondrial cytochrome P450 involved in vitamin D metabolism. J Mol Biol 2010;396:441-51.