Increased ATPase activity produced by mutations at arginine-1380 in nucleotide-binding domain 2 of ABCC8 causes neonatal diabetes

Proceedings of the National Academy of Sciences of the United States of America

Volumn 104, Issue 48, 2007, Pages 18988-18992

  De Wet, Heidi ^a   Rees, Mathew G ^a   Shimomura, Kenju ^a   Aittoniemi, Jussi ^a,b   Patch, Ann Marie ^c   Flanagan, Sarah E ^c   Ellard, Sian ^c   Hattersley, Andrew T ^c   Sansom, Mark S P ^b   Ashcroft, Frances M ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

^b UNIVERSITY OF OXFORD   (United Kingdom)

^c PENINSULA MEDICAL SCHOOL   (United Kingdom)

Author keywords

ATP hydrolysis; KATP channel; Sulfonylurea receptor; SUR1

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ADENOSINE TRIPHOSPHATE; ARGININE; ARGININE 1380; PROTEIN ABCC8; SULFONYLUREA RECEPTOR 1; UNCLASSIFIED DRUG;

ARTICLE; CONTROLLED STUDY; DIABETES MELLITUS; GENE MUTATION; GENETIC ANALYSIS; HYDROLYSIS; NONHUMAN; NUCLEOTIDE SEQUENCE; PANCREAS ISLET BETA CELL; PRIORITY JOURNAL; RAT;

ADENOSINE DIPHOSPHATE; ADENOSINE TRIPHOSPHATE; AMINO ACID SUBSTITUTION; ARGININE; ATP-BINDING CASSETTE TRANSPORTERS; BERYLLIUM; BINDING SITES; DIABETES MELLITUS, TYPE 1; FLUORIDES; HUMANS; HYDROLYSIS; INFANT, NEWBORN; INSULIN; ION CHANNEL GATING; KINETICS; MODELS, MOLECULAR; MUTATION, MISSENSE; POINT MUTATION; POTASSIUM; POTASSIUM CHANNELS; POTASSIUM CHANNELS, INWARDLY RECTIFYING; PROTEIN STRUCTURE, TERTIARY; RECEPTORS, DRUG; STRUCTURE-ACTIVITY RELATIONSHIP;

EID: 37649007432     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0707428104     Document Type: Article

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