Structures of nitric oxide synthase isoforms complexed with the inhibitor AR-R17477 suggest a rational basis for specificity and inhibitor design

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

Volumn 101, Issue 16, 2004, Pages 5892-5897

  Fedorov, Roman ^a,b   Vasan, Ryan ^c   Ghosh, Dipak K ^c   Schlichting, Ilme ^a,b  

^a MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

^b MAX PLANCK INSTITUTE FOR MEDICAL RESEARCH   (Germany)

^c DUKE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AR R 17477; ENZYME INHIBITOR; INDUCIBLE NITRIC OXIDE SYNTHASE; NITRIC OXIDE SYNTHASE; UNCLASSIFIED DRUG;

ARTICLE; CHEMICAL ANALYSIS; COMPLEX FORMATION; CONTROLLED STUDY; CRYSTAL STRUCTURE; ENZYME ACTIVITY; ENZYME ANALYSIS; ENZYME CONFORMATION; ENZYME INHIBITION; ENZYME SPECIFICITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; HUMAN; MOLECULAR INTERACTION; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN DOMAIN; PROTEIN MOTIF; RAT; SITE DIRECTED MUTAGENESIS;

AMIDINES; ANIMALS; DRUG DESIGN; ENZYME INHIBITORS; HUMANS; ISOENZYMES; MICE; MODELS, MOLECULAR; MUTAGENESIS, SITE-DIRECTED; NITRIC OXIDE SYNTHASE; RATS; THIOPHENES;

EID: 1942469472     PISSN: 00278424     EISSN: None     Source Type: Journal    
DOI: 10.1073/pnas.0306588101     Document Type: Article

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