Mechanistic insights into xanthine oxidoreductase from development studies of candidate drugs to treat hyperuricemia and gout

Verfasser / Beitragende:
[Takeshi Nishino, Ken Okamoto]
Ort, Verlag, Jahr:
2015
Enthalten in:
JBIC Journal of Biological Inorganic Chemistry, 20/2(2015-03-01), 195-207
Format:
Artikel (online)
ID: 605507864
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024 7 0 |a 10.1007/s00775-014-1210-x  |2 doi 
035 |a (NATIONALLICENCE)springer-10.1007/s00775-014-1210-x 
245 0 0 |a Mechanistic insights into xanthine oxidoreductase from development studies of candidate drugs to treat hyperuricemia and gout  |h [Elektronische Daten]  |c [Takeshi Nishino, Ken Okamoto] 
520 3 |a Xanthine oxidoreductase (XOR), which is widely distributed from humans to bacteria, has a key role in purine catabolism, catalyzing two steps of sequential hydroxylation from hypoxanthine to xanthine and from xanthine to urate at its molybdenum cofactor (Moco). Human XOR is considered to be a target of drugs not only for therapy of hyperuricemia and gout, but also potentially for a wide variety of other diseases. In this review, we focus on studies of XOR inhibitors and their implications for understanding the chemical nature and reaction mechanism of the Moco active site of XOR. We also discuss further experimental or clinical studies that would be helpful to clarify remaining issues. 
540 |a The Author(s), 2014 
690 7 |a Xanthine oxidase  |2 nationallicence 
690 7 |a Uric acid  |2 nationallicence 
690 7 |a Allopurinol  |2 nationallicence 
690 7 |a Febuxostat  |2 nationallicence 
690 7 |a Gout  |2 nationallicence 
700 1 |a Nishino  |D Takeshi  |u Department of Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5 Sendagi, Bunkyou-ku, 113-8602, Tokyo, Japan  |4 aut 
700 1 |a Okamoto  |D Ken  |u Department of Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5 Sendagi, Bunkyou-ku, 113-8602, Tokyo, Japan  |4 aut 
773 0 |t JBIC Journal of Biological Inorganic Chemistry  |d Springer Berlin Heidelberg  |g 20/2(2015-03-01), 195-207  |x 0949-8257  |q 20:2<195  |1 2015  |2 20  |o 775 
856 4 0 |u https://doi.org/10.1007/s00775-014-1210-x  |q text/html  |z Onlinezugriff via DOI 
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900 7 |a Metadata rights reserved  |b Springer special CC-BY-NC licence  |2 nationallicence 
908 |D 1  |a review-article  |2 jats 
949 |B NATIONALLICENCE  |F NATIONALLICENCE  |b NL-springer 
950 |B NATIONALLICENCE  |P 856  |E 40  |u https://doi.org/10.1007/s00775-014-1210-x  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Nishino  |D Takeshi  |u Department of Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5 Sendagi, Bunkyou-ku, 113-8602, Tokyo, Japan  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Okamoto  |D Ken  |u Department of Biochemistry and Molecular Biology, Nippon Medical School, 1-1-5 Sendagi, Bunkyou-ku, 113-8602, Tokyo, Japan  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t JBIC Journal of Biological Inorganic Chemistry  |d Springer Berlin Heidelberg  |g 20/2(2015-03-01), 195-207  |x 0949-8257  |q 20:2<195  |1 2015  |2 20  |o 775