キサンチンオキシダーゼ (Japanese Wikipedia)

Analysis of information sources in references of the Wikipedia article "キサンチンオキシダーゼ" in Japanese language version.

refsWebsite

Global rank Japanese rank

11nih.gov

4^th place

24^th place

9doi.org

2^nd place

6^th place

1rcsb.org

8,838^th place

low place

1pnas.org

1,293^rd place

1,250^th place

1243sageru.com

low place

1nikkeibp.co.jp

1,415^th place

95^th place

243sageru.com

https://243sageru.com/toranomaki/purine/2_1/index.html

doi.org

PDB: 1FIQ; Enroth C, Eger BT, Okamoto K, Nishino T, Nishino T, Pai EF (September 2000). “Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion”. Proc. Natl. Acad. Sci. U.S.A. 97 (20): 10723–8. doi:10.1073/pnas.97.20.10723. PMC 27090. PMID 11005854.
Ardan T, Kovaceva J, Cejková J (2004). “Comparative histochemical and immunohistochemical study on xanthine oxidoreductase/xanthine oxidase in mammalian corneal epithelium”. Acta Histochem 106 (1): 69–75. doi:10.1016/j.acthis.2003.08.001. PMID 15032331.
Hille R (2005). “Molybdenum-containing hydroxylases”. Arch. Biochem. Biophys. 433 (1): 107–16. doi:10.1016/j.abb.2004.08.012. PMID 15581570.
Harrison R (2002). “Structure and function of xanthine oxidoreductase: where are we now?”. Free Radic. Biol. Med. 33 (6): 774–97. doi:10.1016/S0891-5849(02)00956-5. PMID 12208366.
Hille R. (2006). “Structure and Function of Xanthine Oxidoreductase”. European Journal of Inorganic Chemistry 2006 (10): 1905–2095. doi:10.1002/ejic.200600087.
Metz S, Thiel W. (2009). “A Combined QM/MM Study on the Reductive Half-Reaction of Xanthine Oxidase: Substrate Orientation and Mechanism”. Journal of the American Chemical Society 131 (41): 14885–158902. doi:10.1021/ja9045394. PMID 19788181.
Pacher P, Nivorozhkin A, Szabó C (March 2006). “Therapeutic effects of xanthine oxidase inhibitors: renaissance half a century after the discovery of allopurinol”. Pharmacol. Rev. 58 (1): 87–114. doi:10.1124/pr.58.1.6. PMC 2233605. PMID 16507884.
Spector T (January 1988). “Oxypurinol as an inhibitor of xanthine oxidase-catalyzed production of superoxide radical”. Biochem. Pharmacol. 37 (2): 349–52. doi:10.1016/0006-2952(88)90739-3. PMID 2829916.
Muraoka S, Miura T (February 2004). “Inhibition of xanthine oxidase by phytic acid and its antioxidative action”. Life Sci. 74 (13): 1691–700. doi:10.1016/j.lfs.2003.09.040. PMID 14738912.

nih.gov

pubmed.ncbi.nlm.nih.gov

PDB: 1FIQ; Enroth C, Eger BT, Okamoto K, Nishino T, Nishino T, Pai EF (September 2000). “Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion”. Proc. Natl. Acad. Sci. U.S.A. 97 (20): 10723–8. doi:10.1073/pnas.97.20.10723. PMC 27090. PMID 11005854.
Ardan T, Kovaceva J, Cejková J (2004). “Comparative histochemical and immunohistochemical study on xanthine oxidoreductase/xanthine oxidase in mammalian corneal epithelium”. Acta Histochem 106 (1): 69–75. doi:10.1016/j.acthis.2003.08.001. PMID 15032331.
Hille R (2005). “Molybdenum-containing hydroxylases”. Arch. Biochem. Biophys. 433 (1): 107–16. doi:10.1016/j.abb.2004.08.012. PMID 15581570.
Harrison R (2002). “Structure and function of xanthine oxidoreductase: where are we now?”. Free Radic. Biol. Med. 33 (6): 774–97. doi:10.1016/S0891-5849(02)00956-5. PMID 12208366.
Metz S, Thiel W. (2009). “A Combined QM/MM Study on the Reductive Half-Reaction of Xanthine Oxidase: Substrate Orientation and Mechanism”. Journal of the American Chemical Society 131 (41): 14885–158902. doi:10.1021/ja9045394. PMID 19788181.
Pacher P, Nivorozhkin A, Szabó C (March 2006). “Therapeutic effects of xanthine oxidase inhibitors: renaissance half a century after the discovery of allopurinol”. Pharmacol. Rev. 58 (1): 87–114. doi:10.1124/pr.58.1.6. PMC 2233605. PMID 16507884.
Spector T (January 1988). “Oxypurinol as an inhibitor of xanthine oxidase-catalyzed production of superoxide radical”. Biochem. Pharmacol. 37 (2): 349–52. doi:10.1016/0006-2952(88)90739-3. PMID 2829916.
Muraoka S, Miura T (February 2004). “Inhibition of xanthine oxidase by phytic acid and its antioxidative action”. Life Sci. 74 (13): 1691–700. doi:10.1016/j.lfs.2003.09.040. PMID 14738912.

ncbi.nlm.nih.gov

PDB: 1FIQ; Enroth C, Eger BT, Okamoto K, Nishino T, Nishino T, Pai EF (September 2000). “Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion”. Proc. Natl. Acad. Sci. U.S.A. 97 (20): 10723–8. doi:10.1073/pnas.97.20.10723. PMC 27090. PMID 11005854.
“Entrez Gene: XDH xanthine dehydrogenase”. 2008年12月19日閲覧。
Pacher P, Nivorozhkin A, Szabó C (March 2006). “Therapeutic effects of xanthine oxidase inhibitors: renaissance half a century after the discovery of allopurinol”. Pharmacol. Rev. 58 (1): 87–114. doi:10.1124/pr.58.1.6. PMC 2233605. PMID 16507884.

nikkeibp.co.jp

medical.nikkeibp.co.jp

https://medical.nikkeibp.co.jp/leaf/all/series/drug/update/201308/531906.html

pnas.org

PDB: 1FIQ; Enroth C, Eger BT, Okamoto K, Nishino T, Nishino T, Pai EF (September 2000). “Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion”. Proc. Natl. Acad. Sci. U.S.A. 97 (20): 10723–8. doi:10.1073/pnas.97.20.10723. PMC 27090. PMID 11005854.

rcsb.org

PDB: 1FIQ; Enroth C, Eger BT, Okamoto K, Nishino T, Nishino T, Pai EF (September 2000). “Crystal structures of bovine milk xanthine dehydrogenase and xanthine oxidase: structure-based mechanism of conversion”. Proc. Natl. Acad. Sci. U.S.A. 97 (20): 10723–8. doi:10.1073/pnas.97.20.10723. PMC 27090. PMID 11005854.