Cited by 13Biochemical and Molecular ResearchGout, Hyperuricemia, Uric AcidEnzyme Structure and Function

Xanthine oxidoreductase: dehydrogenase to oxidase conversion

RYAN, MATTHEW G., BALENDRAN, ANUDHARAN, HARRISON, ROGER, WOLSTENHOLME, ADRIAN, BULKLEY, GREGORY B.·1997·Biochemical Society Transactions

Abstract

Conference Article| August 01 1997 Xanthine oxidoreductase: dehydrogenase to oxidase conversion MATTHEW G. RYAN; MATTHEW G. RYAN 1School of Biology and Biochemistry, University of Bath, Bath, BA2 7AY, UK Search for other works by this author on: This Site PubMed Google Scholar ANUDHARAN BALENDRAN; ANUDHARAN BALENDRAN 1School of Biology and Biochemistry, University of Bath, Bath, BA2 7AY, UK Search for other works by this author on: This Site PubMed Google Scholar ROGER HARRISON; ROGER HARRISON 1School of Biology and Biochemistry, University of Bath, Bath, BA2 7AY, UK Search for other works by this author on: This Site PubMed Google Scholar ADRIAN WOLSTENHOLME; ADRIAN WOLSTENHOLME 1School of Biology and Biochemistry, University of Bath, Bath, BA2 7AY, UK Search for other works by this author on: This Site PubMed Google Scholar GREGORY B. BULKLEY GREGORY B. BULKLEY *Johns Hopkins University, School of Medicine, 600 N. Wolfe St., Baltimore, Md 21287-3654, USA Search for other works by this author on: This Site PubMed Google Scholar Biochem Soc Trans (1997) 25 (3): 530S. https://doi.org/10.1042/bst025530s Views Icon Views Article contents Figures & tables Video Audio Supplementary Data Peer Review Share Icon Share Twitter LinkedIn Cite Icon Cite Get Permissions Citation MATTHEW G. RYAN, ANUDHARAN BALENDRAN, ROGER HARRISON, ADRIAN WOLSTENHOLME, GREGORY B. BULKLEY; Xanthine oxidoreductase: dehydrogenase to oxidase conversion. Biochem Soc Trans 1 August 1997; 25 (3): 530S. doi: https://doi.org/10.1042/bst025530s Download citation file: Ris (Zotero) Reference Manager EasyBib Bookends Mendeley Papers EndNote RefWorks BibTex toolbar search Search Dropdown Menu toolbar search search input Search input auto suggest filter your search All ContentAll JournalsBiochemical Society Transactions Search Advanced Search This content is only available as a PDF. © 1997 Biochemical Society1997 Article PDF first page preview Close Modal You do not currently have access to this content.

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Crossref · 10.1042/bst025530s

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  • Through these signaling mechanisms, nitrated lipids mediate a number of physiological effects in animal models including attenuation of inflammatory bowel disease, protection after ischemia/reperfusion, decreases in atherosclerosis, and reversal of obesity-induced pulmonary hypertension.

    “Through these signaling mechanisms, nitrated lipids mediate a number of physiological effects in animal models including attenuation of inflammatory bowel disease (113), protection after ischemia/reperfusion (683, 801), decreases in atherosclerosis (800), and reversal of obesity-induced pulmonary hypertension (495).”

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Authors
RYAN, M. G., BALENDRAN, A., HARRISON, R., WOLSTENHOLME, A., & BULKLEY, G. B.
Affiliations
  • University of Bath (GB)
  • Johns Hopkins University (US)
Venue
Biochemical Society Transactions
Published
1997-08-01
Volume
25
Issue
3
Pages
530S-530S
ISSN
  • 0300-5127 (ISSN-L)
  • 1470-8752
OpenAlex
W2346986920
Cited by
13
References
0
Citations by year
2025: 1 · 2023: 1 · 2022: 1 · 2020: 1 · 2018: 1 · 2017: 1 · 2014: 2 · 2012: 1
FWCI
0.12
Type
journal article
Language
en
Open access
closed
Locations
  • Biochemical Society Transactions (publishedVersion)
  • PubMed (publishedVersion)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Biochemical and Molecular Research
  • Health Sciences › Medicine › Nephrology › Gout, Hyperuricemia, Uric Acid
  • Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
Keywords
xanthine oxidoreductase, xanthine dehydrogenase, xanthine oxidase, enzyme kinetics, substrate specificity, purine metabolism, xanthine, hypoxanthine, uric acid, NAD+, flavin cofactor, FAD, FADH2
MeSH terms
Alanine, Animals, Cloning, Molecular, Liver, Peptide Fragments, Recombinant Proteins, Threonine, Trypsin, Xanthine Dehydrogenase, Xanthine Oxidase, Reperfusion Injury, Mutagenesis, Site-Directed, Amino Acid Substitution, Rats

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