Abstract：
:Quinone reductase 2 has been discovered in 1961 and rediscovered in 1997. Because of its sequence homology with quinone reductase 1, it has been suspected to detoxify quinones. Ten years later, evidences begin to point to a versatile role of this enzyme. Indeed, QR2 is strongly suspected to be the molecular target of anti-malarian drugs such as chloroquin or paraquine, and of red wine-derived resveratrol that might be responsible for the so-called French paradox. It also is identical to the melatonin binding site MT3, and might therefore be a rationale explanation for the antioxidant role of melatonin. Finally QR2 might be implicated in the toxicity, in vivo, of quinones such as menadione. The present commentary attempts to summarize this information and discusses a series of hypotheses.
journal_name
Biochem Pharmacoljournal_title
Biochemical pharmacologyauthors
Vella F,Ferry G,Delagrange P,Boutin JAdoi
10.1016/j.bcp.2005.09.019subject
Has Abstractpub_date
2005-12-19 00:00:00pages
1-12issue
1-2eissn
0006-2952issn
1873-2968pii
S0006-2952(05)00591-5journal_volume
71pub_type
杂志文章,评审abstract：:Tumor-induced neoangiogenesis is an essential event for solid tumor growth. Therefore, a compound able to block angiogenesis-promoting factors could have antitumor activity. The polysulfonated naphthylurea suramin is hypothesized to have this mode of action. A series of sulfonated distamycin A derivatives have been sy...
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pub_type： 杂志文章
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pub_type： 杂志文章
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journal_title：Biochemical pharmacology
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journal_title：Biochemical pharmacology
pub_type： 杂志文章
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journal_title：Biochemical pharmacology
pub_type： 杂志文章
doi：10.1016/j.bcp.2014.05.001
更新日期：2014-07-15 00:00:00
