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IMP Dehydrogenase

Known as: Dehydrogenase, IMP, Dehydrogenase, Inosine-5-Monophosphate, Inosinic Acid Dehydrogenase 
An enzyme that catalyzes the dehydrogenation of inosine 5'-phosphate to xanthosine 5'-phosphate in the presence of NAD. EC 1.1.1.205.
National Institutes of Health

Papers overview

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Highly Cited
2005
Highly Cited
2005
It is not yet clear to what extent depletion of intracellular GTP pools contributes to the antiviral activity of ribavirin… Expand
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Highly Cited
2003
Highly Cited
2003
The recent development of in vitro hepatitis C virus (HCV) RNA replication systems has provided useful tools for studying the… Expand
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2003
2003
IMP dehydrogenase (IMPDH) catalyzes the rate-limiting step in the de novo synthesis of GTP. Yeast with mutations in the… Expand
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Highly Cited
2000
Highly Cited
2000
The enzyme IMP dehydrogenase (IMPDH) catalyzes an essential step in the de novo biosynthesis of guanine nucleotides, namely, the… Expand
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Review
1999
Review
1999
Inosine 5 -monophosphate dehydrogenase (IMPDH) is a rate-limiting enzyme for the synthesis of GTP and dGTP. Two isoforms of IMPDH… Expand
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Highly Cited
1997
Highly Cited
1997
An IMP dehydrogenase gene was isolated from Candida albicans on a approximately 2.9-kb XbaI genomic DNA fragment. The putative… Expand
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Highly Cited
1996
Highly Cited
1996
The structure of inosine-5'-monophosphate dehydrogenase (IMPDH) in complex with IMP and mycophenolic acid (MPA) has been… Expand
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Highly Cited
1993
Highly Cited
1993
Human IMP dehydrogenase, a target for anticancer and immunosuppressive chemotherapy, exists as two isoforms, types I and II… Expand
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Highly Cited
1992
Highly Cited
1992
Human IMP dehydrogenase (IMPDH; EC 1.1.1.205) was recently found to consist of two molecular species (types I and II) with high… Expand
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Highly Cited
1990
Highly Cited
1990
IMP dehydrogenase (EC 1.1.1.205), the rate-limiting enzyme of de novo GTP biosynthesis, is a promising target in antileukemic… Expand
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