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xanthosine 5 monophosphate/neoplasms
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5 results
Crystal structure of human type II inosine monophosphate dehydrogenase: implications for ligand binding and drug design.
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Inosine monophosphate dehydrogenase (IMPDH) controls a key metabolic step in the regulation of cell growth and differentiation. This step is the NAD-dependent oxidation of inosine 5' monophosphate (IMP) to xanthosine 5' monophosphate, the rate-limiting step in the synthesis of the guanine
Mechanism-based design of inosine 5-monophosphate dehydrogenase inhibitors: synthesis and biological activities of 5-ethynyl-1-beta-D-ribofuranosylimidazole-4-carboxamide (EICAR) and its derivatives.
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Inosine 5 -monophosphate dehydrogenase (IMPDH) catalyzes the nicotinamide adenine dinucleotide (NAD)-dependent oxidation of inosine 5 -monophosphate (IMP) to xanthosine 5 -monophosphate (XMP), and is one of the key rate-determining enzymes of de novo guanine nucleotide biosynthesis in mammalian
IMP dehydrogenase : structural aspects of inhibitor binding.
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Inosine monophosphate dehydrogenase (IMPDH, E.C. 1.1.1.205) is recognized as an important target for both antileukemic and immunosuppressive therapy. IMPDH catalyzes the NAD-dependent oxidation of inosine 5 monophosphate (IMP) to xanthosine 5 monophosphate. Several classes of IMPDH inhibitors are
Bacillus anthracis inosine 5'-monophosphate dehydrogenase in action: the first bacterial series of structures of phosphate ion-, substrate-, and product-bound complexes.
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Inosine 5'-monophosphate dehydrogenase (IMPDH) catalyzes the first unique step of the GMP branch of the purine nucleotide biosynthetic pathway. This enzyme is found in organisms of all three kingdoms. IMPDH inhibitors have broad clinical applications in cancer treatment, as antiviral drugs and as
Nucleoside and non-nucleoside IMP dehydrogenase inhibitors as antitumor and antiviral agents.
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IMP dehydrogenase (IMPDH) is an enzyme which catalyzes the NAD-dependent conversion of inosine 5 -monophosphate (IMP) to xanthosine 5 -monophosphate (XMP) at the metabolic branch point in the de novo purine nucleotide synthetic pathway. IMPDH was shown to be increased significantly in cancer cells
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