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Crystal structure of human type II inosine monophosphate dehydrogenase: implications for ligand binding and drug design.
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' monophosphateExpand
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Computational studies of nonbonded sulfur-oxygen and selenium-oxygen interactions in the thiazole and selenazole nucleosides
Computational studies have been performed to investigate the origin and magnitude of a biologically important nonbonded interaction: the sulfur-oxygen and selenium-oxygen interaction observed in theExpand
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Crystal structure and amide H/D exchange of binary complexes of alcohol dehydrogenase from Bacillus stearothermophilus: insight into thermostability and cofactor binding.
The crystal structure of NAD(+)-dependent alcohol dehydrogenase from Bacillus stearothermophilus strain LLD-R (htADH) was determined using X-ray diffraction data at a resolution of 2.35 A. TheExpand
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Analogues of platelet activating factor. 4. Some modifications of the phosphocholine moiety.
Racemic analogues of platelet activating factor (PAF) in which the methylene bridge separating the phosphate and trimethylammonium moieties is altered in length (7a-f) have been prepared. IncreasingExpand
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Synthesis of 3-deazaneplanocin A, a powerful inhibitor of S-adenosylhomocysteine hydrolase with potent and selective in vitro and in vivo antiviral activities.
The neplanocin A analogue 3-deazaneplanocin A (2b) has been synthesized. A direct SN2 displacement on the cyclopentenyl mesylate 3 by the sodium salt of 6-chloro-3-deazapurine afforded the desiredExpand
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Cofactor mimics as selective inhibitors of NAD-dependent inosine monophosphate dehydrogenase (IMPDH)--the major therapeutic target.
IMP dehydrogenase, the key enzyme in de novo synthesis of purine nucleotides, is an important therapeutic target. Three inhibitors of IMP dehydrogenase reached the market; ribavirin (Rebetol) aExpand
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IMP dehydrogenase : structural aspects of inhibitor binding.
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 ofExpand
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A database study of nonbonded intramolecular sulfur-nucleophile contacts.
A search of the Cambridge Structural Database (1991, version 4.5) was performed to investigate nonbonded intramolecular 1,4 S...O close contacts of the kind seen in the thiazole nucleoside tiazofurinExpand
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Carboxamide group conformation in the nicotinamide and thiazole-4-carboxamide rings: implications for enzyme binding.
  • H. Li, B. Goldstein
  • Chemistry, Medicine
  • Journal of medicinal chemistry
  • 18 September 1992
Ab initio computations (RHF/6-31G* parallel 3-21G*) were performed on the thiazole-4-carboxamide group found in the antitumor drug tiazofurin and its dehydrogenase-binding anaboliteExpand
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A link between protein structure and enzyme catalyzed hydrogen tunneling.
We present evidence that the size of an active site side chain may modulate the degree of hydrogen tunneling in an enzyme-catalyzed reaction. Primary and secondary kH/kT and kD/kT kinetic isotopeExpand
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