Paul Cook to Ascaris suum
This is a "connection" page, showing publications Paul Cook has written about Ascaris suum.
Connection Strength
2.735
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Role of residues in the adenosine binding site of NAD of the Ascaris suum malic enzyme. Biochim Biophys Acta. 2008 Dec; 1784(12):2059-64.
Score: 0.311
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Proper positioning of the nicotinamide ring is crucial for the Ascaris suum malic enzyme reaction. Biochemistry. 2008 Feb 26; 47(8):2539-46.
Score: 0.300
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Multiple roles of arginine 181 in binding and catalysis in the NAD-malic enzyme from Ascaris suum. Biochemistry. 2007 Dec 18; 46(50):14578-88.
Score: 0.296
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Optimum activity of the phosphofructokinase from Ascaris suum requires more than one metal ion. Biochemistry. 2006 Feb 21; 45(7):2453-60.
Score: 0.262
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A catalytic triad is responsible for acid-base chemistry in the Ascaris suum NAD-malic enzyme. Biochemistry. 2005 Mar 08; 44(9):3626-35.
Score: 0.245
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Ascaris suum NAD-malic enzyme is activated by L-malate and fumarate binding to separate allosteric sites. Biochemistry. 2003 Aug 19; 42(32):9712-21.
Score: 0.220
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Expression, purification, and characterization of the recombinant NAD-malic enzyme from Ascaris suum. Protein Expr Purif. 1997 Jun; 10(1):51-4.
Score: 0.143
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Isotope partitioning with Ascaris suum phosphofructokinase is consistent with an ordered kinetic mechanism. Biochemistry. 1996 Apr 30; 35(17):5451-7.
Score: 0.133
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A pH-dependent allosteric transition in Ascaris suum phosphofructokinase distinct from that observed with fructose 2,6-bisphosphate. Arch Biochem Biophys. 1995 Oct 01; 322(2):410-6.
Score: 0.128
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Acid-base catalytic mechanism and pH dependence of fructose 2,6-bisphosphate activation of the Ascaris suum phosphofructokinase. Biochemistry. 1995 Jun 20; 34(24):7781-7.
Score: 0.125
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Metal ion activator effects on intrinsic isotope effects for hydride transfer from decarboxylation in the reaction catalyzed by the NAD-malic enzyme from Ascaris suum. Biochemistry. 1995 Mar 14; 34(10):3253-60.
Score: 0.123
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Mechanism of activation of the NAD-malic enzyme from Ascaris suum by fumarate. Arch Biochem Biophys. 1992 Dec; 299(2):214-9.
Score: 0.105
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Crystallographic studies on Ascaris suum NAD-malic enzyme bound to reduced cofactor and identification of an effector site. J Biol Chem. 2003 Sep 26; 278(39):38051-8.
Score: 0.055
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Lysine 199 is the general acid in the NAD-malic enzyme reaction. Biochemistry. 2000 Oct 03; 39(39):11955-60.
Score: 0.045
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Mapping the active site topography of the NAD-malic enzyme via alanine-scanning site-directed mutagenesis. Biochemistry. 1999 Aug 10; 38(32):10527-32.
Score: 0.042
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Kinetic characterization of a T-state of Ascaris suum phosphofructokinase with heterotropic negative cooperativity by ATP eliminated. Arch Biochem Biophys. 1999 May 15; 365(2):335-43.
Score: 0.041
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Alpha-secondary tritium kinetic isotope effects indicate hydrogen tunneling and coupled motion occur in the oxidation of L-malate by NAD-malic enzyme. Biochemistry. 1999 Apr 06; 38(14):4398-402.
Score: 0.041
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Role of the divalent metal ion in the NAD:malic enzyme reaction: an ESEEM determination of the ground state conformation of malate in the E:Mn:malate complex. Protein Sci. 1996 Aug; 5(8):1648-54.
Score: 0.034
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Comparison of the substrate specificities of cAMP-dependent protein kinase from bovine heart and Ascaris suum muscle. Biol Chem Hoppe Seyler. 1996 Mar; 377(3):203-9.
Score: 0.033
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Pre-steady-state kinetics reveal a slow isomerization of the enzyme-NAD complex in the NAD-malic enzyme reaction. Biochemistry. 1993 Mar 02; 32(8):1928-34.
Score: 0.027
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Cloning and nucleotide sequence of a full-length cDNA encoding Ascaris suum malic enzyme. Arch Biochem Biophys. 1993 Jan; 300(1):231-7.
Score: 0.026