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Results: 1-9 |
Results: 9
Dual coenzyme specificity of Archaeoglobus fulgidus HMG-CoA reductase
Authors: Kim, DY Stauffacher, CV Rodwell, VW
Citation: Dy. Kim et al., Dual coenzyme specificity of Archaeoglobus fulgidus HMG-CoA reductase, PROTEIN SCI, 9(6), 2000, pp. 1226-1234
3-hydroxy-3-methylglutaryl-CoA reductase
Authors: Rodwell, VW Beach, MJ Bischoff, KM Bochar, DA Darnay, BG Friesen, JA Gill, JF Hedl, M Jordan-Starck, T Kennelly, PJ Kim, D Wang, YL
Citation: Vw. Rodwell et al., 3-hydroxy-3-methylglutaryl-CoA reductase, METH ENZYM, 324, 2000, pp. 259-280
Essentiality, expression, and characterization of the class II 3-hydroxy-3-methylglutaryl coenzyme A reductase of Staphylococcus aureus
Authors: Wilding, EI Kim, DY Bryant, AP Gwynn, MN Lunsford, RD McDevitt, D Myers, JE Rosenberg, M Sylvester, D Stauffacher, CV Rodwell, VW
Citation: Ei. Wilding et al., Essentiality, expression, and characterization of the class II 3-hydroxy-3-methylglutaryl coenzyme A reductase of Staphylococcus aureus, J BACT, 182(18), 2000, pp. 5147-5152
Engineering of Sulfolobus solfataricus HMG-CoA reductase to a form whose activity is regulated by phosphorylation and dephosphorylation
Authors: Kim, DY Stauffacher, CV Rodwell, VW
Citation: Dy. Kim et al., Engineering of Sulfolobus solfataricus HMG-CoA reductase to a form whose activity is regulated by phosphorylation and dephosphorylation, BIOCHEM, 39(9), 2000, pp. 2269-2275
Sequence comparisons reveal two classes of 3-hydroxy-3-methylglutaryl coenzyme A reductase
Authors: Bochar, DA Stauffacher, CV Rodwell, VW
Citation: Da. Bochar et al., Sequence comparisons reveal two classes of 3-hydroxy-3-methylglutaryl coenzyme A reductase, MOL GEN MET, 66(2), 1999, pp. 122-127
Expression and characterization of the HMG-CoA reductase of the thermophilic archaeon Sulfolobus solfataricus
Authors: Kim, DY Bochar, DA Stauffacher, CV Rodwell, VW
Citation: Dy. Kim et al., Expression and characterization of the HMG-CoA reductase of the thermophilic archaeon Sulfolobus solfataricus, PROT EX PUR, 17(3), 1999, pp. 435-442
Substrate-induced closure of the flap domain in the ternary complex structures provides insights into the mechanism of catalysis by 3-hydroxy-3-methylglutaryl-CoA reductase
Authors: Tabernero, L Bochar, DA Rodwell, VW Stauffacher, CV
Citation: L. Tabernero et al., Substrate-induced closure of the flap domain in the ternary complex structures provides insights into the mechanism of catalysis by 3-hydroxy-3-methylglutaryl-CoA reductase, P NAS US, 96(13), 1999, pp. 7167-7171
Investigation of the conserved lysines of Syrian hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase
Authors: Bochar, DA Stauffacher, CV Rodwell, VW
Citation: Da. Bochar et al., Investigation of the conserved lysines of Syrian hamster 3-hydroxy-3-methylglutaryl coenzyme A reductase, BIOCHEM, 38(48), 1999, pp. 15848-15852
Aminoethylcysteine can replace the function of the essential active site lysine of Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase
Authors: Bochar, DA Tabernero, L Stauffacher, CV Rodwell, VW
Citation: Da. Bochar et al., Aminoethylcysteine can replace the function of the essential active site lysine of Pseudomonas mevalonii 3-hydroxy-3-methylglutaryl coenzyme A reductase, BIOCHEM, 38(28), 1999, pp. 8879-8883
Risultati: 1-9 |