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Results: 1-13 |
Results: 13
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
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
Crystal structures of a low-molecular weight protein tyrosine phosphatase from Saccharomyces cerevisiae and its complex with the substrate p-nitrophenyl phosphate
Authors: Wang, SS Tabernero, L Zhang, M Harms, E Van Etten, RL Stauffacher, CV
Citation: Ss. Wang et al., Crystal structures of a low-molecular weight protein tyrosine phosphatase from Saccharomyces cerevisiae and its complex with the substrate p-nitrophenyl phosphate, BIOCHEM, 39(8), 2000, pp. 1903-1914
Structural and mechanistic basis for the activation of a low-molecular weight protein tyrosine phosphatase by adenine
Authors: Wang, S Stauffacher, CV Van Etten, RL
Citation: S. Wang et al., Structural and mechanistic basis for the activation of a low-molecular weight protein tyrosine phosphatase by adenine, BIOCHEM, 39(6), 2000, pp. 1234-1242
Protein tyrosine phosphatases
Authors: Stauffacher, CV Charbonneau, H
Citation: Cv. Stauffacher et H. Charbonneau, Protein tyrosine phosphatases, PRINCIPLES OF MOLECULAR REGULATION, 2000, pp. 323-347
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
The refined crystal structure of cowpea mosaic virus at 2.8 angstrom resolution
Authors: Lin, TW Chen, ZG Usha, R Stauffacher, CV Dai, JB Schmidt, T Johnson, JE
Citation: Tw. Lin et al., The refined crystal structure of cowpea mosaic virus at 2.8 angstrom resolution, VIROLOGY, 265(1), 1999, pp. 20-34
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
The structure of the bovine protein tyrosine phosphatase dimer reveals a potential self-regulation mechanism
Authors: Tabernero, L Evans, BN Tishmack, PA Van Etten, RL Stauffacher, CV
Citation: L. Tabernero et al., The structure of the bovine protein tyrosine phosphatase dimer reveals a potential self-regulation mechanism, BIOCHEM, 38(36), 1999, pp. 11651-11658
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: 1-13 |