The chemical modification of human liver UDP‐glucuronosyltransferase UGT1*6 reveals the involvement of a carboxyl group in catalysis
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[1] G. Siest,et al. Chemical modification of human UDP-glucuronosyltransferase UGT1*6 by diethyl pyrocarbonate: possible involvement of a histidine residue in the catalytic process. , 1994, Archives of biochemistry and biophysics.
[2] G. Siest,et al. A recombinant phenobarbital-inducible rat liver UDP-glucuronosyltransferase (UDP-glucuronosyltransferase 2B1) stably expressed in V79 cells catalyzes the glucuronidation of morphine, phenols, and carboxylic acids. , 1994, Molecular Pharmacology.
[3] A. Maxwell,et al. Identifying the catalytic residue of the ATPase reaction of DNA gyrase. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[4] B. Burchell,et al. Paracetamol glucuronidation by recombinant rat and human phenol UDP-glucuronosyltransferases. , 1993, Biochemical pharmacology.
[5] A. Burlingame,et al. Evidence for covalent binding of acyl glucuronides to serum albumin via an imine mechanism as revealed by tandem mass spectrometry. , 1993, Proceedings of the National Academy of Sciences of the United States of America.
[6] B. Burchell,et al. Substrate specificities of two stably expressed human liver UDP-glucuronosyltransferases of the UGT1 gene family. , 1993, Drug metabolism and disposition: the biological fate of chemicals.
[7] D. Zakim,et al. The influence of charge and the distribution of charge in the polar region of phospholipids on the activity of UDP-glucuronosyltransferase. , 1992, The Journal of biological chemistry.
[8] G. Mulder. Glucuronidation and its role in regulation of biological activity of drugs. , 1992, Annual review of pharmacology and toxicology.
[9] G. Siest,et al. The UDP glucuronosyltransferase gene superfamily: suggested nomenclature based on evolutionary divergence. , 1991, DNA and cell biology.
[10] M Karplus,et al. Structure of the triosephosphate isomerase-phosphoglycolohydroxamate complex: an analogue of the intermediate on the reaction pathway. , 1991, Biochemistry.
[11] G. Siest,et al. Stable expression of two human UDP-glucuronosyltransferase cDNAs in V79 cell cultures. , 1991, Molecular pharmacology.
[12] K. Bock. Roles of UDP-glucuronosyltransferases in chemical carcinogenesis. , 1991, Critical reviews in biochemistry and molecular biology.
[13] B. Burchell,et al. An investigation of the transverse topology of bilirubin UDP-glucuronosyltransferase in rat hepatic endoplasmic reticulum. , 1989, The Biochemical journal.
[14] M. Jackson,et al. Cloning and substrate specificity of a human phenol UDP-glucuronosyltransferase expressed in COS-7 cells. , 1988, Proceedings of the National Academy of Sciences of the United States of America.
[15] N. Blanckaert,et al. Topology and regulation of bilirubin UDP-glucuronyltransferase in sealed native microsomes from rat liver. , 1988, Archives of biochemistry and biophysics.
[16] C. Mackenzie. Pathology in tropical medicine. , 1986, Parasitology today.
[17] P. Mackenzie. Rat liver UDP-glucuronosyltransferase. Sequence and expression of a cDNA encoding a phenobarbital-inducible form. , 1986, The Journal of biological chemistry.
[18] J. Kaplan,et al. Carbodiimide inactivation of Na,K-ATPase. A consequence of internal cross-linking and not carboxyl group modification. , 1986, The Journal of biological chemistry.
[19] H. DeLuca,et al. Biosynthesis of retinoyl-β-glucuronide, a biologically active metabolite of all-trans-retinoic acid , 1986 .
[20] J. Magdalou,et al. Factors modulating the catalytic specificity of a pure form of UDP-glucuronyltransferase. , 1982, The Journal of biological chemistry.
[21] J. Eyzaguirre,et al. Pig liver phosphomevalonate kinase. 2. Participation of cysteinyl and lysyl groups in catalysis. , 1980, Biochemistry.
[22] M. M. Bradford. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.
[23] A. Fersht,et al. The charge relay system in chymotrypsin and chymotrypsinogen. , 1973, Journal of molecular biology.
[24] D. Koshland,et al. [56] Carbodiimide modification of proteins. , 1972, Methods in enzymology.