메뉴 건너뛰기




Volumn 24, Issue 12, 1997, Pages 907-915

Structure and function of uridine diphosphate glucuronosyltransferases

Author keywords

Endoplasmic reticulum residence; Functional domains; Glucuronidation; Topology; Uridine diphosphate glucuronosyltransferase

Indexed keywords

GLUCURONOSYLTRANSFERASE; ISOENZYME; URIDINE DIPHOSPHATE GLUCURONIC ACID;

EID: 0030778114     PISSN: 03051870     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1440-1681.1997.tb02718.x     Document Type: Review
Times cited : (218)

References (78)
  • 2
    • 0025284207 scopus 로고
    • UDP-glucuronosyltransferases: A family of detoxifying enzymes
    • Tephly TR, Burchell B. UDP-glucuronosyltransferases: A family of detoxifying enzymes. Trends Pharmacol. Sci. 1990; 11: 276-9.
    • (1990) Trends Pharmacol. Sci. , vol.11 , pp. 276-279
    • Tephly, T.R.1    Burchell, B.2
  • 3
    • 0026642306 scopus 로고
    • Glucuronidation and its role in regulation of biological activity of drugs
    • Mulder GJ. Glucuronidation and its role in regulation of biological activity of drugs. Annu. Rev. Pharmacol. Toxicol. 1992; 32: 25-49.
    • (1992) Annu. Rev. Pharmacol. Toxicol. , vol.32 , pp. 25-49
    • Mulder, G.J.1
  • 5
    • 0028295681 scopus 로고
    • 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans
    • Wilson R, Ainscough R, Anderson K et al. 2.2 Mb of contiguous nucleotide sequence from chromosome III of C. elegans. Nature 1994; 368: 32-8.
    • (1994) Nature , vol.368 , pp. 32-38
    • Wilson, R.1    Ainscough, R.2    Anderson, K.3
  • 6
    • 0002051568 scopus 로고
    • The UDP glucuronosyltransferase multigene family
    • Mackenzie PI. The UDP glucuronosyltransferase multigene family. Rev. Biochem. Toxicol. 1995; 11: 29-72.
    • (1995) Rev. Biochem. Toxicol. , vol.11 , pp. 29-72
    • Mackenzie, P.I.1
  • 7
    • 0026090495 scopus 로고
    • Odorant signal termination by olfactory UDP-glucuronosyltransferase
    • Lazard D, Zupko K, Poria Y et al. Odorant signal termination by olfactory UDP-glucuronosyltransferase. Nature 1991; 349: 790-3.
    • (1991) Nature , vol.349 , pp. 790-793
    • Lazard, D.1    Zupko, K.2    Poria, Y.3
  • 8
    • 0025773294 scopus 로고
    • The UDP glucuronosyl-transferase gene family. Suggested nomenclature based on evolutionary divergence
    • Burchell BB, Nebert DW, Nelson DR et al. The UDP glucuronosyl-transferase gene family. Suggested nomenclature based on evolutionary divergence. DNA Cell Biol. 1991; 10: 487-94.
    • (1991) DNA Cell Biol. , vol.10 , pp. 487-494
    • Burchell, B.B.1    Nebert, D.W.2    Nelson, D.R.3
  • 9
    • 0026701911 scopus 로고
    • A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini
    • Ritter JK, Chen F, Sheen YY et al. A novel complex locus UGT1 encodes human bilirubin, phenol, and other UDP-glucuronosyltransferase isozymes with identical carboxyl termini. J. Biol. Chem. 1992; 267: 3257-61.
    • (1992) J. Biol. Chem. , vol.267 , pp. 3257-3261
    • Ritter, J.K.1    Chen, F.2    Sheen, Y.Y.3
  • 10
    • 0028922238 scopus 로고
    • Drug-responsive and tissue-specific alternative expression of multiple first exons in rat UDP-glucuronosyltransferase family 1 (UGT1) gene complex
    • Emi Y, Ikushiro S, Iyanagi T. Drug-responsive and tissue-specific alternative expression of multiple first exons in rat UDP-glucuronosyltransferase family 1 (UGT1) gene complex. J. Biochem. 1995; 117: 392-9.
    • (1995) J. Biochem. , vol.117 , pp. 392-399
    • Emi, Y.1    Ikushiro, S.2    Iyanagi, T.3
  • 11
    • 0026008487 scopus 로고
    • Cloning of two human liver bilirubin UDP-glucuronosyltransferase cDNAs with expression in COS-1 cells
    • Ritter JK, Crawford JM, Owens IS. Cloning of two human liver bilirubin UDP-glucuronosyltransferase cDNAs with expression in COS-1 cells. J. Biol. Chem. 1991; 266: 1043-7.
    • (1991) J. Biol. Chem. , vol.266 , pp. 1043-1047
    • Ritter, J.K.1    Crawford, J.M.2    Owens, I.S.3
  • 12
    • 0013588037 scopus 로고    scopus 로고
    • cDNA cloning and characterisation of the human UDP-glucuronosyltransferase, UGT1 A3
    • Mojarrabi B, Butler R, Mackenzie PI. cDNA cloning and characterisation of the human UDP-glucuronosyltransferase, UGT1 A3. Biochem. Biophys. Res. Commun. 1996; 225: 785-90.
    • (1996) Biochem. Biophys. Res. Commun. , vol.225 , pp. 785-790
    • Mojarrabi, B.1    Butler, R.2    Mackenzie, P.I.3
  • 13
    • 0001036382 scopus 로고
    • Cloning and substrate specificity of a human phenol UDP-glucuronosyltransferase expressed in COS-7 cells
    • Harding D, Fournel Gigleux S, Jackson M et al. Cloning and substrate specificity of a human phenol UDP-glucuronosyltransferase expressed in COS-7 cells. Proc. Natl Acad. Sci. USA 1988; 85: 8381-5.
    • (1988) Proc. Natl Acad. Sci. USA , vol.85 , pp. 8381-8385
    • Harding, D.1    Fournel Gigleux, S.2    Jackson, M.3
  • 14
    • 0025861217 scopus 로고
    • Cloning and stable expression of a new member of the human liver phenol/bilirubin: UDP-glucuronosyltransferase cDNA family
    • Wooster R, Sutherland L, Ebner T et al. Cloning and stable expression of a new member of the human liver phenol/bilirubin: UDP-glucuronosyltransferase cDNA family. Biochem. J. 1991; 278: 465-9.
    • (1991) Biochem. J. , vol.278 , pp. 465-469
    • Wooster, R.1    Sutherland, L.2    Ebner, T.3
  • 15
    • 0026335219 scopus 로고
    • Molecular basis of multiple UDP-glucuronosyltransferase isoenzyme deficiencies in the hyperbilirubinemic rat (Gunn rat)
    • Iyanagi T. Molecular basis of multiple UDP-glucuronosyltransferase isoenzyme deficiencies in the hyperbilirubinemic rat (Gunn rat). J. Biol. Chem. 1991; 266: 24048-52.
    • (1991) J. Biol. Chem. , vol.266 , pp. 24048-24052
    • Iyanagi, T.1
  • 16
    • 0025370878 scopus 로고
    • Isolation and sequencing of rat liver bilirubin UDP-glucuronosyltransferase cDNA: Possible alternate splicing of a common primary transcript
    • Sato H, Koiwai O, Tanabe K, Kashiwamata S. Isolation and sequencing of rat liver bilirubin UDP-glucuronosyltransferase cDNA: Possible alternate splicing of a common primary transcript. Biochem. Biophys. Res. Commun. 1990; 169: 260-4.
    • (1990) Biochem. Biophys. Res. Commun. , vol.169 , pp. 260-264
    • Sato, H.1    Koiwai, O.2    Tanabe, K.3    Kashiwamata, S.4
  • 17
    • 0023019287 scopus 로고
    • Cloning and characterization of cDNA encoding 3-methylcholanthrene inducible rat mRNA for UDP-glucuronosyltransferase
    • Iyanagi T, Haniu M, Sogawa K et al. Cloning and characterization of cDNA encoding 3-methylcholanthrene inducible rat mRNA for UDP-glucuronosyltransferase. J. Biol. Chem. 1986; 261: 15607-14.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15607-15614
    • Iyanagi, T.1    Haniu, M.2    Sogawa, K.3
  • 18
    • 0031038167 scopus 로고    scopus 로고
    • Identification of a rat oltipraz-inducible UDP-glucuronosyltransferase (UGT1A7) with activity towards benzo(a)pyrene-7,8-dihydrodiol
    • Grove AD, Kessler FK, Metz RP, Ritter JK. Identification of a rat oltipraz-inducible UDP-glucuronosyltransferase (UGT1A7) with activity towards benzo(a)pyrene-7,8-dihydrodiol. J. Biol. Chem. 1997; 272: 1621-7.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1621-1627
    • Grove, A.D.1    Kessler, F.K.2    Metz, R.P.3    Ritter, J.K.4
  • 19
    • 0001438682 scopus 로고
    • Congenital familial non-hemolytic jaundice with kernicterus
    • Crigler JF, Najjar VA. Congenital familial non-hemolytic jaundice with kernicterus. Pediatrics 1952; 10: 169-80.
    • (1952) Pediatrics , vol.10 , pp. 169-180
    • Crigler, J.F.1    Najjar, V.A.2
  • 20
    • 0028287482 scopus 로고
    • A new type of defect in the gene for bilirubin UDP-glucuronosyltransferase in a patient with Crigler-Najjar syndrome type I
    • Aono S, Yamada Y, Keino H et al. A new type of defect in the gene for bilirubin UDP-glucuronosyltransferase in a patient with Crigler-Najjar syndrome type I. Pediatr. Res. 1994; 35: 629-32.
    • (1994) Pediatr. Res. , vol.35 , pp. 629-632
    • Aono, S.1    Yamada, Y.2    Keino, H.3
  • 21
    • 0026505255 scopus 로고
    • Sequence of exons and the flanking regions of human bilirubin UDP-glucuronosyltransferase gene complex and identification of a genetic mutation in a patient with Crigler-Najjar syndrome, type I
    • Bosma PJ, Chowdhury NR, Goldhoorn BG et al. Sequence of exons and the flanking regions of human bilirubin UDP-glucuronosyltransferase gene complex and identification of a genetic mutation in a patient with Crigler-Najjar syndrome, type I. Hepatology 1992; 15: 941-7.
    • (1992) Hepatology , vol.15 , pp. 941-947
    • Bosma, P.J.1    Chowdhury, N.R.2    Goldhoorn, B.G.3
  • 22
    • 0028081366 scopus 로고
    • Discrimination between Crigler-Najjar type I and II by expression of bilirubin uridine diphosphate-glucuronosyltransferase
    • Seppen J, Bosma PJ, Goldhorn BG et al. Discrimination between Crigler-Najjar type I and II by expression of bilirubin uridine diphosphate-glucuronosyltransferase. J. Clin. Invest. 1994; 94: 2385-91.
    • (1994) J. Clin. Invest. , vol.94 , pp. 2385-2391
    • Seppen, J.1    Bosma, P.J.2    Goldhorn, B.G.3
  • 23
    • 0028170575 scopus 로고
    • Genetic heterogeneity of Crigler-Najjar syndrome type 1: A study of 14 cases
    • Labrune PH, Myara A, Hadchouel M et al. Genetic heterogeneity of Crigler-Najjar syndrome type 1: A study of 14 cases. Hum. Genet. 1994; 94: 693-7.
    • (1994) Hum. Genet. , vol.94 , pp. 693-697
    • Labrune, P.H.1    Myara, A.2    Hadchouel, M.3
  • 24
    • 0031052397 scopus 로고    scopus 로고
    • Genetic defects at the UGT1 locus associated with Crigler-Najjar type I disease: Including a prenatal diagnosis
    • Ciotti M, Obaray R, Martin MG, Owens IS. Genetic defects at the UGT1 locus associated with Crigler-Najjar type I disease: Including a prenatal diagnosis. Am. J. Med. Genet. 1996; 68: 173-8.
    • (1996) Am. J. Med. Genet. , vol.68 , pp. 173-178
    • Ciotti, M.1    Obaray, R.2    Martin, M.G.3    Owens, I.S.4
  • 25
    • 0027422955 scopus 로고
    • Cosegregation of intragenic markers with a novel mutation that causes Crigler-Najjar syndrome Type 1: Implications in carrier detection and prenatal diagnosis
    • Moghrahi N, Clarke DJ, Burchell B, Boxer M. Cosegregation of intragenic markers with a novel mutation that causes Crigler-Najjar syndrome Type 1: Implications in carrier detection and prenatal diagnosis. Am. J. Hum. Genet. 1993; 53: 722-9.
    • (1993) Am. J. Hum. Genet. , vol.53 , pp. 722-729
    • Moghrahi, N.1    Clarke, D.J.2    Burchell, B.3    Boxer, M.4
  • 26
    • 0028830211 scopus 로고    scopus 로고
    • Altered coding for a strictly conserved di-glycine in the major bilirubin UDP-glucuronosyltransferase of a Crigler-Najjar type I patient
    • Ciotti M, Yeatman MT, Sokol RJ, Owens IS. Altered coding for a strictly conserved di-glycine in the major bilirubin UDP-glucuronosyltransferase of a Crigler-Najjar type I patient. J. Biol. Chem. 1996; 270: 3284-91.
    • (1996) J. Biol. Chem. , vol.270 , pp. 3284-3291
    • Ciotti, M.1    Yeatman, M.T.2    Sokol, R.J.3    Owens, I.S.4
  • 27
    • 0028208939 scopus 로고
    • Identification of two single base substitutions in the UGT1 gene locus which abolish bilirubin uridine diphosphate glucuronosyltransferase activity in vitro
    • Erps LT, Ritter JK, Hersch JH et al. Identification of two single base substitutions in the UGT1 gene locus which abolish bilirubin uridine diphosphate glucuronosyltransferase activity in vitro. J. Clin. Invest. 1994; 93: 564-70.
    • (1994) J. Clin. Invest. , vol.93 , pp. 564-570
    • Erps, L.T.1    Ritter, J.K.2    Hersch, J.H.3
  • 28
    • 0026668559 scopus 로고
    • Mechanism of inherited deficiencies of multiple UDP-glucuronosyltransferase isoforms in two patients with Crigler-Najjar syndrome, type 1
    • Bosma PJ, Chowdhury JR, Huang T et al. Mechanism of inherited deficiencies of multiple UDP-glucuronosyltransferase isoforms in two patients with Crigler-Najjar syndrome, type 1. FASEB J. 1992; 6: 2859-63.
    • (1992) FASEB J. , vol.6 , pp. 2859-2863
    • Bosma, P.J.1    Chowdhury, J.R.2    Huang, T.3
  • 29
    • 0027739943 scopus 로고
    • Identification of defect in the genes for bilirubin UDP-glucuronosyltransferase in a patient with Crigler-Najjar syndrome type 2
    • Aono S, Yamada Y, Keino H et al. Identification of defect in the genes for bilirubin UDP-glucuronosyltransferase in a patient with Crigler-Najjar syndrome type 2. Biochem. Biophys. Res. Commun. 1993; 197: 1239-44.
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 1239-1244
    • Aono, S.1    Yamada, Y.2    Keino, H.3
  • 30
    • 0027234052 scopus 로고
    • A mutation in bilirubin UDP-glucuronosyltransferase isoform 1 causing Crigler-Najjar syndrome, type II
    • Bosma PJ, Goldhoorn BG, Oude Elferink PJ et al. A mutation in bilirubin UDP-glucuronosyltransferase isoform 1 causing Crigler-Najjar syndrome, type II. Gastroenteralogy 1993; 105: 216-20.
    • (1993) Gastroenteralogy , vol.105 , pp. 216-220
    • Bosma, P.J.1    Goldhoorn, B.G.2    Oude Elferink, P.J.3
  • 31
    • 0027524805 scopus 로고
    • Identification of an A-to-G missense mutation in exon 2 of the UGT1 gene complex that causes Crigler-Najjar syndrome type 2
    • Moghrabi N, Clarke DJ, Boxer M, Burchell. B. Identification of an A-to-G missense mutation in exon 2 of the UGT1 gene complex that causes Crigler-Najjar syndrome type 2. Genomics 1993; 18: 171-3.
    • (1993) Genomics , vol.18 , pp. 171-173
    • Moghrabi, N.1    Clarke, D.J.2    Boxer, M.3    Burchell, B.4
  • 32
    • 0030605859 scopus 로고    scopus 로고
    • A mutation which disrupts the hydrophohic core of the signal peptide of bilirubin UDP-glucuronosyltransferase, an endoplasmic reticulum membrane protein, causes Crigler-Najjar type II
    • Seppen J, Steenken E, Lindhout D et al. A mutation which disrupts the hydrophohic core of the signal peptide of bilirubin UDP-glucuronosyltransferase, an endoplasmic reticulum membrane protein, causes Crigler-Najjar type II. FEBS Lett. 1996; 390: 294-8.
    • (1996) FEBS Lett. , vol.390 , pp. 294-298
    • Seppen, J.1    Steenken, E.2    Lindhout, D.3
  • 33
    • 0014664802 scopus 로고
    • Hepatic bilirubin UDP-glucuronyl transferase activity in liver disease and Gilbert's disease
    • Black M, Billing BH. Hepatic bilirubin UDP-glucuronyl transferase activity in liver disease and Gilbert's disease. N. Engl. J. Med. 1969; 280: 1266-71.
    • (1969) N. Engl. J. Med. , vol.280 , pp. 1266-1271
    • Black, M.1    Billing, B.H.2
  • 34
    • 0029015847 scopus 로고
    • Gilbert's syndrome is caused by a heterozygous missense mutation in the gene for bilirubin UDP-glucuronosyltransferase
    • Koiwai O, Nishizawa M, Hasada K et al. Gilbert's syndrome is caused by a heterozygous missense mutation in the gene for bilirubin UDP-glucuronosyltransferase. Hum. Mol. Genet. 1995; 4: 1183-6.
    • (1995) Hum. Mol. Genet. , vol.4 , pp. 1183-1186
    • Koiwai, O.1    Nishizawa, M.2    Hasada, K.3
  • 35
    • 0028867826 scopus 로고
    • The genetic basis of the reduced expression of bilirubin UDP-glucuronosyltransferase 1 in Gilbert's syndrome
    • Bosma PJ, Chowdhury JR, Bakker C et al. The genetic basis of the reduced expression of bilirubin UDP-glucuronosyltransferase 1 in Gilbert's syndrome. N. Engl. J. Med. 1995; 333: 1171-5.
    • (1995) N. Engl. J. Med. , vol.333 , pp. 1171-1175
    • Bosma, P.J.1    Chowdhury, J.R.2    Bakker, C.3
  • 36
    • 0030030762 scopus 로고    scopus 로고
    • Genetic variation in bilirubin UDP-glucuronosyltransferase gene promoter and Gilbert's syndrome
    • Monaghan G, Ryan M, Seddon R et al. Genetic variation in bilirubin UDP-glucuronosyltransferase gene promoter and Gilbert's syndrome. Lancet 1996; 347: 578-81.
    • (1996) Lancet , vol.347 , pp. 578-581
    • Monaghan, G.1    Ryan, M.2    Seddon, R.3
  • 37
    • 0028136583 scopus 로고
    • Isolation of a human YAC contig encompassing a cluster of UGT2 genes and its regional localization to chromosome 4q13
    • Monaghan G, Clarke DJ, Povey S et al. Isolation of a human YAC contig encompassing a cluster of UGT2 genes and its regional localization to chromosome 4q13. Genomics 1994; 23: 496-9.
    • (1994) Genomics , vol.23 , pp. 496-499
    • Monaghan, G.1    Clarke, D.J.2    Povey, S.3
  • 39
    • 0028031069 scopus 로고
    • Recognition of uridine diphosphate glucuronosyl transferases by LKM-3 antibodies in chronic hepatitis D
    • Philipp T, Durazzo M, Trautwein C et al. Recognition of uridine diphosphate glucuronosyl transferases by LKM-3 antibodies in chronic hepatitis D. Lancet 1994; 344: 578-81.
    • (1994) Lancet , vol.344 , pp. 578-581
    • Philipp, T.1    Durazzo, M.2    Trautwein, C.3
  • 40
    • 0021765496 scopus 로고
    • Cleavage of nascent UDP-glucuronosyltransferase from rat liver by pancreatic microsomes
    • Mackenzie PI, Owens IS. Cleavage of nascent UDP-glucuronosyltransferase from rat liver by pancreatic microsomes. Biochem. J. 1984; 122: 1441-9.
    • (1984) Biochem. J. , vol.122 , pp. 1441-1449
    • Mackenzie, P.I.1    Owens, I.S.2
  • 41
    • 0021430832 scopus 로고
    • Cell free translation of mouse liver mRNA coding for two forms of UDP glucuronosyltransferase
    • Mackenzie PI, Gonzalez FJ, Owens IS. Cell free translation of mouse liver mRNA coding for two forms of UDP glucuronosyltransferase. Arch. Biochem. Biophys. 1984; 230: 678-80.
    • (1984) Arch. Biochem. Biophys. , vol.230 , pp. 678-680
    • Mackenzie, P.I.1    Gonzalez, F.J.2    Owens, I.S.3
  • 42
    • 0025098836 scopus 로고
    • The effect of N-linked glycosylation on the substrate preferences of UDP glucuronosyltransferases
    • Mackenzie PI. The effect of N-linked glycosylation on the substrate preferences of UDP glucuronosyltransferases. Biochem. Biophys. Res. Commun. 1990; 166: 1293-9.
    • (1990) Biochem. Biophys. Res. Commun. , vol.166 , pp. 1293-1299
    • Mackenzie, P.I.1
  • 43
    • 0026716833 scopus 로고
    • The jury returns on structure prediction
    • Rost B, Sanders C. The jury returns on structure prediction. Nature 1993; 360: 540.
    • (1993) Nature , vol.360 , pp. 540
    • Rost, B.1    Sanders, C.2
  • 44
    • 0029972534 scopus 로고    scopus 로고
    • Crigler-Najjar syndrome type II inherited as both a dominant and as a recessive trait
    • Koiwai O, Aono S, Adachi Y et al. Crigler-Najjar syndrome type II inherited as both a dominant and as a recessive trait. Hum. Mol. Genet. 1996; 5: 645-7.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 645-647
    • Koiwai, O.1    Aono, S.2    Adachi, Y.3
  • 45
    • 0025236448 scopus 로고
    • Expression of chimeric cDNAs in cell culture defines a region of UDP glucuronosyltransferase involved in substrate selection
    • Mackenzie PI. Expression of chimeric cDNAs in cell culture defines a region of UDP glucuronosyltransferase involved in substrate selection. J. Biol. Chem. 1990; 265: 3432-5.
    • (1990) J. Biol. Chem. , vol.265 , pp. 3432-3435
    • Mackenzie, P.I.1
  • 46
    • 0031034450 scopus 로고    scopus 로고
    • Comparison of stably expressed rat UGT1.1 and UGT2B1 in the glucuronidation of opioid compounds
    • King CD, Rios GR, Green MD, Mackenzie PI, Tephly TR. Comparison of stably expressed rat UGT1.1 and UGT2B1 in the glucuronidation of opioid compounds. Drug Metab. Disp. 1997; 25: 251-5.
    • (1997) Drug Metab. Disp. , vol.25 , pp. 251-255
    • King, C.D.1    Rios, G.R.2    Green, M.D.3    Mackenzie, P.I.4    Tephly, T.R.5
  • 49
    • 0028349889 scopus 로고
    • Photoaffinity labeling for evaluation of uridinyl analogs as specific inhibitors of rat liver microsomal UDP-glucuronosyltransferases
    • Radominska A, Paul P, Treat S et al. Photoaffinity labeling for evaluation of uridinyl analogs as specific inhibitors of rat liver microsomal UDP-glucuronosyltransferases. Biochim. Biophys. Acta 1994; 1205: 336-45.
    • (1994) Biochim. Biophys. Acta , vol.1205 , pp. 336-345
    • Radominska, A.1    Paul, P.2    Treat, S.3
  • 50
    • 0028303560 scopus 로고
    • Chemical modification of human UDP-glucuronosyltransferase UGT1*6 by diethyl pyrocarbonate: Possible involvement of a histidine group in the catalytic process
    • Battaglia E, Pritchard M, Ouzzine M et al. Chemical modification of human UDP-glucuronosyltransferase UGT1*6 by diethyl pyrocarbonate: Possible involvement of a histidine group in the catalytic process. Arch. Biochem. Biophys. 1994; 309: 266-72.
    • (1994) Arch. Biochem. Biophys. , vol.309 , pp. 266-272
    • Battaglia, E.1    Pritchard, M.2    Ouzzine, M.3
  • 51
    • 0027749498 scopus 로고
    • Determination of the human liver UDP-glucuronosyltransferase 2B4 domains involved in the binding of UDP-glucuronic acid using photoaffinity labelling of fusion proteins
    • Pillot T, Ouzzine M, Fournel-Gigleux S et al. Determination of the human liver UDP-glucuronosyltransferase 2B4 domains involved in the binding of UDP-glucuronic acid using photoaffinity labelling of fusion proteins. Biochem. Biophys. Res. Commun. 1993; 197: 785-91.
    • (1993) Biochem. Biophys. Res. Commun. , vol.197 , pp. 785-791
    • Pillot, T.1    Ouzzine, M.2    Fournel-Gigleux, S.3
  • 52
    • 0030889553 scopus 로고    scopus 로고
    • Arginine 52 and histidine 54 located in a conserved amino-terminal hydrophobic region (LX2-R52-G-H54-X3-V-L) are important amino acids for the functional and structural integrity of the human liver UDP glucuronosyltransferase UGT1*6
    • Senay C, Ouzzine M, Battaglia E et al. Arginine 52 and histidine 54 located in a conserved amino-terminal hydrophobic region (LX2-R52-G-H54-X3-V-L) are important amino acids for the functional and structural integrity of the human liver UDP glucuronosyltransferase UGT1*6. Mol. Pharmacol. 1997; 51: 406-13.
    • (1997) Mol. Pharmacol. , vol.51 , pp. 406-413
    • Senay, C.1    Ouzzine, M.2    Battaglia, E.3
  • 53
    • 0029645404 scopus 로고
    • Structures and mechanisms of glycosyl hydrolases
    • Davies G, Henrissat B. Structures and mechanisms of glycosyl hydrolases. Structure 1995; 3: 853-9.
    • (1995) Structure , vol.3 , pp. 853-859
    • Davies, G.1    Henrissat, B.2
  • 54
    • 0017198255 scopus 로고
    • Apparent induction by phenobarbital of uridine diphosphate glucuronosyltransferase activity in nuclear envelopes of embryonic-chick liver
    • Fry DJ, Wishart GJ. Apparent induction by phenobarbital of uridine diphosphate glucuronosyltransferase activity in nuclear envelopes of embryonic-chick liver. Biochem. Soc. Trans. 1976; 4: 265-6.
    • (1976) Biochem. Soc. Trans. , vol.4 , pp. 265-266
    • Fry, D.J.1    Wishart, G.J.2
  • 55
    • 0021246017 scopus 로고
    • Subcellular distribution and regulation of hepatic bilirubin UDP-glucuronosyltransferase
    • Hauser SC, Ziurys JC, Gollan JL. Subcellular distribution and regulation of hepatic bilirubin UDP-glucuronosyltransferase. J. Biol. Chem. 1984; 259: 4527-33.
    • (1984) J. Biol. Chem. , vol.259 , pp. 4527-4533
    • Hauser, S.C.1    Ziurys, J.C.2    Gollan, J.L.3
  • 56
    • 0025184422 scopus 로고
    • Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum
    • Jackson MR, Nilsson T, Peterson PA. Identification of a consensus motif for retention of transmembrane proteins in the endoplasmic reticulum. EMBO J. 1990; 9: 3153-62.
    • (1990) EMBO J. , vol.9 , pp. 3153-3162
    • Jackson, M.R.1    Nilsson, T.2    Peterson, P.A.3
  • 57
    • 0028181745 scopus 로고
    • Coatomer interaction with di-lysine endoplasmic reticulum retention motifs
    • Cosson P, Letourneur F. Coatomer interaction with di-lysine endoplasmic reticulum retention motifs. Science 1994; 263: 1629-31.
    • (1994) Science , vol.263 , pp. 1629-1631
    • Cosson, P.1    Letourneur, F.2
  • 58
    • 0027300360 scopus 로고
    • Intracellular localisation of UDP-glucuronosyltransferase expressed from the transfected cDNA in cultured cells
    • Kinosaki M, Masuko T, Sogawa K et al. Intracellular localisation of UDP-glucuronosyltransferase expressed from the transfected cDNA in cultured cells. Cell Struct. Funct. 1993; 18: 41-51.
    • (1993) Cell Struct. Funct. , vol.18 , pp. 41-51
    • Kinosaki, M.1    Masuko, T.2    Sogawa, K.3
  • 59
    • 0020491333 scopus 로고
    • Factors modulating the catalytic activity of a pure form of UDP glucuronosyltransferase
    • Magdalou J, Hochman Y, Zakim D. Factors modulating the catalytic activity of a pure form of UDP glucuronosyltransferase. J. Biol. Chem. 1982; 257: 13 624-9.
    • (1982) J. Biol. Chem. , vol.257 , pp. 13624-13629
    • Magdalou, J.1    Hochman, Y.2    Zakim, D.3
  • 60
    • 0027451740 scopus 로고
    • Purification and characterization of a catalytically active human liver UDP-glucuronosyltransferase expressed as a fusion protein in E. coli
    • Pillot T, Ouzzine M, Fournel-Gigleux S et al. Purification and characterization of a catalytically active human liver UDP-glucuronosyltransferase expressed as a fusion protein in E. coli. Biochem. Biophys. Res. Commun. 1993; 196: 473-9.
    • (1993) Biochem. Biophys. Res. Commun. , vol.196 , pp. 473-479
    • Pillot, T.1    Ouzzine, M.2    Fournel-Gigleux, S.3
  • 61
    • 0028829564 scopus 로고
    • Enhancement of intestinal bilirubin UDP-glucuronosyltransferase activity by modification of microsomal lipid composition
    • Sanchezpozzi EJ, Catania VA, Rodriguezgaray EA, Mottino AD. Enhancement of intestinal bilirubin UDP-glucuronosyltransferase activity by modification of microsomal lipid composition. Biochim. Biophys. Acta 1995; 1245: 293-8.
    • (1995) Biochim. Biophys. Acta , vol.1245 , pp. 293-298
    • Sanchezpozzi, E.J.1    Catania, V.A.2    Rodriguezgaray, E.A.3    Mottino, A.D.4
  • 62
    • 0025240539 scopus 로고
    • Expression of UDP-glucuronosyltransferase cDNA in Saccharomyces cerevisiae as a membrane bound and cytosolic form
    • Toghrol F, Kimura T, Owens IS. Expression of UDP-glucuronosyltransferase cDNA in Saccharomyces cerevisiae as a membrane bound and cytosolic form. Biochemistry 1990; 29: 2349-56.
    • (1990) Biochemistry , vol.29 , pp. 2349-2356
    • Toghrol, F.1    Kimura, T.2    Owens, I.S.3
  • 64
    • 0027216642 scopus 로고
    • Latency is the major determinant of UDP-glucuronosyltransferase activity in isolated hepatocytes
    • Banhegyi G, Garzo T, Fuleri R et al. Latency is the major determinant of UDP-glucuronosyltransferase activity in isolated hepatocytes. FEBS Lett. 1993; 328: 149-52.
    • (1993) FEBS Lett. , vol.328 , pp. 149-152
    • Banhegyi, G.1    Garzo, T.2    Fuleri, R.3
  • 66
    • 0026505772 scopus 로고
    • How does the microsomal membrane regulate UDP-glucuronosyltransferases?
    • Zakim D, Dannenberg AJ. How does the microsomal membrane regulate UDP-glucuronosyltransferases? Biochem. Pharmacol. 1992; 43: 1385-93.
    • (1992) Biochem. Pharmacol. , vol.43 , pp. 1385-1393
    • Zakim, D.1    Dannenberg, A.J.2
  • 67
    • 0026517062 scopus 로고
    • New developments in glucuronidation research: Report of workshop on 'glucuronidation, its role in health and disease'
    • Jansen PLM, Mulder GJ, Burchell B, Bock KW. New developments in glucuronidation research: Report of workshop on 'glucuronidation, its role in health and disease' Hepatology. 1992; 15: 532-44.
    • (1992) Hepatology , vol.15 , pp. 532-544
    • Jansen, P.L.M.1    Mulder, G.J.2    Burchell, B.3    Bock, K.W.4
  • 68
    • 0026699309 scopus 로고
    • Topological disposition of UDP glucuronosyltransferase in rat liver microsomes
    • Yokota H, Yuasa A, Sata R. Topological disposition of UDP glucuronosyltransferase in rat liver microsomes. J. Biochem. 1992; 112: 192-6.
    • (1992) J. Biochem. , vol.112 , pp. 192-196
    • Yokota, H.1    Yuasa, A.2    Sata, R.3
  • 69
    • 0029956992 scopus 로고    scopus 로고
    • Mutational analysis of the carboxy-terminal region of UDP-glucuronosyltransferase 2B1
    • Meech R, Yogalingam G, Mackenzie PI. Mutational analysis of the carboxy-terminal region of UDP-glucuronosyltransferase 2B1. DNA Cell Biol. 1996; 15: 489-94.
    • (1996) DNA Cell Biol. , vol.15 , pp. 489-494
    • Meech, R.1    Yogalingam, G.2    Mackenzie, P.I.3
  • 70
    • 0025056595 scopus 로고
    • Cellular uptake of conjugated bilirubin and sulphobromophthalein (BSP) by the human hepatoma cell line Hep G2 is mediated by a membrane BSP/bilirubin binding protein
    • Stremmel W, Diede HE. Cellular uptake of conjugated bilirubin and sulphobromophthalein (BSP) by the human hepatoma cell line Hep G2 is mediated by a membrane BSP/bilirubin binding protein. J. Hepatol. 1990; 10: 99-104.
    • (1990) J. Hepatol. , vol.10 , pp. 99-104
    • Stremmel, W.1    Diede, H.E.2
  • 71
    • 0023763078 scopus 로고
    • A membrane transporter mediates access of uridine 5-diphosphoglucuronic acid from the cytosol into the endoplasmic reticulum of rat hepatocytes: Implication for glucuronidation reactions
    • Hauser SC, Ziurys JC, Gollan JL. A membrane transporter mediates access of uridine 5-diphosphoglucuronic acid from the cytosol into the endoplasmic reticulum of rat hepatocytes: Implication for glucuronidation reactions. Biochim. Biophys. Acta 1988; 267: 149-57.
    • (1988) Biochim. Biophys. Acta , vol.267 , pp. 149-157
    • Hauser, S.C.1    Ziurys, J.C.2    Gollan, J.L.3
  • 72
    • 0028036952 scopus 로고
    • Characterization of UDP-glucuronic acid transport in rat liver microsomal vesicles with photoaffinity analogues
    • Radominska A, Treat S, Little JM et al. Characterization of UDP-glucuronic acid transport in rat liver microsomal vesicles with photoaffinity analogues. Biochim. Biophys. Acta 1994; 1195: 63-70.
    • (1994) Biochim. Biophys. Acta , vol.1195 , pp. 63-70
    • Radominska, A.1    Treat, S.2    Little, J.M.3
  • 73
    • 0023734269 scopus 로고
    • Interaction of uridine 5-diphosphoglucuronic acid with microsomal UDP-glucuronosyltransferase in primate liver: The facilitating role of uridine 5-diphospho-N-acetylglucosamine
    • Hauser SC, Ransil BJ, Ziurys JC, Gollan JL. Interaction of uridine 5-diphosphoglucuronic acid with microsomal UDP-glucuronosyltransferase in primate liver: The facilitating role of uridine 5-diphospho-N-acetylglucosamine. Biochim. Biophys. Acta 1988; 267: 141-8.
    • (1988) Biochim. Biophys. Acta , vol.267 , pp. 141-148
    • Hauser, S.C.1    Ransil, B.J.2    Ziurys, J.C.3    Gollan, J.L.4
  • 74
    • 0030922497 scopus 로고    scopus 로고
    • Carrier-mediated transport of uridine diphosphoglucuronic acid across the endoplasmic reticulum membrane is a prerequisite for UDP-glucuronosyltransferase activity in rat liver
    • Bossuyt X, Blanckaert N. Carrier-mediated transport of uridine diphosphoglucuronic acid across the endoplasmic reticulum membrane is a prerequisite for UDP-glucuronosyltransferase activity in rat liver. Biochem. J. 1997; 323: 645-8.
    • (1997) Biochem. J. , vol.323 , pp. 645-648
    • Bossuyt, X.1    Blanckaert, N.2
  • 75
    • 0029862844 scopus 로고    scopus 로고
    • Evidence for an UDP-glucuronic acid phenol glucuronide antiport in rat liver microsomal vesicles
    • Banhegyi G, Braun L, Marcolongo P et al. Evidence for an UDP-glucuronic acid phenol glucuronide antiport in rat liver microsomal vesicles. Biochem. J. 1996; 315: 171-6.
    • (1996) Biochem. J. , vol.315 , pp. 171-176
    • Banhegyi, G.1    Braun, L.2    Marcolongo, P.3
  • 76
    • 0023712304 scopus 로고
    • Hepatocyte cotransport of taurocholate and bilirubin glucuronides: Role of microtubules
    • Crawford JM, Gollan JL. Hepatocyte cotransport of taurocholate and bilirubin glucuronides: Role of microtubules. Am. J. Physiol. 1988; 255: G121-31.
    • (1988) Am. J. Physiol. , vol.255
    • Crawford, J.M.1    Gollan, J.L.2
  • 77
    • 0029981430 scopus 로고    scopus 로고
    • Congenital jaundice in rats with a mutation in a multidrug-resistance-associated protein gene
    • Paulusma CC, Bosma PJ, Zaman GJR et al. Congenital jaundice in rats with a mutation in a multidrug-resistance-associated protein gene. Science 1996; 271: 1126-8.
    • (1996) Science , vol.271 , pp. 1126-1128
    • Paulusma, C.C.1    Bosma, P.J.2    Zaman, G.J.R.3
  • 78
    • 0029895408 scopus 로고    scopus 로고
    • The human gene encoding the UDP-galactose galactosyl transferase (cerebroside synthase): Cloning, characterization and assignment to human chromosome 4, band q26
    • Bosio A, Binczek E, Le Beau MM et al. The human gene encoding the UDP-galactose galactosyl transferase (cerebroside synthase): Cloning, characterization and assignment to human chromosome 4, band q26. Genomics 1996; 34: 69-75.
    • (1996) Genomics , vol.34 , pp. 69-75
    • Bosio, A.1    Binczek, E.2    Le Beau, M.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.