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Volumn 95, Issue 1, 2015, Pages 58-70

Homo- and hetero-dimerization of human UDP-glucuronosyltransferase 2B7 (UGT2B7) wild type and its allelic variants affect zidovudine glucuronidation activity

Author keywords

Dimerization; FRET; nsSNPs; UGT2B7; Zidovudine

Indexed keywords

GLUCURONIDE; GLUCURONOSYLTRANSFERASE; UGT2B7 PROTEIN, HUMAN; ZIDOVUDINE;

EID: 84930921828     PISSN: 00062952     EISSN: 18732968     Source Type: Journal    
DOI: 10.1016/j.bcp.2015.03.002     Document Type: Article
Times cited : (50)

References (45)
  • 1
    • 84875924213 scopus 로고    scopus 로고
    • The UDP-glucuronosyltransferases: Their role in drug metabolism and detoxification
    • A. Rowland, J.O. Miners, and P.I. Mackenzie The UDP-glucuronosyltransferases: their role in drug metabolism and detoxification Int. J. Biochem. Cell Biol. 45 2013 1121 1132
    • (2013) Int. J. Biochem. Cell Biol. , vol.45 , pp. 1121-1132
    • Rowland, A.1    Miners, J.O.2    Mackenzie, P.I.3
  • 4
    • 70149104455 scopus 로고    scopus 로고
    • Crystal structures of glycosyltransferase UGT78G1 reveal the molecular basis for glycosylation and deglycosylation of (iso)flavonoids
    • L.V. Modolo, L. Li, H. Pan, J.W. Blount, R.A. Dixon, and X. Wang Crystal structures of glycosyltransferase UGT78G1 reveal the molecular basis for glycosylation and deglycosylation of (iso)flavonoids J. Mol. Biol. 392 2009 1292 1302
    • (2009) J. Mol. Biol. , vol.392 , pp. 1292-1302
    • Modolo, L.V.1    Li, L.2    Pan, H.3    Blount, J.W.4    Dixon, R.A.5    Wang, X.6
  • 6
    • 84931091004 scopus 로고    scopus 로고
    • Distribution of UGT1A9 C-2152T and UGT2B7 G211T mutants in Chinese Han population
    • J. Yi, H.T. Xie, and H.H. Zhou Distribution of UGT1A9 C-2152T and UGT2B7 G211T mutants in Chinese Han population Chin. J. Clin. Pharmacol. Ther. 2007 12
    • (2007) Chin. J. Clin. Pharmacol. Ther. , pp. 12
    • Yi, J.1    Xie, H.T.2    Zhou, H.H.3
  • 7
    • 4143053975 scopus 로고    scopus 로고
    • Single nucleotide polymorphisms and haplotype frequencies of UGT2B4 and UGT2B7 in a Japanese population
    • M. Saeki, Y. Saito, H. Jinno, T. Tanaka-Kagawa, A. Ohno, and S. Ozawa Single nucleotide polymorphisms and haplotype frequencies of UGT2B4 and UGT2B7 in a Japanese population Drug Metab. Dispos. 32 2004 1048 1054
    • (2004) Drug Metab. Dispos. , vol.32 , pp. 1048-1054
    • Saeki, M.1    Saito, Y.2    Jinno, H.3    Tanaka-Kagawa, T.4    Ohno, A.5    Ozawa, S.6
  • 8
    • 0344950514 scopus 로고    scopus 로고
    • Sequence variability and candidate gene analysis in two cancer patients with complex clinical outcomes during morphine therapy
    • T. Hirota, I. Ieiri, H. Takane, H. Sano, K. Kawamoto, and H. Aono Sequence variability and candidate gene analysis in two cancer patients with complex clinical outcomes during morphine therapy Drug Metab. Dispos. 31 2003 677 680
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 677-680
    • Hirota, T.1    Ieiri, I.2    Takane, H.3    Sano, H.4    Kawamoto, K.5    Aono, H.6
  • 9
    • 0033645752 scopus 로고    scopus 로고
    • Genetic polymorphism of UDP-glucuronosyltransferase 2B7 (UGT2B7) at amino acid 268: Ethnic diversity of alleles and potential clinical significance
    • C.R. Bhasker, W. McKinnon, A. Stone, A.C. Lo, T. Kubota, and T. Ishizaki Genetic polymorphism of UDP-glucuronosyltransferase 2B7 (UGT2B7) at amino acid 268: ethnic diversity of alleles and potential clinical significance Pharmacogenetics 10 2000 679 685
    • (2000) Pharmacogenetics , vol.10 , pp. 679-685
    • Bhasker, C.R.1    McKinnon, W.2    Stone, A.3    Lo, A.C.4    Kubota, T.5    Ishizaki, T.6
  • 10
    • 0036373740 scopus 로고    scopus 로고
    • Morphine glucuronide-to-morphine plasma ratios are unaffected by the UGT2B7 H268Y and UGT1A1∗28 polymorphisms in cancer patients on chronic morphine therapy
    • M. Holthe, P. Klepstad, K. Zahlsen, P.C. Borchgrevink, L. Hagen, and O. Dale Morphine glucuronide-to-morphine plasma ratios are unaffected by the UGT2B7 H268Y and UGT1A1∗28 polymorphisms in cancer patients on chronic morphine therapy Eur. J. Clin. Pharmacol. 58 2002 353 356
    • (2002) Eur. J. Clin. Pharmacol. , vol.58 , pp. 353-356
    • Holthe, M.1    Klepstad, P.2    Zahlsen, K.3    Borchgrevink, P.C.4    Hagen, L.5    Dale, O.6
  • 11
    • 0037251316 scopus 로고    scopus 로고
    • Sequence variations in the UDP-glucuronosyltransferase 2B7 (UGT2B7) gene: Identification of 10 novel single nucleotide polymorphisms (SNPs) and analysis of their relevance to morphine glucuronidation in cancer patients
    • M. Holthe, T.N. Rakvag, P. Klepstad, J.R. Idle, S. Kaasa, and H.E. Krokan Sequence variations in the UDP-glucuronosyltransferase 2B7 (UGT2B7) gene: identification of 10 novel single nucleotide polymorphisms (SNPs) and analysis of their relevance to morphine glucuronidation in cancer patients Pharmacogenomics J. 3 2003 17 26
    • (2003) Pharmacogenomics J. , vol.3 , pp. 17-26
    • Holthe, M.1    Rakvag, T.N.2    Klepstad, P.3    Idle, J.R.4    Kaasa, S.5    Krokan, H.E.6
  • 12
    • 0042858542 scopus 로고    scopus 로고
    • Evaluation of 3′-azido-3′-deoxythymidine, morphine, and codeine as probe substrates for UDP-glucuronosyltransferase 2B7 (UGT2B7) in human liver microsomes: Specificity and influence of the UGT2B7∗2 polymorphism
    • M.H. Court, S. Krishnaswamy, Q. Hao, S.X. Duan, C.J. Patten, and L.L. Von Moltke Evaluation of 3′-azido-3′-deoxythymidine, morphine, and codeine as probe substrates for UDP-glucuronosyltransferase 2B7 (UGT2B7) in human liver microsomes: specificity and influence of the UGT2B7∗2 polymorphism Drug Metab. Dispos. 31 2003 1125 1133
    • (2003) Drug Metab. Dispos. , vol.31 , pp. 1125-1133
    • Court, M.H.1    Krishnaswamy, S.2    Hao, Q.3    Duan, S.X.4    Patten, C.J.5    Von Moltke, L.L.6
  • 13
    • 33747830531 scopus 로고    scopus 로고
    • Influence of nonsynonymous polymorphisms of UGT1A8 and UGT2B7 metabolizing enzymes on the formation of phenolic and acyl glucuronides of mycophenolic acid
    • O. Bernard, J. Tojcic, K. Journault, L. Perusse, and C. Guillemette Influence of nonsynonymous polymorphisms of UGT1A8 and UGT2B7 metabolizing enzymes on the formation of phenolic and acyl glucuronides of mycophenolic acid Drug Metab. Dispos. 34 2006 1539 1545
    • (2006) Drug Metab. Dispos. , vol.34 , pp. 1539-1545
    • Bernard, O.1    Tojcic, J.2    Journault, K.3    Perusse, L.4    Guillemette, C.5
  • 14
    • 0038209379 scopus 로고    scopus 로고
    • A pharmacogenetic study of uridine diphosphate-glucuronosyltransferase 2B7 in patients receiving morphine
    • M.B. Sawyer, F. Innocenti, S. Das, C. Cheng, J. Ramirez, and F.H. Pantle-Fisher A pharmacogenetic study of uridine diphosphate-glucuronosyltransferase 2B7 in patients receiving morphine Clin. Pharmacol. Ther. 73 2003 566 574
    • (2003) Clin. Pharmacol. Ther. , vol.73 , pp. 566-574
    • Sawyer, M.B.1    Innocenti, F.2    Das, S.3    Cheng, C.4    Ramirez, J.5    Pantle-Fisher, F.H.6
  • 15
    • 31544450520 scopus 로고    scopus 로고
    • Characterization of common UGT1A8, UGT1A9, and UGT2B7 variants with different capacities to inactivate mutagenic 4-hydroxylated metabolites of estradiol and estrone
    • J. Thibaudeau, J. Lepine, J. Tojcic, Y. Duguay, G. Pelletier, and M. Plante Characterization of common UGT1A8, UGT1A9, and UGT2B7 variants with different capacities to inactivate mutagenic 4-hydroxylated metabolites of estradiol and estrone Cancer Res. 66 2006 125 133
    • (2006) Cancer Res. , vol.66 , pp. 125-133
    • Thibaudeau, J.1    Lepine, J.2    Tojcic, J.3    Duguay, Y.4    Pelletier, G.5    Plante, M.6
  • 16
    • 0034007340 scopus 로고    scopus 로고
    • 3′-Azido-3′-deoxythimidine (AZT) is glucuronidated by human UDP-glucuronosyltransferase 2B7 (UGT2B7)
    • O. Barbier, D. Turgeon, C. Girard, M.D. Green, T.R. Tephly, and D.W. Hum 3′-Azido-3′-deoxythimidine (AZT) is glucuronidated by human UDP-glucuronosyltransferase 2B7 (UGT2B7) Drug Metab. Dispos. 28 2000 497 502
    • (2000) Drug Metab. Dispos. , vol.28 , pp. 497-502
    • Barbier, O.1    Turgeon, D.2    Girard, C.3    Green, M.D.4    Tephly, T.R.5    Hum, D.W.6
  • 17
    • 84879398289 scopus 로고    scopus 로고
    • The influence of UGT2B7, UGT1A8, MDR1, ALDH, ADH, CYP3A4 and CYP3A5 genetic polymorphisms on the pharmacokinetics of silodosin in healthy Chinese volunteers
    • Z. Wang, Q. Xiang, Y. Cui, X. Zhao, and Y. Zhou The influence of UGT2B7, UGT1A8, MDR1, ALDH, ADH, CYP3A4 and CYP3A5 genetic polymorphisms on the pharmacokinetics of silodosin in healthy Chinese volunteers Drug Metab. Pharmacokinet. 28 2013 239 243
    • (2013) Drug Metab. Pharmacokinet. , vol.28 , pp. 239-243
    • Wang, Z.1    Xiang, Q.2    Cui, Y.3    Zhao, X.4    Zhou, Y.5
  • 18
    • 40949143256 scopus 로고    scopus 로고
    • Pharmacokinetic and pharmacodynamic interaction of lorazepam and valproic acid in relation to UGT2B7 genetic polymorphism in healthy subjects
    • J.Y. Chung, J.Y. Cho, K.S. Yu, J.R. Kim, K.S. Lim, and D.R. Sohn Pharmacokinetic and pharmacodynamic interaction of lorazepam and valproic acid in relation to UGT2B7 genetic polymorphism in healthy subjects Clin. Pharmacol. Ther. 83 2008 595 600
    • (2008) Clin. Pharmacol. Ther. , vol.83 , pp. 595-600
    • Chung, J.Y.1    Cho, J.Y.2    Yu, K.S.3    Kim, J.R.4    Lim, K.S.5    Sohn, D.R.6
  • 19
    • 0842325733 scopus 로고    scopus 로고
    • Correlation between UDP-glucuronosyltransferase genotypes and 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone glucuronidation phenotype in human liver microsomes
    • D. Wiener, J.L. Fang, N. Dossett, and P. Lazarus Correlation between UDP-glucuronosyltransferase genotypes and 4-(methylnitrosamino)-1-(3-pyridyl)-1-butanone glucuronidation phenotype in human liver microsomes Cancer Res. 64 2004 1190 1196
    • (2004) Cancer Res. , vol.64 , pp. 1190-1196
    • Wiener, D.1    Fang, J.L.2    Dossett, N.3    Lazarus, P.4
  • 20
    • 18144382296 scopus 로고    scopus 로고
    • An association of UDP-glucuronosyltransferase 2B7 C802T (His268Tyr) polymorphism with bladder cancer in benzidine-exposed workers in China
    • G.F. Lin, W.C. Guo, J.G. Chen, Y.Q. Qin, K. Golka, and C.Q. Xiang An association of UDP-glucuronosyltransferase 2B7 C802T (His268Tyr) polymorphism with bladder cancer in benzidine-exposed workers in China Toxicol. Sci. 85 2005 502 506
    • (2005) Toxicol. Sci. , vol.85 , pp. 502-506
    • Lin, G.F.1    Guo, W.C.2    Chen, J.G.3    Qin, Y.Q.4    Golka, K.5    Xiang, C.Q.6
  • 21
    • 84878517121 scopus 로고    scopus 로고
    • Association of genotypes of carcinogen-metabolizing enzymes and smoking status with bladder cancer in a Japanese population
    • X. Cui, X. Lu, M. Hiura, H. Omori, W. Miyazaki, and T. Katoh Association of genotypes of carcinogen-metabolizing enzymes and smoking status with bladder cancer in a Japanese population Environ. Health Prev. Med. 18 2013 136 142
    • (2013) Environ. Health Prev. Med. , vol.18 , pp. 136-142
    • Cui, X.1    Lu, X.2    Hiura, M.3    Omori, H.4    Miyazaki, W.5    Katoh, T.6
  • 22
    • 73949088338 scopus 로고    scopus 로고
    • Interactions between human UDP-glucuronosyltransferase (UGT) 2B7 and UGT1A enzymes
    • R. Fujiwara, M. Nakajima, S. Oda, H. Yamanaka, S. Ikushiro, and T. Sakaki Interactions between human UDP-glucuronosyltransferase (UGT) 2B7 and UGT1A enzymes J. Pharm. Sci. 99 2010 442 454
    • (2010) J. Pharm. Sci. , vol.99 , pp. 442-454
    • Fujiwara, R.1    Nakajima, M.2    Oda, S.3    Yamanaka, H.4    Ikushiro, S.5    Sakaki, T.6
  • 23
    • 80555131097 scopus 로고    scopus 로고
    • Homodimerization of UDP-glucuronosyltransferase 2B7 (UGT2B7) and identification of a putative dimerization domain by protein homology modeling
    • B.C. Lewis, P.I. Mackenzie, and J.O. Miners Homodimerization of UDP-glucuronosyltransferase 2B7 (UGT2B7) and identification of a putative dimerization domain by protein homology modeling Biochem. Pharmacol. 82 2011 2016 2023
    • (2011) Biochem. Pharmacol. , vol.82 , pp. 2016-2023
    • Lewis, B.C.1    Mackenzie, P.I.2    Miners, J.O.3
  • 24
    • 50449108087 scopus 로고    scopus 로고
    • Construction, expression and activities of three active variants of human uridine diphosphate glucuronic acid transferase 2B7
    • L.M. Yuan, J. Chen, and S. Zeng Construction, expression and activities of three active variants of human uridine diphosphate glucuronic acid transferase 2B7 Chin. J. Pharmacol. Toxicol. 22 2008 274 283
    • (2008) Chin. J. Pharmacol. Toxicol. , vol.22 , pp. 274-283
    • Yuan, L.M.1    Chen, J.2    Zeng, S.3
  • 25
    • 30344456999 scopus 로고    scopus 로고
    • Quantitative regioselectivity of glucuronidation of quercetin by recombinant UDP-glucuronosyltransferases 1A9 and 1A3 using enzymatic kinetic parameters
    • Y.K. Chen, S.Q. Chen, X. Li, and S. Zeng Quantitative regioselectivity of glucuronidation of quercetin by recombinant UDP-glucuronosyltransferases 1A9 and 1A3 using enzymatic kinetic parameters Xenobiotica 35 2005 943 954
    • (2005) Xenobiotica , vol.35 , pp. 943-954
    • Chen, Y.K.1    Chen, S.Q.2    Li, X.3    Zeng, S.4
  • 26
    • 44949168791 scopus 로고    scopus 로고
    • Imaging protein-protein interactions by fluorescence resonance energy transfer (FRET) microscopy
    • (Chapter 19: Unit19.5)
    • F.S. Wouters, and P.I. Bastiaens Imaging protein-protein interactions by fluorescence resonance energy transfer (FRET) microscopy Curr. Protoc. Protein Sci. 2001 (Chapter 19: Unit19.5)
    • (2001) Curr. Protoc. Protein Sci.
    • Wouters, F.S.1    Bastiaens, P.I.2
  • 27
    • 0037238461 scopus 로고    scopus 로고
    • Fluorescence resonance energy transfer from cyan to yellow fluorescent protein detected by acceptor photobleaching using confocal microscopy and a single laser
    • T.S. Karpova, C.T. Baumann, L. He, X. Wu, A. Grammer, and P. Lipsky Fluorescence resonance energy transfer from cyan to yellow fluorescent protein detected by acceptor photobleaching using confocal microscopy and a single laser J. Microsc. 209 2003 56 70
    • (2003) J. Microsc. , vol.209 , pp. 56-70
    • Karpova, T.S.1    Baumann, C.T.2    He, L.3    Wu, X.4    Grammer, A.5    Lipsky, P.6
  • 28
    • 54549105754 scopus 로고    scopus 로고
    • AccPbFRET: An ImageJ plugin for semi-automatic, fully corrected analysis of acceptor photobleaching FRET images
    • J. Roszik, J. Szollosi, and G. Vereb AccPbFRET: an ImageJ plugin for semi-automatic, fully corrected analysis of acceptor photobleaching FRET images BMC Bioinform. 9 2008 346
    • (2008) BMC Bioinform. , vol.9 , pp. 346
    • Roszik, J.1    Szollosi, J.2    Vereb, G.3
  • 29
    • 84863151462 scopus 로고    scopus 로고
    • Determination of cellulase colocalization on cellulose fiber with quantitative FRET measured by acceptor photobleaching and spectrally unmixing fluorescence microscopy
    • L. Wang, Y. Wang, and A.J. Ragauskas Determination of cellulase colocalization on cellulose fiber with quantitative FRET measured by acceptor photobleaching and spectrally unmixing fluorescence microscopy Analyst 137 2012 1319 1324
    • (2012) Analyst , vol.137 , pp. 1319-1324
    • Wang, L.1    Wang, Y.2    Ragauskas, A.J.3
  • 30
    • 72549085335 scopus 로고    scopus 로고
    • Direct quantitative determination of adsorbed cellulase on lignocellulosic biomass with its application to study cellulase desorption for potential recycling
    • Z. Zhu, N. Sathitsuksanoh, and Y.H. Percival Zhang Direct quantitative determination of adsorbed cellulase on lignocellulosic biomass with its application to study cellulase desorption for potential recycling Analyst 134 2009 2267 2272
    • (2009) Analyst , vol.134 , pp. 2267-2272
    • Zhu, Z.1    Sathitsuksanoh, N.2    Percival Zhang, Y.H.3
  • 31
    • 84888594812 scopus 로고    scopus 로고
    • Modulation of the UGT2B7 enzyme activity by C-terminally truncated proteins derived from alternative splicing
    • V. Menard, P. Collin, G. Margaillan, and C. Guillemette Modulation of the UGT2B7 enzyme activity by C-terminally truncated proteins derived from alternative splicing Drug Metab. Dispos. 41 2013 2197 2205
    • (2013) Drug Metab. Dispos. , vol.41 , pp. 2197-2205
    • Menard, V.1    Collin, P.2    Margaillan, G.3    Guillemette, C.4
  • 32
    • 27544506707 scopus 로고    scopus 로고
    • (3′-Azido-3′-deoxythymidine) glucuronidation kinetics in liver microsomes as an explanation for underprediction of in vivo clearance: Comparison to hepatocytes and effect of incubation environment
    • J.J. Engtrakul, R.S. Foti, T.J. Strelevitz, M.B. Fisher, and A.Z.T. Altered (3′-Azido-3′-deoxythymidine) glucuronidation kinetics in liver microsomes as an explanation for underprediction of in vivo clearance: comparison to hepatocytes and effect of incubation environment Drug Metab. Dispos. 33 2005 1621 1627
    • (2005) Drug Metab. Dispos. , vol.33 , pp. 1621-1627
    • Engtrakul, J.J.1    Foti, R.S.2    Strelevitz, T.J.3    Fisher, M.B.4    Altered, A.Z.T.5
  • 33
    • 33947527347 scopus 로고    scopus 로고
    • Oligomerization of the UDP-glucuronosyltransferase 1A proteins: Homo- and heterodimerization analysis by fluorescence resonance energy transfer and co-immunoprecipitation
    • T.N. Operana, and R.H. Tukey Oligomerization of the UDP-glucuronosyltransferase 1A proteins: homo- and heterodimerization analysis by fluorescence resonance energy transfer and co-immunoprecipitation J. Biol. Chem. 282 2007 4821 4829
    • (2007) J. Biol. Chem. , vol.282 , pp. 4821-4829
    • Operana, T.N.1    Tukey, R.H.2
  • 34
    • 0037423299 scopus 로고    scopus 로고
    • Expression and characterization of recombinant human UDP-glucuronosyltransferases (UGTs), UGT1A9 is more resistant to detergent inhibition than other UGTs and was purified as an active dimeric enzyme
    • M. Kurkela, J.A. Garcia-Horsman, L. Luukkanen, S. Morsky, J. Taskinen, and M. Baumann Expression and characterization of recombinant human UDP-glucuronosyltransferases (UGTs), UGT1A9 is more resistant to detergent inhibition than other UGTs and was purified as an active dimeric enzyme J. Biol. Chem. 278 2003 3536 3544
    • (2003) J. Biol. Chem. , vol.278 , pp. 3536-3544
    • Kurkela, M.1    Garcia-Horsman, J.A.2    Luukkanen, L.3    Morsky, S.4    Taskinen, J.5    Baumann, M.6
  • 35
    • 80255122759 scopus 로고    scopus 로고
    • Characterizing the effect of UDP-glucuronosyltransferase (UGT) 2B7 and UGT1A9 genetic polymorphisms on enantioselective glucuronidation of flurbiprofen
    • H. Wang, L. Yuan, and S. Zeng Characterizing the effect of UDP-glucuronosyltransferase (UGT) 2B7 and UGT1A9 genetic polymorphisms on enantioselective glucuronidation of flurbiprofen Biochem. Pharmacol. 82 2011 1757 1763
    • (2011) Biochem. Pharmacol. , vol.82 , pp. 1757-1763
    • Wang, H.1    Yuan, L.2    Zeng, S.3
  • 36
    • 34247618754 scopus 로고    scopus 로고
    • Crystal structure of the cofactor-binding domain of the human phase II drug-metabolism enzyme UDP-glucuronosyltransferase 2B7
    • M.J. Miley, A.K. Zielinska, J.E. Keenan, S.M. Bratton, A. Radominska-Pandya, and M.R. Redinbo Crystal structure of the cofactor-binding domain of the human phase II drug-metabolism enzyme UDP-glucuronosyltransferase 2B7 J. Mol. Biol. 369 2007 498 511
    • (2007) J. Mol. Biol. , vol.369 , pp. 498-511
    • Miley, M.J.1    Zielinska, A.K.2    Keenan, J.E.3    Bratton, S.M.4    Radominska-Pandya, A.5    Redinbo, M.R.6
  • 37
    • 74549148586 scopus 로고    scopus 로고
    • The crystal structure of human UDP-glucuronosyltransferase 2B7 C-terminal end is the first mammalian UGT target to be revealed: The significance for human UGTs from both the 1A and 2B families
    • A. Radominska-Pandya, S.M. Bratton, M.R. Redinbo, and M.J. Miley The crystal structure of human UDP-glucuronosyltransferase 2B7 C-terminal end is the first mammalian UGT target to be revealed: the significance for human UGTs from both the 1A and 2B families Drug Metab. Rev. 42 2010 133 144
    • (2010) Drug Metab. Rev. , vol.42 , pp. 133-144
    • Radominska-Pandya, A.1    Bratton, S.M.2    Redinbo, M.R.3    Miley, M.J.4
  • 38
    • 84897800778 scopus 로고    scopus 로고
    • Molecular dynamics simulations of the cardiac troponin complex performed with FRET distances as restraints
    • J.J. Jayasundar, J. Xing, J.M. Robinson, H.C. Cheung, and W.J. Dong Molecular dynamics simulations of the cardiac troponin complex performed with FRET distances as restraints PLOS ONE 9 2014 e87135
    • (2014) PLOS ONE , vol.9 , pp. e87135
    • Jayasundar, J.J.1    Xing, J.2    Robinson, J.M.3    Cheung, H.C.4    Dong, W.J.5
  • 39
    • 77957752175 scopus 로고    scopus 로고
    • Evidence for initial non-specific polypeptide chain collapse during the refolding of the SH3 domain of PI3 kinase
    • A. Dasgupta, and J.B. Udgaonkar Evidence for initial non-specific polypeptide chain collapse during the refolding of the SH3 domain of PI3 kinase J. Mol. Biol. 403 2010 430 445
    • (2010) J. Mol. Biol. , vol.403 , pp. 430-445
    • Dasgupta, A.1    Udgaonkar, J.B.2
  • 40
    • 72749092609 scopus 로고    scopus 로고
    • A FRET-based method for probing the conformational behavior of an intrinsically disordered repeat domain from Bordetella pertussis adenylate cyclase
    • G.R. Szilvay, M.A. Blenner, O. Shur, D.M. Cropek, and S. Banta A FRET-based method for probing the conformational behavior of an intrinsically disordered repeat domain from Bordetella pertussis adenylate cyclase Biochemistry 48 2009 11273 11282
    • (2009) Biochemistry , vol.48 , pp. 11273-11282
    • Szilvay, G.R.1    Blenner, M.A.2    Shur, O.3    Cropek, D.M.4    Banta, S.5
  • 42
    • 0037012847 scopus 로고    scopus 로고
    • Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells
    • D.A. Zacharias, J.D. Violin, A.C. Newton, and R.Y. Tsien Partitioning of lipid-modified monomeric GFPs into membrane microdomains of live cells Science 296 2002 913 916
    • (2002) Science , vol.296 , pp. 913-916
    • Zacharias, D.A.1    Violin, J.D.2    Newton, A.C.3    Tsien, R.Y.4
  • 43
    • 0029972534 scopus 로고    scopus 로고
    • Crigler-Najjar syndrome type II is inherited both as a dominant and as a recessive trait
    • O. Koiwai, S. Aono, Y. Adachi, T. Kamisako, Y. Yasui, and M. Nishizawa Crigler-Najjar syndrome type II is inherited both as a dominant and as a recessive trait Hum. Mol. Genet. 5 1996 645 647
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 645-647
    • Koiwai, O.1    Aono, S.2    Adachi, Y.3    Kamisako, T.4    Yasui, Y.5    Nishizawa, M.6
  • 44
    • 33645281589 scopus 로고    scopus 로고
    • Crystal structures of a multifunctional triterpene/flavonoid glycosyltransferase from Medicago truncatula
    • H. Shao, X. He, L. Achnine, J.W. Blount, R.A. Dixon, and X. Wang Crystal structures of a multifunctional triterpene/flavonoid glycosyltransferase from Medicago truncatula Plant Cell 17 2005 3141 3154
    • (2005) Plant Cell , vol.17 , pp. 3141-3154
    • Shao, H.1    He, X.2    Achnine, L.3    Blount, J.W.4    Dixon, R.A.5    Wang, X.6
  • 45
    • 33645290775 scopus 로고    scopus 로고
    • Structure of a flavonoid glucosyltransferase reveals the basis for plant natural product modification
    • W. Offen, C. Martinez-Fleites, M. Yang, E. Kiat-Lim, B.G. Davis, and C.A. Tarling Structure of a flavonoid glucosyltransferase reveals the basis for plant natural product modification EMBO J. 25 2006 1396 1405
    • (2006) EMBO J. , vol.25 , pp. 1396-1405
    • Offen, W.1    Martinez-Fleites, C.2    Yang, M.3    Kiat-Lim, E.4    Davis, B.G.5    Tarling, C.A.6


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