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Volumn 287, Issue 19, 2012, Pages 15684-15695

Substrate selectivity of YgfU, a uric acid transporter from Escherichia coli

Author keywords

[No Author keywords available]

Indexed keywords

COMPREHENSIVE ANALYSIS; GENOMIC LOCUS; HIGH-CAPACITY; HOMOLOGY MODELING; SITE DIRECTED MUTAGENESIS; SITE-SPECIFIC REPLACEMENTS; STRUCTURE-FUNCTION RELATIONSHIP; SUBSTRATE SELECTIVITY; URIC ACIDS; X-RAY STRUCTURE;

EID: 84860862465     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.355818     Document Type: Article
Times cited : (34)

References (44)
  • 2
    • 77949877904 scopus 로고    scopus 로고
    • Identification and functional characterization of the first nucleobase transporter in mammals: Implication in the species difference in the intestinal absorption mechanism of nucleobases and their analogs between higher primates and other mammals
    • Yamamoto, S., Inoue, K., Murata, T., Kamigaso, S., Yasujima, T., Maeda, J. Y., Yoshida, Y., Ohta, K. Y., and Yuasa, H. (2010) Identification and functional characterization of the first nucleobase transporter in mammals: implication in the species difference in the intestinal absorption mechanism of nucleobases and their analogs between higher primates and other mammals. J. Biol. Chem. 285, 6522-6531
    • (2010) J. Biol. Chem. , vol.285 , pp. 6522-6531
    • Yamamoto, S.1    Inoue, K.2    Murata, T.3    Kamigaso, S.4    Yasujima, T.5    Maeda, J.Y.6    Yoshida, Y.7    Ohta, K.Y.8    Yuasa, H.9
  • 4
    • 20444463884 scopus 로고    scopus 로고
    • Cloning and functional characterization of two bacterial members of the NAT/NCS2 family in Escherichia coli
    • DOI 10.1080/09687860500092927
    • Karatza, P., and Frillingos, S. (2005) Cloning and functional characterization of two bacterial members of the NAT/NCS2 family in Escherichia coli. Mol. Membr. Biol. 22, 251-261 (Pubitemid 41020339)
    • (2005) Molecular Membrane Biology , vol.22 , Issue.3 , pp. 251-261
    • Karatza, P.1    Frillingos, S.2
  • 5
    • 33845966781 scopus 로고    scopus 로고
    • Cysteine-scanning analysis of the nucleobase-ascorbate transporter signature motif in YgfO permease of Escherichia coli: Gln-324 and Asn-325 are essential, and Ile-329 -Val-339 form an α-helix
    • DOI 10.1074/jbc.M605748200
    • Karatza, P., Panos, P., Georgopoulou, E., and Frillingos, S. (2006) Cysteine-scanning analysis of the nucleobase-ascorbate transporter signature motif in YgfO permease of Escherichia coli: Gln-324 and Asn-325 are essential, and Ile-329-Val-339 form an α-helix. J. Biol. Chem. 281, 39881-39890 (Pubitemid 46041791)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.52 , pp. 39881-39890
    • Karatza, P.1    Panos, P.2    Georgopoulou, E.3    Frillingos, S.4
  • 6
    • 46649112362 scopus 로고    scopus 로고
    • Cysteine-scanning analysis of putative helix XII in the YgfO xanthine permease: Ile-432 and Asn-430 are important
    • Papakostas, K., Georgopoulou, E., and Frillingos, S. (2008) Cysteine-scanning analysis of putative helix XII in the YgfO xanthine permease: Ile-432 and Asn-430 are important. J. Biol. Chem. 283, 13666-13678
    • (2008) J. Biol. Chem. , vol.283 , pp. 13666-13678
    • Papakostas, K.1    Georgopoulou, E.2    Frillingos, S.3
  • 7
    • 69949131591 scopus 로고    scopus 로고
    • Role of intramembrane polar residues in the YgfO xanthine permease: His-31 and Asn-93 are crucial for affinity and specificity, and Asp-304 and Glu-272 are irreplaceable
    • Karena, E., and Frillingos, S. (2009) Role of intramembrane polar residues in the YgfO xanthine permease: His-31 and Asn-93 are crucial for affinity and specificity, and Asp-304 and Glu-272 are irreplaceable. J. Biol. Chem. 284, 24257-24268
    • (2009) J. Biol. Chem. , vol.284 , pp. 24257-24268
    • Karena, E.1    Frillingos, S.2
  • 8
    • 77953482526 scopus 로고    scopus 로고
    • Purine substrate recognition by the nucleobase-ascorbate transporter signature motif in the YgfO xanthine permease: Asn-325 binds and Ala-323 senses substrate
    • Georgopoulou, E., Mermelekas, G., Karena, E., and Frillingos, S. (2010) Purine substrate recognition by the nucleobase-ascorbate transporter signature motif in the YgfO xanthine permease: Asn-325 binds and Ala-323 senses substrate. J. Biol. Chem. 285, 19422-19433
    • (2010) J. Biol. Chem. , vol.285 , pp. 19422-19433
    • Georgopoulou, E.1    Mermelekas, G.2    Karena, E.3    Frillingos, S.4
  • 9
    • 78049395093 scopus 로고    scopus 로고
    • Cysteine-scanning analysis of helices TM8, TM9a, and TM9b and intervening loops in the YgfO xanthine permease: A carboxyl group is essential at Asp-276
    • Mermelekas, G., Georgopoulou, E., Kallis, A., Botou, M., Vlantos, V., and Frillingos, S. (2010) Cysteine-scanning analysis of helices TM8, TM9a, and TM9b and intervening loops in the YgfO xanthine permease: a carboxyl group is essential at Asp-276. J. Biol. Chem. 285, 35011-35020
    • (2010) J. Biol. Chem. , vol.285 , pp. 35011-35020
    • Mermelekas, G.1    Georgopoulou, E.2    Kallis, A.3    Botou, M.4    Vlantos, V.5    Frillingos, S.6
  • 10
    • 80655144745 scopus 로고    scopus 로고
    • The role of transmembrane segment TM3 in the xanthine permease XanQ of Escherichia coli
    • Karena, E., and Frillingos, S. (2011) The role of transmembrane segment TM3 in the xanthine permease XanQ of Escherichia coli. J. Biol. Chem. 286, 39595-39605
    • (2011) J. Biol. Chem. , vol.286 , pp. 39595-39605
    • Karena, E.1    Frillingos, S.2
  • 11
    • 0032528103 scopus 로고    scopus 로고
    • Chimeric purine transporters of Aspergillus nidulans define a domain critical for function and specificity conserved in bacterial, plant and metazoan homologues
    • DOI 10.1093/emboj/17.14.3827
    • Diallinas, G., Valdez, J., Sophianopoulou, V., Rosa, A., and Scazzocchio, C. (1998) Chimeric purine transporters of Aspergillus nidulans define a domain critical for function and specificity conserved in bacterial, plant, and metazoan homologues. EMBO J. 17, 3827-3837 (Pubitemid 28333969)
    • (1998) EMBO Journal , vol.17 , Issue.14 , pp. 3827-3837
    • Diallinas, G.1    Valdez, J.2    Sophianopoulou, V.3    Rosa, A.4    Scazzocchio, C.5
  • 12
    • 20444448199 scopus 로고    scopus 로고
    • The Nucleobase-ascorbate transporter (NAT) signature motif in UapA defines the function of the purine translocation pathway
    • DOI 10.1016/j.jmb.2005.04.076, PII S0022283605005310
    • Koukaki, M., Vlanti, A., Goudela, S., Pantazopoulou, A., Gioule, H., Tournaviti, S., and Diallinas, G. (2005) The nucleobase-ascorbate transporter (NAT) signature motif in UapA defines the function of the purine translocation pathway. J. Mol. Biol. 350, 499-513 (Pubitemid 40828910)
    • (2005) Journal of Molecular Biology , vol.350 , Issue.3 , pp. 499-513
    • Koukaki, M.1    Vlanti, A.2    Goudela, S.3    Pantazopoulou, A.4    Gioule, H.5    Tournaviti, S.6    Diallinas, G.7
  • 13
    • 51349162011 scopus 로고    scopus 로고
    • Specific interdomain synergy in the UapA transporter determines its unique specificity for uric acid among NAT carriers
    • Papageorgiou, I., Gournas, C., Vlanti, A., Amillis, S., Pantazopoulou, A., and Diallinas, G. (2008) Specific interdomain synergy in the UapA transporter determines its unique specificity for uric acid among NAT carriers. J. Mol. Biol. 382, 1121-1135
    • (2008) J. Mol. Biol. , vol.382 , pp. 1121-1135
    • Papageorgiou, I.1    Gournas, C.2    Vlanti, A.3    Amillis, S.4    Pantazopoulou, A.5    Diallinas, G.6
  • 14
    • 77950519435 scopus 로고    scopus 로고
    • Dynamic elements at both cytoplasmically and extracellularly facing sides of the UapA transporter selectively control the accessibility of substrates to their translocation pathway
    • Kosti, V., Papageorgiou, I., and Diallinas, G. (2010) Dynamic elements at both cytoplasmically and extracellularly facing sides of the UapA transporter selectively control the accessibility of substrates to their translocation pathway. J. Mol. Biol. 397, 1132-1143
    • (2010) J. Mol. Biol. , vol.397 , pp. 1132-1143
    • Kosti, V.1    Papageorgiou, I.2    Diallinas, G.3
  • 15
    • 79960915923 scopus 로고    scopus 로고
    • Mutational analysis and modeling reveal functionally critical residues in transmembrane segments 1 and 3 of the UapA transporter
    • Amillis, S., Kosti, V., Pantazopoulou, A., Mikros, E., and Diallinas, G. (2011) Mutational analysis and modeling reveal functionally critical residues in transmembrane segments 1 and 3 of the UapA transporter. J. Mol. Biol. 411, 567-580
    • (2011) J. Mol. Biol. , vol.411 , pp. 567-580
    • Amillis, S.1    Kosti, V.2    Pantazopoulou, A.3    Mikros, E.4    Diallinas, G.5
  • 16
    • 0028931056 scopus 로고
    • Uracil uptake in Escherichia coli K-12: Isolation of uraA mutants and cloning of the gene
    • Andersen, P.S., Frees, D., Fast, R., and Mygind, B. (1995) Uracil uptake in Escherichia coli K-12: isolation of uraA mutants and cloning of the gene. J. Bacteriol. 177, 2008-2013
    • (1995) J. Bacteriol. , vol.177 , pp. 2008-2013
    • Andersen, P.S.1    Frees, D.2    Fast, R.3    Mygind, B.4
  • 18
    • 77955969370 scopus 로고    scopus 로고
    • The Rut pathway for pyrimidine degradation: Novel chemistry and toxicity problems
    • Kim, K. S., Pelton, J.G., Inwood, W. B., Andersen, U., Kustu, S., and Wemmer, D. E. (2010) The Rut pathway for pyrimidine degradation: novel chemistry and toxicity problems. J. Bacteriol. 192, 4089-4102
    • (2010) J. Bacteriol. , vol.192 , pp. 4089-4102
    • Kim, K.S.1    Pelton, J.G.2    Inwood, W.B.3    Andersen, U.4    Kustu, S.5    Wemmer, D.E.6
  • 19
    • 77955961477 scopus 로고    scopus 로고
    • The surprising Rut pathway: An unexpected way to derive nitrogen from pyrimidines
    • Parales, R. E., and Ingraham, J. L. (2010) The surprising Rut pathway: an unexpected way to derive nitrogen from pyrimidines. J. Bacteriol. 192, 4086-4088
    • (2010) J. Bacteriol. , vol.192 , pp. 4086-4088
    • Parales, R.E.1    Ingraham, J.L.2
  • 20
    • 0033797245 scopus 로고    scopus 로고
    • Purine catabolism in Escherichia coli and function of xanthine dehydrogenase in purine salvage
    • Xi, H., Schneider, B. L., and Reitzer, L. (2000) Purine catabolism in Escherichia coli and function of xanthine dehydrogenase in purine salvage. J. Bacteriol. 182, 5332-5341
    • (2000) J. Bacteriol. , vol.182 , pp. 5332-5341
    • Xi, H.1    Schneider, B.L.2    Reitzer, L.3
  • 21
    • 0035031537 scopus 로고    scopus 로고
    • Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator
    • DOI 10.1128/JB.183.11.3293-3302.2001
    • Schultz, A. C., Nygaard, P., and Saxild, H. H. (2001) Functional analysis of 14 genes that constitute the purine catabolic pathway in Bacillus subtilis and evidence for a novel regulon controlled by the PucR transcription activator. J. Bacteriol. 183, 3293-3302 (Pubitemid 32448592)
    • (2001) Journal of Bacteriology , vol.183 , Issue.11 , pp. 3293-3302
    • Schultz, A.C.1    Nygaard, P.2    Saxild, H.H.3
  • 22
    • 0942276403 scopus 로고    scopus 로고
    • The azgA purine transporter of Aspergillus nidulans: Characterization of a protein belonging to a new phylogenetic cluster
    • DOI 10.1074/jbc.M308826200
    • Cecchetto, G., Amillis, S., Diallinas, G., Scazzocchio, C., and Drevet, C. (2004) The AzgA purine transporter of Aspergillus nidulans: characterization of a protein belonging to a new phylogenetic cluster. J. Biol. Chem. 279, 3132-3141 (Pubitemid 38140545)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.5 , pp. 3132-3141
    • Cecchetto, G.1    Amillis, S.2    Diallinas, G.3    Scazzocchio, C.4    Drevet, C.5
  • 23
    • 58149527702 scopus 로고    scopus 로고
    • AtAzg1 and AtAzg2 comprise a novel family of purine transporters in Arabidopsis
    • Mansfield, T. A., Schultes, N. P., and Mourad, G. S. (2009) AtAzg1 and AtAzg2 comprise a novel family of purine transporters in Arabidopsis. FEBS Lett. 583, 481-486
    • (2009) FEBS Lett. , vol.583 , pp. 481-486
    • Mansfield, T.A.1    Schultes, N.P.2    Mourad, G.S.3
  • 24
    • 0028045064 scopus 로고
    • Adenine transport in Escherichia coli
    • Burton, K. (1994) Adenine transport in Escherichia coli. Proc. Biol. Sci. 255, 153-157
    • (1994) Proc. Biol. Sci. , vol.255 , pp. 153-157
    • Burton, K.1
  • 26
    • 0025675856 scopus 로고
    • High-efficiency transformation of Escherichia coli with plasmids
    • Inoue, H., Nojima, H., and Okayama, H. (1990) High-efficiency transformation of Escherichia coli with plasmids. Gene 96, 23-28
    • (1990) Gene , vol.96 , pp. 23-28
    • Inoue, H.1    Nojima, H.2    Okayama, H.3
  • 27
    • 0018850485 scopus 로고
    • Lactose carrier protein of Escherichia coli: Structure and expression of plasmids carrying the Y gene of the lac operon
    • Teather, R. M., Bramhall, J., Riede, I., Wright, J. K., Fürst, M., Aichele, G., Wilhelm, U., and Overath, P. (1980) Lactose carrier protein of Escherichia coli: structure and expression of plasmids carrying the Y gene of the lac operon. Eur. J. Biochem. 108, 223-231
    • (1980) Eur. J. Biochem. , vol.108 , pp. 223-231
    • Teather, R.M.1    Bramhall, J.2    Riede, I.3    Wright, J.K.4    Fürst, M.5    Aichele, G.6    Wilhelm, U.7    Overath, P.8
  • 28
    • 0024520745 scopus 로고
    • Site-directed mutagenesis by overlap extension using the polymerase chain reaction
    • DOI 10.1016/0378-1119(89)90358-2
    • Ho, S. N., Hunt, H. D., Horton, R. M., Pullen, J. K., and Pease, L. R. (1989) Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene 77, 51-59 (Pubitemid 19125653)
    • (1989) Gene , vol.77 , Issue.1 , pp. 51-59
    • Ho, S.N.1    Hunt, H.D.2    Horton, R.M.3    Pullen, J.K.4    Pease, L.R.5
  • 29
    • 24044436844 scopus 로고    scopus 로고
    • Experimentally constrained topology models for 51,208 bacterial inner membrane proteins
    • DOI 10.1016/j.jmb.2005.07.053, PII S0022283605008545
    • Granseth, E., Daley, D. O., Rapp, M., Melén, K., and von Heijne, G. (2005) Experimentally constrained topology models for 51,208 bacterial inner membrane proteins. J. Mol. Biol. 352, 489-494 (Pubitemid 41225461)
    • (2005) Journal of Molecular Biology , vol.352 , Issue.3 , pp. 489-494
    • Granseth, E.1    Daley, D.O.2    Rapp, M.3    Melen, K.4    Von Heijne, G.5
  • 30
    • 0042622380 scopus 로고    scopus 로고
    • SWISS-MODEL: An automated protein homology-modeling server
    • DOI 10.1093/nar/gkg520
    • Schwede, T., Kopp, J., Guex, N., and Peitsch, M. C. (2003) SWISS-MODEL: an automated protein homology-modeling server. Nucleic Acids Res. 31, 3381-3385 (Pubitemid 37442164)
    • (2003) Nucleic Acids Research , vol.31 , Issue.13 , pp. 3381-3385
    • Schwede, T.1    Kopp, J.2    Guex, N.3    Peitsch, M.C.4
  • 31
    • 0019330788 scopus 로고
    • Quantitative measurements of membrane potential in Escherichia coli
    • Felle, H., Porter, J. S., Slayman, C. L., and Kaback, H. R. (1980) Quantitative measurements of membrane potential in Escherichia coli. Biochemistry 19, 3585-3590
    • (1980) Biochemistry , vol.19 , pp. 3585-3590
    • Felle, H.1    Porter, J.S.2    Slayman, C.L.3    Kaback, H.R.4
  • 32
    • 0015948722 scopus 로고
    • Mechanisms of active transport in isolated bacterial membrane vesicles. 18. The mechanism of action of carbonylcyanide m-chlorophenylhydrazone
    • Kaback, H. R., Reeves, J. P., Short, S. A., and Lombardi, F. J. (1974) Mechanisms of active transport in isolated bacterial membrane vesicles. 18. The mechanism of action of carbonylcyanide m-chlorophenylhydrazone. Arch. Biochem. Biophys. 160, 215-222
    • (1974) Arch. Biochem. Biophys. , vol.160 , pp. 215-222
    • Kaback, H.R.1    Reeves, J.P.2    Short, S.A.3    Lombardi, F.J.4
  • 33
    • 0032762639 scopus 로고    scopus 로고
    • Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli
    • Cusa, E., Obradors, N., Baldomà, L., Badía, J., and Aguilar, J. (1999) Genetic analysis of a chromosomal region containing genes required for assimilation of allantoin nitrogen and linked glyoxylate metabolism in Escherichia coli. J. Bacteriol. 181, 7479-7484
    • (1999) J. Bacteriol. , vol.181 , pp. 7479-7484
    • Cusa, E.1    Obradors, N.2    Baldomà, L.3    Badía, J.4    Aguilar, J.5
  • 34
    • 33646580070 scopus 로고    scopus 로고
    • Completing the uric acid degradation pathway through phylogenetic comparison of whole genomes
    • DOI 10.1038/nchembio768, PII NCHEMBIO768
    • Ramazzina, I., Folli, C., Secchi, A., Berni, R., and Percudani, R. (2006) Completing the uric acid degradation pathway through phylogenetic comparison of whole genomes. Nat. Chem. Biol. 2, 144-148 (Pubitemid 44323865)
    • (2006) Nature Chemical Biology , vol.2 , Issue.3 , pp. 144-148
    • Ramazzina, I.1    Folli, C.2    Secchi, A.3    Berni, R.4    Percudani, R.5
  • 35
    • 0036923450 scopus 로고    scopus 로고
    • Regulation of the Escherichia coli allantoin regulon: Coordinated function of the repressor AllR and the activator AllS
    • DOI 10.1016/S0022-2836(02)01134-8
    • Rintoul, M. R., Cusa, E., Baldomà, L., Badia, J., Reitzer, L., and Aguilar, J. (2002) Regulation of the Escherichia coli allantoin regulon: coordinated function of the repressor AllR and the activator AllS. J. Mol. Biol. 324, 599-610 (Pubitemid 36044100)
    • (2002) Journal of Molecular Biology , vol.324 , Issue.4 , pp. 599-610
    • Rintoul, M.R.1    Cusa, E.2    Baldoma, L.3    Badia, J.4    Reitzer, L.5    Aguilar, J.6
  • 36
    • 24044525647 scopus 로고    scopus 로고
    • Transthyretin-related proteins function to facilitate the hydrolysis of 5-hydroxyisourate, the end product of the uricase reaction
    • DOI 10.1016/j.febslet.2005.07.056, PII S001457930500918X
    • Lee, Y., Lee, D. H., Kho, C. W., Lee, A. Y., Jang, M., Cho, S., Lee, C. H., Lee, J. S., Myung, P. K., Park, B. C., and Park, S. G. (2005) Transthyretin-related proteins function to facilitate the hydrolysis of 5-hydroxyisourate, the end product of the uricase reaction. FEBS Lett. 579, 4769-4774 (Pubitemid 41218661)
    • (2005) FEBS Letters , vol.579 , Issue.21 , pp. 4769-4774
    • Lee, Y.1    Do, H.L.2    Chang, W.K.3    Ah, Y.L.4    Jang, M.5    Cho, S.6    Choong, H.L.7    Jong, S.L.8    Pyung, K.M.9    Park, B.C.10    Park, S.G.11
  • 37
    • 33748969507 scopus 로고    scopus 로고
    • Structure of Zebra fish HIUase: Insights into Evolution of an Enzyme to a Hormone Transporter
    • DOI 10.1016/j.jmb.2006.07.079, PII S0022283606009764
    • Zanotti, G., Cendron, L., Ramazzina, I., Folli, C., Percudani, R., and Berni, R. (2006) Structure of zebra fish HIUase: insights into evolution of an enzyme to a hormone transporter. J. Mol. Biol. 363, 1-9 (Pubitemid 44437562)
    • (2006) Journal of Molecular Biology , vol.363 , Issue.1 , pp. 1-9
    • Zanotti, G.1    Cendron, L.2    Ramazzina, I.3    Folli, C.4    Percudani, R.5    Berni, R.6
  • 38
    • 70349243456 scopus 로고    scopus 로고
    • Evolutionary changes to transthyretin: Structure and function of a transthyretin-like ancestral protein
    • Hennebry, S. C. (2009) Evolutionary changes to transthyretin: structure and function of a transthyretin-like ancestral protein. FEBS J. 276, 5367-5379
    • (2009) FEBS J. , vol.276 , pp. 5367-5379
    • Hennebry, S.C.1
  • 39
    • 57349137274 scopus 로고    scopus 로고
    • The hpx genetic system for hypoxanthine assimilation as a nitrogen source in Klebsiella pneumoniae: Gene organization and transcriptional regulation
    • de la Riva, L., Badia, J., Aguilar, J., Bender, R. A., and Baldoma, L. (2008) The hpx genetic system for hypoxanthine assimilation as a nitrogen source in Klebsiella pneumoniae: gene organization and transcriptional regulation. J. Bacteriol. 190, 7892-7903
    • (2008) J. Bacteriol. , vol.190 , pp. 7892-7903
    • De La Riva, L.1    Badia, J.2    Aguilar, J.3    Bender, R.A.4    Baldoma, L.5
  • 40
    • 63449129765 scopus 로고    scopus 로고
    • Purine utilization by Klebsiella oxytoca M5al: Genes for ring-oxidizing and -opening enzymes
    • Pope, S. D., Chen, L. L., and Stewart, V. (2009) Purine utilization by Klebsiella oxytoca M5al: genes for ring-oxidizing and -opening enzymes. J. Bacteriol. 191, 1006-1017
    • (2009) J. Bacteriol. , vol.191 , pp. 1006-1017
    • Pope, S.D.1    Chen, L.L.2    Stewart, V.3
  • 41
    • 65249186468 scopus 로고    scopus 로고
    • Biochemical characterization of the HpxO enzyme from Klebsiella pneumoniae, a novel FAD-dependent urate oxidase
    • O'Leary, S. E., Hicks, K. A., Ealick, S. E., and Begley, T. P. (2009) Biochemical characterization of the HpxO enzyme from Klebsiella pneumoniae, a novel FAD-dependent urate oxidase. Biochemistry 48, 3033-3035
    • (2009) Biochemistry , vol.48 , pp. 3033-3035
    • O'Leary, S.E.1    Hicks, K.A.2    Ealick, S.E.3    Begley, T.P.4
  • 44
    • 40149096673 scopus 로고    scopus 로고
    • Functional role of conserved transmembrane segment 1 residues in human sodium-dependent vitamin C transported
    • DOI 10.1021/bi701666q
    • Varma, S., Campbell, C. E., and Kuo, S. M. (2008) Functional role of conserved transmembrane segment 1 residues in human sodium-dependent vitamin C transporters. Biochemistry 47, 2952-2960 (Pubitemid 351328848)
    • (2008) Biochemistry , vol.47 , Issue.9 , pp. 2952-2960
    • Varma, S.1    Campbell, C.E.2    Kuo, S.-M.3


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