메뉴 건너뛰기




Volumn 72, Issue 1, 2010, Pages 139-146

Expression and purification of a functional uric acid-xanthine transporter (UapA)

Author keywords

Membrane protein; Nucleobase Ascorbate Transporters; Overexpression; Purification; Uptake assay; Uric acid xanthine permease

Indexed keywords

CARRIER PROTEIN; FUNGAL PROTEIN; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; UAPA PROTEIN, ASPERGILLUS NIDULANS;

EID: 77951119756     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2010.02.002     Document Type: Article
Times cited : (18)

References (46)
  • 1
    • 42149085549 scopus 로고    scopus 로고
    • The nucleobase-ascorbate transporter (NAT) family: genomics, evolution, structure-function relationships and physiological role
    • Gournas C., Papageorgiou I., and Diallinas G. The nucleobase-ascorbate transporter (NAT) family: genomics, evolution, structure-function relationships and physiological role. Mol. Biosyst. 4 (2008) 404-416
    • (2008) Mol. Biosyst. , vol.4 , pp. 404-416
    • Gournas, C.1    Papageorgiou, I.2    Diallinas, G.3
  • 2
    • 67649437020 scopus 로고    scopus 로고
    • Structure-function relationships in the nucleobase-ascorbate transporter (NAT) family: lessons from model microbial genetic systems
    • Diallinas G., and Gournas C. Structure-function relationships in the nucleobase-ascorbate transporter (NAT) family: lessons from model microbial genetic systems. Channels 2 (2008) 363-372
    • (2008) Channels , vol.2 , pp. 363-372
    • Diallinas, G.1    Gournas, C.2
  • 4
    • 0024554561 scopus 로고
    • The purine path to chemotherapy
    • Elion G. The purine path to chemotherapy. Science 244 (1989) 41-47
    • (1989) Science , vol.244 , pp. 41-47
    • Elion, G.1
  • 5
    • 0035071830 scopus 로고    scopus 로고
    • Identification and characterization of trypanocides by functional expression of an adenosine transporter from Trypanosoma brucei in yeast
    • Maser P., Vogel D., Schmid C., Raz B., and Kaminsky R. Identification and characterization of trypanocides by functional expression of an adenosine transporter from Trypanosoma brucei in yeast. J. Mol. Med. 79 (2001) 121-127
    • (2001) J. Mol. Med. , vol.79 , pp. 121-127
    • Maser, P.1    Vogel, D.2    Schmid, C.3    Raz, B.4    Kaminsky, R.5
  • 6
    • 20444463884 scopus 로고    scopus 로고
    • Cloning and functional characterization of two bacterial members of the NAT/NCS2 family in Escherichia coli
    • Karatza P., and Frillingos S. Cloning and functional characterization of two bacterial members of the NAT/NCS2 family in Escherichia coli. Mol. Membr. Biol. 22 (2005) 251-261
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 251-261
    • Karatza, P.1    Frillingos, S.2
  • 7
    • 0034143440 scopus 로고    scopus 로고
    • A new family of high-affinity transporters for adenine, cytosine, and purine derivatives in Arabidopsis
    • Gillissen B., Burkle L., Andre B., Kuhn C., Rentsch D., Brandl B., and Frommer W.B. A new family of high-affinity transporters for adenine, cytosine, and purine derivatives in Arabidopsis. Plant Cell 12 (2000) 291-300
    • (2000) Plant Cell , vol.12 , pp. 291-300
    • Gillissen, B.1    Burkle, L.2    Andre, B.3    Kuhn, C.4    Rentsch, D.5    Brandl, B.6    Frommer, W.B.7
  • 8
    • 33750585062 scopus 로고    scopus 로고
    • Identification and expression analysis of twelve members of the nucleobase-ascorbate transporter (NAT) gene family in Arabidopsis thaliana
    • Maurino V.G., Grube E., Zielinski J., Schild A., Fischer K., and Flugge U.I. Identification and expression analysis of twelve members of the nucleobase-ascorbate transporter (NAT) gene family in Arabidopsis thaliana. Plant Cell. Physiol. 47 (2006) 1381-1393
    • (2006) Plant Cell. Physiol. , vol.47 , pp. 1381-1393
    • Maurino, V.G.1    Grube, E.2    Zielinski, J.3    Schild, A.4    Fischer, K.5    Flugge, U.I.6
  • 10
    • 77951118005 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
    • (Epub ahead of print)
    • Yamamoto S., Inoue K., Murata T., Kamigaso S., Yasujima T., Maeda J.Y., Yoshida Y., Ohta K.Y., and Yuasa H. 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. (2009) (Epub ahead of print)
    • (2009) J. Biol. Chem.
    • 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
  • 11
    • 20444448199 scopus 로고    scopus 로고
    • The nucleobase-ascorbate transporter (NAT) signature motif in UapA defines the function of the purine translocation pathway
    • Koukaki M., Vlanti A., Goudela S., Pantazopoulou A., Gioule H., Tournaviti S., and Diallinas G. The nucleobase-ascorbate transporter (NAT) signature motif in UapA defines the function of the purine translocation pathway. J. Mol. Biol. 350 (2005) 499-513
    • (2005) J. Mol. Biol. , vol.350 , pp. 499-513
    • Koukaki, M.1    Vlanti, A.2    Goudela, S.3    Pantazopoulou, A.4    Gioule, H.5    Tournaviti, S.6    Diallinas, G.7
  • 12
    • 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
    • Diallinas G., Valdez J., Sophianopoulou V., Rosa A., and Scazzocchio C. Chimeric purine transporters of Aspergillus nidulans define a domain critical for function and specificity conserved in bacterial, plant and metazoan homologues. EMBO J. 17 (1998) 3827-3837
    • (1998) EMBO J. , vol.17 , pp. 3827-3837
    • Diallinas, G.1    Valdez, J.2    Sophianopoulou, V.3    Rosa, A.4    Scazzocchio, C.5
  • 13
    • 0034105567 scopus 로고    scopus 로고
    • Amino acid residues N450 and Q449 are critical for the uptake capacity and specificity of UapA, a prototype of a nucleobase-ascorbate transporter family
    • Meintanis C., Karagouni A.D., and Diallinas G. Amino acid residues N450 and Q449 are critical for the uptake capacity and specificity of UapA, a prototype of a nucleobase-ascorbate transporter family. Mol. Membr. Biol. 17 (2000) 47-57
    • (2000) Mol. Membr. Biol. , vol.17 , pp. 47-57
    • Meintanis, C.1    Karagouni, A.D.2    Diallinas, G.3
  • 15
    • 0024676807 scopus 로고
    • A gene coding for the uric acid-xanthine permease of Aspergillus nidulans: inactivational cloning, characterization, and sequence of a cis-acting mutation
    • Diallinas G., and Scazzocchio C. A gene coding for the uric acid-xanthine permease of Aspergillus nidulans: inactivational cloning, characterization, and sequence of a cis-acting mutation. Genetics 122 (1989) 341-350
    • (1989) Genetics , vol.122 , pp. 341-350
    • Diallinas, G.1    Scazzocchio, C.2
  • 16
    • 0028904965 scopus 로고
    • Genetic and molecular characterization of a gene encoding a wide specificity purine permease of Aspergillus nidulans reveals a novel family of transporters conserved in prokaryotes and eukaryotes
    • Diallinas G., Gorfinkiel L., Arst Jr. H.N., Cecchetto G., and Scazzocchio C. Genetic and molecular characterization of a gene encoding a wide specificity purine permease of Aspergillus nidulans reveals a novel family of transporters conserved in prokaryotes and eukaryotes. J. Biol. Chem. 270 (1995) 8610-8622
    • (1995) J. Biol. Chem. , vol.270 , pp. 8610-8622
    • Diallinas, G.1    Gorfinkiel, L.2    Arst Jr., H.N.3    Cecchetto, G.4    Scazzocchio, C.5
  • 17
    • 0027490676 scopus 로고
    • Sequence and regulation of the uapA gene encoding a uric acid-xanthine permease in the fungus Aspergillus nidulans
    • Gorfinkiel L., Diallinas G., and Scazzocchio C. Sequence and regulation of the uapA gene encoding a uric acid-xanthine permease in the fungus Aspergillus nidulans. J. Biol. Chem. 268 (1993) 23376-23381
    • (1993) J. Biol. Chem. , vol.268 , pp. 23376-23381
    • Gorfinkiel, L.1    Diallinas, G.2    Scazzocchio, C.3
  • 18
    • 1942487886 scopus 로고    scopus 로고
    • Transcription of purine transporter genes is activated during the isotropic growth phase of Aspergillus nidulans conidia
    • Amillis S., Cecchetto G., Sophianopoulou V., Koukaki M., Scazzocchio C., and Diallinas G. Transcription of purine transporter genes is activated during the isotropic growth phase of Aspergillus nidulans conidia. Mol. Microbiol. 52 (2004) 205-216
    • (2004) Mol. Microbiol. , vol.52 , pp. 205-216
    • Amillis, S.1    Cecchetto, G.2    Sophianopoulou, V.3    Koukaki, M.4    Scazzocchio, C.5    Diallinas, G.6
  • 19
    • 20444437463 scopus 로고    scopus 로고
    • Comparative substrate recognition by bacterial and fungal purine transporters of the NAT/NCS2 family
    • Goudela S., Karatza P., Koukaki M., Frillingos S., and Diallinas G. Comparative substrate recognition by bacterial and fungal purine transporters of the NAT/NCS2 family. Mol. Membr. Biol. 22 (2005) 263-275
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 263-275
    • Goudela, S.1    Karatza, P.2    Koukaki, M.3    Frillingos, S.4    Diallinas, G.5
  • 20
    • 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. Specific interdomain synergy in the UapA transporter determines its unique specificity for uric acid among NAT carriers. J. Mol. Biol. 382 (2008) 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
  • 21
    • 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 alpha-helix
    • Karatza P., Panos P., Georgopoulou E., and Frillingos S. 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 alpha-helix. J. Biol. Chem. 281 (2006) 39881-39890
    • (2006) J. Biol. Chem. , vol.281 , pp. 39881-39890
    • Karatza, P.1    Panos, P.2    Georgopoulou, E.3    Frillingos, S.4
  • 22
    • 0035798405 scopus 로고    scopus 로고
    • Substitution F569S converts UapA, a specific uric acid-xanthine transporter, into a broad specificity transporter for purine-related solutes
    • Amillis S., Koukaki M., and Diallinas G. Substitution F569S converts UapA, a specific uric acid-xanthine transporter, into a broad specificity transporter for purine-related solutes. J. Mol. Biol. 311 (2001) 765-774
    • (2001) J. Mol. Biol. , vol.311 , pp. 765-774
    • Amillis, S.1    Koukaki, M.2    Diallinas, G.3
  • 23
    • 33644947026 scopus 로고    scopus 로고
    • A novel-type substrate-selectivity filter and ER-exit determinants in the UapA purine transporter
    • Vlanti A., Amillis S., Koukaki M., and Diallina G. A novel-type substrate-selectivity filter and ER-exit determinants in the UapA purine transporter. J. Mol. Biol. 357 (2006) 808-819
    • (2006) J. Mol. Biol. , vol.357 , pp. 808-819
    • Vlanti, A.1    Amillis, S.2    Koukaki, M.3    Diallina, G.4
  • 24
    • 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. Cysteine-scanning analysis of putative helix XII in the YgfO xanthine permease: ILE-432 and ASN-430 are important. J. Biol. Chem. 283 (2008) 13666-13678
    • (2008) J. Biol. Chem. , vol.283 , pp. 13666-13678
    • Papakostas, K.1    Georgopoulou, E.2    Frillingos, S.3
  • 25
    • 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. 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 (2009) 24257-24268
    • (2009) J. Biol. Chem. , vol.284 , pp. 24257-24268
    • Karena, E.1    Frillingos, S.2
  • 27
    • 36148942092 scopus 로고    scopus 로고
    • Breaking the bottleneck: eukaryotic membrane protein expression for high-resolution structural studies
    • Midgett C.R., and Madden D.R. Breaking the bottleneck: eukaryotic membrane protein expression for high-resolution structural studies. J. Struct. Biol. 160 (2007) 265-274
    • (2007) J. Struct. Biol. , vol.160 , pp. 265-274
    • Midgett, C.R.1    Madden, D.R.2
  • 28
    • 0041742381 scopus 로고    scopus 로고
    • Characterisation of mammalian GLUT glucose transporters in a heterologous yeast expression system
    • Wieczorke R., Dlugai S., Krampe S., and Boles E. Characterisation of mammalian GLUT glucose transporters in a heterologous yeast expression system. Cell. Physiol. Biochem. 13 (2003) 123-134
    • (2003) Cell. Physiol. Biochem. , vol.13 , pp. 123-134
    • Wieczorke, R.1    Dlugai, S.2    Krampe, S.3    Boles, E.4
  • 29
    • 33644893341 scopus 로고    scopus 로고
    • Heterologous expression of mammalian Na/H antiporters in Saccharomyces cerevisiae
    • Flegelova H., Haguenauer-Tsapis R., and Sychrova H. Heterologous expression of mammalian Na/H antiporters in Saccharomyces cerevisiae. Biochim. Biophys. Acta 1760 (2006) 504-516
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 504-516
    • Flegelova, H.1    Haguenauer-Tsapis, R.2    Sychrova, H.3
  • 30
    • 0034176255 scopus 로고    scopus 로고
    • Use of chemical chaperones in the yeast Saccharomyces cerevisiae to enhance heterologous membrane protein expression: high-yield expression and purification of human P-glycoprotein
    • Figler R.A., Omote H., Nakamoto R.K., and Al-Shawi M.K. Use of chemical chaperones in the yeast Saccharomyces cerevisiae to enhance heterologous membrane protein expression: high-yield expression and purification of human P-glycoprotein. Arch. Biochem. Biophys. 376 (2000) 34-36
    • (2000) Arch. Biochem. Biophys. , vol.376 , pp. 34-36
    • Figler, R.A.1    Omote, H.2    Nakamoto, R.K.3    Al-Shawi, M.K.4
  • 31
    • 0034677907 scopus 로고    scopus 로고
    • Biochemical characterization and subcellular localization of the sterol C-24(28) reductase, erg4p, from the yeast Saccharomyces cerevisiae
    • Zweytick D., Hrastnik C., Kohlwein S.D., and Daum G. Biochemical characterization and subcellular localization of the sterol C-24(28) reductase, erg4p, from the yeast Saccharomyces cerevisiae. FEBS Lett. 470 (2000) 83-87
    • (2000) FEBS Lett. , vol.470 , pp. 83-87
    • Zweytick, D.1    Hrastnik, C.2    Kohlwein, S.D.3    Daum, G.4
  • 32
    • 4344628611 scopus 로고    scopus 로고
    • Co-expression of a mammalian accessory trafficking protein enables functional expression of the rat MCT1 monocarboxylate transporter in Saccharomyces cerevisiae
    • Makuc J., Cappellaro C., and Boles E. Co-expression of a mammalian accessory trafficking protein enables functional expression of the rat MCT1 monocarboxylate transporter in Saccharomyces cerevisiae. FEMS Yeast Res. 4 (2004) 795-801
    • (2004) FEMS Yeast Res. , vol.4 , pp. 795-801
    • Makuc, J.1    Cappellaro, C.2    Boles, E.3
  • 33
    • 35348832935 scopus 로고    scopus 로고
    • High-throughput fluorescent-based optimization of eukaryotic membrane protein overexpression and purification in Saccharomyces cerevisiae
    • Newstead S., Kim H., von Heijne G., Iwata S., and Drew D. High-throughput fluorescent-based optimization of eukaryotic membrane protein overexpression and purification in Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 104 (2007) 13936-13941
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 13936-13941
    • Newstead, S.1    Kim, H.2    von Heijne, G.3    Iwata, S.4    Drew, D.5
  • 34
    • 43149098999 scopus 로고    scopus 로고
    • GFP-based optimization scheme for the overexpression and purification of eukaryotic membrane proteins in Saccharomyces cerevisiae
    • Drew D., Newstead S., Sonoda Y., Kim H., von Heijne G., and Iwata S. GFP-based optimization scheme for the overexpression and purification of eukaryotic membrane proteins in Saccharomyces cerevisiae. Nat. Protoc. 3 (2008) 784-798
    • (2008) Nat. Protoc. , vol.3 , pp. 784-798
    • Drew, D.1    Newstead, S.2    Sonoda, Y.3    Kim, H.4    von Heijne, G.5    Iwata, S.6
  • 35
    • 0020773011 scopus 로고
    • Study of the positive control of the general amino-acid permease and other ammonia-sensitive uptake systems by the product of the NPR1 gene in the yeast Saccharomyces cerevisiae
    • Grenson M. Study of the positive control of the general amino-acid permease and other ammonia-sensitive uptake systems by the product of the NPR1 gene in the yeast Saccharomyces cerevisiae. Eur. J. Biochem. 133 (1983) 141-144
    • (1983) Eur. J. Biochem. , vol.133 , pp. 141-144
    • Grenson, M.1
  • 36
    • 33847375937 scopus 로고    scopus 로고
    • Membrane chaperone Shr3 assists in folding amino acid permeases preventing precocious ERAD
    • Kota J., Gilstring C.F., and Ljungdahl P.O. Membrane chaperone Shr3 assists in folding amino acid permeases preventing precocious ERAD. J. Cell Biol. 176 (2007) 617-628
    • (2007) J. Cell Biol. , vol.176 , pp. 617-628
    • Kota, J.1    Gilstring, C.F.2    Ljungdahl, P.O.3
  • 37
    • 0022755757 scopus 로고
    • The PEP4 gene encodes an aspartyl protease implicated in the posttranslational regulation of Saccharomyces cerevisiae vacuolar hydrolases
    • Woolford C.A., Daniels L.B., Park F.J., Jones E.W., Van Arsdell J.N., and Innis M.A. The PEP4 gene encodes an aspartyl protease implicated in the posttranslational regulation of Saccharomyces cerevisiae vacuolar hydrolases. Mol. Cell. Biol. 6 (1986) 2500-2510
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 2500-2510
    • Woolford, C.A.1    Daniels, L.B.2    Park, F.J.3    Jones, E.W.4    Van Arsdell, J.N.5    Innis, M.A.6
  • 38
    • 0942276403 scopus 로고    scopus 로고
    • The AzgA purine transporter of Aspergillus nidulans. Characterization of a protein belonging to a new phylogenetic cluster
    • Cecchetto G., Amillis S., Diallinas G., Scazzocchio C., and Drevet C. The AzgA purine transporter of Aspergillus nidulans. Characterization of a protein belonging to a new phylogenetic cluster. J. Biol. Chem. 279 (2004) 3132-3141
    • (2004) J. Biol. Chem. , vol.279 , pp. 3132-3141
    • Cecchetto, G.1    Amillis, S.2    Diallinas, G.3    Scazzocchio, C.4    Drevet, C.5
  • 39
    • 0022474744 scopus 로고
    • Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication
    • Compton L.A., and Johnson W.C. Analysis of protein circular dichroism spectra for secondary structure using a simple matrix multiplication. Anal. Biochem. 155 (1986) 155-167
    • (1986) Anal. Biochem. , vol.155 , pp. 155-167
    • Compton, L.A.1    Johnson, W.C.2
  • 40
    • 0033118410 scopus 로고    scopus 로고
    • Functional production and reconstitution of the human equilibrative nucleoside transporter (hENT 1) in Saccharomyces cerevisiae. Interaction of inhibitors of nucleoside transport with recombinant hENT 1 and a glycosylation-defective derivative (hENT 1/N48Q)
    • Vickers M.F., Mani R.S., Sundaram M., Hogue D.L., Young J.D., Baldwin S.A., and Cass C.E. Functional production and reconstitution of the human equilibrative nucleoside transporter (hENT 1) in Saccharomyces cerevisiae. Interaction of inhibitors of nucleoside transport with recombinant hENT 1 and a glycosylation-defective derivative (hENT 1/N48Q). Biochem. J. 339 (2001) 21-32
    • (2001) Biochem. J. , vol.339 , pp. 21-32
    • Vickers, M.F.1    Mani, R.S.2    Sundaram, M.3    Hogue, D.L.4    Young, J.D.5    Baldwin, S.A.6    Cass, C.E.7
  • 42
    • 0035572666 scopus 로고    scopus 로고
    • Functional expression and cellular localization of a green fluorescent protein-tagged proline transporter in Aspergillus nidulans
    • Tavoularis S., Scazzocchio C., and Sophianopoulou V. Functional expression and cellular localization of a green fluorescent protein-tagged proline transporter in Aspergillus nidulans. Fungal Genet. Biol. 33 (2001) 115-125
    • (2001) Fungal Genet. Biol. , vol.33 , pp. 115-125
    • Tavoularis, S.1    Scazzocchio, C.2    Sophianopoulou, V.3
  • 43
    • 41549100692 scopus 로고    scopus 로고
    • Kinetic and mutational analysis of the Trypanosoma brucei NBT 1 nucleobase transporter expressed in Saccharomyces cerevisiae reveals structural similarities between ENT and MFS transporters
    • Papageorgiou I., De Koning H.P., Soteriadou K., and Diallinas G. Kinetic and mutational analysis of the Trypanosoma brucei NBT 1 nucleobase transporter expressed in Saccharomyces cerevisiae reveals structural similarities between ENT and MFS transporters. Int. J. Parasitol. 38 (2008) 641-653
    • (2008) Int. J. Parasitol. , vol.38 , pp. 641-653
    • Papageorgiou, I.1    De Koning, H.P.2    Soteriadou, K.3    Diallinas, G.4
  • 44
    • 42549104322 scopus 로고    scopus 로고
    • The Aspergillus nidulans FcyB cytosine-purine scavenger is highly expressed during germination and in reproductive compartments and is downregulated by endocytosis
    • Vlanti A., and Diallinas G. The Aspergillus nidulans FcyB cytosine-purine scavenger is highly expressed during germination and in reproductive compartments and is downregulated by endocytosis. Mol. Microbiol. 68 (2008) 959-977
    • (2008) Mol. Microbiol. , vol.68 , pp. 959-977
    • Vlanti, A.1    Diallinas, G.2
  • 45
    • 34249057464 scopus 로고    scopus 로고
    • Regulations of expression and kinetic modeling of substrate interactions of a uracil transporter in Aspergillus nidulans
    • Amillis S., Hamari Z., Roumelioti K., Scazzocchio C., and Diallinas G. Regulations of expression and kinetic modeling of substrate interactions of a uracil transporter in Aspergillus nidulans. Mol. Membr. Biol. 24 (2007) 206-214
    • (2007) Mol. Membr. Biol. , vol.24 , pp. 206-214
    • Amillis, S.1    Hamari, Z.2    Roumelioti, K.3    Scazzocchio, C.4    Diallinas, G.5
  • 46
    • 0242653300 scopus 로고
    • Biochemical and genetical studies of purine breakdown in Aspergillus
    • Darlington A.J., Scazzocchio C., and Pateman J.A. Biochemical and genetical studies of purine breakdown in Aspergillus. Nature 206 (1965) 599-600
    • (1965) Nature , vol.206 , pp. 599-600
    • Darlington, A.J.1    Scazzocchio, C.2    Pateman, J.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.