메뉴 건너뛰기




Volumn 47, Issue 1, 1996, Pages 595-626

Membrane transport carriers

Author keywords

Carriers of Saccharomyces cerevisiae; Helix packing; Membrane topology; Plant carriers; Regulation

Indexed keywords

ESCHERICHIA COLI; SACCHAROMYCES CEREVISIAE;

EID: 0001245939     PISSN: 10402519     EISSN: None     Source Type: Journal    
DOI: 10.1146/annurev.arplant.47.1.595     Document Type: Article
Times cited : (79)

References (191)
  • 1
    • 0022633030 scopus 로고
    • Sequences required for delivery and localization of the ADP/ATP translocator to the mitochondrial inner membrane
    • Adrian GS, McCammon MT, Montgomery DL, Douglas MG. 1986. Sequences required for delivery and localization of the ADP/ATP translocator to the mitochondrial inner membrane. Mol. Cell. Biol. 6:626-34
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 626-634
    • Adrian, G.S.1    McCammon, M.T.2    Montgomery, D.L.3    Douglas, M.G.4
  • 2
    • 0026472873 scopus 로고
    • Traffic ATPases: A superfamily of transport proteins operating from Escherichia coli to humans
    • Ames GFL, Mimura CS, Holbrook SR, Shyamala V. 1992. Traffic ATPases: a superfamily of transport proteins operating from Escherichia coli to humans. Adv. Enzymol. 65:1-47
    • (1992) Adv. Enzymol. , vol.65 , pp. 1-47
    • Ames, G.F.L.1    Mimura, C.S.2    Holbrook, S.R.3    Shyamala, V.4
  • 5
    • 0027394328 scopus 로고
    • Cloning and expression of the UGA4 gene coding for the inducible GABA-specific transport protein of Saccharomyces cerevisiae
    • Andre B, Hein B, Grenson M, Jauniaux JC. 1993. Cloning and expression of the UGA4 gene coding for the inducible GABA-specific transport protein of Saccharomyces cerevisiae. Mol. Gen. Genet. 237:17-25
    • (1993) Mol. Gen. Genet. , vol.237 , pp. 17-25
    • Andre, B.1    Hein, B.2    Grenson, M.3    Jauniaux, J.C.4
  • 6
    • 85009581671 scopus 로고
    • +/hexose cotransporter from Chlorella in Xenopus oocytes and its characterization with respect to sugar specificity, pH and membrane potential
    • +/hexose cotransporter from Chlorella in Xenopus oocytes and its characterization with respect to sugar specificity, pH and membrane potential. J. Plant Physiol. 141: 293-97
    • (1993) J. Plant Physiol. , vol.141 , pp. 293-297
    • Aoshima, H.1    Yamada, M.2    Sauer, N.3    Komor, E.4    Schobert, C.5
  • 8
    • 0022432935 scopus 로고
    • Isolation and sequence analysis of a cDNA encoding the ATP/ADP translocator of Zea mays L
    • Baker A, Leaver CJ. 1985. Isolation and sequence analysis of a cDNA encoding the ATP/ADP translocator of Zea mays L. Nucleic Acids Res. 13: 5857-67
    • (1985) Nucleic Acids Res. , vol.13 , pp. 5857-5867
    • Baker, A.1    Leaver, C.J.2
  • 9
    • 0026744892 scopus 로고
    • Probing the structure and function of the human erythrocyte glucose transporter
    • Baldwin SA. 1992. Probing the structure and function of the human erythrocyte glucose transporter. Biochem. Soc. Trans. 20:533-37
    • (1992) Biochem. Soc. Trans. , vol.20 , pp. 533-537
    • Baldwin, S.A.1
  • 10
    • 0028932101 scopus 로고
    • Yeast multidrug resistance: The PDR network
    • Balzi E, Goffeau A. 1995. Yeast multidrug resistance: the PDR network. J. Bioenerg. Biomembr. 27:71-76
    • (1995) J. Bioenerg. Biomembr. , vol.27 , pp. 71-76
    • Balzi, E.1    Goffeau, A.2
  • 11
    • 0024710298 scopus 로고
    • Two genes encode the adenine nucleotide translocator of maize mitochondria: Isolation, characterisation and expression of the structural genes
    • Bathgate B, Baker A, Leaver CJ. 1989. Two genes encode the adenine nucleotide translocator of maize mitochondria: isolation, characterisation and expression of the structural genes. Eur. J. Biochem. 183:303-10
    • (1989) Eur. J. Biochem. , vol.183 , pp. 303-310
    • Bathgate, B.1    Baker, A.2    Leaver, C.J.3
  • 12
    • 3142597081 scopus 로고
    • Characterization of the physiological role of the SNF3 gene of Saccharomyces
    • Bisson LF, Coons DM, Fong NM, Mazer J, Vagnoli P. 1995. Characterization of the physiological role of the SNF3 gene of Saccharomyces. Yeast 11:527
    • (1995) Yeast , vol.11 , pp. 527
    • Bisson, L.F.1    Coons, D.M.2    Fong, N.M.3    Mazer, J.4    Vagnoli, P.5
  • 16
    • 0026582987 scopus 로고
    • Function expression of a plant plasma membrane transporter in Xenopus oocytes
    • Boorer KJ, Forde BG, Leigh RA, Miller AJ. 1992. Function expression of a plant plasma membrane transporter in Xenopus oocytes. FEBS Lett. 302:166-68
    • (1992) FEBS Lett. , vol.302 , pp. 166-168
    • Boorer, K.J.1    Forde, B.G.2    Leigh, R.A.3    Miller, A.J.4
  • 17
    • 0028067762 scopus 로고
    • +/hexose cotransporter (STP1) from Arabidopsis thaliana expressed in Xenopus oocytes
    • +/hexose cotransporter (STP1) from Arabidopsis thaliana expressed in Xenopus oocytes. J. Biol. Chem. 269:1-8
    • (1994) J. Biol. Chem. , vol.269 , pp. 1-8
    • Boorer, K.J.1    Loo, D.D.F.2    Wright, E.M.3
  • 18
    • 0025865006 scopus 로고
    • The PHO84 gene of Saccharomyces cerevisiae encodes an : Inorganic phosphate transporter
    • Bun YM, Nishimura M, Harashima S, Oshima Y. 1991. The PHO84 gene of Saccharomyces cerevisiae encodes an : inorganic phosphate transporter. Mol. Cell. Biol. 11:3229-38
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3229-3238
    • Bun, Y.M.1    Nishimura, M.2    Harashima, S.3    Oshima, Y.4
  • 19
    • 4243107522 scopus 로고
    • Proton-coupled sugar and amino acid transporters in plants
    • Bush DR. 1993. Proton-coupled sugar and amino acid transporters in plants. Annu. Rev. Plant Physiol. Plant Mol. Biol. 44:513-42
    • (1993) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.44 , pp. 513-542
    • Bush, D.R.1
  • 21
    • 0025330038 scopus 로고
    • Lac permease of Escherichia coli. Topology and sequence elements promoting membrane insertion
    • Calamia J, Manoil C. 1990. Lac permease of Escherichia coli. Topology and sequence elements promoting membrane insertion. Proc. Natl. Acad. Sci. USA 87:4937-11
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4937-5011
    • Calamia, J.1    Manoil, C.2
  • 24
    • 85033001759 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 25
    • 0024121499 scopus 로고
    • The yeast SNF3 gene encodes a glucose transporter homologous to the mammalian protein
    • Celenza JL, Marshall-Carlson L. Carlson M. 1988. The yeast SNF3 gene encodes a glucose transporter homologous to the mammalian protein. Proc. Natl. Acad. Sci. USA 85:2130-34
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 2130-2134
    • Celenza, J.L.1    Marshall-Carlson, L.2    Carlson, M.3
  • 26
    • 0027140518 scopus 로고
    • Active transport of proton and calcium in higher plant cells
    • Chanson A. 1993. Active transport of proton and calcium in higher plant cells. Plant Physiol. Biochem. 31:943-55
    • (1993) Plant Physiol. Biochem. , vol.31 , pp. 943-955
    • Chanson, A.1
  • 27
    • 0024762032 scopus 로고
    • The maltose permease encoded by the MAL61 gene of Saccharomyces cerevisiae exhibits both sequence and structural homology to other sugar transporters
    • Cheng Q, Michels CA. 1989. The maltose permease encoded by the MAL61 gene of Saccharomyces cerevisiae exhibits both sequence and structural homology to other sugar transporters. Genetics 123:477-84
    • (1989) Genetics , vol.123 , pp. 477-484
    • Cheng, Q.1    Michels, C.A.2
  • 29
    • 84910418342 scopus 로고
    • The rate of absorption of a mixture of glucose and galactose
    • Cori CF. 1925. The rate of absorption of a mixture of glucose and galactose. Proc. Soc. Exp. Biol. Med. 23:290-91
    • (1925) Proc. Soc. Exp. Biol. Med. , vol.23 , pp. 290-291
    • Cori, C.F.1
  • 30
    • 0000340808 scopus 로고
    • The fate of sugar in the animal body. I. The rate of absorption of hexoses and pentoses from the intestinal tract
    • Cori CF. 1925. The fate of sugar in the animal body. I. The rate of absorption of hexoses and pentoses from the intestinal tract. J. Biol. Chem. 66:691-715
    • (1925) J. Biol. Chem. , vol.66 , pp. 691-715
    • Cori, C.F.1
  • 31
    • 0014784665 scopus 로고
    • Regulation of histidine uptake by a specific feedback inhibition of two histidine permeases in Saccharomyces cerevisiae
    • Crabeel M, Grenson M. 1970. Regulation of histidine uptake by a specific feedback inhibition of two histidine permeases in Saccharomyces cerevisiae. Eur. J. Biochem. 14:197-204
    • (1970) Eur. J. Biochem. , vol.14 , pp. 197-204
    • Crabeel, M.1    Grenson, M.2
  • 32
    • 0001102017 scopus 로고
    • Hypothesis for mechanism of intestinal active transport of sugars
    • Crane RK. 1962. Hypothesis for mechanism of intestinal active transport of sugars. Federation Proc. 21:891-95
    • (1962) Federation Proc. , vol.21 , pp. 891-895
    • Crane, R.K.1
  • 33
    • 0023024676 scopus 로고
    • Inactivation of the galactose transport system in Saccharomyces cerevisiae
    • DeJuan C, Lagunas R. 1986. Inactivation of the galactose transport system in Saccharomyces cerevisiae. FEBS Lett. 207:258-61
    • (1986) FEBS Lett. , vol.207 , pp. 258-261
    • DeJuan, C.1    Lagunas, R.2
  • 34
    • 0001085272 scopus 로고
    • A quantitative study of the roots and root hairs of a winter rye plant (Secale cereale)
    • Dittmer H. 1937. A quantitative study of the roots and root hairs of a winter rye plant (Secale cereale). Ann. J. Bot. 24:414-20
    • (1937) Ann. J. Bot. , vol.24 , pp. 414-420
    • Dittmer, H.1
  • 35
    • 0022427790 scopus 로고
    • The size of the lactose permease derived from rotational diffusion measurements
    • Dornmair K, Corin AF, Wright JK, Jähnig F. 1985. The size of the lactose permease derived from rotational diffusion measurements. EMBO J. 4:3633-38
    • (1985) EMBO J. , vol.4 , pp. 3633-3638
    • Dornmair, K.1    Corin, A.F.2    Wright, J.K.3    Jähnig, F.4
  • 36
    • 0027325787 scopus 로고
    • Insertion of lipids and proteins into bacterial membranes by fusion with liposomes
    • Driessen AJM, Konings WN. 1993. Insertion of lipids and proteins into bacterial membranes by fusion with liposomes. Methods Enzymol. 221:394-408
    • (1993) Methods Enzymol. , vol.221 , pp. 394-408
    • Driessen, A.J.M.1    Konings, W.N.2
  • 37
    • 0002602003 scopus 로고
    • The fidelity of DNA polymerase used in the polymerase chain reactions
    • ed. MJ Mc Pherson, Oxford: Oxford Univ. Press
    • Eckert KA, Kunkel TA. 1991. The fidelity of DNA polymerase used in the polymerase chain reactions. In PCR - A Practical Approach, ed. MJ Mc Pherson, pp. 225-44. Oxford: Oxford Univ. Press
    • (1991) PCR - A Practical Approach , pp. 225-244
    • Eckert, K.A.1    Kunkel, T.A.2
  • 38
    • 0018837284 scopus 로고
    • In vitro and in vivo products of E. coli lactose permease gene are identical
    • Ehring R, Beyreuther K, Wright JK. Overath P. 1980. In vitro and in vivo products of E. coli lactose permease gene are identical. Nature 283:537-40
    • (1980) Nature , vol.283 , pp. 537-540
    • Ehring, R.1    Beyreuther, K.2    Wright, J.K.3    Overath, P.4
  • 40
    • 0028800729 scopus 로고
    • Conversion of antagonist-binding site to metal-ion site in the tachykinin NK-1 receptor
    • Elling CE, Nielsen SM, Schwartz TW. 1995. Conversion of antagonist-binding site to metal-ion site in the tachykinin NK-1 receptor. Nature 374:74-77
    • (1995) Nature , vol.374 , pp. 74-77
    • Elling, C.E.1    Nielsen, S.M.2    Schwartz, T.W.3
  • 41
    • 0026077266 scopus 로고
    • The ADP/ATP translocator from potato has a long amino-terminal extension
    • Emmermann M, Braun HP, Schmitz UK. 1991. The ADP/ATP translocator from potato has a long amino-terminal extension. Curr. Genet. 20:405-40
    • (1991) Curr. Genet. , vol.20 , pp. 405-440
    • Emmermann, M.1    Braun, H.P.2    Schmitz, U.K.3
  • 42
    • 0006111446 scopus 로고
    • Roots
    • Epstein E. 1973. Roots. Sci. Am. 228/5: 48-58
    • (1973) Sci. Am. , vol.228 , Issue.5 , pp. 48-58
    • Epstein, E.1
  • 43
    • 0000524971 scopus 로고
    • Mechanisms of ion transport through plant cell membranes
    • Epstein E. 1973. Mechanisms of ion transport through plant cell membranes. Int. Rev. Cytol. 34:123-68
    • (1973) Int. Rev. Cytol. , vol.34 , pp. 123-168
    • Epstein, E.1
  • 44
    • 0000815628 scopus 로고
    • A kinetic study of the absorption of alkali cations by barley roots
    • Epstein E, Hagen CE. 1952. A kinetic study of the absorption of alkali cations by barley roots. Plant Physiol 27:457-74
    • (1952) Plant Physiol , vol.27 , pp. 457-474
    • Epstein, E.1    Hagen, C.E.2
  • 45
    • 0028333611 scopus 로고
    • Expression cloning of a mammalian proton-coupled oligopeptide transporter
    • Fei YJ, Kanai Y, Nussberger S, Ganapathy V, Leibach FH, et al. 1994. Expression cloning of a mammalian proton-coupled oligopeptide transporter. Nature 368:563-66
    • (1994) Nature , vol.368 , pp. 563-566
    • Fei, Y.J.1    Kanai, Y.2    Nussberger, S.3    Ganapathy, V.4    Leibach, F.H.5
  • 47
    • 0028371131 scopus 로고
    • Cloning and in vivo expression of functional triose phosphate/phosphate translocators from C3- and C4-plants: Evidence for the putative participation of specific amino acid residues in the recognition of phosphoenolpyruvate
    • Fischer K, Arbinger B, Kammerer B, Busch C, Brink S, et al. 1994. Cloning and in vivo expression of functional triose phosphate/phosphate translocators from C3- and C4-plants: evidence for the putative participation of specific amino acid residues in the recognition of phosphoenolpyruvate. Plant. J. 5: 215-26
    • (1994) Plant. J. , vol.5 , pp. 215-226
    • Fischer, K.1    Arbinger, B.2    Kammerer, B.3    Busch, C.4    Brink, S.5
  • 48
    • 0029007621 scopus 로고
    • Substrate specificity and expression profile of amino acid transporters (AAPs) in Arabidopsis
    • Fischer WN, Kwart M, Hummel S, Frommer WB. 1995. Substrate specificity and expression profile of amino acid transporters (AAPs) in Arabidopsis. J. Biol. Chem. 270:16315-20
    • (1995) J. Biol. Chem. , vol.270 , pp. 16315-16320
    • Fischer, W.N.1    Kwart, M.2    Hummel, S.3    Frommer, W.B.4
  • 49
    • 0029653518 scopus 로고
    • Whole-genome random sequencing and assembly of Haemophilus influenzae Rd
    • Fleischmann RD, Adams MD, White W, Clayton RA, Kirkness EF, et al. 1995. Whole-genome random sequencing and assembly of Haemophilus influenzae Rd. Science 269:449-604
    • (1995) Science , vol.269 , pp. 449-604
    • Fleischmann, R.D.1    Adams, M.D.2    White, W.3    Clayton, R.A.4    Kirkness, E.F.5
  • 50
    • 0024574552 scopus 로고
    • The triose phosphate-3-phosphoglycerate-phosphate translocator from spinach chloroplasts
    • Flügge UI, Fischer K, Gross A, Sebald W, Lottspeich F, Eckerskorn C. 1989. The triose phosphate-3-phosphoglycerate-phosphate translocator from spinach chloroplasts. EMBO J. 8:39-45
    • (1989) EMBO J. , vol.8 , pp. 39-45
    • Flügge, U.I.1    Fischer, K.2    Gross, A.3    Sebald, W.4    Lottspeich, F.5    Eckerskorn, C.6
  • 52
    • 0013802324 scopus 로고
    • Specific labeling and partial purification of the M protein, a component of the galactoside transport system of Escherichia coli
    • Fox CF, Kennedy EP. 1965. Specific labeling and partial purification of the M protein, a component of the galactoside transport system of Escherichia coli. Proc. Natl. Acad. Sci. USA 54:891-99
    • (1965) Proc. Natl. Acad. Sci. USA , vol.54 , pp. 891-899
    • Fox, C.F.1    Kennedy, E.P.2
  • 53
    • 0028200440 scopus 로고
    • Cloning of an Arabidopsis histidine transporting protein related to nitrate and peptide transporters
    • Frommer WB, Hummel S, Rentsch D. 1994. Cloning of an Arabidopsis histidine transporting protein related to nitrate and peptide transporters. FEBS Lett. 347: 185-89
    • (1994) FEBS Lett. , vol.347 , pp. 185-189
    • Frommer, W.B.1    Hummel, S.2    Rentsch, D.3
  • 54
    • 0027208074 scopus 로고
    • Expression cloning in yeast of a cDNA encoding a broad specificity amino acid permease from Arabidopsis thaliana
    • Frommer WB, Hummel S, Riesmeier JW. 1993. Expression cloning in yeast of a cDNA encoding a broad specificity amino acid permease from Arabidopsis thaliana. Proc. Natl. Acad. Sci. USA 90:5944-48
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5944-5948
    • Frommer, W.B.1    Hummel, S.2    Riesmeier, J.W.3
  • 57
    • 0028836545 scopus 로고
    • Heterologous expression of genes in bacterial, fungal, animal, and plant cells
    • Frommer WB, Ninnemann O. 1995. Heterologous expression of genes in bacterial, fungal, animal, and plant cells. Annu. Rev. Plant Physiol. Plant Mol. Biol. 46:419-44
    • (1995) Annu. Rev. Plant Physiol. Plant Mol. Biol. , vol.46 , pp. 419-444
    • Frommer, W.B.1    Ninnemann, O.2
  • 59
    • 0026463553 scopus 로고
    • Molecular genetics of yeast ion transport
    • Gaber RF. 1992. Molecular genetics of yeast ion transport. Int. Rev. Cytol. 137A: 299-353
    • (1992) Int. Rev. Cytol. , vol.137 A , pp. 299-353
    • Gaber, R.F.1
  • 60
    • 0024042922 scopus 로고
    • TRK1 encodes a plasma membrane protein required for high-affinity potassium transport in Saccharomyces cerevisiae
    • Gaber RF, Styles CA, Fink GR. 1988. TRK1 encodes a plasma membrane protein required for high-affinity potassium transport in Saccharomyces cerevisiae. Mol Cell. Biol. 8:2848-59
    • (1988) Mol Cell. Biol. , vol.8 , pp. 2848-2859
    • Gaber, R.F.1    Styles, C.A.2    Fink, G.R.3
  • 61
    • 0030020457 scopus 로고    scopus 로고
    • Expression of the PmSUC1 sucrose carrier gene from Plantago major L. is induced during seed development
    • Gahrtz M, Schmelzer E, Stolz J, Sauer N. 1996. Expression of the PmSUC1 sucrose carrier gene from Plantago major L. is induced during seed development. Plant J. 9:93-100
    • (1996) Plant J. , vol.9 , pp. 93-100
    • Gahrtz, M.1    Schmelzer, E.2    Stolz, J.3    Sauer, N.4
  • 62
    • 0028533453 scopus 로고
    • + symporter from Plantaga major supports the model of apoplastic phloem loading
    • + symporter from Plantaga major supports the model of apoplastic phloem loading. Plant. J. 6:697-706
    • (1994) Plant. J. , vol.6 , pp. 697-706
    • Gahrtz, M.1    Stolz, J.2    Sauer, N.3
  • 63
    • 0000676550 scopus 로고
    • Energy yielding metabolism in yeast
    • ed. JS Harrison, AH Rose, New York: Academic. 2nd ed.
    • Gancedo C, Serrano R. 1989. Energy yielding metabolism in yeast. In The Yeasts, ed. JS Harrison, AH Rose, 3: 205-59. New York: Academic. 2nd ed.
    • (1989) The Yeasts , vol.3 , pp. 205-259
    • Gancedo, C.1    Serrano, R.2
  • 64
    • 0020486715 scopus 로고
    • Calculation of half-lives of proteins in vivo: Heterogeneity in the rate of degradation of yeast proteins
    • Gancedo JM, Lopez S, Ballesteros F. 1982. Calculation of half-lives of proteins in vivo: heterogeneity in the rate of degradation of yeast proteins. Mol. Cell. Biochem. 43:89-95
    • (1982) Mol. Cell. Biochem. , vol.43 , pp. 89-95
    • Gancedo, J.M.1    Lopez, S.2    Ballesteros, F.3
  • 65
    • 0041371758 scopus 로고
    • Amino acid transporters in yeast: Structure, function and regulation
    • ed. JJHHM de Pont, Amsterdam: Elsevier Sci.
    • Grenson M. 1992. Amino acid transporters in yeast: structure, function and regulation. In Molecular Aspects of Transport Proteins, ed. JJHHM de Pont, pp. 219-45. Amsterdam: Elsevier Sci.
    • (1992) Molecular Aspects of Transport Proteins , pp. 219-245
    • Grenson, M.1
  • 66
    • 0029117303 scopus 로고
    • Conformational states of CFTR associated with channel gating: The role of ATP binding and hydrolysis
    • Gunderson KL, Kopito RR. 1995. Conformational states of CFTR associated with channel gating: the role of ATP binding and hydrolysis. Cell 82:231-39
    • (1995) Cell , vol.82 , pp. 231-239
    • Gunderson, K.L.1    Kopito, R.R.2
  • 67
    • 85033001106 scopus 로고
    • + symporter is a useful selectable marker and biochemical reagent when expressed in Volvox
    • + symporter is a useful selectable marker and biochemical reagent when expressed in Volvox. Proc. Natl. Acad. Sci. USA. 91:11562-66
    • (1995) Proc. Natl. Acad. Sci. USA. , vol.91 , pp. 11562-11566
    • Hallmann, A.1    Sumper, M.2
  • 68
    • 84919227046 scopus 로고
    • Glucose-induced inactivation of maltose permease in Saccharomvces
    • Han EK, Michels CA. 1992. Glucose-induced inactivation of maltose permease in Saccharomvces. Yeast 8:S512
    • (1992) Yeast , vol.8
    • Han, E.K.1    Michels, C.A.2
  • 69
    • 0000396293 scopus 로고
    • The physiology of ion channels and electrogenic pumps in higher plants
    • Hedrich R, Schroeder JI. 1989. The physiology of ion channels and electrogenic pumps in higher plants. Annu. Rev. Plant Physiol. 40:539-69
    • (1989) Annu. Rev. Plant Physiol. , vol.40 , pp. 539-569
    • Hedrich, R.1    Schroeder, J.I.2
  • 71
    • 0029164287 scopus 로고
    • The ABC of channel regulation
    • Higgins CF. 1995. The ABC of channel regulation. Cell 82:693-96
    • (1995) Cell , vol.82 , pp. 693-696
    • Higgins, C.F.1
  • 73
    • 0024980904 scopus 로고
    • Genetic transfer of the pigment bacteriorhodopsin into the eukaryote Schizosaccharomyces pombe
    • Hildebrandt V, Ramezani-Rad M, Swida U, Wrede P, Grzesiek S, et al. 1989. Genetic transfer of the pigment bacteriorhodopsin into the eukaryote Schizosaccharomyces pombe. FEBS Lett. 243:137-40
    • (1989) FEBS Lett. , vol.243 , pp. 137-140
    • Hildebrandt, V.1    Ramezani-Rad, M.2    Swida, U.3    Wrede, P.4    Grzesiek, S.5
  • 74
    • 0026355871 scopus 로고
    • Glucose increases the expression of the ATP/ADP translocator and the glyceraldehyde-3-phosphate dehydrogenase genes in Chlorella
    • Hilgarth C, Sauer N, Tanner W. 1991. Glucose increases the expression of the ATP/ADP translocator and the glyceraldehyde-3-phosphate dehydrogenase genes in Chlorella. J. Biol. Chem. 266: 24044-47
    • (1991) J. Biol. Chem. , vol.266 , pp. 24044-24047
    • Hilgarth, C.1    Sauer, N.2    Tanner, W.3
  • 75
    • 0022212597 scopus 로고
    • Molecular characterization of the CAN1 locus in Saccharomyces cerevisiae
    • Hoffmann W. 1985. Molecular characterization of the CAN1 locus in Saccharomyces cerevisiae. J. Biol. Chem. 260:11831-37
    • (1985) J. Biol. Chem. , vol.260 , pp. 11831-11837
    • Hoffmann, W.1
  • 77
    • 0028131474 scopus 로고
    • Topology of the Glut1 glucose transporter deduced from glycosylation scanning mutagenesis
    • Hresko RC, Kruse M, Strube M, Mueckler M. 1994. Topology of the Glut1 glucose transporter deduced from glycosylation scanning mutagenesis. J. Biol. Chem. 269:20482-88
    • (1994) J. Biol. Chem. , vol.269 , pp. 20482-20488
    • Hresko, R.C.1    Kruse, M.2    Strube, M.3    Mueckler, M.4
  • 78
    • 0027290722 scopus 로고
    • Cloning a plant amino acid transporter by functional complementation of a yeast amino acid transport mutant
    • Hsu LC, Chiou TJ, Chen L, Bush DR. 1993. Cloning a plant amino acid transporter by functional complementation of a yeast amino acid transport mutant. Proc. Natl. Acad. Sci. USA 90:7441-45
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7441-7445
    • Hsu, L.C.1    Chiou, T.J.2    Chen, L.3    Bush, D.R.4
  • 79
    • 0028890031 scopus 로고
    • Structure at 2.8 Å resolution of cytochrome oxidase from Paracoccus denitrificans
    • Iwata S, Ostermeier C, Ludwig B, Michel H. 1995. Structure at 2.8 Å resolution of cytochrome oxidase from Paracoccus denitrificans. Nature 376: 660-69
    • (1995) Nature , vol.376 , pp. 660-669
    • Iwata, S.1    Ostermeier, C.2    Ludwig, B.3    Michel, H.4
  • 80
    • 0022893751 scopus 로고
    • Electrogenic properties of the sodium-alanine cotransporter in pancreatic acinar cells. II. Comparison with transport models
    • Jauch P, Läuger P. 1986. Electrogenic properties of the sodium-alanine cotransporter in pancreatic acinar cells. II. Comparison with transport models. J. Membr. Biol. 94:117-27
    • (1986) J. Membr. Biol. , vol.94 , pp. 117-127
    • Jauch, P.1    Läuger, P.2
  • 81
    • 0022870012 scopus 로고
    • Electrogenic properties of the sodium-alanine cotransporter in pancreatic acinar cells. I. Tight-seal whole-cell recordings
    • Jauch P, Petersen OH, Läuger P. 1986. Electrogenic properties of the sodium-alanine cotransporter in pancreatic acinar cells. I. Tight-seal whole-cell recordings. J. Membr. Biol. 94:99-115
    • (1986) J. Membr. Biol. , vol.94 , pp. 99-115
    • Jauch, P.1    Petersen, O.H.2    Läuger, P.3
  • 82
    • 0025372080 scopus 로고
    • GAP1, the general amino acid permease gene of Saccharomyces cerevisiae: Nucleotide sequence, protein similarity with the other bakers yeast amino acid permeases, and nitrogen catabolite repression
    • Jauniaux JC, Grenson M. 1990. GAP1, the general amino acid permease gene of Saccharomyces cerevisiae: nucleotide sequence, protein similarity with the other bakers yeast amino acid permeases, and nitrogen catabolite repression. Eur. J. Biochem. 190:39-44
    • (1990) Eur. J. Biochem. , vol.190 , pp. 39-44
    • Jauniaux, J.C.1    Grenson, M.2
  • 83
    • 0023871832 scopus 로고
    • Primary structure of the uracil transport protein of Saccharomyces cerevisiae
    • Jund R, Weber E, Chevallier MR. 1988. Primary structure of the uracil transport protein of Saccharomyces cerevisiae. Eur. J. Biochem. 171:417-24
    • (1988) Eur. J. Biochem. , vol.171 , pp. 417-424
    • Jund, R.1    Weber, E.2    Chevallier, M.R.3
  • 84
    • 0028281534 scopus 로고
    • Dynamics of lactose permease of E. coli determined by site-directed fluorescence labeling
    • Jung K, Jung H, Kaback HR. 1994. Dynamics of lactose permease of E. coli determined by site-directed fluorescence labeling. Biochemistry 33:3980-85
    • (1994) Biochemistry , vol.33 , pp. 3980-3985
    • Jung, K.1    Jung, H.2    Kaback, H.R.3
  • 85
    • 0029041299 scopus 로고
    • Engineering a metal binding site within a polytopic membrane protein, the lactose permease of Escherichia coli
    • Jung K, Voss J, He M, Hubbell WL, Kaback HR. 1995. Engineering a metal binding site within a polytopic membrane protein, the lactose permease of Escherichia coli. Biochemistry 34: 6272-77
    • (1995) Biochemistry , vol.34 , pp. 6272-6277
    • Jung, K.1    Voss, J.2    He, M.3    Hubbell, W.L.4    Kaback, H.R.5
  • 86
    • 0026497327 scopus 로고
    • In and out and up and down with lac permease
    • Kaback HR. 1992. In and out and up and down with lac permease. Int. Rev. Cytol 137A:97-125
    • (1992) Int. Rev. Cytol , vol.137 A , pp. 97-125
    • Kaback, H.R.1
  • 88
    • 85033025353 scopus 로고
    • Molecular characterization of an Arabidopsis thaliana cDNA encoding a novel putative adenylate translocator of higher plants
    • Abstr.
    • Kampfenkel K, Neuhaus E. 1995. Molecular characterization of an Arabidopsis thaliana cDNA encoding a novel putative adenylate translocator of higher plants. Int. Workshop Plant Membr. Biol., 10th, Regensburg, R47 (Abstr.)
    • (1995) Int. Workshop Plant Membr. Biol., 10th, Regensburg
    • Kampfenkel, K.1    Neuhaus, E.2
  • 89
    • 0026640887 scopus 로고
    • Structure-function of the ADP/ATP carrier
    • Klingenberg M. 1992. Structure-function of the ADP/ATP carrier. Biochem. Soc. Trans. 20:547-50
    • (1992) Biochem. Soc. Trans. , vol.20 , pp. 547-550
    • Klingenberg, M.1
  • 90
    • 0025822954 scopus 로고
    • + transporters in Saccharomyces cerevisiae
    • + transporters in Saccharomyces cerevisiae. Mol Cell. Biol. 11:4266-73
    • (1991) Mol Cell. Biol. , vol.11 , pp. 4266-4273
    • Ko, C.H.1    Gaber, R.F.2
  • 91
    • 0027391981 scopus 로고
    • Roles of multiple glucose transporters in Saccharomyces cerevisiae
    • Ko CH, Liang H, Gaber RF. 1993. Roles of multiple glucose transporters in Saccharomyces cerevisiae. Mol. Cell. Biol. 13:638-48
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 638-648
    • Ko, C.H.1    Liang, H.2    Gaber, R.F.3
  • 92
    • 0025282180 scopus 로고
    • A third ADP/ATP translocator gene in yeast
    • Kolarov J, Kolarov N, Nelson N. 1990. A third ADP/ATP translocator gene in yeast. J. Biol. Chem. 265:12711-16
    • (1990) J. Biol. Chem. , vol.265 , pp. 12711-12716
    • Kolarov, J.1    Kolarov, N.2    Nelson, N.3
  • 93
    • 0015720319 scopus 로고
    • Proton-coupled hexose transport in Chlorella vulgaris
    • Komor E. 1973. Proton-coupled hexose transport in Chlorella vulgaris. FEBS Lett. 38:16-18
    • (1973) FEBS Lett. , vol.38 , pp. 16-18
    • Komor, E.1
  • 94
    • 0015907496 scopus 로고
    • m values for 6-deoxyglucose influx and efflux and their contribution to sugar accumulation
    • m values for 6-deoxyglucose influx and efflux and their contribution to sugar accumulation. Eur. J. Biochem. 39:193-200
    • (1973) Eur. J. Biochem. , vol.39 , pp. 193-200
    • Komor, E.1    Haass, D.2    Komor, B.3    Tanner, W.4
  • 95
    • 0002652371 scopus 로고
    • A proton-cotransport system in a higher plant: Sucrose transport in Ricinus communis
    • Komor E, Rotter M, Tanner W. 1977. A proton-cotransport system in a higher plant: sucrose transport in Ricinus communis. Plant Sci. Lett. 9:153-62
    • (1977) Plant Sci. Lett. , vol.9 , pp. 153-162
    • Komor, E.1    Rotter, M.2    Tanner, W.3
  • 96
    • 0008392778 scopus 로고
    • The hexose uptake system of Chlorella: Is it a proton symport or a hydroxyl ion antiport system?
    • Komor E, Schobert C, Cho BH. 1983. The hexose uptake system of Chlorella: Is it a proton symport or a hydroxyl ion antiport system? FEBS Lett. 156:6-10
    • (1983) FEBS Lett. , vol.156 , pp. 6-10
    • Komor, E.1    Schobert, C.2    Cho, B.H.3
  • 97
    • 0016277413 scopus 로고
    • m values and translocation constants of the uptake system
    • m values and translocation constants of the uptake system. J. Gen. Physiol. 64:568-81
    • (1974) J. Gen. Physiol. , vol.64 , pp. 568-581
    • Komor, E.1    Tanner, W.2
  • 98
    • 0017621850 scopus 로고
    • Reconstitution of adenine nucleotide transport with purified ADP/ATP-carrier protein
    • Krämer R, Klingenberg M. 1977. Reconstitution of adenine nucleotide transport with purified ADP/ATP-carrier protein. FEBS Lett. 82:363-67
    • (1977) FEBS Lett. , vol.82 , pp. 363-367
    • Krämer, R.1    Klingenberg, M.2
  • 99
    • 0025016105 scopus 로고
    • The HXT2 gene of Saccharomyces cerevisiae is required for high-affinity glucose transport
    • Kruckeberg AL, Bisson LF. 1990. The HXT2 gene of Saccharomyces cerevisiae is required for high-affinity glucose transport. Mol. Cell. Biol. 10: 5903-13
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5903-5913
    • Kruckeberg, A.L.1    Bisson, L.F.2
  • 100
    • 0027160122 scopus 로고
    • The mitochondrial carrier family of transport proteins: Structural, functional, and evolutionary relationships
    • Kuan J, Saier MH Jr. 1993. The mitochondrial carrier family of transport proteins: structural, functional, and evolutionary relationships. Crit. Rev. Biochem. Mol. Biol. 28:209-33
    • (1993) Crit. Rev. Biochem. Mol. Biol. , vol.28 , pp. 209-233
    • Kuan, J.1    Saier Jr., M.H.2
  • 102
    • 0028819235 scopus 로고
    • Regulation of inositol transport in Saccharomyces cerevisiae involves inositol-induced changes in permease stability and endocytic degradation in the vacuole
    • Lai K, Bolognese CP, Swift S, McGraw P. 1995. Regulation of inositol transport in Saccharomyces cerevisiae involves inositol-induced changes in permease stability and endocytic degradation in the vacuole. J. Biol. Chem. 270:2525-34
    • (1995) J. Biol. Chem. , vol.270 , pp. 2525-2534
    • Lai, K.1    Bolognese, C.P.2    Swift, S.3    McGraw, P.4
  • 103
    • 0024288852 scopus 로고
    • Separate genes encode functionally equivalent ADP/ATP carrier proteins in Saccharomyces cerevisiae: Isolation and analysis of AAC2
    • Lawson JE, Douglas MG. 1988. Separate genes encode functionally equivalent ADP/ATP carrier proteins in Saccharomyces cerevisiae: isolation and analysis of AAC2. J. Biol. Chem. 263: 14813-18
    • (1988) J. Biol. Chem. , vol.263 , pp. 14813-14818
    • Lawson, J.E.1    Douglas, M.G.2
  • 104
    • 0025764220 scopus 로고
    • The HXT1 gene product of Saccharomyces cerevisiae is a new member of the family of hexose transporters
    • Lewis DA, Bisson LF. 1991. The HXT1 gene product of Saccharomyces cerevisiae is a new member of the family of hexose transporters. Mol. Cell. Biol. 11:3804-13
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3804-3813
    • Lewis, D.A.1    Bisson, L.F.2
  • 105
    • 0026446549 scopus 로고
    • SHR3: A novel component of the secretory pathway specifically required for localization of amino acid permeases in yeast
    • Ljungdahl PO, Gimeno CJ, Styles CA, Fink GR. 1992. SHR3: a novel component of the secretory pathway specifically required for localization of amino acid permeases in yeast. Cell 71:463-78
    • (1992) Cell , vol.71 , pp. 463-478
    • Ljungdahl, P.O.1    Gimeno, C.J.2    Styles, C.A.3    Fink, G.R.4
  • 106
    • 0027411773 scopus 로고
    • Expression of the functional mature chloroplast triose phosphate translocator in yeast internal membranes and purification of the histidine-tagged protein by a single metalaffinity chromatography step
    • Loddenkötter B, Kammerer B, Fischer K, Flügge UI. 1993. Expression of the functional mature chloroplast triose phosphate translocator in yeast internal membranes and purification of the histidine-tagged protein by a single metalaffinity chromatography step. Proc. Natl Acad. Sci. USA 90:2155-59
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 2155-2159
    • Loddenkötter, B.1    Kammerer, B.2    Fischer, K.3    Flügge, U.I.4
  • 107
    • 0027507306 scopus 로고
    • A major superfamily of transmembrane facilitators that catalyse uniport, symport and antiport
    • Marger MD, Saier MH Jr. 1993. A major superfamily of transmembrane facilitators that catalyse uniport, symport and antiport. Trends Biol. Sci. 18:13-20
    • (1993) Trends Biol. Sci. , vol.18 , pp. 13-20
    • Marger, M.D.1    Saier Jr., M.H.2
  • 108
    • 0027980905 scopus 로고
    • Cloning and expression of the MEP1 gene encoding an ammonium transporter in Saccharomyces cerevisiae
    • Marini AM, Vissers S, Urrestarazu A, Andre B. 1994. Cloning and expression of the MEP1 gene encoding an ammonium transporter in Saccharomyces cerevisiae. EMBO J. 13:3456-63
    • (1994) EMBO J. , vol.13 , pp. 3456-3463
    • Marini, A.M.1    Vissers, S.2    Urrestarazu, A.3    Andre, B.4
  • 109
    • 0027210070 scopus 로고
    • ATP-dependent glutathione S-conjugate "export" pump in the vacuolar membrane of plants
    • Martinoia E, Grill E, Tommasini R, Kreuz K, Amrhein N. 1993. ATP-dependent glutathione S-conjugate "export" pump in the vacuolar membrane of plants. Nature 364:247-49
    • (1993) Nature , vol.364 , pp. 247-249
    • Martinoia, E.1    Grill, E.2    Tommasini, R.3    Kreuz, K.4    Amrhein, N.5
  • 110
    • 0017659917 scopus 로고
    • Catabolite inactivation of the galactose uptake system in yeast
    • Matern H, Holzer H. 1977. Catabolite inactivation of the galactose uptake system in yeast. J. Biol. Chem. 252:6399-6402
    • (1977) J. Biol. Chem. , vol.252 , pp. 6399-6402
    • Matern, H.1    Holzer, H.2
  • 111
    • 0027087217 scopus 로고
    • Insertional mutagenesis of hydrophilic domains in the lactose permease of Escherichia coli
    • McKenna E, Hardy D, Kaback HR. 1992. Insertional mutagenesis of hydrophilic domains in the lactose permease of Escherichia coli. Proc. Natl. Acad. Sci. USA 89:11954-58
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 11954-11958
    • McKenna, E.1    Hardy, D.2    Kaback, H.R.3
  • 112
    • 0028080928 scopus 로고
    • Glucose-transport-deficient mutants of Schizosaccharomyces pombe: Phenotype, genetics and use for genetic complementation
    • Milbradt B, Höfer M. 1994. Glucose-transport-deficient mutants of Schizosaccharomyces pombe: phenotype, genetics and use for genetic complementation. Microbiology 140:2617-23
    • (1994) Microbiology , vol.140 , pp. 2617-2623
    • Milbradt, B.1    Höfer, M.2
  • 113
    • 0026864596 scopus 로고
    • Complementation of Saccharomyces cerevisiae auxotrophic mutants by Arabidopsis thaliana cDNAs
    • Minet M, Dufour M, Lacroute F. 1992. Complementation of Saccharomyces cerevisiae auxotrophic mutants by Arabidopsis thaliana cDNAs. Plant J. 2:417-22
    • (1992) Plant J. , vol.2 , pp. 417-422
    • Minet, M.1    Dufour, M.2    Lacroute, F.3
  • 114
    • 0000413253 scopus 로고
    • Molecule, group and electron translocation through natural membranes
    • Mitchell P. 1963. Molecule, group and electron translocation through natural membranes. Biochem. Soc. Symp. 22: 142-68
    • (1963) Biochem. Soc. Symp. , vol.22 , pp. 142-168
    • Mitchell, P.1
  • 115
    • 0002291359 scopus 로고
    • The mechanism of proton translocation in reversible proton-translocating adenosine triphosphatase
    • Mitchell P, Moyle J. 1974. The mechanism of proton translocation in reversible proton-translocating adenosine triphosphatase. Biochem. Soc. Spec. Publ. 4:91-111
    • (1974) Biochem. Soc. Spec. Publ. , vol.4 , pp. 91-111
    • Mitchell, P.1    Moyle, J.2
  • 116
    • 0019888608 scopus 로고
    • Purification and reconstitution of functional lactose carrier from Escherichia coli
    • Newman MJ, Foster DL, Wilson TH, Kaback HR. 1981. Purification and reconstitution of functional lactose carrier from Escherichia coli. J. Biol. Chem. 256:11804-8
    • (1981) J. Biol. Chem. , vol.256 , pp. 11804-11808
    • Newman, M.J.1    Foster, D.L.2    Wilson, T.H.3    Kaback, H.R.4
  • 117
    • 0025063163 scopus 로고
    • Primary structure of the yeast choline transport gene and regulation of its expression
    • Nikawa J, Hosaka K, Tsukagoshi Y, Yamashita S. 1990. Primary structure of the yeast choline transport gene and regulation of its expression. J. Biol. Chem. 265:15996-6003
    • (1990) J. Biol. Chem. , vol.265 , pp. 15996-16003
    • Nikawa, J.1    Hosaka, K.2    Tsukagoshi, Y.3    Yamashita, S.4
  • 118
    • 0025848024 scopus 로고
    • Isolation and characterisation of two distinct myo-inositol transporter genes of Saccharomyces cerevisiae
    • Nikawa JI, Tsukagoshi Y, Yamashita S. 1991. Isolation and characterisation of two distinct myo-inositol transporter genes of Saccharomyces cerevisiae. J. Biol. Chem. 266:11184-91
    • (1991) J. Biol. Chem. , vol.266 , pp. 11184-11191
    • Nikawa, J.I.1    Tsukagoshi, Y.2    Yamashita, S.3
  • 120
    • 0028895422 scopus 로고
    • Substrate recognition domain of the Gal2 galactose transporter in yeast Saccharomyces cerevisiae as revealed by chimeric galactose-glucose transporters
    • Nishizawa K, Shimoda E, Kasahara M. 1995. Substrate recognition domain of the Gal2 galactose transporter in yeast Saccharomyces cerevisiae as revealed by chimeric galactose-glucose transporters. J. Biol. Chem. 270:2423-26
    • (1995) J. Biol. Chem. , vol.270 , pp. 2423-2426
    • Nishizawa, K.1    Shimoda, E.2    Kasahara, M.3
  • 121
    • 0026673416 scopus 로고
    • The intracellular targeting and membrane topology of 3-hydroxy-3-methylglutaryl-CoA reductase
    • Olander EH, Simoni RD. 1992. The intracellular targeting and membrane topology of 3-hydroxy-3-methylglutaryl-CoA reductase. J. Biol. Chem. 267: 4223-35
    • (1992) J. Biol. Chem. , vol.267 , pp. 4223-4235
    • Olander, E.H.1    Simoni, R.D.2
  • 122
    • 0027418823 scopus 로고
    • Unidirectional arginine transport in reconstituted plasma-membrane vesicles from yeast overexpressing CAN1
    • Opekarova M, Caspari T, Tanner W. 1993. Unidirectional arginine transport in reconstituted plasma-membrane vesicles from yeast overexpressing CAN1. Eur. J. Biochem. 211:683-88
    • (1993) Eur. J. Biochem. , vol.211 , pp. 683-688
    • Opekarova, M.1    Caspari, T.2    Tanner, W.3
  • 124
    • 0028872732 scopus 로고
    • Three different regulatory mechanisms enable yeast hexose transporter (HXT) genes to be induced by different levels of glucose
    • Ozean S, Johnston M. 1995. Three different regulatory mechanisms enable yeast hexose transporter (HXT) genes to be induced by different levels of glucose. Mol. Cell. Biol. 15: 1564-72
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1564-1572
    • Ozean, S.1    Johnston, M.2
  • 127
    • 0028115836 scopus 로고
    • Isolation and characterization of a Saccharomyces cerevisiae peptide transport gene
    • Perry JR, Basrai MA, Steiner HY, Naider F, Becker JM. 1994. Isolation and characterization of a Saccharomyces cerevisiae peptide transport gene. Mol. Cell. Biol. 14:104-15
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 104-115
    • Perry, J.R.1    Basrai, M.A.2    Steiner, H.Y.3    Naider, F.4    Becker, J.M.5
  • 128
    • 0026016272 scopus 로고
    • Cloning and characterization of the mitochondrial phosphate transport protein gene from the yeast Saccharomyces cerevisiae
    • Phelps A, Schobert CT, Wohlrab H. 1991. Cloning and characterization of the mitochondrial phosphate transport protein gene from the yeast Saccharomyces cerevisiae. Biochemistry 30: 248-52
    • (1991) Biochemistry , vol.30 , pp. 248-252
    • Phelps, A.1    Schobert, C.T.2    Wohlrab, H.3
  • 129
    • 0028384701 scopus 로고
    • Identification of nitrate transporter genes in Chlamydomonas reinhardtii
    • Quesada A, Galvan A, Fernandes E. 1994. Identification of nitrate transporter genes in Chlamydomonas reinhardtii. Plant. J. 5:407-19
    • (1994) Plant. J. , vol.5 , pp. 407-419
    • Quesada, A.1    Galvan, A.2    Fernandes, E.3
  • 130
    • 0023674297 scopus 로고
    • Structure and transcription of the allantoate permease gene (DAL5) from Saccharomvces cerevisiae
    • Rai R, Genbauffe FS, Cooper TG. 1988. Structure and transcription of the allantoate permease gene (DAL5) from Saccharomvces cerevisiae. J. Bacteriol. 170: 266-71
    • (1988) J. Bacteriol. , vol.170 , pp. 266-271
    • Rai, R.1    Genbauffe, F.S.2    Cooper, T.G.3
  • 131
    • 84989713965 scopus 로고
    • The hexose transporters at the plasma membrane and the tonoplast of higher plants
    • Rausch T. 1991. The hexose transporters at the plasma membrane and the tonoplast of higher plants. Physiol. Plant. 82:134-42
    • (1991) Physiol. Plant. , vol.82 , pp. 134-142
    • Rausch, T.1
  • 133
    • 0028949280 scopus 로고
    • Identification of novel HXT genes in Saccharomyces cerevisiae reveals the impact of individual hexose transporters on glycolytic flux
    • Reifenberger E, Freidel K, Ciriacy M. 1995. Identification of novel HXT genes in Saccharomyces cerevisiae reveals the impact of individual hexose transporters on glycolytic flux. Mol. Microbiol. 16: 157-67
    • (1995) Mol. Microbiol. , vol.16 , pp. 157-167
    • Reifenberger, E.1    Freidel, K.2    Ciriacy, M.3
  • 135
    • 0029560314 scopus 로고
    • Catabolite inactivation of the yeast maltose transporter occurs in the vacuole after internalization by endocytosis
    • Riballo E, Herweijer M, Wolf D, Lagunas R. 1995. Catabolite inactivation of the yeast maltose transporter occurs in the vacuole after internalization by endocytosis. J. Bacteriol. 177:5622-27
    • (1995) J. Bacteriol. , vol.177 , pp. 5622-5627
    • Riballo, E.1    Herweijer, M.2    Wolf, D.3    Lagunas, R.4
  • 137
    • 0027692824 scopus 로고
    • Potato sucrose transporter expression in minor veins indicates a role in phloem loading
    • Riesmeier JW, Hirner B, Frommer WB. 1993. Potato sucrose transporter expression in minor veins indicates a role in phloem loading. Plant Cell 5:1591-98
    • (1993) Plant Cell , vol.5 , pp. 1591-1598
    • Riesmeier, J.W.1    Hirner, B.2    Frommer, W.B.3
  • 138
    • 0027092284 scopus 로고
    • Isolation and characterization of a sucrose carrier cDNA from spinach by functional expression in yeast
    • Riesmeier JW, Willmitzer L, Frommer WB. 1992. Isolation and characterization of a sucrose carrier cDNA from spinach by functional expression in yeast. EMBO J. 11:4705-13
    • (1992) EMBO J. , vol.11 , pp. 4705-4713
    • Riesmeier, J.W.1    Willmitzer, L.2    Frommer, W.B.3
  • 139
    • 0028130972 scopus 로고
    • Expression of a sugar-transporter gene family in a photoautotrophic suspension culture of Chenopodium rubrum L
    • Roitsch T, Tanner W. 1994. Expression of a sugar-transporter gene family in a photoautotrophic suspension culture of Chenopodium rubrum L. Planta 193: 365-71
    • (1994) Planta , vol.193 , pp. 365-371
    • Roitsch, T.1    Tanner, W.2
  • 141
    • 34250140267 scopus 로고
    • Generalized kinetic analysis of ion-driven cotransport systems: A unified interpretation of selective ionic effects on Michaelis parameters
    • Sanders D, Hansen UP, Gradmann D, Slayman CL. 1984. Generalized kinetic analysis of ion-driven cotransport systems: a unified interpretation of selective ionic effects on Michaelis parameters. J. Membr. Biol. 77: 123-52
    • (1984) J. Membr. Biol. , vol.77 , pp. 123-152
    • Sanders, D.1    Hansen, U.P.2    Gradmann, D.3    Slayman, C.L.4
  • 143
    • 0025151984 scopus 로고
    • Functional expression of the Chlorella hexose transporter in Schizosaccharomyces pombe
    • Sauer N, Caspari T, Klebl F, Tanner W. 1990. Functional expression of the Chlorella hexose transporter in Schizosaccharomyces pombe. Proc. Natl. Acad. Sci. USA 87:7949-52
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 7949-7952
    • Sauer, N.1    Caspari, T.2    Klebl, F.3    Tanner, W.4
  • 144
    • 0025042752 scopus 로고
    • Primary structure, genomic organization and heterologous expression of a glucose transporter from Arabidopsis thaliana
    • Sauer N, Friedländer K. Gräml-Wicke U. 1990. Primary structure, genomic organization and heterologous expression of a glucose transporter from Arabidopsis thaliana. EMBO J. 9:3045-50
    • (1990) EMBO J. , vol.9 , pp. 3045-3050
    • Sauer, N.1    Friedländer, K.2    Gräml-Wicke, U.3
  • 145
    • 0003057425 scopus 로고
    • Regulation and characterization of two inducible amino-acid transport systems in Chlorella vulgaris
    • Sauer N, Komor E, Tanner W. 1983. Regulation and characterization of two inducible amino-acid transport systems in Chlorella vulgaris. Planta 159:404-10
    • (1983) Planta , vol.159 , pp. 404-410
    • Sauer, N.1    Komor, E.2    Tanner, W.3
  • 146
    • 0027673539 scopus 로고
    • +/monosaccharide co-transporter from Nicotiana tabacum: Cloning and heterologous expression in baker's yeast
    • +/monosaccharide co-transporter from Nicotiana tabacum: cloning and heterologous expression in baker's yeast. Plant J. 4:601-10
    • (1993) Plant J. , vol.4 , pp. 601-610
    • Sauer, N.1    Stadler, R.2
  • 147
    • 0028465445 scopus 로고
    • SUC1 and SUC2: Two sucrose transporters from Arabidopsis thaliana, expression and characterization in baker's yeast and identification of the histidine-tagged protein
    • Sauer N, Stolz J. 1994. SUC1 and SUC2: two sucrose transporters from Arabidopsis thaliana, expression and characterization in baker's yeast and identification of the histidine-tagged protein. Plant J. 6:67-77
    • (1994) Plant J. , vol.6 , pp. 67-77
    • Sauer, N.1    Stolz, J.2
  • 149
    • 84995094150 scopus 로고
    • Molecular biology of sugar transporters in plants
    • Sauer N, Tanner W. 1993. Molecular biology of sugar transporters in plants. Bot. Acta 4:277-86
    • (1993) Bot. Acta , vol.4 , pp. 277-286
    • Sauer, N.1    Tanner, W.2
  • 150
    • 0028114234 scopus 로고
    • Structure and transport mechanism of a high-affinity potassium uptake transporter from higher plants
    • Schachtman DP, Schroeder JI. 1994. Structure and transport mechanism of a high-affinity potassium uptake transporter from higher plants. Nature 370: 655-58
    • (1994) Nature , vol.370 , pp. 655-658
    • Schachtman, D.P.1    Schroeder, J.I.2
  • 151
    • 0027959012 scopus 로고
    • Two FK506 resistance-conferring genes in Saccharomyces cerevisiae, TAT1 and TAT2. encode amino acid permeases mediating tyrosine and tryptophan uptake
    • Schmidt A, Hall MN, Koller A. 1994. Two FK506 resistance-conferring genes in Saccharomyces cerevisiae, TAT1 and TAT2. encode amino acid permeases mediating tyrosine and tryptophan uptake. Mol. Cell. Biol. 14: 6597-6606
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6597-6606
    • Schmidt, A.1    Hall, M.N.2    Koller, A.3
  • 152
    • 0002855808 scopus 로고
    • Heterologous expression and functional analysis of higher plant transport proteins in Xenopus oocytes
    • Schroeder JI. 1994. Heterologous expression and functional analysis of higher plant transport proteins in Xenopus oocytes. METHODS: A Companion to Methods of Enzymology 6:70-81
    • (1994) METHODS: A Companion to Methods of Enzymology , vol.6 , pp. 70-81
    • Schroeder, J.I.1
  • 154
    • 0017798812 scopus 로고
    • A possible mechanistic role of the membrane potential in proton-sugar cotransport of Chlorella
    • Schwab WGW. Komor E. 1978. A possible mechanistic role of the membrane potential in proton-sugar cotransport of Chlorella. FEBS Lett 87:157-60
    • (1978) FEBS Lett , vol.87 , pp. 157-160
    • Schwab, W.G.W.1    Komor, E.2
  • 155
    • 0028149758 scopus 로고
    • Ion channel properties of the reconstituted chloroplast triose phosphate/ phosphate translocator
    • Schwarz M, Gross A. Steinkamp T. Flügge UI, Wagner R. 1994. Ion channel properties of the reconstituted chloroplast triose phosphate/ phosphate translocator. J. Biol. them. 269:29481-89
    • (1994) J. Biol. Them. , vol.269 , pp. 29481-29489
    • Schwarz, M.1    Gross, A.2    Steinkamp, T.3    Flügge, U.I.4    Wagner, R.5
  • 156
    • 0015804117 scopus 로고
    • The absorption of protons with specific amino acids and carbohydrates by yeast
    • Seaston A, Inkson C, Eddy AA. 1973. The absorption of protons with specific amino acids and carbohydrates by yeast. Biochem. J. 134:1031-43
    • (1973) Biochem. J. , vol.134 , pp. 1031-1043
    • Seaston, A.1    Inkson, C.2    Eddy, A.A.3
  • 157
    • 0026579591 scopus 로고
    • Cloning and expression in yeast of a plant potassium ion transport system
    • Sentenac H, Bonneaud N, Minet M, Lacroute F, Salmon JM, et al. 1992. Cloning and expression in yeast of a plant potassium ion transport system. Science 256:663-65
    • (1992) Science , vol.256 , pp. 663-665
    • Sentenac, H.1    Bonneaud, N.2    Minet, M.3    Lacroute, F.4    Salmon, J.M.5
  • 158
    • 0000871808 scopus 로고
    • Transport across yeast vacuolar and plasma mebranes
    • Cold Spring Harbor, NY: Cold Spring Harbor Lab. Press
    • Serrano R. 1991. Transport across yeast vacuolar and plasma mebranes. In The Molecular and Cellular Biology of the Yeast Saccharomyces, 1:523-85. Cold Spring Harbor, NY: Cold Spring Harbor Lab. Press
    • (1991) The Molecular and Cellular Biology of the Yeast Saccharomyces , vol.1 , pp. 523-585
    • Serrano, R.1
  • 159
    • 0006744051 scopus 로고
    • Depolarisation of the plasma membrane of Neurospora during active transport of glucose: Evidence for a proton-dependent cotransport system
    • Slayman CL, Slayman CW. 1974. Depolarisation of the plasma membrane of Neurospora during active transport of glucose: evidence for a proton-dependent cotransport system. Proc. Natl. Acad. Sci. USA 71:1935-39
    • (1974) Proc. Natl. Acad. Sci. USA , vol.71 , pp. 1935-1939
    • Slayman, C.L.1    Slayman, C.W.2
  • 161
    • 0029053572 scopus 로고
    • Isolation of a cDNA from Saccharomyces cerevisiae that encodes a high affinity sulfate transporter of the plasma membrane
    • Smith FW, Hawkesford MJ, Prosser IM, Clarkson DT. 1995. Isolation of a cDNA from Saccharomyces cerevisiae that encodes a high affinity sulfate transporter of the plasma membrane. Mol. Gen. Genet. 247:709-15
    • (1995) Mol. Gen. Genet. , vol.247 , pp. 709-715
    • Smith, F.W.1    Hawkesford, M.J.2    Prosser, I.M.3    Clarkson, D.T.4
  • 162
    • 0028996131 scopus 로고
    • Phloem loading by the PmSUC2 sucrose carrier from Plantago major occurs into companion cells
    • Stadier R, Brandner J, Schulz A, Gahrtz M, Sauer N. 1995. Phloem loading by the PmSUC2 sucrose carrier from Plantago major occurs into companion cells. Plant Cell 7:9545-54
    • (1995) Plant Cell , vol.7 , pp. 9545-9554
    • Stadier, R.1    Brandner, J.2    Schulz, A.3    Gahrtz, M.4    Sauer, N.5
  • 164
    • 0028876606 scopus 로고
    • Transcriptional and posttranslational regulation of the general amino acid permease of Saccharomyces cerevisiae
    • Stanbrough M, Magasanik B. 1995. Transcriptional and posttranslational regulation of the general amino acid permease of Saccharomyces cerevisiae. J. Bacteriol. 177:94-102
    • (1995) J. Bacteriol. , vol.177 , pp. 94-102
    • Stanbrough, M.1    Magasanik, B.2
  • 165
    • 0028501449 scopus 로고
    • An Arabidopsis peptide transporter is a member of a new class of membrane transport proteins
    • Steiner HY, Song W, Zhang L, Naider F, Becker JM, Stacey G. 1994. An Arabidopsis peptide transporter is a member of a new class of membrane transport proteins. Plant Cell 6:1289-99
    • (1994) Plant Cell , vol.6 , pp. 1289-1299
    • Steiner, H.Y.1    Song, W.2    Zhang, L.3    Naider, F.4    Becker, J.M.5    Stacey, G.6
  • 166
    • 0029560181 scopus 로고
    • Rapid purification of a functionally active sucrose carriers from transgenic yeast using a bacterial biotin acceptor domain
    • Stolz J, Darnhofer-Demar B, Sauer N. 1995. Rapid purification of a functionally active sucrose carriers from transgenic yeast using a bacterial biotin acceptor domain. FEBS Lett. 377:167-71
    • (1995) FEBS Lett. , vol.377 , pp. 167-171
    • Stolz, J.1    Darnhofer-Demar, B.2    Sauer, N.3
  • 167
    • 0028484080 scopus 로고
    • + symporter in lipid vesicles and purification of the histidine tagged protein from transgenic Saccharomyces cerevisiae
    • + symporter in lipid vesicles and purification of the histidine tagged protein from transgenic Saccharomyces cerevisiae. Plant J. 6: 225-33
    • (1994) Plant J. , vol.6 , pp. 225-233
    • Stolz, J.1    Stadier, R.2    Opekarova, M.3    Sauer, N.4
  • 168
    • 0027977678 scopus 로고
    • Molecular analysis of proteins in the plant plasma membrane
    • Sussman MR. 1995. Molecular analysis of proteins in the plant plasma membrane. Annu. Rev. Plant Phys. Plant Mol. Biol. 45:211-34
    • (1995) Annu. Rev. Plant Phys. Plant Mol. Biol. , vol.45 , pp. 211-234
    • Sussman, M.R.1
  • 169
    • 0027184991 scopus 로고
    • Cloning and sequencing of the Saccharomyces cerevisiae gene LYP1 coding for a lysine-specific permease
    • Sychrova H, Chevallier MR. 1993. Cloning and sequencing of the Saccharomyces cerevisiae gene LYP1 coding for a lysine-specific permease. Yeast 9:771-82
    • (1993) Yeast , vol.9 , pp. 771-782
    • Sychrova, H.1    Chevallier, M.R.2
  • 171
    • 0022340382 scopus 로고
    • The histidine permease gene (HIP1) of Saccharomyces cerevisiae
    • Tanaka JI, Fink GR. 1985. The histidine permease gene (HIP1) of Saccharomyces cerevisiae. Gene 38:205-14
    • (1985) Gene , vol.38 , pp. 205-214
    • Tanaka, J.I.1    Fink, G.R.2
  • 172
    • 0014688628 scopus 로고
    • Light-driven active uptake of 3-O-methylglucose via an inducible hexose uptake system of Chlorella
    • Tanner W. 1969. Light-driven active uptake of 3-O-methylglucose via an inducible hexose uptake system of Chlorella. Biochem. Biophys. Res. Commun. 36:278-83
    • (1969) Biochem. Biophys. Res. Commun. , vol.36 , pp. 278-283
    • Tanner, W.1
  • 173
    • 0028145245 scopus 로고
    • High-copy suppression of glucose transport defects by HXT4 and regulatory elements in the promotors of the HXT genes in Saccharomyces cerevisiae
    • Theodoris G, Fong NM, Coons DM, Bisson LF. 1994. High-copy suppression of glucose transport defects by HXT4 and regulatory elements in the promotors of the HXT genes in Saccharomyces cerevisiae. Genetics 137: 957-66
    • (1994) Genetics , vol.137 , pp. 957-966
    • Theodoris, G.1    Fong, N.M.2    Coons, D.M.3    Bisson, L.F.4
  • 174
    • 0028813459 scopus 로고
    • + symporter gene directs expression of β-glucuronidase to the phloem: Evidence for phloem loading and unloading by SUC2
    • + symporter gene directs expression of β-glucuronidase to the phloem: evidence for phloem loading and unloading by SUC2. Planta 196:564-70
    • (1995) Planta , vol.196 , pp. 564-570
    • Truernit, E.1    Sauer, N.2
  • 175
    • 0027526320 scopus 로고
    • The herbicide sensitivity gene CHL1 of Arabidopsis encodes a nitrate-inducible nitrate transporter
    • Tsay Y-F, Schroeder JI, Feldmann KA, Crawford NM. 1993. The herbicide sensitivity gene CHL1 of Arabidopsis encodes a nitrate-inducible nitrate transporter. Cell 72:705-13
    • (1993) Cell , vol.72 , pp. 705-713
    • Tsay, Y.-F.1    Schroeder, J.I.2    Feldmann, K.A.3    Crawford, N.M.4
  • 177
    • 0026536805 scopus 로고
    • Volume-regulated chloride channels associated with the human multidrug-resistance P-glycoprotein
    • Valverde MA, Diaz M, Sepulveda FV, Gill DR, Hyde SC, Higgins CF. 1992. Volume-regulated chloride channels associated with the human multidrug-resistance P-glycoprotein. Nature 355: 830-33
    • (1992) Nature , vol.355 , pp. 830-833
    • Valverde, M.A.1    Diaz, M.2    Sepulveda, F.V.3    Gill, D.R.4    Hyde, S.C.5    Higgins, C.F.6
  • 178
    • 0024470598 scopus 로고
    • Nucleotide sequence of the Saccharomyces cerevisiae PUT4 proline-permease-encoding gene: Similarities between CAN1, HIP1 and PUT4 permeases
    • Vandenbol M, Jauniaux JC, Grenson M. 1989. Nucleotide sequence of the Saccharomyces cerevisiae PUT4 proline-permease-encoding gene: similarities between CAN1, HIP1 and PUT4 permeases. Gene 83:153-59
    • (1989) Gene , vol.83 , pp. 153-159
    • Vandenbol, M.1    Jauniaux, J.C.2    Grenson, M.3
  • 179
    • 0022427814 scopus 로고
    • The structure of the lactose permease derived from Raman spectroscopy and prediction methods
    • Vogel H, Wright JK, Jähnig F. 1985. The structure of the lactose permease derived from Raman spectroscopy and prediction methods. EMBO J. 5:3625-31
    • (1985) EMBO J. , vol.5 , pp. 3625-3631
    • Vogel, H.1    Wright, J.K.2    Jähnig, F.3
  • 180
    • 0027057980 scopus 로고
    • In vivo phosphorylation of the yeast uracil permease
    • Volland C, Gamier C, Haguenauer-Tsapis R. 1992. In vivo phosphorylation of the yeast uracil permease. J. Biol. Chem. 267:23767-71
    • (1992) J. Biol. Chem. , vol.267 , pp. 23767-23771
    • Volland, C.1    Gamier, C.2    Haguenauer-Tsapis, R.3
  • 181
    • 0028307059 scopus 로고
    • Endocytosis and degradation of the yeast uracil permease under adverse conditions
    • Volland C, Urban-Grimal D, Geraud G, Haguenauer-Tsapis R. 1994. Endocytosis and degradation of the yeast uracil permease under adverse conditions. J. Biol. Chem. 269:9833-41
    • (1994) J. Biol. Chem. , vol.269 , pp. 9833-9841
    • Volland, C.1    Urban-Grimal, D.2    Geraud, G.3    Haguenauer-Tsapis, R.4
  • 182
    • 0028917799 scopus 로고
    • The 3-oxo-glutarate/malate translocator of chloroplast envelope membranes: Molecular cloning of a transporter containing a 12-helix motif and expression of the functional protein in yeast cells
    • Weber A, Menzlaff E, Arbinger B, Gutensohn M, Eckerskorn C, et al. 1995. The 3-oxo-glutarate/malate translocator of chloroplast envelope membranes: molecular cloning of a transporter containing a 12-helix motif and expression of the functional protein in yeast cells. Biochemistry 34:2621-27
    • (1995) Biochemistry , vol.34 , pp. 2621-2627
    • Weber, A.1    Menzlaff, E.2    Arbinger, B.3    Gutensohn, M.4    Eckerskorn, C.5
  • 183
    • 0025329820 scopus 로고
    • The purine-cytosine permease gene of Saccharomyces cerevisiae: Primary structure and deduced protein sequence of the FCY2 gene product
    • Weber E, Rodriguez C, Chevallier MR, Jund R. 1990. The purine-cytosine permease gene of Saccharomyces cerevisiae: primary structure and deduced protein sequence of the FCY2 gene product. Mol. Microbiol. 4:585-96
    • (1990) Mol. Microbiol. , vol.4 , pp. 585-596
    • Weber, E.1    Rodriguez, C.2    Chevallier, M.R.3    Jund, R.4
  • 184
    • 0028005654 scopus 로고
    • Isolation of a family of cDNA clones from Ricinus communis L. with close homology to the hexose carriers
    • Weig A, Franz J, Sauer N, Komor E. 1994. Isolation of a family of cDNA clones from Ricinus communis L. with close homology to the hexose carriers. J. Plant. Physiol. 143:178-83
    • (1994) J. Plant. Physiol. , vol.143 , pp. 178-183
    • Weig, A.1    Franz, J.2    Sauer, N.3    Komor, E.4
  • 185
    • 0014938483 scopus 로고
    • Lactose transport coupled to proton movements in Escherichia coli
    • West IC. 1970. Lactose transport coupled to proton movements in Escherichia coli. Biochem. Biophys. Res. Commun. 41:655-61
    • (1970) Biochem. Biophys. Res. Commun. , vol.41 , pp. 655-661
    • West, I.C.1
  • 189
    • 0000939796 scopus 로고
    • Molecular cloning and structural analysis of the phosphate translocator from pea chloroplasts and its comparison to the spinach phosphate translocator
    • Willey DL, Fischer K. Wachter E. Link TA, Flügge UI. 1991. Molecular cloning and structural analysis of the phosphate translocator from pea chloroplasts and its comparison to the spinach phosphate translocator. Planta 183:451-J61
    • (1991) Planta , vol.183
    • Willey, D.L.1    Fischer, K.2    Wachter, E.3    Link, T.A.4    Flügge, U.I.5
  • 191
    • 0029074762 scopus 로고
    • Helix packing of lactose permease in Escherichia coli studied by site-directed chemical cleavage
    • Wu J, Perrin DM, Sigman DS, Kaback HR. 1995. Helix packing of lactose permease in Escherichia coli studied by site-directed chemical cleavage. Proc.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9186-9190
    • Wu, J.1    Perrin, D.M.2    Sigman, D.S.3    Kaback, H.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.