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Volumn , Issue , 2006, Pages 433-448

Bacterial and eukaryotic transport systems

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EID: 40549094520     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1007/978-1-59745-145-1_25     Document Type: Chapter
Times cited : (5)

References (67)
  • 1
    • 0004139057 scopus 로고    scopus 로고
    • Oxford University Press, Oxford, UK
    • Cohen, S. S. (1998) A Guide to the Polyamines. Oxford University Press, Oxford, UK, pp. 1-543.
    • (1998) A Guide to the Polyamines , pp. 1-543
    • Cohen, S.S.1
  • 2
    • 0034685624 scopus 로고    scopus 로고
    • Polyamines: Mysterious modulators of cellular functions
    • Igarashi, K. and Kashiwagi, K. (2000) Polyamines: Mysterious modulators of cellular functions. Biochem. Biophys. Res. Commun. 271, 559-564.
    • (2000) Biochem. Biophys. Res. Commun. , vol.271 , pp. 559-564
    • Igarashi, K.1    Kashiwagi, K.2
  • 3
    • 0345688128 scopus 로고    scopus 로고
    • A perspective of polyamine metabolism
    • Wallace, H. M., Fraser, A. V., and Hughes, A. (2003) A perspective of polyamine metabolism. Biochem. J. 376, 1-14.
    • (2003) Biochem. J. , vol.376 , pp. 1-14
    • Wallace, H.M.1    Fraser, A.V.2    Hughes, A.3
  • 5
    • 0033572636 scopus 로고    scopus 로고
    • Polyamine transport in bacteria and yeast
    • Igarashi, K. and Kashiwagi, K. (1999) Polyamine transport in bacteria and yeast. Biochem. J. 344, 633-642.
    • (1999) Biochem. J. , vol.344 , pp. 633-642
    • Igarashi, K.1    Kashiwagi, K.2
  • 6
    • 0035002972 scopus 로고    scopus 로고
    • Polyamine uptake systems in Escherichia coli
    • Igarashi, K., Ito, K., and Kashiwagi, K. (2001) Polyamine uptake systems in Escherichia coli. Res. Microbiol. 152, 271-278.
    • (2001) Res. Microbiol. , vol.152 , pp. 271-278
    • Igarashi, K.1    Ito, K.2    Kashiwagi, K.3
  • 7
    • 0025786779 scopus 로고
    • Estimation of polyamine binding to macromolecules and ATP in bovine lymphocytes and rat liver
    • Watanabe, S., Kusama-Eguchi, K., Kobayashi, H., and Igarashi, K. (1991) Estimation of polyamine binding to macromolecules and ATP in bovine lymphocytes and rat liver. J. Biol. Chem. 266, 20,803-20,809.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20803-20809
    • Watanabe, S.1    Kusama-Eguchi, K.2    Kobayashi, H.3    Igarashi, K.4
  • 8
    • 0027265852 scopus 로고
    • Estimation of polyamine distribution and polyamine stimulation of protein synthesis in Escherichia coli
    • Miyamoto, S., Kashiwagi, K., Ito, K., Watanabe, S., and Igarashi, K. (1993) Estimation of polyamine distribution and polyamine stimulation of protein synthesis in Escherichia coli. Arch. Biochem. Biophys. 300, 63-68.
    • (1993) Arch. Biochem. Biophys. , vol.300 , pp. 63-68
    • Miyamoto, S.1    Kashiwagi, K.2    Ito, K.3    Watanabe, S.4    Igarashi, K.5
  • 9
    • 0030853492 scopus 로고    scopus 로고
    • Interactions of polyamines with ion channels
    • Williams, K. (1997) Interactions of polyamines with ion channels. Biochem. J. 325, 289-297.
    • (1997) Biochem. J. , vol.325 , pp. 289-297
    • Williams, K.1
  • 10
    • 0345689423 scopus 로고    scopus 로고
    • Glypican-1 is a vehicle for polyamine uptake in mammalian cells. A pivotal role for nitrosothiol-derived nitric oxide
    • Belting, M., Mani, K., Jönsson, M., et al. (2003) Glypican-1 is a vehicle for polyamine uptake in mammalian cells. A pivotal role for nitrosothiol-derived nitric oxide. J. Biol. Chem. 278, 47,181-47,189.
    • (2003) J. Biol. Chem. , vol.278 , pp. 47181-47189
    • Belting, M.1    Mani, K.2    Jönsson, M.3
  • 11
    • 0022512208 scopus 로고
    • Formation of a compensatory polyamine by Escherichia coli polyamine-requiring mutants during growth in the absence of polyamines
    • Igarashi, K., Kashiwagi, K., Hamasaki, H., et al. (1986) Formation of a compensatory polyamine by Escherichia coli polyamine-requiring mutants during growth in the absence of polyamines. J. Bacteriol. 166, 128-134.
    • (1986) J. Bacteriol. , vol.166 , pp. 128-134
    • Igarashi, K.1    Kashiwagi, K.2    Hamasaki, H.3
  • 12
    • 0025687503 scopus 로고
    • Isolation of polyamine transportdeficient mutants of Escherichia coli and cloning of the genes for polyamine transport proteins
    • Kashiwagi, K., Hosokawa, N., Furuchi, T., et al. (1990) Isolation of polyamine transportdeficient mutants of Escherichia coli and cloning of the genes for polyamine transport proteins. J. Biol. Chem. 265, 20,893-20,897.
    • (1990) J. Biol. Chem. , vol.265 , pp. 20893-20897
    • Kashiwagi, K.1    Hosokawa, N.2    Furuchi, T.3
  • 13
    • 0026542813 scopus 로고
    • Identification of elements involved in transcriptional regulation of the Escherichia coli cad operon by external pH
    • Watson, N., Dunyak, D. S., Rosey, E. L., Slonczewski, J. L., and Olson, E. R. (1992) Identification of elements involved in transcriptional regulation of the Escherichia coli cad operon by external pH. J. Bacteriol. 174, 530-540.
    • (1992) J. Bacteriol. , vol.174 , pp. 530-540
    • Watson, N.1    Dunyak, D.S.2    Rosey, E.L.3    Slonczewski, J.L.4    Olson, E.R.5
  • 14
    • 0026772547 scopus 로고
    • Nucleotide sequence of the Escherichia coli cad operon: A system for neutralization of low extracellular pH
    • Meng, S. Y. and Bennett, G. N. (1992) Nucleotide sequence of the Escherichia coli cad operon: A system for neutralization of low extracellular pH. J. Bacteriol. 174, 2659-2669.
    • (1992) J. Bacteriol. , vol.174 , pp. 2659-2669
    • Meng, S.Y.1    Bennett, G.N.2
  • 15
    • 0025838225 scopus 로고
    • Characteristics of the gene for a spermidine and putrescine transport system that maps at 15 min on the Escherichia coli chromosome
    • Furuchi, T., Kashiwagi, K., Kobayashi, H., and Igarashi, K. (1991) Characteristics of the gene for a spermidine and putrescine transport system that maps at 15 min on the Escherichia coli chromosome. J. Biol. Chem. 266, 20,928-20,933.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20928-20933
    • Furuchi, T.1    Kashiwagi, K.2    Kobayashi, H.3    Igarashi, K.4
  • 16
    • 0027389106 scopus 로고
    • Characteristics of the operon for a putrescine transport system that maps at 19 minutes on the Escherichia coli chromosome
    • Pistocchi, R., Kashiwagi, K., Miyamoto, S., et al. (1993) Characteristics of the operon for a putrescine transport system that maps at 19 minutes on the Escherichia coli chromosome. J. Biol. Chem. 268, 146-152.
    • (1993) J. Biol. Chem. , vol.268 , pp. 146-152
    • Pistocchi, R.1    Kashiwagi, K.2    Miyamoto, S.3
  • 17
    • 0001607723 scopus 로고
    • Distantly related sequences in the ?-and ?-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold
    • Walker, J. E., Saraste, M., Runswick, M. J., and Gay, N. J. (1982) Distantly related sequences in the ?-and ?-subunits of ATP synthase, myosin, kinases and other ATP-requiring enzymes and a common nucleotide binding fold. EMBO J. 1, 945-951.
    • (1982) EMBO J. , vol.1 , pp. 945-951
    • Walker, J.E.1    Saraste, M.2    Runswick, M.J.3    Gay, N.J.4
  • 18
    • 0022555851 scopus 로고
    • Bacterial periplasmic transport systems: Structure, mechanism, and evolution
    • Ames, G. F. (1986) Bacterial periplasmic transport systems: Structure, mechanism, and evolution. Annu. Rev. Biochem. 55, 397-425.
    • (1986) Annu. Rev. Biochem. , vol.55 , pp. 397-425
    • Ames, G.F.1
  • 19
    • 0028863669 scopus 로고
    • Spermidinepreferential uptake system in Escherichia coli. ATP hydrolysis by PotA protein and its association with membranes
    • Kashiwagi, K., Endo, H., Kobayashi, H., Takio, K., and Igarashi, K. (1995) Spermidinepreferential uptake system in Escherichia coli. ATP hydrolysis by PotA protein and its association with membranes. J. Biol. Chem. 270, 25,377-25,382.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25377-25382
    • Kashiwagi, K.1    Endo, H.2    Kobayashi, H.3    Takio, K.4    Igarashi, K.5
  • 20
    • 0027250513 scopus 로고
    • Functions of PotA and PotD proteins in spermidine-preferential uptake system in Escherichia coli
    • Kashiwagi, K., Miyamoto, S., Nukui, E., Kobayashi, H., and Igarashi, K. (1993) Functions of PotA and PotD proteins in spermidine-preferential uptake system in Escherichia coli. J. Biol. Chem. 268, 19,358-19,363.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19358-19363
    • Kashiwagi, K.1    Miyamoto, S.2    Nukui, E.3    Kobayashi, H.4    Igarashi, K.5
  • 21
    • 0037025302 scopus 로고    scopus 로고
    • The ATPase activity and the functional domain of PotA, a component of the spermidine-preferential uptake system in Escherichia coli
    • Kashiwagi, K., Innami, A., Zenda, R., Tomitori, H., and Igarashi, K. (2002) The ATPase activity and the functional domain of PotA, a component of the spermidine-preferential uptake system in Escherichia coli. J. Biol. Chem. 277, 24,212-24,219.
    • (2002) J. Biol. Chem. , vol.277 , pp. 24212-24219
    • Kashiwagi, K.1    Innami, A.2    Zenda, R.3    Tomitori, H.4    Igarashi, K.5
  • 22
    • 0030822352 scopus 로고    scopus 로고
    • Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium. Solubility, dimerization, and ATPase activity
    • Nikaido, K., Liu, P. Q., and Ames, G. F. (1997) Purification and characterization of HisP, the ATP-binding subunit of a traffic ATPase (ABC transporter), the histidine permease of Salmonella typhimurium. Solubility, dimerization, and ATPase activity. J. Biol. Chem. 272, 27,745-27,752.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27745-27752
    • Nikaido, K.1    Liu, P.Q.2    Ames, G.F.3
  • 23
    • 0033578760 scopus 로고    scopus 로고
    • One intact ATP-binding subunit is sufficient to support ATP hydrolysis and translocation in an ABC transporter, the histidine permease
    • Nikaido, K. and Ames, G. F. (1999) One intact ATP-binding subunit is sufficient to support ATP hydrolysis and translocation in an ABC transporter, the histidine permease. J. Biol. Chem. 274, 26,727-26,735.
    • (1999) J. Biol. Chem. , vol.274 , pp. 26727-26735
    • Nikaido, K.1    Ames, G.F.2
  • 24
    • 0030803791 scopus 로고    scopus 로고
    • Characterization of the adenosine triphosphatase activity of the periplasmic histidine permease, a traffic ATPase (ABC transporter)
    • Liu, C. E., Liu, P. Q., and Ames, G. F. (1997) Characterization of the adenosine triphosphatase activity of the periplasmic histidine permease, a traffic ATPase (ABC transporter). J. Biol. Chem. 272, 21,883-21,891.
    • (1997) J. Biol. Chem. , vol.272 , pp. 21883-21891
    • Liu, C.E.1    Liu, P.Q.2    Ames, G.F.3
  • 25
    • 0032542358 scopus 로고    scopus 로고
    • Crystal structure of the ATP-binding subunit of an ABC transporter
    • Hung, L. W., Wang, I. X., Nikaido, K., Liu, P. Q., Ames, G. F., and Kim, S. H. (1998) Crystal structure of the ATP-binding subunit of an ABC transporter. Nature 396, 703-707.
    • (1998) Nature , vol.396 , pp. 703-707
    • Hung, L.W.1    Wang, I.X.2    Nikaido, K.3    Liu, P.Q.4    Ames, G.F.5    Kim, S.H.6
  • 26
    • 0025904264 scopus 로고
    • The activity of the Escherichia coli MalK protein in maltose transport, regulation, and inducer exclusion can be separated by mutations
    • Kühnau, S., Reyes, M., Sievertsen, A., Shuman, H. A., and Boos, W. (1991) The activity of the Escherichia coli MalK protein in maltose transport, regulation, and inducer exclusion can be separated by mutations. J. Bacteriol. 173, 2180-2186.
    • (1991) J. Bacteriol. , vol.173 , pp. 2180-2186
    • Kühnau, S.1    Reyes, M.2    Sievertsen, A.3    Shuman, H.A.4    Boos, W.5
  • 27
    • 0033954071 scopus 로고    scopus 로고
    • Novel missense mutations that affect the transport function of MalK, the ATP-binding-cassette subunit of the Salmonella enterica serovar typhimurium maltose transport system
    • Hunke, S., Landmesser, H., and Schneider, E. (2000) Novel missense mutations that affect the transport function of MalK, the ATP-binding-cassette subunit of the Salmonella enterica serovar typhimurium maltose transport system. J. Bacteriol. 182, 1432-1436.
    • (2000) J. Bacteriol. , vol.182 , pp. 1432-1436
    • Hunke, S.1    Landmesser, H.2    Schneider, E.3
  • 28
    • 0029933361 scopus 로고    scopus 로고
    • Crystal structure of PotD, the primary receptor of the polyamine transport system in Escherichia coli
    • Sugiyama, S., Vassylyev, D. G., Matsushima, M., Kashiwagi, K., Igarashi, K., and Morikawa, K. (1996) Crystal structure of PotD, the primary receptor of the polyamine transport system in Escherichia coli. J. Biol. Chem. 271, 9519-9525.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9519-9525
    • Sugiyama, S.1    Vassylyev, D.G.2    Matsushima, M.3    Kashiwagi, K.4    Igarashi, K.5    Morikawa, K.6
  • 29
    • 0026493924 scopus 로고
    • Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis
    • Sharff, A. J., Rodseth, L. E., Spurlino, J. C., and Quiocho, F. A. (1992) Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis. Biochemistry 31, 10,657-10,663.
    • (1992) Biochemistry , vol.31 , pp. 10657-10663
    • Sharff, A.J.1    Rodseth, L.E.2    Spurlino, J.C.3    Quiocho, F.A.4
  • 30
    • 15844379305 scopus 로고    scopus 로고
    • Spermidine-preferential uptake system in Escherichia coli. Identification of amino acids involved in polyamine binding in PotD protein
    • Kashiwagi, K., Pistocchi, R., Shibuya, S., Sugiyama, S., Morikawa, K., and Igarashi, K. (1996) Spermidine-preferential uptake system in Escherichia coli. Identification of amino acids involved in polyamine binding in PotD protein. J. Biol. Chem. 271, 12,205-12,208.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12205-12208
    • Kashiwagi, K.1    Pistocchi, R.2    Shibuya, S.3    Sugiyama, S.4    Morikawa, K.5    Igarashi, K.6
  • 31
    • 0032504154 scopus 로고    scopus 로고
    • Crystal structure and mutational analysis of the Escherichia coli putrescine receptor. Structural basis for substrate specificity
    • Vassylyev, D. G., Tomitori, H., Kashiwagi, K., Morikawa, K., and Igarashi, K. (1998) Crystal structure and mutational analysis of the Escherichia coli putrescine receptor. Structural basis for substrate specificity. J. Biol. Chem. 273, 17,604-17,609.
    • (1998) J. Biol. Chem. , vol.273 , pp. 17604-17609
    • Vassylyev, D.G.1    Tomitori, H.2    Kashiwagi, K.3    Morikawa, K.4    Igarashi, K.5
  • 32
    • 0033593344 scopus 로고    scopus 로고
    • Transcriptional inhibition of the operon for the spermidine uptake system by the substrate-binding protein PotD
    • Antognoni, F., Del Duca, S., Kuraishi, A., et al. (1999) Transcriptional inhibition of the operon for the spermidine uptake system by the substrate-binding protein PotD. J. Biol. Chem. 274, 1942-1948.
    • (1999) J. Biol. Chem. , vol.274 , pp. 1942-1948
    • Antognoni, F.1    Del Duca, S.2    Kuraishi, A.3
  • 33
    • 0028787734 scopus 로고
    • Regulation of RNA polymerase sigma subunit synthesis in Escherichia coli: Intracellular levels of ?70 and ?38
    • Jishage, M. and Ishihama, A. (1995) Regulation of RNA polymerase sigma subunit synthesis in Escherichia coli: Intracellular levels of ?70 and ?38. J. Bacteriol. 177, 6832-6835.
    • (1995) J. Bacteriol. , vol.177 , pp. 6832-6835
    • Jishage, M.1    Ishihama, A.2
  • 34
    • 0025720216 scopus 로고
    • Coexistence of the genes for putrescine transport protein and ornithine decarboxylase at 16 min on Escherichia coli chromosome
    • Kashiwagi, K., Suzuki, T., Suzuki, F., Furuchi, T., Kobayashi, H., and Igarashi, K. (1991) Coexistence of the genes for putrescine transport protein and ornithine decarboxylase at 16 min on Escherichia coli chromosome. J. Biol. Chem. 266, 20,922-20,927.
    • (1991) J. Biol. Chem. , vol.266 , pp. 20922-20927
    • Kashiwagi, K.1    Suzuki, T.2    Suzuki, F.3    Furuchi, T.4    Kobayashi, H.5    Igarashi, K.6
  • 35
    • 0026583203 scopus 로고
    • Excretion of putrescine by the putrescine-ornithine antiporter encoded by the PotE gene of Escherichia coli
    • Kashiwagi, K., Miyamoto, S., Suzuki, F., Kobayashi, H., and Igarashi, K. (1992) Excretion of putrescine by the putrescine-ornithine antiporter encoded by the PotE gene of Escherichia coli. Proc. Natl. Acad. Sci. USA 89, 4529-4533.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 4529-4533
    • Kashiwagi, K.1    Miyamoto, S.2    Suzuki, F.3    Kobayashi, H.4    Igarashi, K.5
  • 36
    • 0030889906 scopus 로고    scopus 로고
    • Excretion and uptake of putrescine by the PotE protein in Escherichia coli
    • Kashiwagi, K., Shibuya, S., Tomitori, H., Kuraishi, A., and Igarashi, K. (1997) Excretion and uptake of putrescine by the PotE protein in Escherichia coli. J. Biol. Chem. 272, 6318-6323.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6318-6323
    • Kashiwagi, K.1    Shibuya, S.2    Tomitori, H.3    Kuraishi, A.4    Igarashi, K.5
  • 37
    • 0034680862 scopus 로고    scopus 로고
    • Identification of the putrescine recognition site on polyamine transport protein PotE
    • Kashiwagi, K., Kuraishi, A., Tomitori, H., et al. (2000) Identification of the putrescine recognition site on polyamine transport protein PotE. J. Biol. Chem. 275, 36,007-36,012.
    • (2000) J. Biol. Chem. , vol.275 , pp. 36007-36012
    • Kashiwagi, K.1    Kuraishi, A.2    Tomitori, H.3
  • 38
    • 1542721578 scopus 로고    scopus 로고
    • Excretion and uptake of cadaverine by CadB and its physiological functions in Escherichia coli
    • Soksawatmaekhin, W., Kuraishi, A., Sakata, K., Kashiwagi, K., and Igarashi, K. (2004) Excretion and uptake of cadaverine by CadB and its physiological functions in Escherichia coli. Mol. Microbiol. 51, 1401-1412.
    • (2004) Mol. Microbiol. , vol.51 , pp. 1401-1412
    • Soksawatmaekhin, W.1    Kuraishi, A.2    Sakata, K.3    Kashiwagi, K.4    Igarashi, K.5
  • 39
    • 0028337298 scopus 로고
    • Involvement of ribonuclease III in the enhancement of expression of the speF-potE operon encoding inducible ornithine decarboxylase and polyamine transport protein
    • Kashiwagi, K.,Watanabe, R., and Igarashi, K. (1994) Involvement of ribonuclease III in the enhancement of expression of the speF-potE operon encoding inducible ornithine decarboxylase and polyamine transport protein. Biochem. Biophys. Res. Commun. 200, 591-597.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 591-597
    • Kashiwagi, K.1    Watanabe, R.2    Igarashi, K.3
  • 40
  • 41
    • 0016587983 scopus 로고
    • Effect of RNAase III, cleavage on translation of bacteriophage T7 messenger RNAs
    • Dunn, J. J. and Studier, F. W. (1975) Effect of RNAase III, cleavage on translation of bacteriophage T7 messenger RNAs. J. Mol. Biol. 99, 487-499.
    • (1975) J. Mol. Biol. , vol.99 , pp. 487-499
    • Dunn, J.J.1    Studier, F.W.2
  • 42
    • 0028111321 scopus 로고
    • Polyamine-sensitive magnesium transport in Saccharomyces cerevisiae
    • Maruyama, T., Masuda, N., Kakinuma, Y., and Igarashi, K. (1994) Polyamine-sensitive magnesium transport in Saccharomyces cerevisiae. Biochim. Biophys. Acta 1194, 289-295.
    • (1994) Biochim. Biophys. Acta , vol.1194 , pp. 289-295
    • Maruyama, T.1    Masuda, N.2    Kakinuma, Y.3    Igarashi, K.4
  • 43
    • 0028784707 scopus 로고
    • Cloning of the gene encoding a putative serine/threonine protein kinase which enhances spermine uptake in Saccharomyces cerevisiae
    • Kakinuma, Y., Maruyama, T., Nozaki, T., Wada, Y., Ohsumi, Y., and Igarashi, K. (1995) Cloning of the gene encoding a putative serine/threonine protein kinase which enhances spermine uptake in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 216, 985-992.
    • (1995) Biochem. Biophys. Res. Commun. , vol.216 , pp. 985-992
    • Kakinuma, Y.1    Maruyama, T.2    Nozaki, T.3    Wada, Y.4    Ohsumi, Y.5    Igarashi, K.6
  • 44
    • 0343373759 scopus 로고    scopus 로고
    • A second gene encoding a putative serine/threonine protein kinase which enhances spermine uptake in Saccharomyces cerevisiae
    • Nozaki, T., Nishimura, K., Michael, A. J., Maruyama, T., Kakinuma, Y., and Igarashi, K. (1996) A second gene encoding a putative serine/threonine protein kinase which enhances spermine uptake in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 228, 452-458.
    • (1996) Biochem. Biophys. Res. Commun. , vol.228 , pp. 452-458
    • Nozaki, T.1    Nishimura, K.2    Michael, A.J.3    Maruyama, T.4    Kakinuma, Y.5    Igarashi, K.6
  • 45
    • 0030977164 scopus 로고    scopus 로고
    • The STK2 gene, which encodes a putative Ser/Thr protein kinase, is required for high-affinity spermidine transport in Saccharomyces cerevisiae
    • Kaouass, M., Audette, M., Ramotar, D., et al. (1997) The STK2 gene, which encodes a putative Ser/Thr protein kinase, is required for high-affinity spermidine transport in Saccharomyces cerevisiae. Mol. Cell. Biol. 17, 2994-3004.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 2994-3004
    • Kaouass, M.1    Audette, M.2    Ramotar, D.3
  • 46
    • 0031917190 scopus 로고    scopus 로고
    • The spermidine transport system is regulated by ligand inactivation, endocytosis, and by the Npr1p Ser/Thr protein kinase in Saccharomyces cerevisiae
    • Kaouass, M., Gamache, I., Ramotar, D., Audette, M., and Poulin, R. (1998) The spermidine transport system is regulated by ligand inactivation, endocytosis, and by the Npr1p Ser/Thr protein kinase in Saccharomyces cerevisiae. J. Biol. Chem. 273, 2109-2117.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2109-2117
    • Kaouass, M.1    Gamache, I.2    Ramotar, D.3    Audette, M.4    Poulin, R.5
  • 47
    • 1342281677 scopus 로고    scopus 로고
    • Uptake of GABA and putrescine by UGA4 on the vacuolar membrane in Saccharomyces cerevisiae
    • Uemura, T., Tomonari, Y., Kashiwagi, K., and Igarashi, K. (2004) Uptake of GABA and putrescine by UGA4 on the vacuolar membrane in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 315, 1082-1087.
    • (2004) Biochem. Biophys. Res. Commun. , vol.315 , pp. 1082-1087
    • Uemura, T.1    Tomonari, Y.2    Kashiwagi, K.3    Igarashi, K.4
  • 48
    • 13844266300 scopus 로고    scopus 로고
    • Uptake of putrescine and spermidine by Gap1p on the plasma membrane in Saccharomyces cerevisiae
    • Uemura, T., Kashiwagi, K., and Igarashi, K. (2005) Uptake of putrescine and spermidine by Gap1p on the plasma membrane in Saccharomyces cerevisiae. Biochem. Biophys. Res. Commun. 328, 1028-1033.
    • (2005) Biochem. Biophys. Res. Commun. , vol.328 , pp. 1028-1033
    • Uemura, T.1    Kashiwagi, K.2    Igarashi, K.3
  • 49
    • 0030910587 scopus 로고    scopus 로고
    • Efflux of the natural polyamine spermidine facilitated by the Bacillus subtilis multidrug transporter Blt
    • Woolridge, D. P., Vazquez-Laslop, N., Markham, P. N., Chevalier, M. S., Gerner, E. W., and Neyfakh, A. A. (1997) Efflux of the natural polyamine spermidine facilitated by the Bacillus subtilis multidrug transporter Blt. J. Biol. Chem. 272, 8864-8866.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8864-8866
    • Woolridge, D.P.1    Vazquez-Laslop, N.2    Markham, P.N.3    Chevalier, M.S.4    Gerner, E.W.5    Neyfakh, A.A.6
  • 50
  • 51
    • 0033525210 scopus 로고    scopus 로고
    • Identification of a gene for a polyamine transport protein in yeast
    • Tomitori, H., Kashiwagi, K., Sakata, K., Kakinuma, Y., and Igarashi, K. (1999) Identification of a gene for a polyamine transport protein in yeast. J. Biol. Chem. 274, 3265-3267.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3265-3267
    • Tomitori, H.1    Kashiwagi, K.2    Sakata, K.3    Kakinuma, Y.4    Igarashi, K.5
  • 53
    • 0037630437 scopus 로고    scopus 로고
    • Localization and function of the yeast multidrug transporter Tpolp
    • Albertsen, M., Bellahn, I., Krämer, R., and Waffenschmidt, S. (2003) Localization and function of the yeast multidrug transporter Tpolp. J. Biol. Chem. 278, 12,820-12,825.
    • (2003) J. Biol. Chem. , vol.278 , pp. 12820-12825
    • Albertsen, M.1    Bellahn, I.2    Krämer, R.3    Waffenschmidt, S.4
  • 54
    • 15744391238 scopus 로고    scopus 로고
    • Characteristics of the polyamine transporter TPO1 and regulation of its activity and cellular localization by phosphorylation
    • Uemura, T., Tachihara, K., Tomitori, H., Kashiwagi, K., and Igarashi, K. (2005) Characteristics of the polyamine transporter TPO1 and regulation of its activity and cellular localization by phosphorylation. J. Biol. Chem. 280, 9646-9652.
    • (2005) J. Biol. Chem. , vol.280 , pp. 9646-9652
    • Uemura, T.1    Tachihara, K.2    Tomitori, H.3    Kashiwagi, K.4    Igarashi, K.5
  • 55
    • 0023689180 scopus 로고
    • Characterization of the inducible polyamine transporter in bovine lymphocytes
    • Kakinuma, Y., Hoshino, K., and Igarashi, K. (1988) Characterization of the inducible polyamine transporter in bovine lymphocytes. Eur. J. Biochem. 176, 409-414.
    • (1988) Eur. J. Biochem. , vol.176 , pp. 409-414
    • Kakinuma, Y.1    Hoshino, K.2    Igarashi, K.3
  • 56
    • 0017255395 scopus 로고
    • Putrescine transport is greatly increased in human fibroblasts initiated to proliferate
    • Pohjanpelto, P. (1976) Putrescine transport is greatly increased in human fibroblasts initiated to proliferate. J. Cell. Biol. 68, 512-520.
    • (1976) J. Cell. Biol. , vol.68 , pp. 512-520
    • Pohjanpelto, P.1
  • 57
    • 0017155843 scopus 로고
    • Polyamine transport and metabolism in mouse mammary gland. General properties and hormonal regulation
    • Kano, K. and Oka, T. (1976) Polyamine transport and metabolism in mouse mammary gland. General properties and hormonal regulation. J. Biol. Chem. 251, 2795-2800.
    • (1976) J. Biol. Chem. , vol.251 , pp. 2795-2800
    • Kano, K.1    Oka, T.2
  • 58
    • 0026523144 scopus 로고
    • Antizyme, a protein induced by polyamines, accelerates the degradation of ornithine decarboxylase in Chinese-hamster ovary-cell extracts
    • Murakami, Y., Tanaka, K., Matsufuji, S., Miyazaki, Y., and Hayashi, S. (1992) Antizyme, a protein induced by polyamines, accelerates the degradation of ornithine decarboxylase in Chinese-hamster ovary-cell extracts. Biochem. J. 283, 661-664.
    • (1992) Biochem. J. , vol.283 , pp. 661-664
    • Murakami, Y.1    Tanaka, K.2    Matsufuji, S.3    Miyazaki, Y.4    Hayashi, S.5
  • 59
    • 0026714435 scopus 로고
    • Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination
    • Murakami Y, Matsufuji S, Kameji T, et al. (1992) Ornithine decarboxylase is degraded by the 26S proteasome without ubiquitination. Nature 360, 597-599.
    • (1992) Nature , vol.360 , pp. 597-599
    • Murakami, S.1    Matsufuji, Y.2    Kameji, T.3
  • 60
    • 0028598524 scopus 로고
    • Antizyme protects against abnormal accumulation and toxicity of polyamines in ornithine decarboxylase-overproducing cells
    • Suzuki, T., He, Y., Kashiwagi, K., Murakami, Y., Hayashi, S., and Igarashi, K. (1994) Antizyme protects against abnormal accumulation and toxicity of polyamines in ornithine decarboxylase-overproducing cells. Proc. Natl. Acad. Sci. USA 91, 8930-8934.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8930-8934
    • Suzuki, T.1    He, Y.2    Kashiwagi, K.3    Murakami, Y.4    Hayashi, S.5    Igarashi, K.6
  • 61
    • 0028296140 scopus 로고
    • Feedback repression of polyamine transport is mediated by antizyme in mammalian tissue-culture cells
    • Mitchell, J. L., Judd, G. G., Bareyal-Leyser, A., and Ling, S. Y. (1994) Feedback repression of polyamine transport is mediated by antizyme in mammalian tissue-culture cells. Biochem. J. 299, 19-22.
    • (1994) Biochem. J. , vol.299 , pp. 19-22
    • Mitchell, J.L.1    Judd, G.G.2    Bareyal-Leyser, A.3    Ling, S.Y.4
  • 62
    • 0031577527 scopus 로고    scopus 로고
    • Identification of regulatory region of antizyme necessary for the negative regulation of polyamine transport
    • Sakata, K., Fukuchi-Shimogori, T., Kashiwagi, K., and Igarashi, K. (1997) Identification of regulatory region of antizyme necessary for the negative regulation of polyamine transport. Biochem. Biophys. Res. Commun. 238, 415-419.
    • (1997) Biochem. Biophys. Res. Commun. , vol.238 , pp. 415-419
    • Sakata, K.1    Fukuchi-Shimogori, T.2    Kashiwagi, K.3    Igarashi, K.4
  • 63
    • 0034177792 scopus 로고    scopus 로고
    • Properties of a polyamine transporter regulated by antizyme
    • Sakata, K., Kashiwagi, K., and Igarashi, K. (2000) Properties of a polyamine transporter regulated by antizyme. Biochem. J. 347, 297-303.
    • (2000) Biochem. J. , vol.347 , pp. 297-303
    • Sakata, K.1    Kashiwagi, K.2    Igarashi, K.3
  • 64
    • 0018233850 scopus 로고
    • Isolation of mutant mammalian cells altered in polyamine transport
    • Mandel, J. L. and Flintoff, W. F. (1978) Isolation of mutant mammalian cells altered in polyamine transport. J. Cell. Physiol. 97, 335-343.
    • (1978) J. Cell. Physiol. , vol.97 , pp. 335-343
    • Mandel, J.L.1    Flintoff, W.F.2
  • 65
    • 3142686000 scopus 로고    scopus 로고
    • TATA-binding protein-associated factor 7 regulates polyamine transport activity and polyamine analog-induced apoptosis
    • Fukuchi, J., Hiipakka, R. A., Kokontis, J. M., Nishimura, K., Igarashi, K., and Liao, S. (2004) TATA-binding protein-associated factor 7 regulates polyamine transport activity and polyamine analog-induced apoptosis. J. Biol. Chem. 279, 29,921-29,929.
    • (2004) J. Biol. Chem. , vol.279 , pp. 29921-29929
    • Fukuchi, J.1    Hiipakka, R.A.2    Kokontis, J.M.3    Nishimura, K.4    Igarashi, K.5    Liao, S.6
  • 66
    • 10444227401 scopus 로고    scopus 로고
    • A fluorescent probe of polyamine transport accumulates into intracellular acidic vesicles via a two-step mechanism
    • Soulet, D., Gagnon, B., Rivest, S., Audette, M., and Poulin, R. (2004) A fluorescent probe of polyamine transport accumulates into intracellular acidic vesicles via a two-step mechanism. J. Biol. Chem. 279, 49,355-49,366.
    • (2004) J. Biol. Chem. , vol.279 , pp. 49355-49366
    • Soulet, D.1    Gagnon, B.2    Rivest, S.3    Audette, M.4    Poulin, R.5
  • 67
    • 0033051714 scopus 로고    scopus 로고
    • A regulatory domain (R1-R2) in the amino terminus of the N-methyl-D-aspartate receptor: Effects of spermine, protons, and ifenprodil, and structural similarity to bacterial leucine/isoleucine/valine binding protein
    • Masuko, T., Kashiwagi, K., Kuno, T., et al. (1999) A regulatory domain (R1-R2) in the amino terminus of the N-methyl-D-aspartate receptor: effects of spermine, protons, and ifenprodil, and structural similarity to bacterial leucine/isoleucine/valine binding protein. Mol. Pharmacol. 55, 957-969.
    • (1999) Mol. Pharmacol. , vol.55 , pp. 957-969
    • Masuko, T.1    Kashiwagi, K.2    Kuno, T.3


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