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Volumn 1778, Issue 6, 2008, Pages 1483-1492

Membrane partitioning of various δ-opioid receptor forms before and after agonist activations: The effect of cholesterol

Author keywords

Cholesterol; GPCR; hDOR; Hydrophobic mismatch; Lateral organization; Raft

Indexed keywords

CHOLESTEROL; DELTA OPIATE RECEPTOR; DETERGENT; GREEN FLUORESCENT PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; HYBRID PROTEIN;

EID: 43649092317     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2008.03.017     Document Type: Article
Times cited : (19)

References (57)
  • 1
    • 0030822255 scopus 로고    scopus 로고
    • Lipid microdomains in cell surface membranes
    • Edidin M. Lipid microdomains in cell surface membranes. Curr. Opin. Struct. Biol. 7 (1997) 528-532
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 528-532
    • Edidin, M.1
  • 3
    • 15544387138 scopus 로고    scopus 로고
    • Consequences of lipid raft association on G-protein-coupled receptor function
    • Becher A., and McIlhinney R.A. Consequences of lipid raft association on G-protein-coupled receptor function. Biochem. Soc. Symp. (2005) 151-164
    • (2005) Biochem. Soc. Symp. , pp. 151-164
    • Becher, A.1    McIlhinney, R.A.2
  • 5
    • 0022568619 scopus 로고
    • Spin-label studies on phosphatidylcholine-cholesterol membranes: effects of alkyl chain length and unsaturation in the fluid phase
    • Kusumi A., Subczynski W.K., Pasenkiewicz-Gierula M., Hyde J.S., and Merkle H. Spin-label studies on phosphatidylcholine-cholesterol membranes: effects of alkyl chain length and unsaturation in the fluid phase. Biochim. Biophys. Acta 854 (1986) 307-317
    • (1986) Biochim. Biophys. Acta , vol.854 , pp. 307-317
    • Kusumi, A.1    Subczynski, W.K.2    Pasenkiewicz-Gierula, M.3    Hyde, J.S.4    Merkle, H.5
  • 6
    • 0026767199 scopus 로고
    • Lateral diffusion in the liquid phases of dimyristoylphosphatidylcholine/cholesterol lipid bilayers: a free volume analysis
    • Almeida P.F., Vaz W.L., and Thompson T.E. Lateral diffusion in the liquid phases of dimyristoylphosphatidylcholine/cholesterol lipid bilayers: a free volume analysis. Biochemistry 31 (1992) 6739-6747
    • (1992) Biochemistry , vol.31 , pp. 6739-6747
    • Almeida, P.F.1    Vaz, W.L.2    Thompson, T.E.3
  • 7
    • 0026058545 scopus 로고
    • Cholesterol-induced fluid-phase immiscibility in membranes
    • Sankaram M.B., and Thompson T.E. Cholesterol-induced fluid-phase immiscibility in membranes. Proc. Natl. Acad. Sci. U. S. A. 88 (1991) 8686-8690
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 8686-8690
    • Sankaram, M.B.1    Thompson, T.E.2
  • 8
    • 0035823586 scopus 로고    scopus 로고
    • Effect of the structure of natural sterols and sphingolipids on the formation of ordered sphingolipid/sterol domains (rafts). Comparison of cholesterol to plant, fungal, and disease-associated sterols and comparison of sphingomyelin, cerebrosides, and ceramide
    • Xu X., Bittman R., Duportail G., Heissler D., Vilcheze C., and London E. Effect of the structure of natural sterols and sphingolipids on the formation of ordered sphingolipid/sterol domains (rafts). Comparison of cholesterol to plant, fungal, and disease-associated sterols and comparison of sphingomyelin, cerebrosides, and ceramide. J. Biol. Chem. 276 (2001) 33540-33546
    • (2001) J. Biol. Chem. , vol.276 , pp. 33540-33546
    • Xu, X.1    Bittman, R.2    Duportail, G.3    Heissler, D.4    Vilcheze, C.5    London, E.6
  • 9
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: elusive or illusive?
    • Munro S. Lipid rafts: elusive or illusive?. Cell 115 (2003) 377-388
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 10
    • 0037959071 scopus 로고    scopus 로고
    • The state of lipid rafts: from model membranes to cells
    • Edidin M. The state of lipid rafts: from model membranes to cells. Annu. Rev. Biophys. Biomol. Struct. 32 (2003) 257-283
    • (2003) Annu. Rev. Biophys. Biomol. Struct. , vol.32 , pp. 257-283
    • Edidin, M.1
  • 11
    • 0033055564 scopus 로고    scopus 로고
    • Detergent-insoluble glycosphingolipid/cholesterol-rich membrane domains, lipid rafts and caveolae
    • (review)
    • Hooper N.M. Detergent-insoluble glycosphingolipid/cholesterol-rich membrane domains, lipid rafts and caveolae. (review). Mol. Membr. Biol. 16 (1999) 145-156
    • (1999) Mol. Membr. Biol. , vol.16 , pp. 145-156
    • Hooper, N.M.1
  • 12
    • 0029101114 scopus 로고
    • Reconstitution of membrane proteins into liposomes: application to energy-transducing membrane proteins
    • Rigaud J.L., Pitard B., and Levy D. Reconstitution of membrane proteins into liposomes: application to energy-transducing membrane proteins. Biochim. Biophys. Acta 1231 (1995) 223-246
    • (1995) Biochim. Biophys. Acta , vol.1231 , pp. 223-246
    • Rigaud, J.L.1    Pitard, B.2    Levy, D.3
  • 14
    • 38949168914 scopus 로고    scopus 로고
    • Visualisation of detergent solubilisation of membranes: implications for the isolation of rafts
    • Garner A.E., Smith A., and Hooper N.M. Visualisation of detergent solubilisation of membranes: implications for the isolation of rafts. Biophys. J. 94 (2008) 1326-1340
    • (2008) Biophys. J. , vol.94 , pp. 1326-1340
    • Garner, A.E.1    Smith, A.2    Hooper, N.M.3
  • 15
    • 33746928724 scopus 로고    scopus 로고
    • Biochemical characterization of detergent-resistant membranes: a systematic approach
    • Babiychuk E.B., and Draeger A. Biochemical characterization of detergent-resistant membranes: a systematic approach. Biochem. J. 397 (2006) 407-416
    • (2006) Biochem. J. , vol.397 , pp. 407-416
    • Babiychuk, E.B.1    Draeger, A.2
  • 16
    • 0034695484 scopus 로고    scopus 로고
    • Lipid-dependent targeting of G proteins into rafts
    • Moffett S., Brown D.A., and Linder M.E. Lipid-dependent targeting of G proteins into rafts. J. Biol. Chem. 275 (2000) 2191-2198
    • (2000) J. Biol. Chem. , vol.275 , pp. 2191-2198
    • Moffett, S.1    Brown, D.A.2    Linder, M.E.3
  • 17
    • 2342451911 scopus 로고    scopus 로고
    • G-protein coupled receptors in lipid rafts and caveolae: how, when and why do they go there?
    • Chini B., and Parenti M. G-protein coupled receptors in lipid rafts and caveolae: how, when and why do they go there?. J. Mol. Endocrinol. 32 (2004) 325-338
    • (2004) J. Mol. Endocrinol. , vol.32 , pp. 325-338
    • Chini, B.1    Parenti, M.2
  • 18
    • 0033747206 scopus 로고    scopus 로고
    • Plasmon resonance studies of agonist/antagonist binding to the human delta-opioid receptor: new structural insights into receptor-ligand interactions
    • Salamon Z., Cowell S., Varga E., Yamamura H.I., Hruby V.J., and Tollin G. Plasmon resonance studies of agonist/antagonist binding to the human delta-opioid receptor: new structural insights into receptor-ligand interactions. Biophys. J. 79 (2000) 2463-2474
    • (2000) Biophys. J. , vol.79 , pp. 2463-2474
    • Salamon, Z.1    Cowell, S.2    Varga, E.3    Yamamura, H.I.4    Hruby, V.J.5    Tollin, G.6
  • 19
    • 2142766875 scopus 로고    scopus 로고
    • Different structural states of the proteolipid membrane are produced by ligand binding to the human delta-opioid receptor as shown by plasmon-waveguide resonance spectroscopy
    • Alves I.D., Cowell S.M., Salamon Z., Devanathan S., Tollin G., and Hruby V.J. Different structural states of the proteolipid membrane are produced by ligand binding to the human delta-opioid receptor as shown by plasmon-waveguide resonance spectroscopy. Mol. Pharmacol. 65 (2004) 1248-1257
    • (2004) Mol. Pharmacol. , vol.65 , pp. 1248-1257
    • Alves, I.D.1    Cowell, S.M.2    Salamon, Z.3    Devanathan, S.4    Tollin, G.5    Hruby, V.J.6
  • 20
    • 21744442451 scopus 로고    scopus 로고
    • Ligand modulation of lateral segregation of a G-protein-coupled receptor into lipid microdomains in sphingomyelin/phosphatidylcholine solid-supported bilayers
    • Alves I.D., Salamon Z., Hruby V.J., and Tollin G. Ligand modulation of lateral segregation of a G-protein-coupled receptor into lipid microdomains in sphingomyelin/phosphatidylcholine solid-supported bilayers. Biochemistry 44 (2005) 9168-9178
    • (2005) Biochemistry , vol.44 , pp. 9168-9178
    • Alves, I.D.1    Salamon, Z.2    Hruby, V.J.3    Tollin, G.4
  • 21
    • 29744432410 scopus 로고    scopus 로고
    • Membrane organization of the human serotonin(1A) receptor monitored by detergent insolubility using GFP fluorescence
    • Kalipatnapu S., and Chattopadhyay A. Membrane organization of the human serotonin(1A) receptor monitored by detergent insolubility using GFP fluorescence. Mol. Membr. Biol. 22 (2005) 539-547
    • (2005) Mol. Membr. Biol. , vol.22 , pp. 539-547
    • Kalipatnapu, S.1    Chattopadhyay, A.2
  • 22
    • 33748758457 scopus 로고    scopus 로고
    • Diffusion of the mu opioid receptor at the surface of human neuroblastoma SH-SY5Y cells is restricted to permeable domains
    • Saulière A., Gaibelet G., Millot C., Mazères S., Lopez A., and Salomé L. Diffusion of the mu opioid receptor at the surface of human neuroblastoma SH-SY5Y cells is restricted to permeable domains. FEBS. Lett. 580 (2006) 5227-5231
    • (2006) FEBS. Lett. , vol.580 , pp. 5227-5231
    • Saulière, A.1    Gaibelet, G.2    Millot, C.3    Mazères, S.4    Lopez, A.5    Salomé, L.6
  • 23
    • 0015861774 scopus 로고
    • Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction
    • Cheng Y., and Prusoff W.H. Relationship between the inhibition constant (K1) and the concentration of inhibitor which causes 50 per cent inhibition (I50) of an enzymatic reaction. Biochem. Pharmacol. 22 (1973) 3099-3108
    • (1973) Biochem. Pharmacol. , vol.22 , pp. 3099-3108
    • Cheng, Y.1    Prusoff, W.H.2
  • 25
    • 33845261493 scopus 로고
    • A rapid method of total lipid extraction and purification
    • Bligh E.G., and Dyer W.J. A rapid method of total lipid extraction and purification. Can. J. Med. Sci. 37 (1959) 911-917
    • (1959) Can. J. Med. Sci. , vol.37 , pp. 911-917
    • Bligh, E.G.1    Dyer, W.J.2
  • 27
    • 0014779155 scopus 로고
    • Two dimensional then layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots
    • Rouser G., Fkeischer S., and Yamamoto A. Two dimensional then layer chromatographic separation of polar lipids and determination of phospholipids by phosphorus analysis of spots. Lipids 5 (1970) 494-496
    • (1970) Lipids , vol.5 , pp. 494-496
    • Rouser, G.1    Fkeischer, S.2    Yamamoto, A.3
  • 28
    • 43649092379 scopus 로고    scopus 로고
    • H. Bullova, P. Balgavy, Turbidimetric study of unilamellar extruded egg phosphatidylcholine liposomes, Acta Facultatis Pharmaceuticae Universitatis Comenianae Tomus II (2005).
    • H. Bullova, P. Balgavy, Turbidimetric study of unilamellar extruded egg phosphatidylcholine liposomes, Acta Facultatis Pharmaceuticae Universitatis Comenianae Tomus II (2005).
  • 30
    • 0030004338 scopus 로고    scopus 로고
    • 7-nitrobenz-2-oxa-1,3-diazole-4-yl-labeled phospholipids in lipid membranes: differences in fluorescence behavior
    • Mazères S., Schram V., Tocanne J.F., and Lopez A. 7-nitrobenz-2-oxa-1,3-diazole-4-yl-labeled phospholipids in lipid membranes: differences in fluorescence behavior. Biophys. J. 71 (1996) 327-335
    • (1996) Biophys. J. , vol.71 , pp. 327-335
    • Mazères, S.1    Schram, V.2    Tocanne, J.F.3    Lopez, A.4
  • 34
    • 0025840389 scopus 로고
    • Topographical requirements for delta opioid ligands: presence of a carboxyl group in position 4 is not critical for deltorphin high delta receptor affinity and analgesic activity
    • Misicka A., Lipkowski A.W., Fang L., Knapp R.J., Davis P., Kramer T., Burks T.F., Yamamura H.I., Carr D.B., and Hruby V.J. Topographical requirements for delta opioid ligands: presence of a carboxyl group in position 4 is not critical for deltorphin high delta receptor affinity and analgesic activity. Biochem. Biophys. Res. Commun. 180 (1991) 1290-1297
    • (1991) Biochem. Biophys. Res. Commun. , vol.180 , pp. 1290-1297
    • Misicka, A.1    Lipkowski, A.W.2    Fang, L.3    Knapp, R.J.4    Davis, P.5    Kramer, T.6    Burks, T.F.7    Yamamura, H.I.8    Carr, D.B.9    Hruby, V.J.10
  • 35
    • 33646179776 scopus 로고    scopus 로고
    • Detergent-resistant, ceramide-enriched domains in sphingomyelin/ceramide bilayers
    • Sot J., Bagatolli L.A., Goni F.M., and Alonso A. Detergent-resistant, ceramide-enriched domains in sphingomyelin/ceramide bilayers. Biophys. J. 90 (2006) 903-914
    • (2006) Biophys. J. , vol.90 , pp. 903-914
    • Sot, J.1    Bagatolli, L.A.2    Goni, F.M.3    Alonso, A.4
  • 36
    • 43149099647 scopus 로고    scopus 로고
    • Characterizing the interactions between GPI-anchored alkaline phosphatases and membrane domains by AFM
    • Giocondi M.C., Seantier B., Dosset P., Milhiet P.E., and Le Grimellec C. Characterizing the interactions between GPI-anchored alkaline phosphatases and membrane domains by AFM. Pflugers. Arch. 456 (2008) 179-188
    • (2008) Pflugers. Arch. , vol.456 , pp. 179-188
    • Giocondi, M.C.1    Seantier, B.2    Dosset, P.3    Milhiet, P.E.4    Le Grimellec, C.5
  • 38
    • 0037065727 scopus 로고    scopus 로고
    • Lipid rafts are enriched in arachidonic acid and plasmenylethanolamine and their composition is independent of caveolin-1 expression: a quantitative electrospray ionization/mass spectrometric analysis
    • Pike L.J., Han X., Chung K.N., and Gross R.W. Lipid rafts are enriched in arachidonic acid and plasmenylethanolamine and their composition is independent of caveolin-1 expression: a quantitative electrospray ionization/mass spectrometric analysis. Biochemistry 41 (2002) 2075-2088
    • (2002) Biochemistry , vol.41 , pp. 2075-2088
    • Pike, L.J.1    Han, X.2    Chung, K.N.3    Gross, R.W.4
  • 40
    • 0036215273 scopus 로고    scopus 로고
    • Apo AI/ABCA1-dependent and HDL3-mediated lipid efflux from compositionally distinct cholesterol-based microdomains
    • Drobnik W., Borsukova H., Bottcher A., Pfeiffer A., Liebisch G., Schutz G.J., Schindler H., and Schmitz G. Apo AI/ABCA1-dependent and HDL3-mediated lipid efflux from compositionally distinct cholesterol-based microdomains. Traffic 3 (2002) 268-278
    • (2002) Traffic , vol.3 , pp. 268-278
    • Drobnik, W.1    Borsukova, H.2    Bottcher, A.3    Pfeiffer, A.4    Liebisch, G.5    Schutz, G.J.6    Schindler, H.7    Schmitz, G.8
  • 41
    • 0034282003 scopus 로고    scopus 로고
    • Retention of prominin in microvilli reveals distinct cholesterol-based lipid micro-domains in the apical plasma membrane
    • Röper K., Corbei D., and Huttner W.B. Retention of prominin in microvilli reveals distinct cholesterol-based lipid micro-domains in the apical plasma membrane. Nat. Cell Biol. 2 (2000) 582-592
    • (2000) Nat. Cell Biol. , vol.2 , pp. 582-592
    • Röper, K.1    Corbei, D.2    Huttner, W.B.3
  • 43
    • 22244469306 scopus 로고    scopus 로고
    • A simplified method for the preparation of detergent-free lipid rafts
    • Macdonald J.L., and Pike L.J. A simplified method for the preparation of detergent-free lipid rafts. J. Lipid Res. 46 (2005) 1061-1067
    • (2005) J. Lipid Res. , vol.46 , pp. 1061-1067
    • Macdonald, J.L.1    Pike, L.J.2
  • 44
    • 1642354334 scopus 로고    scopus 로고
    • Lipid rafts: heterogeneity on the high seas
    • Pike L.J. Lipid rafts: heterogeneity on the high seas. Biochem. J. 378 (2004) 281-292
    • (2004) Biochem. J. , vol.378 , pp. 281-292
    • Pike, L.J.1
  • 45
    • 0027513982 scopus 로고
    • A mutation-induced activated state of the beta 2-adrenergic receptor. Extending the ternary complex model
    • Samama P., Cotecchia S., Costa T., and Lefkowitz R.J. A mutation-induced activated state of the beta 2-adrenergic receptor. Extending the ternary complex model. J. Biol. Chem. 268 (1993) 4625-4636
    • (1993) J. Biol. Chem. , vol.268 , pp. 4625-4636
    • Samama, P.1    Cotecchia, S.2    Costa, T.3    Lefkowitz, R.J.4
  • 46
    • 33845938227 scopus 로고    scopus 로고
    • Cholesterol reduction by methyl-beta-cyclodextrin attenuates the delta opioid receptor-mediated signaling in neuronal cells but enhances it in non-neuronal cells
    • Huang P., Xu W., Yoon S.I., Chen C., Chong P.L., and Liu-Chen L.Y. Cholesterol reduction by methyl-beta-cyclodextrin attenuates the delta opioid receptor-mediated signaling in neuronal cells but enhances it in non-neuronal cells. Biochem. Pharmacol. 73 (2007) 534-549
    • (2007) Biochem. Pharmacol. , vol.73 , pp. 534-549
    • Huang, P.1    Xu, W.2    Yoon, S.I.3    Chen, C.4    Chong, P.L.5    Liu-Chen, L.Y.6
  • 47
    • 0035943423 scopus 로고    scopus 로고
    • Emerging themes in lipid rafts and caveolae
    • Galbiati F., Razani B., and Lisanti M.P. Emerging themes in lipid rafts and caveolae. Cell 106 (2001) 403-411
    • (2001) Cell , vol.106 , pp. 403-411
    • Galbiati, F.1    Razani, B.2    Lisanti, M.P.3
  • 48
    • 0037423007 scopus 로고    scopus 로고
    • Lipid rafts of purified mouse brain synaptosomes prepared with or without detergent reveal different lipid and protein domains
    • Eckert G.P., Igbavboa U., Muller W.E., and Wood W.G. Lipid rafts of purified mouse brain synaptosomes prepared with or without detergent reveal different lipid and protein domains. Brain Res. 962 (2003) 144-150
    • (2003) Brain Res. , vol.962 , pp. 144-150
    • Eckert, G.P.1    Igbavboa, U.2    Muller, W.E.3    Wood, W.G.4
  • 49
    • 0035164003 scopus 로고    scopus 로고
    • Segregation of heterotrimeric G proteins in cell surface microdomains. G(q) binds caveolin to concentrate in caveolae, whereas G(i) and G(s) target lipid rafts by default
    • Oh P., and Schnitzer J.E. Segregation of heterotrimeric G proteins in cell surface microdomains. G(q) binds caveolin to concentrate in caveolae, whereas G(i) and G(s) target lipid rafts by default. Mol. Biol. Cell 12 (2001) 685-698
    • (2001) Mol. Biol. Cell , vol.12 , pp. 685-698
    • Oh, P.1    Schnitzer, J.E.2
  • 50
    • 0029082412 scopus 로고
    • Separation of caveolae from associated microdomains of GPI-anchored proteins
    • Schnitzer J.E., McIntosh D.P., Dvorak A.M., Liu J., and Oh P. Separation of caveolae from associated microdomains of GPI-anchored proteins. Science 269 (1995) 1435-1439
    • (1995) Science , vol.269 , pp. 1435-1439
    • Schnitzer, J.E.1    McIntosh, D.P.2    Dvorak, A.M.3    Liu, J.4    Oh, P.5
  • 51
    • 0030582573 scopus 로고    scopus 로고
    • Rhodopsin-cholesterol interactions in bovine rod outer segment disk membranes
    • Albert A.D., Young J.E., and Yeagle P.L. Rhodopsin-cholesterol interactions in bovine rod outer segment disk membranes. Biochim. Biophys. Acta 1285 (1996) 47-55
    • (1996) Biochim. Biophys. Acta , vol.1285 , pp. 47-55
    • Albert, A.D.1    Young, J.E.2    Yeagle, P.L.3
  • 52
    • 0034721934 scopus 로고    scopus 로고
    • Role of sterols in modulating the human mu-opioid receptor function in Saccharomyces cerevisiae
    • Lagane B., Gaibelet G., Meilhoc E., Masson J.M., Cézanne L., and Lopez A. Role of sterols in modulating the human mu-opioid receptor function in Saccharomyces cerevisiae. J. Biol. Chem. 275 (2000) 33197-33200
    • (2000) J. Biol. Chem. , vol.275 , pp. 33197-33200
    • Lagane, B.1    Gaibelet, G.2    Meilhoc, E.3    Masson, J.M.4    Cézanne, L.5    Lopez, A.6
  • 53
    • 33744543610 scopus 로고    scopus 로고
    • Role of cholesterol in the function and organization of G-protein coupled receptors
    • Pucadyil T.J., and Chattopadhyay A. Role of cholesterol in the function and organization of G-protein coupled receptors. Prog. Lipid Res. 45 (2006) 295-333
    • (2006) Prog. Lipid Res. , vol.45 , pp. 295-333
    • Pucadyil, T.J.1    Chattopadhyay, A.2
  • 54
    • 0030049488 scopus 로고    scopus 로고
    • Constitutive activation of a single effector pathway: evidence for multiple activation states of a G protein-coupled receptor
    • Perez D.M., Hwa J., Gaivin R., Mathur M., Brown F., and Graham R.M. Constitutive activation of a single effector pathway: evidence for multiple activation states of a G protein-coupled receptor. Mol. Pharmacol. 49 (1996) 112-122
    • (1996) Mol. Pharmacol. , vol.49 , pp. 112-122
    • Perez, D.M.1    Hwa, J.2    Gaivin, R.3    Mathur, M.4    Brown, F.5    Graham, R.M.6
  • 55
    • 0029054965 scopus 로고
    • Agonist-receptor efficacy. II. Agonist trafficking of receptor signals
    • Kenakin T. Agonist-receptor efficacy. II. Agonist trafficking of receptor signals. Trends Pharmacol. Sci. 16 (1995) 232-238
    • (1995) Trends Pharmacol. Sci. , vol.16 , pp. 232-238
    • Kenakin, T.1
  • 56
    • 0033793871 scopus 로고    scopus 로고
    • Regulation of receptor function by cholesterol
    • Burger K., Gimpl G., and Fahrenholz F. Regulation of receptor function by cholesterol. Cell. Mol. Life Sci. 57 (2000) 1577-1592
    • (2000) Cell. Mol. Life Sci. , vol.57 , pp. 1577-1592
    • Burger, K.1    Gimpl, G.2    Fahrenholz, F.3
  • 57
    • 0142123218 scopus 로고    scopus 로고
    • Pressure-induced differential regulation of the two tryptophan permeases Tat1 and Tat2 by ubiquitin ligase Rsp5 and its binding proteins, Bul1 and Bul2
    • Abe F., and Iida H. Pressure-induced differential regulation of the two tryptophan permeases Tat1 and Tat2 by ubiquitin ligase Rsp5 and its binding proteins, Bul1 and Bul2. Mol. Cell. Biol. 23 (2003) 7566-7584
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 7566-7584
    • Abe, F.1    Iida, H.2


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