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Volumn 49, Issue 10, 2010, Pages 2235-2245

Mutational analysis of threonine 402 adjacent to the GXXXG dimerization motif in transmembrane segment 1 of ABCG2

Author keywords

[No Author keywords available]

Indexed keywords

ATP-BINDING CASSETTE; BAFILOMYCIN; DIMER INTERFACE; DRUG DISTRIBUTION; ENDOPLASMIC RETICULUM; HOMODIMERIZATION; HOMOLOGY MODELING; IMMUNOBLOT ANALYSIS; IMMUNOSTAINING; MUTATIONAL ANALYSIS; NORMAL TISSUE; SIGNIFICANT IMPACTS; SINGLE MUTATION; TRANSMEMBRANE SEGMENTS; WILD TYPES;

EID: 77949344456     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi902085q     Document Type: Article
Times cited : (35)

References (54)
  • 1
    • 0034953105 scopus 로고    scopus 로고
    • The human ATPbinding cassette (ABC) transporter superfamily
    • Dean, M., Hamon, Y., and Chimini, G. (2001) The human ATPbinding cassette (ABC) transporter superfamily. J. Lipid Res. 42, 1007-1017.
    • (2001) J. Lipid Res. , vol.42 , pp. 1007-1017
    • Dean, M.1    Hamon, Y.2    Chimini, G.3
  • 2
    • 0032404092 scopus 로고    scopus 로고
    • A human placenta-specific ATP-binding cassette gene (ABCP) on chromosome 4q22 that is involved in multidrug resistance
    • Allikmets, R., Schriml, L. M., Hutchinson, A., Romano-Spica, V., and Dean, M. (1998) A human placenta-specific ATP-binding cassette gene (ABCP) on chromosome 4q22 that is involved in multidrug resistance. Cancer Res. 58, 5337-5339.
    • (1998) Cancer Res. , vol.58 , pp. 5337-5339
    • Allikmets, R.1    Schriml, L.M.2    Hutchinson, A.3    Romano-Spica, V.4    Dean, M.5
  • 5
    • 0042354831 scopus 로고    scopus 로고
    • Transport of methotrexate, methotrexate polyglutamates, and 17βestradiol 17-(β-D-glucuronide) by ABCG2: Effects of acquired mutations at R482 on methotrexate transport
    • Chen, Z. S., Robey, R. W., Belinsky, M. G., Shchaveleva, I., Ren, X. Q., Sugimoto, Y., Ross, D. D., Bates, S. E., and Kruh, G. D. (2003) Transport of methotrexate, methotrexate polyglutamates, and 17βestradiol 17-(β-D-glucuronide) by ABCG2: Effects of acquired mutations at R482 on methotrexate transport. Cancer Res. 63,4048-4054.
    • (2003) Cancer Res. , vol.63 , pp. 4048-4054
    • Chen, Z.S.1    Robey, R.W.2    Belinsky, M.G.3    Shchaveleva, I.4    Ren, X.Q.5    Sugimoto, Y.6    Ross, D.D.7    Bates, S.E.8    Kruh, G.D.9
  • 11
    • 50149108146 scopus 로고    scopus 로고
    • Pharmacogenomic importance of ABCG2
    • Cusatis, G., and Sparreboom, A. (2008) Pharmacogenomic importance of ABCG2. Pharmacogenomics 9,1005-1009.
    • (2008) Pharmacogenomics , vol.9 , pp. 1005-1009
    • Cusatis, G.1    Sparreboom, A.2
  • 12
    • 0037125973 scopus 로고    scopus 로고
    • Bcrpl gene expression is required, for normal numbers of side population stem cells in mice, and confers relative protection, to mitoxantrone in hematopoietic cells in vivo
    • Zhou, S., Morris, J. J., Barnes, Y., Lan, L., Schuetz, J. D., and Sorrentino, B. P. (2002) Bcrpl gene expression is required, for normal numbers of side population stem cells in mice, and confers relative protection, to mitoxantrone in hematopoietic cells in vivo. Proc. Natl. Ami Sci, U.S.A- 99, 12339-12344.
    • (2002) Proc. Natl. Ami Sci, U.S.A , vol.99 , pp. 12339-12344
    • Zhou, S.1    Morris, J.J.2    Barnes, Y.3    Lan, L.4    Schuetz, J.D.5    Sorrentino, B.P.6
  • 13
    • 27744459366 scopus 로고    scopus 로고
    • Identification of intra- And intermolecular disulfide bridges in the multidrug resistance transporter ABCG2
    • Henriksen, U., Fog, J. U., Litman, T., and Gether, U. (2005) Identification of intra- and intermolecular disulfide bridges in the multidrug resistance transporter ABCG2. J. Biol. Chem, 280, 36926-36934.
    • (2005) J. Biol. Chem , vol.280 , pp. 36926-36934
    • Henriksen, U.1    Fog, J.U.2    Litman, T.3    Gether, U.4
  • 14
    • 30344485123 scopus 로고    scopus 로고
    • Role of Cys-603 in dimer/oligomer formation of the breast cancer resistance protein. BCRP/ABCG2
    • Kage, K., Fujita, T., and Sugimoto, Y. (2005) Role of Cys-603 in dimer/oligomer formation of the breast cancer resistance protein. BCRP/ABCG2. Cancer Sci. 96, 866-872.
    • (2005) Cancer Sci. , vol.96 , pp. 866-872
    • Kage, K.1    Fujita, T.2    Sugimoto, Y.3
  • 15
    • 33646703561 scopus 로고    scopus 로고
    • Identification of cysteine residues critically involved in homodimer formation and protein expression of human ATP-binding cassette transporter ABCG2: A new approach using the flp recombinase system
    • Wakabayashi, K., Nakagawa, H., Adachi, T., Kii, I., Kobatake, E., Kudo, A., and Ishikawa, T. (2006) Identification of cysteine residues critically involved in homodimer formation and protein expression of human ATP-binding cassette transporter ABCG2: A new approach using the flp recombinase system. J. Exn. Ther. Oncol. 5, 205-222.
    • (2006) J. Exn. Ther. Oncol. , vol.5 , pp. 205-222
    • Wakabayashi, K.1    Nakagawa, H.2    Adachi, T.3    Kii, I.4    Kobatake, E.5    Kudo, A.6    Ishikawa, T.7
  • 16
    • 45749107106 scopus 로고    scopus 로고
    • Effect of cysteine mutagenesis on the function and disulfide bond formation of human. ABCG2
    • Liu, Y., Yang, Y., Qi, J., Peng, H., and Zhang, J. T. (2008) Effect of cysteine mutagenesis on the function and disulfide bond formation of human. ABCG2. J. Pharmacol, Exp. Ther. 326, 33-40.
    • (2008) J. Pharmacol, Exp. Ther. , vol.326 , pp. 33-40
    • Liu, Y.1    Yang, Y.2    Qi, J.3    Peng, H.4    Zhang, J.T.5
  • 17
    • 0037044743 scopus 로고    scopus 로고
    • The transmembrane domains of the ABC multidrug transporter LmrA form a cytoplasmic exposed, aqueous chamber within, the membrane
    • Poelarends, G. J., and Konings, W. N. (2002) The transmembrane domains of the ABC multidrug transporter LmrA form a cytoplasmic exposed, aqueous chamber within, the membrane. J. Biol. Chem. 277, 42891-42898.
    • (2002) J. Biol. Chem. , vol.277 , pp. 42891-42898
    • Poelarends, G.J.1    Konings, W.N.2
  • 18
    • 0037413849 scopus 로고    scopus 로고
    • Functional, cysteine-less subunits of the transporter associated with antigen processing (TAPl and. TAP2) by de novo gene assembly
    • Heintke, S., Chen, M., Ritz, U., Lankat-Buttgereit, B., Koch, J., Abele, R., Seliger, B., and Tampe, R. (2003) Functional, cysteine-less subunits of the transporter associated with antigen processing (TAPl and. TAP2) by de novo gene assembly. FEBS Lett. 533, 42-46.
    • (2003) FEBS Lett. , vol.533 , pp. 42-46
    • Heintke, S.1    Chen, M.2    Ritz, U.3    Lankat-Buttgereit, B.4    Koch, J.5    Abele, R.6    Seliger, B.7    Tampe, R.8
  • 20
    • 0034711953 scopus 로고    scopus 로고
    • The GxxxG motif: A framework for transmembrane helix-helix association
    • Russ, W. P., and Engelman, D. M. (2000) The GxxxG motif: A framework for transmembrane helix-helix association. J. Mol. Biol. 296, 911-919.
    • (2000) J. Mol. Biol. , vol.296 , pp. 911-919
    • Russ, W.P.1    Engelman, D.M.2
  • 21
    • 0031956790 scopus 로고    scopus 로고
    • The dimerization motif of the glycophorin A transmembrane segment in membranes: Importance of glycine residues
    • Brosig, B., and Langosch, D. (1998) The dimerization motif of the glycophorin A transmembrane segment in membranes: Importance of glycine residues. Protein Sci. 7, 1052-1056.
    • (1998) Protein Sci. , vol.7 , pp. 1052-1056
    • Brosig, B.1    Langosch, D.2
  • 22
  • 23
    • 0035884595 scopus 로고    scopus 로고
    • Acquired mutations in the MXR/BCRP/ABCP gene alter substrate specificity in MXR/BCRP/ABCP-overexpressing cells
    • Honjo,Y., Hrycyna, C. A., Yan,Q. W., Medina-Perez, W. Y., Robey, R. W., van de Laar, A., Litman, T., Dean, M., and Bates, S. E. (2001) Acquired mutations in the MXR/BCRP/ABCP gene alter substrate specificity in MXR/BCRP/ABCP-overexpressing cells. Cancer Res. 61, 6635-6639.
    • (2001) Cancer Res. , vol.61 , pp. 6635-6639
    • Hrycyna, C.A.1    Yan, Q.W.2    Medina-Perez, W.Y.3    Robey, R.W.4    Van De Laar, A.5    Litman, T.6    Dean, M.7    Bates, S.E.8
  • 25
    • 0033514311 scopus 로고    scopus 로고
    • TOXCAT: A measure of transmembrane helix association in a biological membrane
    • Russ, W. P., and. Engelman, D. M. (1999) TOXCAT: A measure of transmembrane helix association in a biological membrane. Proc. Natl, Acad. Sci. U.S.A. 96, 863-868.
    • (1999) Proc. Natl, Acad. Sci. U.S.A. , vol.96 , pp. 863-868
    • Russ, W.P.1    Engelman, D.M.2
  • 26
    • 33846827217 scopus 로고    scopus 로고
    • Towards understanding the mechanism of action of the multidrug resistance-linked half-ABC transporter ABCG2: A molecular modeling study
    • Li, Y., Polgar, O., Okada, M., Esser, L., Bates, S., and Xia, D. (2006) Towards understanding the mechanism of action of the multidrug resistance-linked half-ABC transporter ABCG2: A molecular modeling study. J. Mol. Graphics Modell. 25, 837-851.
    • (2006) J. Mol. Graphics Modell. , vol.25 , pp. 837-851
    • Li, Y.1    Polgar, O.2    Okada, M.3    Esser, L.4    Bates, S.5    Xia, D.6
  • 27
    • 33747184794 scopus 로고    scopus 로고
    • Prediction of transmembrane helix orientation in polytopic membrane proteins
    • Adamian, L., and Liang, J. (2006) Prediction of transmembrane helix orientation in polytopic membrane proteins. BMC Struct. Biol. 6, 13.
    • (2006) BMC Struct. Biol. , vol.6 , pp. 13
    • Adamian, L.1    Liang, J.2
  • 28
    • 33748644877 scopus 로고    scopus 로고
    • Structure of a bacterial multidrug ABC transporter
    • Dawson, R. J., and Locher, K. P. (2006) Structure of a bacterial multidrug ABC transporter. Nature 443, 180-185.
    • (2006) Nature , vol.443 , pp. 180-185
    • Dawson, R.J.1    Locher, K.P.2
  • 29
    • 0141527345 scopus 로고    scopus 로고
    • A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle
    • Chen, J., Lu, G., Lin, J., Davodson, A. L., and Quiocho, F. A. (2003) A tweezers-like motion of the ATP-binding cassette dimer in an ABC transport cycle. Mol. Cell 12, 651-661.
    • (2003) Mol. Cell , vol.12 , pp. 651-661
    • Chen, J.1    Lu, G.2    Lin, J.3    Davodson, A.L.4    Quiocho, F.A.5
  • 31
    • 16844386327 scopus 로고    scopus 로고
    • N-Linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane
    • Diop, N. K., and Hrycyna, C. A. (2005) N-Linked glycosylation of the human ABC transporter ABCG2 on asparagine 596 is not essential for expression, transport activity, or trafficking to the plasma membrane Biochemhtry 44, 5420-5429.
    • (2005) Biochemhtry , vol.44 , pp. 5420-5429
    • Diop, N.K.1    Hrycyna, C.A.2
  • 32
    • 59049087689 scopus 로고    scopus 로고
    • Quality control of human ABCG2 protein in the endoplasmatic reticulum: Ubiquitination and proteosomal degradation
    • Wakabayashi-Nakao, K., Tamura, A., Furukawa, T., Nakagawa, H., and Ishikawa, T. (2009) Quality control of human ABCG2 protein in the endoplasmatic reticulum: Ubiquitination and proteosomal degradation. Adv. Drug Delivery Rev. 61, 66-72.
    • (2009) Adv. Drug Delivery Rev. , vol.61 , pp. 66-72
    • Wakabayashi-Nakao, K.1    Tamura, A.2    Furukawa, T.3    Nakagawa, H.4    Ishikawa, T.5
  • 33
    • 58549097067 scopus 로고    scopus 로고
    • Major SNP (Q141K) variant of human ABC transporter ABCG2 undergoes lysosomal and proteasomal degradations
    • Furukawa, T., Wakabayashi, K., Tamura, A., Nakagava, H., Morishima, Y., Osawa, Y., and Ishikawa, T. (2009) Major SNP (Q141K) variant of human ABC transporter ABCG2 undergoes lysosomal and proteasomal degradations. Pharm, Res. 26, 469-479.
    • (2009) Pharm, Res. , vol.26 , pp. 469-479
    • Furukawa, T.1    Wakabayashi, K.2    Tamura, A.3    Nakagava, H.4    Morishima, Y.5    Osawa, Y.6    Ishikawa, T.7
  • 34
    • 34547105186 scopus 로고    scopus 로고
    • Chemical and pharmacological chaperones as new therapeutic agents
    • Loo, T. W., and Clarke, D. M. (2007) Chemical and pharmacological chaperones as new therapeutic agents. Expert Rev. Mol, Med 9,1-18.
    • (2007) Expert Rev. Mol, Med , vol.9 , pp. 1-18
    • Loo, T.W.1    Clarke, D.M.2
  • 35
    • 33646578825 scopus 로고    scopus 로고
    • Rescue of folding defects in ABC transporters using pharmacological chaperones
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2005) Rescue of folding defects in ABC transporters using pharmacological chaperones. J. Bioenerg. Biomembr. 37, 501-507.
    • (2005) J. Bioenerg. Biomembr. , vol.37 , pp. 501-507
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 36
    • 0037145061 scopus 로고    scopus 로고
    • Ligand-induced, receptor-mediated dimerization and activation of EGF receptor
    • Schlessinger, J. (2002) Ligand-Induced, Receptor-Mediated Dimerization and Activation of EGF Receptor. Cell; 110, 669-672.
    • (2002) Cell , vol.110 , pp. 669-672
    • Schlessinger, J.1
  • 37
    • 1242276192 scopus 로고    scopus 로고
    • Roles of G-protein-coupled receptor dimerization
    • Terrillon, S., and Bouvier, M. (2003) Roles of G-protein-coupled receptor dimerization. EMBO Rep. 5, 30-34.
    • (2003) EMBO Rep. , vol.5 , pp. 30-34
    • Terrillon, S.1    Bouvier, M.2
  • 38
    • 0348111456 scopus 로고    scopus 로고
    • ABCG5 and ABCG8 are obligate heterodimers for protein trafficking and biliary cholesterol excretion
    • Graf, G. A., Yu, L., Li, W. P., Gerard, R., Tuma, P. L., Cohen, J. C., and Hobbs, H. H. (2003) ABCG5 and ABCG8 are obligate heterodimers for protein trafficking and biliary cholesterol excretion. J. Biol. Chem. 278, 48275-48282.
    • (2003) J. Biol. Chem. , vol.278 , pp. 48275-48282
    • Graf, G.A.1    Yu, L.2    Li, W.P.3    Gerard, R.4    Tuma, P.L.5    Cohen, J.C.6    Hobbs, H.H.7
  • 39
    • 0036731990 scopus 로고    scopus 로고
    • Coexpression of ATP-binding cassette proteins ABCG5 andABCG8 permits their transport to the apical surface
    • Graf, G. A., Li, W. P., Gerard, R. D., Gelissen, I., White, A., Cohen, J. C., and Hobbs, H. H. (2002) Coexpression of ATP-binding cassette proteins ABCG5 and. ABCG8 permits their transport to the apical surface. J. Clin. Invest. 110, 659-669.
    • (2002) J. Clin. Invest. , vol.110 , pp. 659-669
    • Graf, G.A.1    Li, W.P.2    Gerard, R.D.3    Gelissen, I.4    White, A.5    Cohen, J.C.6    Hobbs, H.H.7
  • 40
    • 44049094995 scopus 로고    scopus 로고
    • Hydrogen-bonding and packing features of membrane proteins: Functional implications
    • Hildebrand, P. W., Gunther, S., Goede, A., Forrest, L., Frommel, C., and Preissner, R. (2008) Hydrogen-bonding and packing features of membrane proteins: Functional implications. Biophys. J. 94, 1945-1953.
    • (2008) Biophys. J. , vol.94 , pp. 1945-1953
    • Hildebrand, P.W.1    Gunther, S.2    Goede, A.3    Forrest, L.4    Frommel, C.5    Preissner, R.6
  • 41
    • 0035811042 scopus 로고    scopus 로고
    • Structure of the transmembrane dimer interface of glycophorin A in membrane bilayers
    • Smith, S. O., Song, D., Shekar, S., Groesbeek, M., Ziliox, M., and. Aimoto, S. (2001) Structure of the transmembrane dimer interface of glycophorin A in membrane bilayers. Biochemistry 40, 6553-6558.
    • (2001) Biochemistry , vol.40 , pp. 6553-6558
    • Smith, S.O.1    Song, D.2    Shekar, S.3    Groesbeek, M.4    Ziliox, M.5    Aimoto, S.6
  • 43
    • 0030932407 scopus 로고    scopus 로고
    • A transmembrane helix, dimer: Structure and implications
    • MacKenzie, K. R., Prestegard, J. H., and Engelman, D. M. (1997) A. transmembrane helix, dimer: Structure and implications. Science 276, 131-133.
    • (1997) Science , vol.276 , pp. 131-133
    • MacKenzie, K.R.1    Prestegard, J.H.2    Engelman, D.M.3
  • 44
    • 33845316118 scopus 로고    scopus 로고
    • Transmembrane helix-helix interactions: Comparative simulations of the glycophorin a dimer
    • Cuthbertson, J. M., Bond, P. J., and Sansom, M. S. (2006) Transmembrane helix-helix interactions: Comparative simulations of the glycophorin a dimer. Biochemistry 45, 14298-14310.
    • (2006) Biochemistry , vol.45 , pp. 14298-14310
    • Cuthbertson, J.M.1    Bond, P.J.2    Sansom, M.S.3
  • 45
    • 0035979146 scopus 로고    scopus 로고
    • The Cα-H ⋯O hydrogen bond: A determinant of stability and specificity in transmembrane helix interactions
    • Senes, A., Ubarretxena-Belandia, I., and Engelman, D. M. (2001) The Cα-H ⋯O hydrogen bond: A determinant of stability and specificity in transmembrane helix interactions. Proc. Natl, Acad, Sci. U.S.A- 98, 9056-9061.
    • (2001) Proc. Natl, Acad, Sci. U.S.A , vol.98 , pp. 9056-9061
    • Senes, A.1    Ubarretxena-Belandia, I.2    Engelman, D.M.3
  • 46
    • 34447271539 scopus 로고    scopus 로고
    • Changes in apparent free energy of helix-helix dimerization in a biological membrane due to point mutations
    • Duong, M. T., Jaszewki, T. M., Fleming, K. G., and MacKenzie, K. R. (2007) Changes in apparent free energy of helix-helix dimerization in a biological membrane due to point mutations. J. Mol. Biol. 371, 422-434.
    • (2007) J. Mol. Biol. , vol.371 , pp. 422-434
    • Duong, M.T.1    Jaszewki, T.M.2    Fleming, K.G.3    MacKenzie, K.R.4
  • 47
    • 69949167524 scopus 로고    scopus 로고
    • Identification of residues in the drug translocation pathway of the human multidrug resistance P-glycoprotein by argininemutagenesis
    • Loo, T. W., Bartlett, M. C., and Clarke, D. M. (2009) Identification of residues in the drug translocation pathway of the human multidrug resistance P-glycoprotein by argininemutagenesis. J. Biol. Chem. 284, 24074-24087.
    • (2009) J. Biol. Chem. , vol.284 , pp. 24074-24087
    • Loo, T.W.1    Bartlett, M.C.2    Clarke, D.M.3
  • 48
    • 16644366865 scopus 로고    scopus 로고
    • Pharmacological chaperone action on G-protein-coupled receptors
    • Bernier, V., Bichet, D. G., and Bouvier, M. (2004) Pharmacological chaperone action on G-protein-coupled receptors. Curr. Opin. Pharmacol, 4, 520-533.
    • (2004) Curr. Opin. Pharmacol , vol.4 , pp. 520-533
    • Bernier, V.1    Bichet, D.G.2    Bouvier, M.3
  • 49
    • 67649951498 scopus 로고    scopus 로고
    • Functional. rescue of β1-adrenoceptor dimerization and trafficking by pharmacological chaperones
    • Kobayashi, H., Ogawa, K., Yao, R., Lichtarge, O., and Bouvier, M. (2009) Functional. Rescue of β1-Adrenoceptor Dimerization and Trafficking by Pharmacological Chaperones. Traffic 10, 10191033.
    • (2009) Traffic , vol.10 , pp. 10191033
    • Kobayashi, H.1    Ogawa, K.2    Yao, R.3    Lichtarge, O.4    Bouvier, M.5
  • 50
    • 0028006681 scopus 로고
    • Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins
    • Ward, C. L., and Kopito, R. R. (1994) Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins. J. Biol. Chem. 269. 25710-25718.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25710-25718
    • Ward, C.L.1    Kopito, R.R.2
  • 51
    • 0035026558 scopus 로고    scopus 로고
    • Increased functional cell surface expression of CFTR and ΔF508CFTR by the anthracycline doxorubicin
    • Maitra, R., Shaw, C. M., Stanton, B. A., and Hamilton, J. W. (2001) Increased functional cell surface expression of CFTR and ΔF508CFTR by the anthracycline doxorubicin. Am. J. Physiol. 280, C1031C1037.
    • (2001) Am. J. Physiol. , vol.280
    • Maitra, R.1    Shaw, C.M.2    Stanton, B.A.3    Hamilton, J.W.4
  • 52
    • 11944265976 scopus 로고    scopus 로고
    • Sildenafil (Viagra) corrects AF508-CFTR location in nasal epithelial cells from patients with cystic fibrosis
    • Donner, R. L., Harris, C. M., Clark, Z., Pereira, M. M., Doull, I. J., Norez, C., Becq, F., and McPherson, M. A. (2005) Sildenafil (Viagra) corrects AF508-CFTR location in nasal epithelial cells from patients with cystic fibrosis. Thorax 60, 55-59.
    • (2005) Thorax , vol.60 , pp. 55-59
    • Donner, R.L.1    Harris, C.M.2    Clark, Z.3    Pereira, M.M.4    Doull, I.J.5    Norez, C.6    Becq, F.7    McPherson, M.A.8
  • 54
    • 2442520293 scopus 로고    scopus 로고
    • Characterization of oligomeric human half-ABC transporter ATPbinding cassette G2
    • Xu, J., Liu, Y., Yang, Y., Bates, S., and Zhang, J. T. (2004) Characterization of oligomeric human half-ABC transporter ATPbinding cassette G2. J. Biol. Chem. 279, 19781-19789.
    • (2004) J. Biol. Chem. , vol.279 , pp. 19781-19789
    • Xu, J.1    Liu, Y.2    Yang, Y.3    Bates, S.4    Zhang, J.T.5


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