메뉴 건너뛰기




Volumn 170, Issue 3, 2010, Pages 540-547

Structure of a human multidrug transporter in an inward-facing conformation

Author keywords

ABCC1; ATP binding cassette; Cryo electron microscopy; Electron crystallography; MRP1; Multidrug resistance; Structure

Indexed keywords

ABC TRANSPORTER; ABC TRANSPORTER C1; UNCLASSIFIED DRUG;

EID: 77952567948     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2010.01.011     Document Type: Article
Times cited : (28)

References (58)
  • 2
    • 0032560144 scopus 로고    scopus 로고
    • Three-dimensional map of the plasma membrane H+-ATPase in the open conformation
    • Auer M., Scarborough G.A., Kuhlbrandt W. Three-dimensional map of the plasma membrane H+-ATPase in the open conformation. Nature 1998, 392:840-843.
    • (1998) Nature , vol.392 , pp. 840-843
    • Auer, M.1    Scarborough, G.A.2    Kuhlbrandt, W.3
  • 3
    • 0033574521 scopus 로고    scopus 로고
    • Surface crystallisation of the plasma membrane H+-ATPase on a carbon support film for electron crystallography
    • Auer M., Scarborough G.A., Kuhlbrandt W. Surface crystallisation of the plasma membrane H+-ATPase on a carbon support film for electron crystallography. J. Mol. Biol. 1999, 287:961-968.
    • (1999) J. Mol. Biol. , vol.287 , pp. 961-968
    • Auer, M.1    Scarborough, G.A.2    Kuhlbrandt, W.3
  • 4
    • 27844520938 scopus 로고    scopus 로고
    • Crystallographic and single-particle analyses of native and nucleotide-bound forms of the cystic fibrosis transmembrane conductance regulator (CFTR) protein
    • Awayn N.H., Rosenberg M.F., Kamis A.B., Aleksandrov L.A., Riordan J.R., Ford R.C. Crystallographic and single-particle analyses of native and nucleotide-bound forms of the cystic fibrosis transmembrane conductance regulator (CFTR) protein. Biochem. Soc. Trans. 2005, 33:996-999.
    • (2005) Biochem. Soc. Trans. , vol.33 , pp. 996-999
    • Awayn, N.H.1    Rosenberg, M.F.2    Kamis, A.B.3    Aleksandrov, L.A.4    Riordan, J.R.5    Ford, R.C.6
  • 7
    • 0035902506 scopus 로고    scopus 로고
    • Functional expression of multidrug resistance protein 1 in Pichia pastoris
    • Cai J., Daoud R., Georges E., Gros P. Functional expression of multidrug resistance protein 1 in Pichia pastoris. Biochemistry 2001, 40:8307-8316.
    • (2001) Biochemistry , vol.40 , pp. 8307-8316
    • Cai, J.1    Daoud, R.2    Georges, E.3    Gros, P.4
  • 8
    • 0347683446 scopus 로고    scopus 로고
    • Molecular modeling correctly predicts the functional importance of Phe(594) in transmembrane Helix 11 of the multidrug resistance protein, MRP1(ABCC1)
    • Campbell J.D., Koike K., Moreau C., Sansom M.S.P., Deeley R.G., Cole S.P.C. Molecular modeling correctly predicts the functional importance of Phe(594) in transmembrane Helix 11 of the multidrug resistance protein, MRP1(ABCC1). J. Biol. Chem. 2004, 279:463-468.
    • (2004) J. Biol. Chem. , vol.279 , pp. 463-468
    • Campbell, J.D.1    Koike, K.2    Moreau, C.3    Sansom, M.S.P.4    Deeley, R.G.5    Cole, S.P.C.6
  • 9
    • 0023874147 scopus 로고
    • A method for the determination of inorganic-phosphate in the presence of labile organic phosphate, high-concentrations of protein - application to lens ATPases
    • Chifflet S., Torriglia A., Chiesa R., Tolosa S. A method for the determination of inorganic-phosphate in the presence of labile organic phosphate, high-concentrations of protein - application to lens ATPases. Anal. Biochem. 1988, 168:1-4.
    • (1988) Anal. Biochem. , vol.168 , pp. 1-4
    • Chifflet, S.1    Torriglia, A.2    Chiesa, R.3    Tolosa, S.4
  • 10
    • 33745897902 scopus 로고    scopus 로고
    • Transport of glutathione and glutathione conjugates by MRP1
    • Cole S.P., Deeley R.G. Transport of glutathione and glutathione conjugates by MRP1. Trends Pharmacol. Sci. 2006, 27:438-446.
    • (2006) Trends Pharmacol. Sci. , vol.27 , pp. 438-446
    • Cole, S.P.1    Deeley, R.G.2
  • 13
    • 31844446751 scopus 로고    scopus 로고
    • Functional importance of three basic residues clustered at the cytosolic interface of transmembrane helix 15 in the multidrug and organic anion transporter MRP1 (ABCC1)
    • Conseil G., Deeley R.G., Cole S.P.C. Functional importance of three basic residues clustered at the cytosolic interface of transmembrane helix 15 in the multidrug and organic anion transporter MRP1 (ABCC1). J. Biol. Chem. 2006, 281:43-50.
    • (2006) J. Biol. Chem. , vol.281 , pp. 43-50
    • Conseil, G.1    Deeley, R.G.2    Cole, S.P.C.3
  • 15
    • 33847134349 scopus 로고    scopus 로고
    • Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP
    • Dawson R.J., Locher K.P. Structure of the multidrug ABC transporter Sav1866 from Staphylococcus aureus in complex with AMP-PNP. FEBS Lett. 2007, 581:935-938.
    • (2007) FEBS Lett. , vol.581 , pp. 935-938
    • Dawson, R.J.1    Locher, K.P.2
  • 16
    • 31844455959 scopus 로고    scopus 로고
    • Substrate recognition and transport by multidrug resistance protein 1 (ABCC1)
    • Deeley R.G., Cole S.P.C. Substrate recognition and transport by multidrug resistance protein 1 (ABCC1). FEBS Lett. 2006, 580:1103-1111.
    • (2006) FEBS Lett. , vol.580 , pp. 1103-1111
    • Deeley, R.G.1    Cole, S.P.C.2
  • 18
    • 0026672405 scopus 로고
    • ATPase activity of partially purified P-glycoprotein from multidrug- resistant Chinese hamster ovary cells
    • Doige C.A., Yu X., Sharom F.J. ATPase activity of partially purified P-glycoprotein from multidrug- resistant Chinese hamster ovary cells. Biochim. Biophys. Acta 1992, 24:149-160.
    • (1992) Biochim. Biophys. Acta , vol.24 , pp. 149-160
    • Doige, C.A.1    Yu, X.2    Sharom, F.J.3
  • 19
    • 37749008623 scopus 로고    scopus 로고
    • Electron crystallography of biomolecules: mysterious membranes and missing cones
    • Ford R.C., Holzenburg A. Electron crystallography of biomolecules: mysterious membranes and missing cones. Trends Biochem. Sci. 2008, 33:38-43.
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 38-43
    • Ford, R.C.1    Holzenburg, A.2
  • 20
    • 0032562616 scopus 로고    scopus 로고
    • Multidrug resistance protein - Identification of regions required for active transport of leukotriene C-4
    • Gao M., Yamazaki M., Loe D.W., Westlake C.J., Grant C.E., Cole S.P.C., Deeley R.G. Multidrug resistance protein - Identification of regions required for active transport of leukotriene C-4. J. Biol. Chem. 1998, 273:10733-10740.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10733-10740
    • Gao, M.1    Yamazaki, M.2    Loe, D.W.3    Westlake, C.J.4    Grant, C.E.5    Cole, S.P.C.6    Deeley, R.G.7
  • 21
    • 0034724680 scopus 로고    scopus 로고
    • Comparison of the functional characteristics of the nucleotide binding domains of multidrug resistance protein 1
    • Gao M., Cui H.R., Loe D.W., Grant C.E., Almquist K.C., Cole S.P., Deeley R.G. Comparison of the functional characteristics of the nucleotide binding domains of multidrug resistance protein 1. J. Biol. Chem. 2000, 275:13098-13108.
    • (2000) J. Biol. Chem. , vol.275 , pp. 13098-13108
    • Gao, M.1    Cui, H.R.2    Loe, D.W.3    Grant, C.E.4    Almquist, K.C.5    Cole, S.P.6    Deeley, R.G.7
  • 22
    • 47249110343 scopus 로고    scopus 로고
    • Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter
    • Gerber S., Comellas-Bigler M., Goetz B.A., Locher K.P. Structural basis of trans-inhibition in a molybdate/tungstate ABC transporter. Science 2008, 321:246-250.
    • (2008) Science , vol.321 , pp. 246-250
    • Gerber, S.1    Comellas-Bigler, M.2    Goetz, B.A.3    Locher, K.P.4
  • 23
    • 0036828695 scopus 로고    scopus 로고
    • Charged amino acids in the sixth transmembrane helix of multidrug resistance protein 1 (MRP1/ABCC1) are critical determinants of transport activity
    • Haimeur A., Deeley R.G., Cole S.P.C. Charged amino acids in the sixth transmembrane helix of multidrug resistance protein 1 (MRP1/ABCC1) are critical determinants of transport activity. J. Biol. Chem. 2002, 277:41326-41333.
    • (2002) J. Biol. Chem. , vol.277 , pp. 41326-41333
    • Haimeur, A.1    Deeley, R.G.2    Cole, S.P.C.3
  • 24
    • 1242335471 scopus 로고    scopus 로고
    • The MRP-related and BCRP/ABCG2 multidrug resistance proteins: biology, substrate specificity and regulation
    • Haimeur A., Conseil G., Deeley R.G., Cole S.P.C. The MRP-related and BCRP/ABCG2 multidrug resistance proteins: biology, substrate specificity and regulation. Curr. Drug Metab. 2004, 5:21-53.
    • (2004) Curr. Drug Metab. , vol.5 , pp. 21-53
    • Haimeur, A.1    Conseil, G.2    Deeley, R.G.3    Cole, S.P.C.4
  • 25
    • 0039507411 scopus 로고
    • Structure of purple membrane from Halobacterium-Halobium - recording, measurement and evaluation of electron-micrographs at 3.5 a resolution
    • Henderson R., Baldwin J.M., Downing K.H., Lepault J., Zemlin F. Structure of purple membrane from Halobacterium-Halobium - recording, measurement and evaluation of electron-micrographs at 3.5 a resolution. Ultramicroscopy 1986, 19:147-178.
    • (1986) Ultramicroscopy , vol.19 , pp. 147-178
    • Henderson, R.1    Baldwin, J.M.2    Downing, K.H.3    Lepault, J.4    Zemlin, F.5
  • 28
    • 33947154878 scopus 로고    scopus 로고
    • Structure of an ABC transporter in complex with its binding protein
    • Hollenstein K., Frei D.C., Locher K.P. Structure of an ABC transporter in complex with its binding protein. Nature 2007, 446:213-216.
    • (2007) Nature , vol.446 , pp. 213-216
    • Hollenstein, K.1    Frei, D.C.2    Locher, K.P.3
  • 31
    • 0042009288 scopus 로고    scopus 로고
    • Mutation of proline residues in the NH2-terminal region of the multidrug resistance protein, MRP1 (ABCC1): effects on protein expression, membrane localization, and transport function
    • Ito K., Weigl K.E., Deeley R.G., Cole S.P.C. Mutation of proline residues in the NH2-terminal region of the multidrug resistance protein, MRP1 (ABCC1): effects on protein expression, membrane localization, and transport function. Biochim. Biophys. Acta, Biomembr. 2003, 1615:103-114.
    • (2003) Biochim. Biophys. Acta, Biomembr. , vol.1615 , pp. 103-114
    • Ito, K.1    Weigl, K.E.2    Deeley, R.G.3    Cole, S.P.C.4
  • 32
    • 47249084799 scopus 로고    scopus 로고
    • The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation
    • Kadaba N.S., Kaiser J.T., Johnson E., Lee A., Rees D.C. The high-affinity E. coli methionine ABC transporter: structure and allosteric regulation. Science 2008, 321:250-253.
    • (2008) Science , vol.321 , pp. 250-253
    • Kadaba, N.S.1    Kaiser, J.T.2    Johnson, E.3    Lee, A.4    Rees, D.C.5
  • 33
    • 60549097035 scopus 로고    scopus 로고
    • Alternating access in maltose transporter mediated by rigid-body rotations
    • Khare D., Oldham M.L., Orelle C., Davidson A.L., Chen J. Alternating access in maltose transporter mediated by rigid-body rotations. Mol. Cell 2009, 33:528-536.
    • (2009) Mol. Cell , vol.33 , pp. 528-536
    • Khare, D.1    Oldham, M.L.2    Orelle, C.3    Davidson, A.L.4    Chen, J.5
  • 34
    • 0037882044 scopus 로고    scopus 로고
    • Functional and structural consequences of cysteine substitutions in the NH2 proximal region of the human multidrug resistance protein 1 (MRP1/ABCC1)
    • Leslie E.M., Letourneau I.J., Deeley R.G., Cole S.P.C. Functional and structural consequences of cysteine substitutions in the NH2 proximal region of the human multidrug resistance protein 1 (MRP1/ABCC1). Biochemistry 2003, 42:5214-5224.
    • (2003) Biochemistry , vol.42 , pp. 5214-5224
    • Leslie, E.M.1    Letourneau, I.J.2    Deeley, R.G.3    Cole, S.P.C.4
  • 35
    • 17544368685 scopus 로고    scopus 로고
    • Multidrug resistance proteins: role of P-glycoprotein, MRP1, MRP2, and BCRP (ABCG2) in tissue defense
    • Leslie E.M., Deeley R.G., Cole S.P.C. Multidrug resistance proteins: role of P-glycoprotein, MRP1, MRP2, and BCRP (ABCG2) in tissue defense. Toxicol. Appl. Pharmacol. 2005, 204:216-237.
    • (2005) Toxicol. Appl. Pharmacol. , vol.204 , pp. 216-237
    • Leslie, E.M.1    Deeley, R.G.2    Cole, S.P.C.3
  • 36
    • 4143115811 scopus 로고    scopus 로고
    • Structure and mechanism of ABC transporters
    • Locher K.P. Structure and mechanism of ABC transporters. Curr. Opin. Struct. Biol. 2004, 14:426-431.
    • (2004) Curr. Opin. Struct. Biol. , vol.14 , pp. 426-431
    • Locher, K.P.1
  • 37
    • 0030009305 scopus 로고    scopus 로고
    • Multidrug resistance protein (MRP)-mediated transport of leukotriene C-4 and chemotherapeutic agents in membrane vesicles - demonstration of glutathione-dependent vincristine transport
    • Loe D.W., Almquist K.C., Deeley R.G., Cole S.P.C. Multidrug resistance protein (MRP)-mediated transport of leukotriene C-4 and chemotherapeutic agents in membrane vesicles - demonstration of glutathione-dependent vincristine transport. J. Biol. Chem. 1996, 271:9675-9682.
    • (1996) J. Biol. Chem. , vol.271 , pp. 9675-9682
    • Loe, D.W.1    Almquist, K.C.2    Deeley, R.G.3    Cole, S.P.C.4
  • 38
    • 0034602270 scopus 로고    scopus 로고
    • Functional reconstitution of substrate transport by purified multidrug resistance protein MRP1 (ABCC1) in phospholipid vesicles
    • Mao Q., Deeley R.G., Cole S.P. Functional reconstitution of substrate transport by purified multidrug resistance protein MRP1 (ABCC1) in phospholipid vesicles. J. Biol. Chem. 2000, 275:34166-34172.
    • (2000) J. Biol. Chem. , vol.275 , pp. 34166-34172
    • Mao, Q.1    Deeley, R.G.2    Cole, S.P.3
  • 39
    • 73449085784 scopus 로고    scopus 로고
    • Angiotensin II triggers release of leukotriene C(4) in vascular smooth muscle cells via the multidrug resistance-related protein 1
    • Mueller C.F., Becher M.U., Zimmer S., Wassmann S., Keuler B., Nickenig G. Angiotensin II triggers release of leukotriene C(4) in vascular smooth muscle cells via the multidrug resistance-related protein 1. Mol. Cell Biochem. 2009, 333:261-267.
    • (2009) Mol. Cell Biochem. , vol.333 , pp. 261-267
    • Mueller, C.F.1    Becher, M.U.2    Zimmer, S.3    Wassmann, S.4    Keuler, B.5    Nickenig, G.6
  • 40
    • 36549018568 scopus 로고    scopus 로고
    • Crystal structure of a catalytic intermediate of the maltose transporter
    • Oldham M.L., Khare D., Quiocho F.A., Davidson A.L., Chen J. Crystal structure of a catalytic intermediate of the maltose transporter. Nature 2007, 450:515-521.
    • (2007) Nature , vol.450 , pp. 515-521
    • Oldham, M.L.1    Khare, D.2    Quiocho, F.A.3    Davidson, A.L.4    Chen, J.5
  • 42
    • 15544376626 scopus 로고    scopus 로고
    • Dynamics of glutathione conjugation and conjugate efflux in detoxification of the carcinogen, 4-nitroquinoline 1-oxide: contributions of glutathione, glutathione S-transferase, and MRP1
    • Peklak-Scott C., Townsend A.J., Morrow C.S. Dynamics of glutathione conjugation and conjugate efflux in detoxification of the carcinogen, 4-nitroquinoline 1-oxide: contributions of glutathione, glutathione S-transferase, and MRP1. Biochemistry 2005, 44:4426-4433.
    • (2005) Biochemistry , vol.44 , pp. 4426-4433
    • Peklak-Scott, C.1    Townsend, A.J.2    Morrow, C.S.3
  • 44
    • 0035844237 scopus 로고    scopus 로고
    • The structure of the multidrug resistance protein 1 (MRP1/ABCC1) - crystallization and single-particle analysis
    • Rosenberg M.F., Mao Q.C., Holzenburg A., Ford R.C., Deeley R.G., Cole S.P.C. The structure of the multidrug resistance protein 1 (MRP1/ABCC1) - crystallization and single-particle analysis. J. Biol. Chem. 2001, 276:16076-16082.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16076-16082
    • Rosenberg, M.F.1    Mao, Q.C.2    Holzenburg, A.3    Ford, R.C.4    Deeley, R.G.5    Cole, S.P.C.6
  • 45
    • 0037424343 scopus 로고    scopus 로고
    • Three-dimensional structures of the mammalian multidrug resistance P-glycoprotein demonstrate major conformational changes in the transmembrane domains upon nucleotide binding
    • Rosenberg M.F., Kamis A.B., Callaghan R., Higgins C.F., Ford R.C. Three-dimensional structures of the mammalian multidrug resistance P-glycoprotein demonstrate major conformational changes in the transmembrane domains upon nucleotide binding. J. Biol. Chem. 2003, 278:8294-8299.
    • (2003) J. Biol. Chem. , vol.278 , pp. 8294-8299
    • Rosenberg, M.F.1    Kamis, A.B.2    Callaghan, R.3    Higgins, C.F.4    Ford, R.C.5
  • 46
    • 4544378176 scopus 로고    scopus 로고
    • Purification and crystallization of the cystic fibrosis transmembrane conductance regulator (CFTR)
    • Rosenberg M.F., Kamis A.B., Aleksandrov L.A., Ford R.C., Riordan J.R. Purification and crystallization of the cystic fibrosis transmembrane conductance regulator (CFTR). J. Biol. Chem. 2004, 279:39051-39057.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39051-39057
    • Rosenberg, M.F.1    Kamis, A.B.2    Aleksandrov, L.A.3    Ford, R.C.4    Riordan, J.R.5
  • 47
    • 13244292479 scopus 로고    scopus 로고
    • Three-dimensional structure of P-glycoprotein: the transmembrane regions adopt an asymmetric configuration in the nucleotide-bound state
    • Rosenberg M.F., Callaghan R., Modok S., Higgins C.F., Ford R.C. Three-dimensional structure of P-glycoprotein: the transmembrane regions adopt an asymmetric configuration in the nucleotide-bound state. J. Biol. Chem. 2005, 280:2857-2862.
    • (2005) J. Biol. Chem. , vol.280 , pp. 2857-2862
    • Rosenberg, M.F.1    Callaghan, R.2    Modok, S.3    Higgins, C.F.4    Ford, R.C.5
  • 48
    • 33744946318 scopus 로고    scopus 로고
    • Role of GSH in estrone sulfate binding and translocation by the multidrug resistance protein 1 (MRP1/ABCC1)
    • Rothnie A., Callaghan R., Deeley R.G., Cole S.P.C. Role of GSH in estrone sulfate binding and translocation by the multidrug resistance protein 1 (MRP1/ABCC1). J. Biol. Chem. 2006, 281:13906-13914.
    • (2006) J. Biol. Chem. , vol.281 , pp. 13906-13914
    • Rothnie, A.1    Callaghan, R.2    Deeley, R.G.3    Cole, S.P.C.4
  • 49
    • 0000059880 scopus 로고
    • Large single-crystals of the neurospora-crassa plasma-membrane H(+)- ATPase - an approach to the crystallization of integral membrane-proteins
    • Scarborough G.A. Large single-crystals of the neurospora-crassa plasma-membrane H(+)- ATPase - an approach to the crystallization of integral membrane-proteins. Acta Crystallogr., Sect. D: Biol. Crystallogr. 1994, 50:643-649.
    • (1994) Acta Crystallogr., Sect. D: Biol. Crystallogr. , vol.50 , pp. 643-649
    • Scarborough, G.A.1
  • 52
    • 0028059991 scopus 로고
    • Analysis of electron-microscope images and electron-diffraction patterns of thin-crystals of 029-connectors in ice
    • Valpuesta J.M., Carrascosa J.L., Henderson R. Analysis of electron-microscope images and electron-diffraction patterns of thin-crystals of 029-connectors in ice. J. Mol. Biol. 1994, 240:281-287.
    • (1994) J. Mol. Biol. , vol.240 , pp. 281-287
    • Valpuesta, J.M.1    Carrascosa, J.L.2    Henderson, R.3
  • 53
    • 37649004412 scopus 로고    scopus 로고
    • Flexibility in the ABC transporter MsbA: alternating access with a twist
    • Ward A., Reyes C.L., Yu J., Roth C.B., Chang G. Flexibility in the ABC transporter MsbA: alternating access with a twist. Proc. Natl. Acad. Sci. USA 2007, 104:19005-19010.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 19005-19010
    • Ward, A.1    Reyes, C.L.2    Yu, J.3    Roth, C.B.4    Chang, G.5
  • 54
    • 0344629891 scopus 로고    scopus 로고
    • Identification of the structural and functional boundaries of the multidrug resistance protein 1 cytoplasmic loop 3
    • Westlake C.J., Qian Y.M., Gao M., Vasa M., Cole S.P.C., Deeley R.G. Identification of the structural and functional boundaries of the multidrug resistance protein 1 cytoplasmic loop 3. Biochemistry 2003, 42:14099-14113.
    • (2003) Biochemistry , vol.42 , pp. 14099-14113
    • Westlake, C.J.1    Qian, Y.M.2    Gao, M.3    Vasa, M.4    Cole, S.P.C.5    Deeley, R.G.6
  • 55
    • 18244399574 scopus 로고    scopus 로고
    • Role of the NH2-terminal membrane spanning domain of multidrug resistance protein 1/ABCC1 in protein processing and trafficking
    • Westlake C.J., Cole S.P.C., Deeley R.G. Role of the NH2-terminal membrane spanning domain of multidrug resistance protein 1/ABCC1 in protein processing and trafficking. Mol. Biol. Cell 2005, 16:2483-2492.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 2483-2492
    • Westlake, C.J.1    Cole, S.P.C.2    Deeley, R.G.3
  • 56
    • 0032780181 scopus 로고    scopus 로고
    • Situs: a package for docking crystal structures into low-resolution maps from electron microscopy
    • Wriggers W., Milligan R.A., Mccammon J.A. Situs: a package for docking crystal structures into low-resolution maps from electron microscopy. J. Struct. Biol. 1999, 125:185-195.
    • (1999) J. Struct. Biol. , vol.125 , pp. 185-195
    • Wriggers, W.1    Milligan, R.A.2    Mccammon, J.A.3
  • 57
    • 27544483046 scopus 로고    scopus 로고
    • Analysis of human multidrug resistance protein 1 (ABCC1) by matrix-assisted laser desorption ionization/time of flight mass spectrometry: toward identification of leukotriene C4 binding sites
    • Wu P., Oleschuk C.J., Mao Q.C., Keller B.O., Deeley R.G., Cole S.P.C. Analysis of human multidrug resistance protein 1 (ABCC1) by matrix-assisted laser desorption ionization/time of flight mass spectrometry: toward identification of leukotriene C4 binding sites. Mol. Pharmacol. 2005, 68:1455-1465.
    • (2005) Mol. Pharmacol. , vol.68 , pp. 1455-1465
    • Wu, P.1    Oleschuk, C.J.2    Mao, Q.C.3    Keller, B.O.4    Deeley, R.G.5    Cole, S.P.C.6
  • 58
    • 3242738307 scopus 로고    scopus 로고
    • Transmembrane helix 11 of multidrug resistance protein 1 (MRPI/ABCC1): identification of polar amino acids important for substrate specificity and binding of ATP at nucleotide binding domain 1
    • Zhang D.W., Nunoya K., Vasa M., Gu H.M., Theis A., Cole S.P.C., Deeley R.G. Transmembrane helix 11 of multidrug resistance protein 1 (MRPI/ABCC1): identification of polar amino acids important for substrate specificity and binding of ATP at nucleotide binding domain 1. Biochemistry 2004, 43:9413-9425.
    • (2004) Biochemistry , vol.43 , pp. 9413-9425
    • Zhang, D.W.1    Nunoya, K.2    Vasa, M.3    Gu, H.M.4    Theis, A.5    Cole, S.P.C.6    Deeley, R.G.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.