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Volumn 580, Issue 4, 2006, Pages 1171-1177

ABC lipid transporters: Extruders, flippases, or flopless activators?

Author keywords

Flippase; Lipid asymmetry; Lipid translocation; Transbilayer movement

Indexed keywords

ABC LIPID TRANSPORTER; ABC TRANSPORTER; ADENOSINE TRIPHOSPHATE; FLIPPASE; MEMBRANE LIPID; UNCLASSIFIED DRUG;

EID: 31844438479     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2005.12.019     Document Type: Short Survey
Times cited : (102)

References (89)
  • 1
    • 0027363563 scopus 로고
    • Homozygous disruption of the murine mdr2 P-glycoprotein gene leads to a complete absence of phospholipid from bile and to liver disease
    • J.J. Smit Homozygous disruption of the murine mdr2 P-glycoprotein gene leads to a complete absence of phospholipid from bile and to liver disease Cell 75 1993 451 462
    • (1993) Cell , vol.75 , pp. 451-462
    • Smit, J.J.1
  • 2
    • 31844437042 scopus 로고    scopus 로고
    • The molecular basis of multidrug resistance in cancer: The early years of P-glycoprotein research
    • Gottesman, M.M. and Ling, V. (2005) The molecular basis of multidrug resistance in cancer: The early years of P-glycoprotein research. FEBS Lett., this issue.
    • (2005) FEBS Lett. , Issue.THIS ISSUE
    • Gottesman, M.M.1    Ling, V.2
  • 3
    • 0027532282 scopus 로고
    • Putative X-linked adrenoleukodystrophy gene shares unexpected homology with ABC transporters
    • J. Mosser Putative X-linked adrenoleukodystrophy gene shares unexpected homology with ABC transporters Nature 361 1993 726 730
    • (1993) Nature , vol.361 , pp. 726-730
    • Mosser, J.1
  • 4
    • 0007544439 scopus 로고    scopus 로고
    • MDR1 P-glycoprotein is a lipid translocase of broad specificity, while MDR3 P-glycoprotein specifically translocates phosphatidylcholine
    • A. van Helvoort, A.J. Smith, H. Sprong, I. Fritzsche, A.H. Schinkel, P. Borst, and G. van Meer MDR1 P-glycoprotein is a lipid translocase of broad specificity, while MDR3 P-glycoprotein specifically translocates phosphatidylcholine Cell 87 1996 507 517
    • (1996) Cell , vol.87 , pp. 507-517
    • Van Helvoort, A.1    Smith, A.J.2    Sprong, H.3    Fritzsche, I.4    Schinkel, A.H.5    Borst, P.6    Van Meer, G.7
  • 6
    • 14644404294 scopus 로고    scopus 로고
    • Function of prokaryotic and eukaryotic ABC proteins in lipid transport
    • A. Pohl, P.F. Devaux, and A. Herrmann Function of prokaryotic and eukaryotic ABC proteins in lipid transport Biochim. Biophys. Acta 1733 2005 29 52
    • (2005) Biochim. Biophys. Acta , vol.1733 , pp. 29-52
    • Pohl, A.1    Devaux, P.F.2    Herrmann, A.3
  • 7
  • 8
    • 4143128760 scopus 로고    scopus 로고
    • Chemical modification identifies two populations of glycerophospholipid flippase in rat liver ER
    • Q.L. Chang, S.N. Gummadi, and A.K. Menon Chemical modification identifies two populations of glycerophospholipid flippase in rat liver ER Biochemistry 43 2004 10710 10718
    • (2004) Biochemistry , vol.43 , pp. 10710-10718
    • Chang, Q.L.1    Gummadi, S.N.2    Menon, A.K.3
  • 9
    • 0032896265 scopus 로고    scopus 로고
    • Enhancement of endocytosis due to aminophospholipid transport across the plasma membrane of living cells
    • E. Farge, D.M. Ojcius, A. Subtil, and A. Dautry-Varsat Enhancement of endocytosis due to aminophospholipid transport across the plasma membrane of living cells Am. J. Physiol. 276 1999 C725 C733
    • (1999) Am. J. Physiol. , vol.276
    • Farge, E.1    Ojcius, D.M.2    Subtil, A.3    Dautry-Varsat, A.4
  • 10
    • 9644264229 scopus 로고    scopus 로고
    • Flippases and vesicle-mediated protein transport
    • T.R. Graham Flippases and vesicle-mediated protein transport Trends Cell. Biol. 14 2004 670 677
    • (2004) Trends Cell. Biol. , vol.14 , pp. 670-677
    • Graham, T.R.1
  • 11
    • 1642378564 scopus 로고    scopus 로고
    • Tracking down lipid flippases and their biological functions
    • T. Pomorski, J.C. Holthuis, A. Herrmann, and G. van Meer Tracking down lipid flippases and their biological functions J. Cell Sci. 117 2004 805 813
    • (2004) J. Cell Sci. , vol.117 , pp. 805-813
    • Pomorski, T.1    Holthuis, J.C.2    Herrmann, A.3    Van Meer, G.4
  • 12
    • 0034700981 scopus 로고    scopus 로고
    • Changes of intrinsic membrane potentials induced by flip-flop of long-chain fatty acids
    • E.E. Pohl, U. Peterson, J. Sun, and P. Pohl Changes of intrinsic membrane potentials induced by flip-flop of long-chain fatty acids Biochemistry 39 2000 1834 1839
    • (2000) Biochemistry , vol.39 , pp. 1834-1839
    • Pohl, E.E.1    Peterson, U.2    Sun, J.3    Pohl, P.4
  • 13
    • 0036789540 scopus 로고    scopus 로고
    • Probing red cell membrane cholesterol movement with cyclodextrin
    • T.L. Steck, J. Ye, and Y. Lange Probing red cell membrane cholesterol movement with cyclodextrin Biophys. J. 83 2002 2118 2125
    • (2002) Biophys. J. , vol.83 , pp. 2118-2125
    • Steck, T.L.1    Ye, J.2    Lange, Y.3
  • 14
    • 0037832573 scopus 로고    scopus 로고
    • Fast flip-flop of cholesterol and fatty acids in membranes: Implications for membrane transport proteins
    • J.A. Hamilton Fast flip-flop of cholesterol and fatty acids in membranes: implications for membrane transport proteins Curr. Opin. Lipidol. 14 2003 263 271
    • (2003) Curr. Opin. Lipidol. , vol.14 , pp. 263-271
    • Hamilton, J.A.1
  • 15
    • 0030743667 scopus 로고    scopus 로고
    • Measurement of spontaneous transfer and transbilayer movement of BODIPY-labeled lipids in lipid vesicles
    • J. Bai, and R.E. Pagano Measurement of spontaneous transfer and transbilayer movement of BODIPY-labeled lipids in lipid vesicles Biochemistry 36 1997 8840 8848
    • (1997) Biochemistry , vol.36 , pp. 8840-8848
    • Bai, J.1    Pagano, R.E.2
  • 16
    • 21844477032 scopus 로고    scopus 로고
    • Rapid transbilayer movement of ceramides in phospholipid vesicles and in human erythrocytes
    • I. López-Montero, N. Rodriguez, S. Cribier, A. Pohl, M. Velez, and P.F. Devaux Rapid transbilayer movement of ceramides in phospholipid vesicles and in human erythrocytes J. Biol. Chem. 280 2005 25811 25819
    • (2005) J. Biol. Chem. , vol.280 , pp. 25811-25819
    • López-Montero, I.1    Rodriguez, N.2    Cribier, S.3    Pohl, A.4    Velez, M.5    Devaux, P.F.6
  • 17
    • 22244449240 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of association of a fluorescent lysophospholipid derivative with lipid bilayers in liquid-ordered and liquid-disordered phases
    • J.L. Sampaio, M.J. Moreno, and W.L. Vaz Kinetics and thermodynamics of association of a fluorescent lysophospholipid derivative with lipid bilayers in liquid-ordered and liquid-disordered phases Biophys. J. 88 2005 4064 4071
    • (2005) Biophys. J. , vol.88 , pp. 4064-4071
    • Sampaio, J.L.1    Moreno, M.J.2    Vaz, W.L.3
  • 18
    • 3042773990 scopus 로고    scopus 로고
    • Kinetics and thermodynamics of association of a phospholipid derivative with lipid bilayers in liquid-disordered and liquid-ordered phases
    • M.S. Abreu, M.J. Moreno, and W.L. Vaz Kinetics and thermodynamics of association of a phospholipid derivative with lipid bilayers in liquid-disordered and liquid-ordered phases Biophys. J. 87 2004 353 365
    • (2004) Biophys. J. , vol.87 , pp. 353-365
    • Abreu, M.S.1    Moreno, M.J.2    Vaz, W.L.3
  • 19
    • 0023663531 scopus 로고
    • Mechanism and consequences of cellular cholesterol exchange and transfer
    • M.C. Phillips, W.J. Johnson, and G.H. Rothblat Mechanism and consequences of cellular cholesterol exchange and transfer Biochim. Biophys. Acta 906 1987 223 276
    • (1987) Biochim. Biophys. Acta , vol.906 , pp. 223-276
    • Phillips, M.C.1    Johnson, W.J.2    Rothblat, G.H.3
  • 20
    • 0025162276 scopus 로고
    • Mechanism of spontaneous, concentration-dependent phospholipid transfer between bilayers
    • J.D. Jones, and T.E. Thompson Mechanism of spontaneous, concentration-dependent phospholipid transfer between bilayers Biochemistry 29 1990 1593 1600
    • (1990) Biochemistry , vol.29 , pp. 1593-1600
    • Jones, J.D.1    Thompson, T.E.2
  • 23
    • 2442640305 scopus 로고    scopus 로고
    • Predicting function from structure: 3D structure studies of the mammalian Golgi complex
    • S. Mogelsvang, B.J. Marsh, M.S. Ladinsky, and K.E. Howell Predicting function from structure: 3D structure studies of the mammalian Golgi complex Traffic 5 2004 338 345
    • (2004) Traffic , vol.5 , pp. 338-345
    • Mogelsvang, S.1    Marsh, B.J.2    Ladinsky, M.S.3    Howell, K.E.4
  • 25
    • 0040284751 scopus 로고    scopus 로고
    • Mutations in the MDR3 gene cause progressive familial intrahepatic cholestasis
    • J.M. de Vree Mutations in the MDR3 gene cause progressive familial intrahepatic cholestasis Proc. Natl. Acad. Sci. USA 95 1998 282 287
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 282-287
    • De Vree, J.M.1
  • 28
    • 17344366172 scopus 로고    scopus 로고
    • A gene encoding a liver-specific ABC transporter is mutated in progressive familial intrahepatic cholestas is
    • S.S. Strautnieks A gene encoding a liver-specific ABC transporter is mutated in progressive familial intrahepatic cholestas is Nat. Genet. 20 1998 233 238
    • (1998) Nat. Genet. , vol.20 , pp. 233-238
    • Strautnieks, S.S.1
  • 30
    • 17744390348 scopus 로고    scopus 로고
    • Accumulation of dietary cholesterol in sitosterolemia caused by mutations in adjacent ABC transporters
    • K.E. Berge Accumulation of dietary cholesterol in sitosterolemia caused by mutations in adjacent ABC transporters Science 290 2000 1771 1775
    • (2000) Science , vol.290 , pp. 1771-1775
    • Berge, K.E.1
  • 31
    • 0032813660 scopus 로고    scopus 로고
    • Tangier disease is caused by mutations in the gene encoding ATP-binding cassette transporter 1
    • S. Rust Tangier disease is caused by mutations in the gene encoding ATP-binding cassette transporter 1 Nat. Genet. 22 1999 352 355
    • (1999) Nat. Genet. , vol.22 , pp. 352-355
    • Rust, S.1
  • 32
    • 0032813808 scopus 로고    scopus 로고
    • Mutations in ABC1 in Tangier disease and familial high-density lipoprotein deficiency
    • A. Brooks-Wilson Mutations in ABC1 in Tangier disease and familial high-density lipoprotein deficiency Nat. Genet. 22 1999 336 345
    • (1999) Nat. Genet. , vol.22 , pp. 336-345
    • Brooks-Wilson, A.1
  • 33
    • 0032813809 scopus 로고    scopus 로고
    • The gene encoding ATP-binding cassette transporter 1 is mutated in Tangier disease
    • M. Bodzioch The gene encoding ATP-binding cassette transporter 1 is mutated in Tangier disease Nat. Genet. 22 1999 347 351
    • (1999) Nat. Genet. , vol.22 , pp. 347-351
    • Bodzioch, M.1
  • 34
    • 12944286618 scopus 로고    scopus 로고
    • ABCG1 (ABC8), the human homolog of the Drosophila white gene, is a regulator of macrophage cholesterol and phospholipid transport
    • J. Klucken ABCG1 (ABC8), the human homolog of the Drosophila white gene, is a regulator of macrophage cholesterol and phospholipid transport Proc. Natl. Acad. Sci. USA 97 2000 817 822
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 817-822
    • Klucken, J.1
  • 35
    • 3042798281 scopus 로고    scopus 로고
    • ATP-binding cassette transporters G1 and G4 mediate cellular cholesterol efflux to high-density lipoproteins
    • N. Wang, D. Lan, W. Chen, F. Matsuura, and A.R. Tall ATP-binding cassette transporters G1 and G4 mediate cellular cholesterol efflux to high-density lipoproteins Proc. Natl. Acad. Sci. USA 101 2004 9774 9779
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9774-9779
    • Wang, N.1    Lan, D.2    Chen, W.3    Matsuura, F.4    Tall, A.R.5
  • 36
    • 0035900369 scopus 로고    scopus 로고
    • ABCA3 is a lamellar body membrane protein in human lung alveolar type II cells
    • G. Yamano ABCA3 is a lamellar body membrane protein in human lung alveolar type II cells FEBS Lett. 508 2001 221 225
    • (2001) FEBS Lett. , vol.508 , pp. 221-225
    • Yamano, G.1
  • 38
    • 4744347103 scopus 로고    scopus 로고
    • Human ABCA3, a product of a responsible gene for abca3 for fatal surfactant deficiency in newborns, exhibits unique ATP hydrolysis activity and generates intracellular multilamellar vesicles
    • K. Nagata, A. Yamamoto, N. Ban, A.R. Tanaka, M. Matsuo, N. Kioka, N. Inagaki, and K. Ueda Human ABCA3, a product of a responsible gene for abca3 for fatal surfactant deficiency in newborns, exhibits unique ATP hydrolysis activity and generates intracellular multilamellar vesicles Biochem. Biophys. Res. Commun. 324 2004 262 268
    • (2004) Biochem. Biophys. Res. Commun. , vol.324 , pp. 262-268
    • Nagata, K.1    Yamamoto, A.2    Ban, N.3    Tanaka, A.R.4    Matsuo, M.5    Kioka, N.6    Inagaki, N.7    Ueda, K.8
  • 39
    • 10744220980 scopus 로고    scopus 로고
    • Mutations in the transporter ABCA12 are associated with lamellar ichthyosis type 2
    • C. Lefevre Mutations in the transporter ABCA12 are associated with lamellar ichthyosis type 2 Hum. Mol. Genet. 12 2003 2369 2378
    • (2003) Hum. Mol. Genet. , vol.12 , pp. 2369-2378
    • Lefevre, C.1
  • 40
    • 22144437692 scopus 로고    scopus 로고
    • Mutations in lipid transporter ABCA12 in harlequin ichthyosis and functional recovery by corrective gene transfer
    • M. Akiyama Mutations in lipid transporter ABCA12 in harlequin ichthyosis and functional recovery by corrective gene transfer J. Clin. Invest. 115 2005 1777 1784
    • (2005) J. Clin. Invest. , vol.115 , pp. 1777-1784
    • Akiyama, M.1
  • 41
    • 20244379129 scopus 로고    scopus 로고
    • Mutations in ABCA12 underlie the severe congenital skin disease harlequin ichthyosis
    • D.P. Kelsell Mutations in ABCA12 underlie the severe congenital skin disease harlequin ichthyosis Am. J. Human Genet. 76 2005 794 803
    • (2005) Am. J. Human Genet. , vol.76 , pp. 794-803
    • Kelsell, D.P.1
  • 42
    • 0033781690 scopus 로고    scopus 로고
    • Origin of the corneocyte lipid envelope (CLE): Observations in harlequin ichthyosis and cultured human keratinocytes
    • P.M. Elias, M. Fartasch, D. Crumrine, M. Behne, Y. Uchida, and W.M. Holleran Origin of the corneocyte lipid envelope (CLE): observations in harlequin ichthyosis and cultured human keratinocytes J. Invest. Dermatol. 115 2000 765 769
    • (2000) J. Invest. Dermatol. , vol.115 , pp. 765-769
    • Elias, P.M.1    Fartasch, M.2    Crumrine, D.3    Behne, M.4    Uchida, Y.5    Holleran, W.M.6
  • 43
    • 28744450445 scopus 로고    scopus 로고
    • Inactivation of the peroxisomal ABCD2 transporter in the mouse leads to late-onset ataxia involving mitochondria, Golgi and endoplasmic reticulum
    • I. Ferrer Inactivation of the peroxisomal ABCD2 transporter in the mouse leads to late-onset ataxia involving mitochondria, Golgi and endoplasmic reticulum Hum. Mol. Genet. 23 2005 3565 3577
    • (2005) Hum. Mol. Genet. , vol.23 , pp. 3565-3577
    • Ferrer, I.1
  • 44
    • 15944408418 scopus 로고    scopus 로고
    • Probing substrate-induced conformational alterations in adrenoleukodystrophy protein by proteolysis
    • C.P. Guimaraes, C. Sa-Miranda, and J.E. Azevedo Probing substrate-induced conformational alterations in adrenoleukodystrophy protein by proteolysis J. Human Genet. 50 2005 99 105
    • (2005) J. Human Genet. , vol.50 , pp. 99-105
    • Guimaraes, C.P.1    Sa-Miranda, C.2    Azevedo, J.E.3
  • 45
    • 0033538438 scopus 로고    scopus 로고
    • Insights into the function of Rim protein in photoreceptors and etiology of Stargardt's disease from the phenotype in abcr knockout mice
    • J. Weng, N.L. Mata, S.M. Azarian, R.T. Tzekov, D.G. Birch, and G.H. Travis Insights into the function of Rim protein in photoreceptors and etiology of Stargardt's disease from the phenotype in abcr knockout mice Cell 98 1999 13 23
    • (1999) Cell , vol.98 , pp. 13-23
    • Weng, J.1    Mata, N.L.2    Azarian, S.M.3    Tzekov, R.T.4    Birch, D.G.5    Travis, G.H.6
  • 46
    • 11144240503 scopus 로고    scopus 로고
    • N-retinylidene-phosphatidylethanolamine is the preferred retinoid substrate for the photoreceptor-specific ABC transporter ABCA4 (ABCR)
    • S. Beharry, M. Zhong, and R.S. Molday N-retinylidene- phosphatidylethanolamine is the preferred retinoid substrate for the photoreceptor-specific ABC transporter ABCA4 (ABCR) J. Biol. Chem. 279 2004 53972 53979
    • (2004) J. Biol. Chem. , vol.279 , pp. 53972-53979
    • Beharry, S.1    Zhong, M.2    Molday, R.S.3
  • 47
    • 21244451958 scopus 로고    scopus 로고
    • The retinal pigment epithelium in visual function
    • O. Strauss The retinal pigment epithelium in visual function Physiol. Rev. 85 2005 845 881
    • (2005) Physiol. Rev. , vol.85 , pp. 845-881
    • Strauss, O.1
  • 48
    • 31844450741 scopus 로고    scopus 로고
    • On the putative co-transport of drugs by multidrug resistance proteins
    • doi:10.1016/j.febslet.2005.12.039.
    • Borst, P., Zelcer, N., van de Wetering, K. and Poolman, B. (2005) On the putative co-transport of drugs by multidrug resistance proteins. FEBS Lett., this issue, doi:10.1016/j.febslet.2005.12.039.
    • (2005) FEBS Lett. , Issue.THIS ISSUE
    • Borst, P.1    Zelcer, N.2    Van De Wetering, K.3    Poolman, B.4
  • 49
    • 31844455959 scopus 로고    scopus 로고
    • Substrate recognition and transport by multidrug resistance protein (MRP)1 (ABCC1)
    • doi:10.1016/j.febslet.2005.12.036.
    • Deeley, R.G. and Cole, S.P.C. (2005) Substrate recognition and transport by multidrug resistance protein (MRP)1 (ABCC1). FEBS Lett., this issue, doi:10.1016/j.febslet.2005.12.036.
    • (2005) FEBS Lett. , Issue.THIS ISSUE
    • Deeley, R.G.1    Cole, S.P.C.2
  • 50
    • 0032709624 scopus 로고    scopus 로고
    • Secretion of platelet-activating factor is mediated by MDR1 P- glycoprotein in cultured human mesangial cells
    • S. Ernest, and E. Bello-Reuss Secretion of platelet-activating factor is mediated by MDR1 P- glycoprotein in cultured human mesangial cells J. Am. Soc. Nephrol. 10 1999 2306 2313
    • (1999) J. Am. Soc. Nephrol. , vol.10 , pp. 2306-2313
    • Ernest, S.1    Bello-Reuss, E.2
  • 51
    • 0035425507 scopus 로고    scopus 로고
    • Multidrug-resistance P-glycoprotein (MDR1) secretes platelet-activating factor
    • R.J. Raggers, I. Vogels, and G. van Meer Multidrug-resistance P-glycoprotein (MDR1) secretes platelet-activating factor Biochem. J. 357 2001 859 865
    • (2001) Biochem. J. , vol.357 , pp. 859-865
    • Raggers, R.J.1    Vogels, I.2    Van Meer, G.3
  • 52
    • 0034717836 scopus 로고    scopus 로고
    • Progress towards understanding the role of microsomal triglyceride transfer protein in apolipoprotein-B lipoprotein assembly
    • D.A. Gordon, and H. Jamil Progress towards understanding the role of microsomal triglyceride transfer protein in apolipoprotein-B lipoprotein assembly Biochim. Biophys. Acta 1486 2000 72 83
    • (2000) Biochim. Biophys. Acta , vol.1486 , pp. 72-83
    • Gordon, D.A.1    Jamil, H.2
  • 53
    • 10744232076 scopus 로고    scopus 로고
    • Saposin C is required for lipid presentation by human CD1b
    • F. Winau Saposin C is required for lipid presentation by human CD1b Nat. Immunol. 5 2004 169 174
    • (2004) Nat. Immunol. , vol.5 , pp. 169-174
    • Winau, F.1
  • 55
    • 0034731676 scopus 로고    scopus 로고
    • Functional and histochemical analysis of MDR3 P-glycoprotein in a tetracycline-controlled gene expression system
    • B.A. Fitscher, R. Ehehalt, C. Jochims, J. Pohl, T. Herrmann, and W. Stremmel Functional and histochemical analysis of MDR3 P-glycoprotein in a tetracycline-controlled gene expression system Eur. J. Med. Res. 5 2000 517 522
    • (2000) Eur. J. Med. Res. , vol.5 , pp. 517-522
    • Fitscher, B.A.1    Ehehalt, R.2    Jochims, C.3    Pohl, J.4    Herrmann, T.5    Stremmel, W.6
  • 56
    • 0033776534 scopus 로고    scopus 로고
    • ABC1 promotes engulfment of apoptotic cells and transbilayer redistribution of phosphatidylserine
    • Y. Hamon ABC1 promotes engulfment of apoptotic cells and transbilayer redistribution of phosphatidylserine Nat. Cell Biol. 2 2000 399 406
    • (2000) Nat. Cell Biol. , vol.2 , pp. 399-406
    • Hamon, Y.1
  • 57
    • 22144479426 scopus 로고    scopus 로고
    • A novel missense mutation in ABCA1 results in altered protein trafficking and reduced phosphatidylserine translocation in a patient with Scott syndrome
    • C. Albrecht A novel missense mutation in ABCA1 results in altered protein trafficking and reduced phosphatidylserine translocation in a patient with Scott syndrome Blood 106 2005 542 549
    • (2005) Blood , vol.106 , pp. 542-549
    • Albrecht, C.1
  • 58
    • 0017250826 scopus 로고
    • Topological asymmetry of phospholipid metabolism in rat erythrocyte membranes. Evidence for flip-flop of lecithin
    • W. Renooij, L.M. Van Golde, R.F. Zwaal, and L.L. van Deenen Topological asymmetry of phospholipid metabolism in rat erythrocyte membranes. Evidence for flip-flop of lecithin Eur. J. Biochem. 61 1976 53 58
    • (1976) Eur. J. Biochem. , vol.61 , pp. 53-58
    • Renooij, W.1    Van Golde, L.M.2    Zwaal, R.F.3    Van Deenen, L.L.4
  • 59
    • 4043096982 scopus 로고    scopus 로고
    • Natural phosphatidylcholine is actively translocated across the plasma membrane to the surface of mammalian cells
    • N. Kälin, J. Fernandes, S. Hrafnsdottir, and G. van Meer Natural phosphatidylcholine is actively translocated across the plasma membrane to the surface of mammalian cells J. Biol. Chem. 279 2004 33228 33236
    • (2004) J. Biol. Chem. , vol.279 , pp. 33228-33236
    • Kälin, N.1    Fernandes, J.2    Hrafnsdottir, S.3    Van Meer, G.4
  • 60
    • 0033058419 scopus 로고    scopus 로고
    • The human multidrug resistance protein MRP1 translocates sphingolipid analogs across the plasma membrane
    • R.J. Raggers, A. van Helvoort, R. Evers, and G. van Meer The human multidrug resistance protein MRP1 translocates sphingolipid analogs across the plasma membrane J. Cell Sci. 112 1999 415 422
    • (1999) J. Cell Sci. , vol.112 , pp. 415-422
    • Raggers, R.J.1    Van Helvoort, A.2    Evers, R.3    Van Meer, G.4
  • 61
    • 0030977145 scopus 로고    scopus 로고
    • Phosphatidylcholine and phosphatidylethanolamine behave as substrates of the human MDR1 P-glycoprotein
    • I. Bosch, K. Dunussi-Joannopoulos, R.-L. Wu, S.T. Furlong, and J. Croop Phosphatidylcholine and phosphatidylethanolamine behave as substrates of the human MDR1 P-glycoprotein Biochemistry 36 1997 5685 5694
    • (1997) Biochemistry , vol.36 , pp. 5685-5694
    • Bosch, I.1    Dunussi-Joannopoulos, K.2    Wu, R.-L.3    Furlong, S.T.4    Croop, J.5
  • 62
    • 0036646107 scopus 로고    scopus 로고
    • Transport of phosphatidylserine via MDR1 (multidrug resistance 1)P-glycoprotein in a human gastric carcinoma cell line
    • A. Pohl, H. Lage, P. Muller, T. Pomorski, and A. Herrmann Transport of phosphatidylserine via MDR1 (multidrug resistance 1)P-glycoprotein in a human gastric carcinoma cell line Biochem. J. 365 2002 259 268
    • (2002) Biochem. J. , vol.365 , pp. 259-268
    • Pohl, A.1    Lage, H.2    Muller, P.3    Pomorski, T.4    Herrmann, A.5
  • 64
    • 0032553014 scopus 로고    scopus 로고
    • Transbilayer movement of NBD-labeled phospholipids in red blood cell membranes: Outward-directed transport by the multidrug resistance protein 1 (MRP1)
    • D.W. Dekkers, P. Comfurius, A.J. Schroit, E.M. Bevers, and R.F. Zwaal Transbilayer movement of NBD-labeled phospholipids in red blood cell membranes: outward-directed transport by the multidrug resistance protein 1 (MRP1) Biochemistry 37 1998 14833 14837
    • (1998) Biochemistry , vol.37 , pp. 14833-14837
    • Dekkers, D.W.1    Comfurius, P.2    Schroit, A.J.3    Bevers, E.M.4    Zwaal, R.F.5
  • 65
    • 0032562990 scopus 로고    scopus 로고
    • Evidence for a role of the multidrug resistance protein (MRP) in the outward translocation of NBD-phospholipids in the erythrocyte membrane
    • D. Kamp, and C.W.M. Haest Evidence for a role of the multidrug resistance protein (MRP) in the outward translocation of NBD-phospholipids in the erythrocyte membrane Biochim. Biophys. Acta 1372 1998 91 101
    • (1998) Biochim. Biophys. Acta , vol.1372 , pp. 91-101
    • Kamp, D.1    Haest, C.W.M.2
  • 66
    • 0028307550 scopus 로고
    • Phosphatidylcholine translocase: A physiological role for the mdr2 gene
    • S. Ruetz, and P. Gros Phosphatidylcholine translocase: a physiological role for the mdr2 gene Cell 77 1994 1 20
    • (1994) Cell , vol.77 , pp. 1-20
    • Ruetz, S.1    Gros, P.2
  • 67
    • 0035849506 scopus 로고    scopus 로고
    • Phospholipid flippase activity of the reconstituted p-glycoprotein multidrug transporter
    • Y. Romsicki, and F.J. Sharom Phospholipid flippase activity of the reconstituted p-glycoprotein multidrug transporter Biochemistry 40 2001 6937 6947
    • (2001) Biochemistry , vol.40 , pp. 6937-6947
    • Romsicki, Y.1    Sharom, F.J.2
  • 68
    • 22544457473 scopus 로고    scopus 로고
    • The reconstituted P-glycoprotein multidrug transporter is a flippase for glucosylceramide and other simple glycosphingolipids
    • P.D. Eckford, and F.J. Sharom The reconstituted P-glycoprotein multidrug transporter is a flippase for glucosylceramide and other simple glycosphingolipids Biochem. J. 389 2005 517 526
    • (2005) Biochem. J. , vol.389 , pp. 517-526
    • Eckford, P.D.1    Sharom, F.J.2
  • 70
    • 0025193531 scopus 로고
    • Photosensitized labeling of a functional multidrug transporter in living drug-resistant tumor cells
    • Y. Raviv, H.B. Pollard, E.P. Bruggemann, I. Pastan, and M.M. Gottesman Photosensitized labeling of a functional multidrug transporter in living drug-resistant tumor cells J. Biol. Chem. 265 1990 3975 3980
    • (1990) J. Biol. Chem. , vol.265 , pp. 3975-3980
    • Raviv, Y.1    Pollard, H.B.2    Bruggemann, E.P.3    Pastan, I.4    Gottesman, M.M.5
  • 71
    • 0037422545 scopus 로고    scopus 로고
    • Role of ABC transporters in secretion of cholesterol from liver into bile
    • D.M. Small Role of ABC transporters in secretion of cholesterol from liver into bile Proc. Natl. Acad. Sci. USA 100 2003 4 6
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4-6
    • Small, D.M.1
  • 72
    • 0035914448 scopus 로고    scopus 로고
    • Endocytosis is enhanced in Tangier fibroblasts. Possible role of ATP-binding cassette protein A1 in endosomal vesicular transport
    • X. Zha, J. Genest Jr., and R. McPherson Endocytosis is enhanced in Tangier fibroblasts. Possible role of ATP-binding cassette protein A1 in endosomal vesicular transport J. Biol. Chem. 276 2001 39476 39483
    • (2001) J. Biol. Chem. , vol.276 , pp. 39476-39483
    • Zha, X.1    Genest Jr., J.2    McPherson, R.3
  • 73
  • 74
    • 0022357345 scopus 로고
    • Thermodynamics and kinetics of phospholipid monomer-vesicle interaction
    • J.W. Nichols Thermodynamics and kinetics of phospholipid monomer-vesicle interaction Biochemistry 24 1985 6390 6398
    • (1985) Biochemistry , vol.24 , pp. 6390-6398
    • Nichols, J.W.1
  • 76
    • 7244248683 scopus 로고    scopus 로고
    • MsbA-dependent translocation of lipids across the inner membrane of Escherichia coli
    • W.T. Doerrler, H.S. Gibbons, and C.R. Raetz MsbA-dependent translocation of lipids across the inner membrane of Escherichia coli J. Biol. Chem. 279 2004 45102 45109
    • (2004) J. Biol. Chem. , vol.279 , pp. 45102-45109
    • Doerrler, W.T.1    Gibbons, H.S.2    Raetz, C.R.3
  • 77
    • 31944431842 scopus 로고    scopus 로고
    • ABC transporter architecture and regulatory roles of accessory domains
    • doi:10.1016/j.febslet.2005.11.079.
    • Biemans-Oldehinkel, E., Doeven, M.K. and Poolman, B. (2005) ABC transporter architecture and regulatory roles of accessory domains. FEBS Lett., this issue, doi:10.1016/j.febslet.2005.11.079.
    • (2005) FEBS Lett. , Issue.THIS ISSUE
    • Biemans-Oldehinkel, E.1    Doeven, M.K.2    Poolman, B.3
  • 78
    • 0035929556 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane regulator regulates uptake of sphingoid base phosphates and lysophosphatidic acid: Modulation of cellular activity of sphingosine 1-phosphate
    • L.C. Boujaoude, C. Bradshaw-Wilder, C. Mao, J. Cohn, B. Ogretmen, Y.A. Hannun, and L.M. Obeid Cystic fibrosis transmembrane regulator regulates uptake of sphingoid base phosphates and lysophosphatidic acid: modulation of cellular activity of sphingosine 1-phosphate J. Biol. Chem. 276 2001 35258 35264
    • (2001) J. Biol. Chem. , vol.276 , pp. 35258-35264
    • Boujaoude, L.C.1    Bradshaw-Wilder, C.2    Mao, C.3    Cohn, J.4    Ogretmen, B.5    Hannun, Y.A.6    Obeid, L.M.7
  • 79
    • 31844431988 scopus 로고    scopus 로고
    • An ABC transporter mediating the membrane detachment of bacterial lipoproteins depending on their sorting signals
    • doi:10.1016/j.febslet.2005.10.038.
    • Narita, S.-i. and Tokuda, H. (2005) An ABC transporter mediating the membrane detachment of bacterial lipoproteins depending on their sorting signals. FEBS Lett., this issue, doi:10.1016/j.febslet.2005.10.038.
    • (2005) FEBS Lett. , Issue.THIS ISSUE
    • Narita, S.-I.1    Tokuda, H.2
  • 80
    • 18344378499 scopus 로고    scopus 로고
    • Lipoprotein particles are required for Hedgehog and Wingless signalling
    • D. Panáková, H. Sprong, E. Marois, C. Thiele, and S. Eaton Lipoprotein particles are required for Hedgehog and Wingless signalling Nature 435 2005 58 65
    • (2005) Nature , vol.435 , pp. 58-65
    • Panáková, D.1    Sprong, H.2    Marois, E.3    Thiele, C.4    Eaton, S.5
  • 81
    • 31844450185 scopus 로고    scopus 로고
    • ABCA7, a molecule with unknown function
    • doi:10.1016/j.febslet.2005.12.029.
    • Abe-Dohmae, S., Ueda, K. and Yokoyama, S. (2005) ABCA7, a molecule with unknown function. FEBS Lett., this issue, doi:10.1016/j.febslet.2005.12.029.
    • (2005) FEBS Lett. , Issue.THIS ISSUE
    • Abe-Dohmae, S.1    Ueda, K.2    Yokoyama, S.3
  • 82
    • 25444442926 scopus 로고    scopus 로고
    • A phylogenetic survey of biliary lipids in vertebrates
    • A. Moschetta A phylogenetic survey of biliary lipids in vertebrates J. Lipid Res. 46 2005 2221 2232
    • (2005) J. Lipid Res. , vol.46 , pp. 2221-2232
    • Moschetta, A.1
  • 83
    • 31844451628 scopus 로고    scopus 로고
    • Reevaluation of the role of the multidrug resistant P-glycoprotein in cellular cholesterol homeostasis
    • in press.
    • Le Goff, W., Settle, M., Greene, D.J., Morton, R.E. and Smith, J.D. (2005) Reevaluation of the role of the multidrug resistant P-glycoprotein in cellular cholesterol homeostasis. J. Lipid Res., in press.
    • (2005) J. Lipid Res.
    • Le Goff, W.1    Settle, M.2    Greene, D.J.3    Morton, R.E.4    Smith, J.D.5
  • 84
    • 0034604707 scopus 로고    scopus 로고
    • MDR3 P-glycoprotein, a phosphatidylcholine translocase, transports several cytotoxic drugs and directly interacts with drugs as judged by interference with nucleotide trapping
    • A.J. Smith MDR3 P-glycoprotein, a phosphatidylcholine translocase, transports several cytotoxic drugs and directly interacts with drugs as judged by interference with nucleotide trapping J. Biol. Chem. 275 2000 23530 23539
    • (2000) J. Biol. Chem. , vol.275 , pp. 23530-23539
    • Smith, A.J.1
  • 85
    • 25144443228 scopus 로고    scopus 로고
    • Cellular lipidomics
    • G. van Meer Cellular lipidomics EMBO J. 24 2005 3159 3165
    • (2005) EMBO J. , vol.24 , pp. 3159-3165
    • Van Meer, G.1
  • 86
    • 22144478635 scopus 로고    scopus 로고
    • The emerging field of lipidomics
    • M.R. Wenk The emerging field of lipidomics Nat. Rev. Drug Discov. 4 2005 594 610
    • (2005) Nat. Rev. Drug Discov. , vol.4 , pp. 594-610
    • Wenk, M.R.1
  • 88
    • 0000853942 scopus 로고
    • Measured work of deformation and repulsion of lecithin bilayers
    • V.A. Parsegian, N. Fuller, and R.P. Rand Measured work of deformation and repulsion of lecithin bilayers Proc. Natl. Acad. Sci. USA 76 1979 2750 2754
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 2750-2754
    • Parsegian, V.A.1    Fuller, N.2    Rand, R.P.3
  • 89
    • 0032996357 scopus 로고    scopus 로고
    • Lipid transfer between vesicles: Effect of high vesicle concentration
    • P.F. Almeida Lipid transfer between vesicles: effect of high vesicle concentration Biophys. J. 76 1999 1922 1928
    • (1999) Biophys. J. , vol.76 , pp. 1922-1928
    • Almeida, P.F.1


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