메뉴 건너뛰기




Volumn 226, Issue 10, 2001, Pages 873-890

Recent advances in membrane microdomains: Rafts, caveolae, and intracellular cholesterol trafficking

Author keywords

Caveolae; Cholesterol; Domain; Fatty acid; Membrane; Rafts; Sterol carrier protein

Indexed keywords

BINDING PROTEIN; CARRIER PROTEIN; CAVEOLIN; CELL PROTEIN; CHOLESTEROL; CHOLESTEROL ESTER; FATTY ACID; HIGH DENSITY LIPOPROTEIN RECEPTOR; LOW DENSITY LIPOPROTEIN RECEPTOR; NIEMANN PICK C1 PROTEIN; STEROIDOGENIC ACUTE REGULATORY PROTEIN; STEROL CARRIER PROTEIN 2; UNCLASSIFIED DRUG;

EID: 18544367674     PISSN: 00379727     EISSN: None     Source Type: Journal    
DOI: 10.1177/153537020122601002     Document Type: Short Survey
Times cited : (123)

References (194)
  • 1
    • 0029840406 scopus 로고    scopus 로고
    • Fibroblast membrane sterol kinetic domains: Modulation by sterol carrier protein 2 and liver fatty acid binding protein
    • Frolov AA, Woodford JK, Murphy EJ, Billheimer JT, Schroeder F. Fibroblast membrane sterol kinetic domains: Modulation by sterol carrier protein 2 and liver fatty acid binding protein. J Lipid Res 37:1862-1874, 1996.
    • (1996) J Lipid Res , vol.37 , pp. 1862-1874
    • Frolov, A.A.1    Woodford, J.K.2    Murphy, E.J.3    Billheimer, J.T.4    Schroeder, F.5
  • 2
    • 0030037450 scopus 로고    scopus 로고
    • Spontaneous and protein-mediated sterol transfer between intracellular membranes
    • Frolov A, Woodford JK, Murphy EJ, Billheimer JT, Schroeder F. Spontaneous and protein-mediated sterol transfer between intracellular membranes. J Biol Chem 271:16075-16083, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 16075-16083
    • Frolov, A.1    Woodford, J.K.2    Murphy, E.J.3    Billheimer, J.T.4    Schroeder, F.5
  • 3
    • 0030809601 scopus 로고    scopus 로고
    • Intracellular cholesterol transport
    • Fielding CJ, Fielding PE. Intracellular cholesterol transport. J Lipid Res 38:1503-1521, 1997.
    • (1997) J Lipid Res , vol.38 , pp. 1503-1521
    • Fielding, C.J.1    Fielding, P.E.2
  • 5
    • 0032512758 scopus 로고    scopus 로고
    • Evidence for a cholesterol transport pathway from lysosomes to endoplasmic reticulum that is independent of the plasma membrane
    • Underwood KW, Jacobs NL, Howley A, Liscum L. Evidence for a cholesterol transport pathway from lysosomes to endoplasmic reticulum that is independent of the plasma membrane. J Biol Chem 273:4266-4274, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 4266-4274
    • Underwood, K.W.1    Jacobs, N.L.2    Howley, A.3    Liscum, L.4
  • 6
    • 0002671647 scopus 로고    scopus 로고
    • Analysis of somatic cell mutants that express defective intracellular cholesterol transport
    • Chang TY, Freeman DA, Eds. Kluwer Academic Publishers, Boston
    • Liscum L. Analysis of somatic cell mutants that express defective intracellular cholesterol transport. In: Chang TY, Freeman DA, Eds. Intracellular Cholesterol Trafficking. Kluwer Academic Publishers, Boston: pp75-92, 1998.
    • (1998) Intracellular Cholesterol Trafficking , pp. 75-92
    • Liscum, L.1
  • 7
    • 0002078231 scopus 로고    scopus 로고
    • Selective uptake of lipoprotein free cholesterol and its intracellular transport-role of caveolin
    • Chang TY, Freeman DA, Eds. Kluwer Academic Publishers, Boston
    • Fielding CJ, Bist A, Fielding PE. Selective uptake of lipoprotein free cholesterol and its intracellular transport-role of caveolin. In: Chang TY, Freeman DA, Eds. Intracellular Cholesterol Trafficking. Kluwer Academic Publishers, Boston: pp273-288, 1998.
    • (1998) Intracellular Cholesterol Trafficking , pp. 273-288
    • Fielding, C.J.1    Bist, A.2    Fielding, P.E.3
  • 8
    • 0033596725 scopus 로고    scopus 로고
    • Intracellular cholesterol transport in synchronized human skin fibroblasts
    • Fielding CJ, Bist A, Fielding PE. Intracellular cholesterol transport in synchronized human skin fibroblasts. Biochemistry 38:2506-2513, 1999.
    • (1999) Biochemistry , vol.38 , pp. 2506-2513
    • Fielding, C.J.1    Bist, A.2    Fielding, P.E.3
  • 9
    • 0000061610 scopus 로고    scopus 로고
    • Scavenger receptors, caveolae, caveolin, and cholesterol trafficking
    • Chang TY, Freeman DA, Eds. Kluwer Academic Publishers, Boston
    • Smart EJ, van der Westhuyzen DR. Scavenger receptors, caveolae, caveolin, and cholesterol trafficking. In Chang TY, Freeman DA, Eds. Intracellular Cholesterol Trafficking. Kluwer Academic Publishers, Boston: pp253-272, 1998.
    • (1998) Intracellular Cholesterol Trafficking , pp. 253-272
    • Smart, E.J.1    Van der Westhuyzen, D.R.2
  • 10
    • 0002995671 scopus 로고    scopus 로고
    • What the Niemann-Pick C gene has taught us about cholesterol transport
    • Chang TY, Freeman DA, Eds. Kluwer Academic Publishers, Boston
    • Neufeld EB. What the Niemann-Pick C gene has taught us about cholesterol transport. In Chang TY, Freeman DA, Eds. Intracellular Cholesterol Trafficking. Kluwer Academic Publishers, Boston: pp93-121, 1998.
    • (1998) Intracellular Cholesterol Trafficking , pp. 93-121
    • Neufeld, E.B.1
  • 11
    • 0000057417 scopus 로고    scopus 로고
    • Direct evidence for sterol carrier protein-2 (SCP-2) participation in ACTH stimulated steroidogenesis in isolated adrenal cells
    • Chang TY, Freeman DA, Eds. Kluwer Academic Publishers, Boston
    • Chanderbhan RF, Kharroubi A, Pastuszyn A, Gallo LL, Scallen T. Direct evidence for sterol carrier protein-2 (SCP-2) participation in ACTH stimulated steroidogenesis in isolated adrenal cells. In Chang TY, Freeman DA, Eds. Intracellular Cholesterol Trafficking. Kluwer Academic Publishers, Boston: pp197-212, 1998.
    • (1998) Intracellular Cholesterol Trafficking , pp. 197-212
    • Chanderbhan, R.F.1    Kharroubi, A.2    Pastuszyn, A.3    Gallo, L.L.4    Scallen, T.5
  • 12
    • 0001934896 scopus 로고    scopus 로고
    • Intracellular cholesterol movement and homeostasis
    • Chang TY. Freeman DA, Eds. Kluwer Academic Publishers. Boston
    • Lange Y. Intracellular cholesterol movement and homeostasis. In Chang TY. Freeman DA, Eds. Intracellular Cholesterol Trafficking. Kluwer Academic Publishers. Boston: pp15-27, 1998.
    • (1998) Intracellular Cholesterol Trafficking , pp. 15-27
    • Lange, Y.1
  • 13
    • 0002115929 scopus 로고    scopus 로고
    • Cholesterol distribution in Golgi, lysosomes, and endoplasmic reticulum
    • Chang TY, Freeman DA, Eds. Kluwer Academic Publishers, Boston
    • Blanchette-Mackie EJ, Pentchev P. Cholesterol distribution in Golgi, lysosomes, and endoplasmic reticulum. In Chang TY, Freeman DA, Eds. Intracellular Cholesterol Trafficking. Kluwer Academic Publishers, Boston: pp53-73, 1998.
    • (1998) Intracellular Cholesterol Trafficking , pp. 53-73
    • Blanchette-Mackie, E.J.1    Pentchev, P.2
  • 14
    • 0010331113 scopus 로고    scopus 로고
    • The movement of plasma membrane cholesterol through the cell
    • Chang TY, Freeman DA, Eds. Kluwer Academic Publishers, Boston
    • Choi Y-S, Freeman DA. The movement of plasma membrane cholesterol through the cell. In Chang TY, Freeman DA, Eds. Intracellular Cholesterol Trafficking. Kluwer Academic Publishers, Boston: pp109-121, 1998.
    • (1998) Intracellular Cholesterol Trafficking , pp. 109-121
    • Choi, Y.-S.1    Freeman, D.A.2
  • 15
    • 0010409111 scopus 로고    scopus 로고
    • Cholesterol trafficking in CACO-2 cells
    • Chang TY, Freeman DA, Eds. Kluwer Academic Publishers, Boston
    • Field FJ. Cholesterol trafficking in CACO-2 cells. In Chang TY, Freeman DA, Eds. Intracellular Cholesterol Trafficking. Kluwer Academic Publishers, Boston: pp123-145, 1998.
    • (1998) Intracellular Cholesterol Trafficking , pp. 123-145
    • Field, F.J.1
  • 16
    • 0010328809 scopus 로고    scopus 로고
    • Efflux and plasma transport of biosynthetic sterols
    • Chang TY, Freeman DA, Eds. Kluwer Academic Publishers, Boston
    • Phillips JE, Johnson WJ. Efflux and plasma transport of biosynthetic sterols. In Chang TY, Freeman DA, Eds. Intracellular Cholesterol Trafficking. Kluwer Academic Publishers, Boston: pp147-168, 1998.
    • (1998) Intracellular Cholesterol Trafficking , pp. 147-168
    • Phillips, J.E.1    Johnson, W.J.2
  • 17
    • 0002108867 scopus 로고    scopus 로고
    • Functional analysis of sterol carrier protein-2 (SCP2) in SCP2 knockout mouse
    • Chang TY, Freeman DA, Eds. Kluwer Academic Publishers, Boston
    • Seedorf U. Functional analysis of sterol carrier protein-2 (SCP2) in SCP2 knockout mouse. In Chang TY, Freeman DA, Eds. Intracellular Cholesterol Trafficking. Kluwer Academic Publishers, Boston: pp233-252, 1998.
    • (1998) Intracellular Cholesterol Trafficking , pp. 233-252
    • Seedorf, U.1
  • 18
    • 0032925484 scopus 로고    scopus 로고
    • Recent advances in brain cholesterol dynamics: Transport, domains, and Alzheimer's disease
    • Wood WG, Schroeder F, Avdulov NA, Chochina SV, Igbavboa U. Recent advances in brain cholesterol dynamics: transport, domains, and Alzheimer's disease. Lipids 34:225-234, 1999.
    • (1999) Lipids , vol.34 , pp. 225-234
    • Wood, W.G.1    Schroeder, F.2    Avdulov, N.A.3    Chochina, S.V.4    Igbavboa, U.5
  • 19
    • 0033922431 scopus 로고    scopus 로고
    • Lipid trafficking and sorting: How cholesterol is filling gaps
    • Hoekstra D, van Jzendoorn SCD. Lipid trafficking and sorting: How cholesterol is filling gaps. Curr Opin Cell Biol 12:496-502, 2000.
    • (2000) Curr Opin Cell Biol , vol.12 , pp. 496-502
    • Hoekstra, D.1    Van Jzendoorn, S.C.D.2
  • 20
    • 0034724682 scopus 로고    scopus 로고
    • High density lipoprotein mediated cholesterol uptake and targeting to lipid droplets in intact L-cell fibroblasts
    • Frolov A, Petrescu A, Atshaves BP, So PTC, Gratton E, Serrero G, Schroeder F. High density lipoprotein mediated cholesterol uptake and targeting to lipid droplets in intact L-cell fibroblasts. J Biol Chem 275:12769-12780, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 12769-12780
    • Frolov, A.1    Petrescu, A.2    Atshaves, B.P.3    So, P.T.C.4    Gratton, E.5    Serrero, G.6    Schroeder, F.7
  • 24
    • 0029034940 scopus 로고
    • Intracellular cholesterol transport and compartmentation
    • Liscum L, Underwood KW. Intracellular cholesterol transport and compartmentation. J Biol Chem 270:15443-15446, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 15443-15446
    • Liscum, L.1    Underwood, K.W.2
  • 26
    • 0031687965 scopus 로고    scopus 로고
    • Cholesterol distribution in living cells: Fluorescence imaging using dehydroergosterol as a fluorescent cholesterol analog
    • Mukherjee S, Zha X, Tabas I. Maxfield FR. Cholesterol distribution in living cells: Fluorescence imaging using dehydroergosterol as a fluorescent cholesterol analog. Biophys J 75:1915-1925, 1998.
    • (1998) Biophys J , vol.75 , pp. 1915-1925
    • Mukherjee, S.1    Zha, X.2    Tabas, I.3    Maxfield, F.R.4
  • 28
    • 0029113734 scopus 로고
    • Cholesterol uptake by the selective pathway of ovarian granulosa cells: Early intracellular events
    • Reaven E, Tsai L, Azhar S. Cholesterol uptake by the selective pathway of ovarian granulosa cells: Early intracellular events. J Lip Res 36:1602-1617, 1995.
    • (1995) J Lip Res , vol.36 , pp. 1602-1617
    • Reaven, E.1    Tsai, L.2    Azhar, S.3
  • 29
    • 0001876095 scopus 로고
    • Transmembrane cholesterol distribution
    • Esfahami M, Swaney J, Eds. Telford Press, Caldwell, NJ
    • Schroeder F, Nemecz G. Transmembrane cholesterol distribution. In: Esfahami M, Swaney J, Eds. Advances in Cholesterol Research. Telford Press, Caldwell, NJ: pp47-87, 1990.
    • (1990) Advances in Cholesterol Research , pp. 47-87
    • Schroeder, F.1    Nemecz, G.2
  • 31
    • 0027892019 scopus 로고
    • Cholesterol and the Golgi apparatus
    • Bretscher MS, Munro S. Cholesterol and the Golgi apparatus. Science 261:1280-1281, 1993.
    • (1993) Science , vol.261 , pp. 1280-1281
    • Bretscher, M.S.1    Munro, S.2
  • 32
    • 0027443234 scopus 로고
    • Caveolae: Where incoming and outgoing messengers meet
    • Anderson RGW. Caveolae: Where incoming and outgoing messengers meet. Proc Natl Acad Sci U S A 90:10909-10913, 1993.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 10909-10913
    • Anderson, R.G.W.1
  • 33
    • 0027639941 scopus 로고
    • Plasmalemmal caveolae and GPI-anchored membrane proteins
    • Anderson RGW. Plasmalemmal caveolae and GPI-anchored membrane proteins. Cell Biol 5:647-652, 1993.
    • (1993) Cell Biol , vol.5 , pp. 647-652
    • Anderson, R.G.W.1
  • 34
    • 0030222108 scopus 로고    scopus 로고
    • Caveolae and caveolins
    • Parton RG. Caveolae and caveolins. Curr Opin Cell Biol 8:542-548, 1996.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 542-548
    • Parton, R.G.1
  • 35
    • 0030600130 scopus 로고    scopus 로고
    • And still they are moving....dynamic properties of caveolae
    • Kurzchalia TV, Parton RG. And still they are moving....dynamic properties of caveolae. FEBS Lett 389:52-54, 1996.
    • (1996) FEBS Lett , vol.389 , pp. 52-54
    • Kurzchalia, T.V.1    Parton, R.G.2
  • 36
    • 0027970448 scopus 로고
    • Detergent insoluble glycolipid microdomains in lympohocytes in the absence of caveolae
    • Fra AMWE, Simons K, Parton RG. Detergent insoluble glycolipid microdomains in lympohocytes in the absence of caveolae. J Biol Chem 269:30745-30748, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 30745-30748
    • Fra, A.M.W.E.1    Simons, K.2    Parton, R.G.3
  • 37
    • 0030222108 scopus 로고    scopus 로고
    • Caveolae and caveolins
    • Parton RG. Caveolae and caveolins. Curr Opin Cell Biol 8:542-548, 1996.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 542-548
    • Parton, R.G.1
  • 38
    • 0030878573 scopus 로고    scopus 로고
    • Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains
    • Harder T, Simons K, Caveolae, DIGs, and the dynamics of sphingolipid-cholesterol microdomains. Curr Opin Cell Biol 9:534-542, 1997.
    • (1997) Curr Opin Cell Biol , vol.9 , pp. 534-542
    • Harder, T.1    Simons, K.2
  • 39
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • Simons K, Ikonen E. Functional rafts in cell membranes. Nature 387:569-572, 1997.
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 40
    • 0030919779 scopus 로고    scopus 로고
    • Cell surface anchored dynamics of GPI-anchored proteins
    • Haag B, Koch-Nolte E, Eds. Kluwer Academic Publishers, Boston
    • Maxfield FR, Mayor S. Cell surface anchored dynamics of GPI-anchored proteins. In: Haag B, Koch-Nolte E, Eds. ADP-Ribosylation in Animal Tissues. Kluwer Academic Publishers, Boston: pp355-364, 1997.
    • (1997) ADP-Ribosylation in Animal Tissues , pp. 355-364
    • Maxfield, F.R.1    Mayor, S.2
  • 41
    • 0031692336 scopus 로고    scopus 로고
    • The caveolar system
    • Anderson R. The caveolar system. Annu Rev Biochem 67:199-225, 1998.
    • (1998) Annu Rev Biochem , vol.67 , pp. 199-225
    • Anderson, R.1
  • 43
    • 0031765341 scopus 로고    scopus 로고
    • Role of plasmalemmal caveolae in signal transduction
    • Shaul PW, Anderson RGW. Role of plasmalemmal caveolae in signal transduction. Am J Physiol 19:L843-L851, 1998.
    • (1998) Am J Physiol , vol.19
    • Shaul, P.W.1    Anderson, R.G.W.2
  • 44
    • 0032552054 scopus 로고    scopus 로고
    • GPI-anchored proteins are organized in submicron domains at the cell surface
    • Varma R, Mayor S. GPI-anchored proteins are organized in submicron domains at the cell surface. Nature 394:798-801, 1998.
    • (1998) Nature , vol.394 , pp. 798-801
    • Varma, R.1    Mayor, S.2
  • 45
    • 0032552072 scopus 로고    scopus 로고
    • Microdomains of GPI-anchored proteins in living cells revealed by cross-linking
    • Friedrichson T, Kurzchalia TV. Microdomains of GPI-anchored proteins in living cells revealed by cross-linking. Nature 394:802-805, 1998.
    • (1998) Nature , vol.394 , pp. 802-805
    • Friedrichson, T.1    Kurzchalia, T.V.2
  • 46
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown DA, London E. Functions of lipid rafts in biological membranes. Annu Rev Cell Dev Biol 14:111-136, 1998.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 47
    • 0032489443 scopus 로고    scopus 로고
    • Caveolins, a family of scaffolding proteins for organizing "preassembled signaling complexes" at the plasma membrane
    • Okamoto T, Schlegel A, Scherer PE, Lisanti MP. Caveolins, a family of scaffolding proteins for organizing "preassembled signaling complexes" at the plasma membrane. J Biol Chem 273:5419-5422, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 5419-5422
    • Okamoto, T.1    Schlegel, A.2    Scherer, P.E.3    Lisanti, M.P.4
  • 48
    • 0033055564 scopus 로고    scopus 로고
    • Detergent-insoluble glycosphingolipid/cholesterol rich membrane domains, lipid rafts, and caveolae
    • Hooper NM. Detergent-insoluble glycosphingolipid/cholesterol rich membrane domains, lipid rafts, and caveolae. Mol Membr Biol 16:145-156, 1999.
    • (1999) Mol Membr Biol , vol.16 , pp. 145-156
    • Hooper, N.M.1
  • 50
    • 0033431772 scopus 로고    scopus 로고
    • A role for lipid rafts in B cell antigen receptor signaling and antigen targeting
    • Cheng PC, Dykstra ML, Mitchell RN, Pierce SK. A role for lipid rafts in B cell antigen receptor signaling and antigen targeting. J Exp Med 190:1549-1560, 1999.
    • (1999) J Exp Med , vol.190 , pp. 1549-1560
    • Cheng, P.C.1    Dykstra, M.L.2    Mitchell, R.N.3    Pierce, S.K.4
  • 52
    • 0010408356 scopus 로고    scopus 로고
    • Focus on cellular biochemistry: Pathogens, toxins, and lipid rafts
    • Fivaz M, Abramin L, van der Groot FG. Focus on cellular biochemistry: Pathogens, toxins, and lipid rafts. Protoplasma 212:1-2, 2000.
    • (2000) Protoplasma , vol.212 , pp. 1-2
    • Fivaz, M.1    Abramin, L.2    Van der Groot, F.G.3
  • 53
    • 0034625373 scopus 로고    scopus 로고
    • Structure and function of sphingolipid- and cholesterol-rich membrane rafts
    • Brown DA, London E. Structure and function of sphingolipid- and cholesterol-rich membrane rafts. J Biol Chem 275:17221-17224, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 17221-17224
    • Brown, D.A.1    London, E.2
  • 54
    • 0034142110 scopus 로고    scopus 로고
    • Sphingolipid signalling domains: Floating on rafts or buried in caves?
    • Dobrowsky RT. Sphingolipid signalling domains: Floating on rafts or buried in caves? Cell Signal 12:81-90, 2000.
    • (2000) Cell Signal , vol.12 , pp. 81-90
    • Dobrowsky, R.T.1
  • 55
  • 57
    • 0015386072 scopus 로고
    • Fluorometric investigations of the interaction of polyene antibiotics with sterols
    • Schroeder F, Holland JF, Bieber LL. Fluorometric investigations of the interaction of polyene antibiotics with sterols. Biochemistry 11:3105-3111, 1972.
    • (1972) Biochemistry , vol.11 , pp. 3105-3111
    • Schroeder, F.1    Holland, J.F.2    Bieber, L.L.3
  • 58
    • 0015887557 scopus 로고
    • Reversible interconversions of sterol-binding and sterol-nonbinding forms of filipin as determined by fluorimetric and light scattering properties
    • Schroeder F, Holland JF, Bieber LL. Reversible interconversions of sterol-binding and sterol-nonbinding forms of filipin as determined by fluorimetric and light scattering properties. Biochemistry 12:4785-4789, 1973.
    • (1973) Biochemistry , vol.12 , pp. 4785-4789
    • Schroeder, F.1    Holland, J.F.2    Bieber, L.L.3
  • 59
    • 0021101145 scopus 로고
    • Detection of microdomains in biomembranes: An appraisal of recent developments in freeze fracture cytochemistry
    • Severs NJ, Robenek H. Detection of microdomains in biomembranes: An appraisal of recent developments in freeze fracture cytochemistry. Biochim Biophys Acta 737:373-408, 1983.
    • (1983) Biochim Biophys Acta , vol.737 , pp. 373-408
    • Severs, N.J.1    Robenek, H.2
  • 60
    • 0021459790 scopus 로고
    • The use and abuse of filipin to localize cholesterol in membranes
    • Miller RG. The use and abuse of filipin to localize cholesterol in membranes. Cell Biol Int Rep 8:519-535, 1984.
    • (1984) Cell Biol Int Rep , vol.8 , pp. 519-535
    • Miller, R.G.1
  • 61
    • 0021272476 scopus 로고
    • Detection of membrane cholesterol by filipin in isolated rat liver coated vesicles is dependent upon removal of the clothium coat
    • Steer CJ, Bisher M, Blumenthal R, Steven AC. Detection of membrane cholesterol by filipin in isolated rat liver coated vesicles is dependent upon removal of the clothium coat. J Cell Biol 99:315-319, 1984.
    • (1984) J Cell Biol , vol.99 , pp. 315-319
    • Steer, C.J.1    Bisher, M.2    Blumenthal, R.3    Steven, A.C.4
  • 62
    • 0006496113 scopus 로고
    • Clathrin: A unique protein associated with intracellular transfer of membrane by coated vesicles
    • Pearse BMF. Clathrin: A unique protein associated with intracellular transfer of membrane by coated vesicles. Proc Natl Acad Sci U S A 73:1255-1259, 1976.
    • (1976) Proc Natl Acad Sci U S A , vol.73 , pp. 1255-1259
    • Pearse, B.M.F.1
  • 63
    • 0034685807 scopus 로고    scopus 로고
    • Characterization of rapid membrane internalization and recycling
    • Hao M, Maxfield FR. Characterization of rapid membrane internalization and recycling. J Biol Chem 275:15279-15286, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 15279-15286
    • Hao, M.1    Maxfield, F.R.2
  • 64
    • 0030879972 scopus 로고    scopus 로고
    • A role for retrosomes in intracellular cholesterol transport from endosomes to the plasma membrane
    • Homick CA, Hui DY, DeLamatre JG. A role for retrosomes in intracellular cholesterol transport from endosomes to the plasma membrane. Am J Physiol 273:C1075-C1081, 1997.
    • (1997) Am J Physiol , vol.273
    • Homick, C.A.1    Hui, D.Y.2    DeLamatre, J.G.3
  • 65
    • 0022549920 scopus 로고
    • A receptor-mediated pathway for cholesterol homeostasis
    • Brown MS, Goldstein JL. A receptor-mediated pathway for cholesterol homeostasis. Science 232:34-47, 1986.
    • (1986) Science , vol.232 , pp. 34-47
    • Brown, M.S.1    Goldstein, J.L.2
  • 66
    • 0025189987 scopus 로고
    • Rapid intracellular transport of LDL-derived cholesterol to the plasma membrane in cultured fibroblasts
    • Brasaemle DL, Attie AD. Rapid intracellular transport of LDL-derived cholesterol to the plasma membrane in cultured fibroblasts. J Lipid Res 31:103-112, 1990.
    • (1990) J Lipid Res , vol.31 , pp. 103-112
    • Brasaemle, D.L.1    Attie, A.D.2
  • 67
    • 0033597141 scopus 로고    scopus 로고
    • Association of sterol and glycosylphosphatidylinositol-linked proteins with Drosophila raft lipid microdomains
    • Rietveld A, Neutz S, Simons K, Eaton S. Association of sterol and glycosylphosphatidylinositol-linked proteins with Drosophila raft lipid microdomains. J Biol Chem 274:12049-12054, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 12049-12054
    • Rietveld, A.1    Neutz, S.2    Simons, K.3    Eaton, S.4
  • 69
    • 0031795591 scopus 로고    scopus 로고
    • Identification of Reggie-1 and Reggie-2 as plasma membrane-associated proteins which cocluster with activated GPI-anchored cell adhesion molecules in noncaveolar micropatches in neurons
    • Lang DM, Lommel S, Jung M, Ankerhold R, Petrausch B, Laessing U, Wiechers MF, Plattner H, Stuermer CAO. Identification of Reggie-1 and Reggie-2 as plasma membrane-associated proteins which cocluster with activated GPI-anchored cell adhesion molecules in noncaveolar micropatches in neurons. J Neurobiol 37:502-523, 1998.
    • (1998) J Neurobiol , vol.37 , pp. 502-523
    • Lang, D.M.1    Lommel, S.2    Jung, M.3    Ankerhold, R.4    Petrausch, B.5    Laessing, U.6    Wiechers, M.F.7    Plattner, H.8    Stuermer, C.A.O.9
  • 70
    • 0032509356 scopus 로고    scopus 로고
    • Separation of "glycosphingolipid signaling domain" from caveolin-containing membrane fraction in mouse melanoma B16 cells and its role in cell adhesion coupled with signaling
    • Iwabuchi K, Handa K, Hakomori S. Separation of "glycosphingolipid signaling domain" from caveolin-containing membrane fraction in mouse melanoma B16 cells and its role in cell adhesion coupled with signaling. J Biol Chem 273:33766-33773, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 33766-33773
    • Iwabuchi, K.1    Handa, K.2    Hakomori, S.3
  • 71
    • 0031740079 scopus 로고    scopus 로고
    • The differential miscibility of lipids as the basis for the formation of functional membrane rafts
    • Rietveld A, Simons K. The differential miscibility of lipids as the basis for the formation of functional membrane rafts. Biochim Biophys Acta 1376:467-479, 1998.
    • (1998) Biochim Biophys Acta , vol.1376 , pp. 467-479
    • Rietveld, A.1    Simons, K.2
  • 72
    • 0032489443 scopus 로고    scopus 로고
    • Caveolins, a family of scaffolding proteins for organizing preassembled signaling complexes at the plasma membrane
    • Okamoto T, Schlegel A, Scherer PE, Lisanti MP. Caveolins, a family of scaffolding proteins for organizing preassembled signaling complexes at the plasma membrane. J Biol Chem 273:5419-5422, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 5419-5422
    • Okamoto, T.1    Schlegel, A.2    Scherer, P.E.3    Lisanti, M.P.4
  • 74
    • 0032553417 scopus 로고    scopus 로고
    • Scavenger receptor, class B, type 1-dependent stimulation of cholesterol esterification by high density lipoproteins, and nonlipoprotein cholesterol
    • Stangl H, Cao G, Wyne KL, Hobbs HH. Scavenger receptor, class B, type 1-dependent stimulation of cholesterol esterification by high density lipoproteins, and nonlipoprotein cholesterol. J Biol Chem 273:31008, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 31008
    • Stangl, H.1    Cao, G.2    Wyne, K.L.3    Hobbs, H.H.4
  • 75
    • 0030997431 scopus 로고    scopus 로고
    • Murine SR-BI a high density lipoprotein receptor that mediates selective lipid uptake, is N-glycosylated and fatty acylated and colocalizes with plasma membrane caveolae
    • Babitt J, Trigatti B, Rigotti A, Smart EJ, Anderson RGW, Xu S, Krieger M. Murine SR-BI, a high density lipoprotein receptor that mediates selective lipid uptake, is N-glycosylated and fatty acylated and colocalizes with plasma membrane caveolae. J Biol Chem 272:13242-13249, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 13242-13249
    • Babitt, J.1    Trigatti, B.2    Rigotti, A.3    Smart, E.J.4    Anderson, R.G.W.5    Xu, S.6    Krieger, M.7
  • 77
    • 0029799891 scopus 로고    scopus 로고
    • A role for caveolin in transport of cholesterol from endoplasmic reticulum to plasma membrane
    • Smart EJ, Ying Y, Donzell WC, Anderson RGW. A role for caveolin in transport of cholesterol from endoplasmic reticulum to plasma membrane. J Biol Chem 271:29427-29435, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 29427-29435
    • Smart, E.J.1    Ying, Y.2    Donzell, W.C.3    Anderson, R.G.W.4
  • 79
    • 0032513038 scopus 로고    scopus 로고
    • Characterization of a cytosolic heat-shock protein-caveolin chaperone complex
    • Uittenbogaard A, Ying YS, Smart EJ. Characterization of a cytosolic heat-shock protein-caveolin chaperone complex. J Biol Chem 273:6525-6532, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 6525-6532
    • Uittenbogaard, A.1    Ying, Y.S.2    Smart, E.J.3
  • 80
    • 0030046797 scopus 로고    scopus 로고
    • Identification of scavenger receptor SR-BI as a high-density lipoprotein receptor
    • Acton S, Rigotti A, Landschulz KT, Xu S, Hobbs HH, Krieger M. Identification of scavenger receptor SR-BI as a high-density lipoprotein receptor. Science 271:518-520, 1996.
    • (1996) Science , vol.271 , pp. 518-520
    • Acton, S.1    Rigotti, A.2    Landschulz, K.T.3    Xu, S.4    Hobbs, H.H.5    Krieger, M.6
  • 82
    • 0030057435 scopus 로고    scopus 로고
    • Intracellular events in the "selective" transport of lipoprotein-derived cholesteryl esters
    • Reaven E, Tsai L, Azhar S. Intracellular events in the "selective" transport of lipoprotein-derived cholesteryl esters. J Biol Chem 271:16208-16217, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 16208-16217
    • Reaven, E.1    Tsai, L.2    Azhar, S.3
  • 83
    • 0027139362 scopus 로고
    • SREBP-2, a second basic-helix-loop-helix-leucine zipper protein that stimulates transcription by binding to a sterol regulatory element
    • Hua X, Yokoyama C, Wu J, Briggs MR, Brown MS, Goldstein JL, Wang X. SREBP-2, a second basic-helix-loop-helix-leucine zipper protein that stimulates transcription by binding to a sterol regulatory element. Proc Natl Acad Sci U S A 90:11603-11607, 1993.
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 11603-11607
    • Hua, X.1    Yokoyama, C.2    Wu, J.3    Briggs, M.R.4    Brown, M.S.5    Goldstein, J.L.6    Wang, X.7
  • 84
    • 0029797604 scopus 로고    scopus 로고
    • Overproduction of cholesterol and fatty acids causes massive liver enlargement in transgenic mice expressing truncated SREBP-1a
    • Shimano H, Horton JD, Hammer RE, Shimomura I, Brown MS, Goldstein JL. Overproduction of cholesterol and fatty acids causes massive liver enlargement in transgenic mice expressing truncated SREBP-1a. J Clin Invest 98:1575-1584, 1996.
    • (1996) J Clin Invest , vol.98 , pp. 1575-1584
    • Shimano, H.1    Horton, J.D.2    Hammer, R.E.3    Shimomura, I.4    Brown, M.S.5    Goldstein, J.L.6
  • 85
    • 0032555479 scopus 로고    scopus 로고
    • Transcriptional activation of the stearoyl-CoA desaturase 2 gene by sterol regulatory element-binding protein/adipocyte determination and differentiation factor 1
    • Tabor DE, Kim JB, Spiegelman BM, Edwards PA. Transcriptional activation of the stearoyl-CoA desaturase 2 gene by sterol regulatory element-binding protein/adipocyte determination and differentiation factor 1. J Biol Chem 273:22052-22058, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 22052-22058
    • Tabor, D.E.1    Kim, J.B.2    Spiegelman, B.M.3    Edwards, P.A.4
  • 88
    • 0032475841 scopus 로고    scopus 로고
    • Polyunsaturated fatty acids decrease expression of promoters with sterol regulatory elements by decreasing levels of mature sterol regulatory element-binding protein
    • Worgall TS, Sturley SL, Seo T, Osborne TF, Deckelbaum RJ. Polyunsaturated fatty acids decrease expression of promoters with sterol regulatory elements by decreasing levels of mature sterol regulatory element-binding protein. J Biol Chem 273:25537-25540, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 25537-25540
    • Worgall, T.S.1    Sturley, S.L.2    Seo, T.3    Osborne, T.F.4    Deckelbaum, R.J.5
  • 89
    • 0032475889 scopus 로고    scopus 로고
    • Differential stimulation of cholesterol and unsaturated fatty acid biosynthesis in the cells expressing individual nuclear sterol reglatory element-binding protein
    • Pai JT, Guryev O, Brown MS, Goldstein JL. Differential stimulation of cholesterol and unsaturated fatty acid biosynthesis in the cells expressing individual nuclear sterol reglatory element-binding protein. J Biol Chem 273(40):26138-26148, 1998.
    • (1998) J Biol Chem , vol.273 , Issue.40 , pp. 26138-26148
    • Pai, J.T.1    Guryev, O.2    Brown, M.S.3    Goldstein, J.L.4
  • 90
    • 0026459464 scopus 로고
    • Fatty acids regulate hepatic low density lipoprotein receptor activity through redistribution of intracellular cholesterol pools
    • Daumerie CM, Woollett LA, Dietschy JM. Fatty acids regulate hepatic low density lipoprotein receptor activity through redistribution of intracellular cholesterol pools. Proc Natl Acad Sci U S A 89:10797-10801, 1992.
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 10797-10801
    • Daumerie, C.M.1    Woollett, L.A.2    Dietschy, J.M.3
  • 91
    • 0023856232 scopus 로고
    • Polyunsaturated fatty acids alter sterol transbilayer domains in LM fibroblast plasma membrane
    • Sweet WD, Schroeder F. Polyunsaturated fatty acids alter sterol transbilayer domains in LM fibroblast plasma membrane. FEBS Lett 229:188-192, 1988.
    • (1988) FEBS Lett , vol.229 , pp. 188-192
    • Sweet, W.D.1    Schroeder, F.2
  • 92
    • 0029853096 scopus 로고    scopus 로고
    • Biochemical isolation of a membrane microdomain from resting platelets highly enriched in the plasma membrane glycoprotein CD36
    • Dorahy DJ, Burns CF, Meldrum CJ, Linz LF. Biochemical isolation of a membrane microdomain from resting platelets highly enriched in the plasma membrane glycoprotein CD36. Biochem J 319:67-72, 2001.
    • (2001) Biochem J , vol.319 , pp. 67-72
    • Dorahy, D.J.1    Burns, C.F.2    Meldrum, C.J.3    Linz, L.F.4
  • 93
    • 0025721161 scopus 로고
    • Photoaffinity labeling and fatty acid permeation in 3T3-L1 adipocytes
    • Trigatti BL, Mangroo D, Gerber GE. Photoaffinity labeling and fatty acid permeation in 3T3-L1 adipocytes. J Biol Chem 266:22621-22625, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 22621-22625
    • Trigatti, B.L.1    Mangroo, D.2    Gerber, G.E.3
  • 94
    • 0027323805 scopus 로고
    • Identification of high affinity membrane-bound fatty acid-binding proteins using a photoreactive fatty acid
    • Gerber GE, Mangroo D, Trigatti BL. Identification of high affinity membrane-bound fatty acid-binding proteins using a photoreactive fatty acid. Mol Cell Biochem 123:39-44, 1993.
    • (1993) Mol Cell Biochem , vol.123 , pp. 39-44
    • Gerber, G.E.1    Mangroo, D.2    Trigatti, B.L.3
  • 95
    • 0029295334 scopus 로고
    • Membrane permeation and in tracellular trafficking of long chain fatty acids: Insights from Escherichia coli and 3T3-L1 adipocytes
    • Mangroo D, Trigatti B, Gerber GE. Membrane permeation and in tracellular trafficking of long chain fatty acids: insights from Escherichia coli and 3T3-L1 adipocytes. Biochem Cell Biol 73:223-234, 1995.
    • (1995) Biochem Cell Biol , vol.73 , pp. 223-234
    • Mangroo, D.1    Trigatti, B.2    Gerber, G.E.3
  • 96
    • 0025802818 scopus 로고
    • Labeling of adipocyte membranes by sulfo-N-succinimidyl derivatives of long-chain fatty acids: Inhibition of fatty acid transport
    • Harmon CM, Luce P, Beth AH, Abumrad NA. Labeling of adipocyte membranes by sulfo-N-succinimidyl derivatives of long-chain fatty acids: inhibition of fatty acid transport. J Membr Biol 121:261-268, 1991.
    • (1991) J Membr Biol , vol.121 , pp. 261-268
    • Harmon, C.M.1    Luce, P.2    Beth, A.H.3    Abumrad, N.A.4
  • 98
    • 0034693232 scopus 로고    scopus 로고
    • Defective uptake and utilization of long chain fatty acids in muscle and adipose tissues of CD36 knockout mice
    • Coburn CT, Knapp FFJr, Febbraio M, Beets AL, Silverstein RL, Abumrad NA. Defective uptake and utilization of long chain fatty acids in muscle and adipose tissues of CD36 knockout mice. J Biol Chem 275:32523-32529, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 32523-32529
    • Coburn, C.T.1    Knapp F.F., Jr.2    Febbraio, M.3    Beets, A.L.4    Silverstein, R.L.5    Abumrad, N.A.6
  • 99
    • 0016291431 scopus 로고
    • Chemical characterization of isolated epidermal desmosomes
    • Skerrow CJ, Matoltsy AG. Chemical characterization of isolated epidermal desmosomes. J Cell Biol 63:524-530, 1974.
    • (1974) J Cell Biol , vol.63 , pp. 524-530
    • Skerrow, C.J.1    Matoltsy, A.G.2
  • 101
    • 0031899062 scopus 로고    scopus 로고
    • Physical effects of cholesterol on arterial smooth muscle membranes: Evidence of immiscible cholesterol domains and alterations in bilayer width during atherogenesis
    • Tulenko TN, Chen M, Mason PE, Mason RP. Physical effects of cholesterol on arterial smooth muscle membranes: evidence of immiscible cholesterol domains and alterations in bilayer width during atherogenesis. J Lipid Res 39:947-956, 1998.
    • (1998) J Lipid Res , vol.39 , pp. 947-956
    • Tulenko, T.N.1    Chen, M.2    Mason, P.E.3    Mason, R.P.4
  • 102
    • 0031908941 scopus 로고    scopus 로고
    • Identification of different lipid phases and calcium phosphate deposits in human carotid artery plaques by MAS NMR spectroscopy
    • Guo W, Morrisett JD, Lawrie GM, DeBakey ME, Hamilton JA. Identification of different lipid phases and calcium phosphate deposits in human carotid artery plaques by MAS NMR spectroscopy. Mag Resonance Med 39:184-189, 1998.
    • (1998) Mag Resonance Med , vol.39 , pp. 184-189
    • Guo, W.1    Morrisett, J.D.2    Lawrie, G.M.3    DeBakey, M.E.4    Hamilton, J.A.5
  • 103
    • 0034048209 scopus 로고    scopus 로고
    • Quantification in situ of crystalline cholesterol and calcium phosphate hydroxyapatite in human atherosclerotic plaques by solid-state magic angle spinning NMR
    • Guo W, Morrisett JD, DeBakey ME, Lawrie GM, Hamilton JA. Quantification in situ of crystalline cholesterol and calcium phosphate hydroxyapatite in human atherosclerotic plaques by solid-state magic angle spinning NMR. Arteriosclerosis Thromb Vasc Biol 20:1630-1636, 2000.
    • (2000) Arteriosclerosis Thromb Vasc Biol , vol.20 , pp. 1630-1636
    • Guo, W.1    Morrisett, J.D.2    DeBakey, M.E.3    Lawrie, G.M.4    Hamilton, J.A.5
  • 104
    • 0010378268 scopus 로고
    • The role of membrane lipid and structure asymmetry on transport systems
    • Jorgensen PL, Verna R, Eds. Lippincott-Raven Publishers, New York
    • Schroeder F, Sweet WD. The role of membrane lipid and structure asymmetry on transport systems. In: Jorgensen PL, Verna R, Eds. Advances in Biotechnology of Membrane Ion Transport. Lippincott-Raven Publishers, New York: pp183-195, 1988.
    • (1988) Advances in Biotechnology of Membrane Ion Transport , pp. 183-195
    • Schroeder, F.1    Sweet, W.D.2
  • 106
    • 0021746481 scopus 로고
    • Role of membrane lipid asymmetry in aging
    • Schroeder F. Role of membrane lipid asymmetry in aging. Neurobiol Aging 5:323-333, 1984.
    • (1984) Neurobiol Aging , vol.5 , pp. 323-333
    • Schroeder, F.1
  • 107
    • 0002527787 scopus 로고
    • Cholesterol and the cell membrane
    • Yeagle PL, Ed. Biology of Cholesterol. Franklin Book Co., Inc., Boca Raton, FL
    • Yeagle PL. Cholesterol and the cell membrane. In: Yeagle PL, Ed. Biology of Cholesterol. Franklin Book Co., Inc., Boca Raton, FL: pp121-145, 1988.
    • (1988) Biology of Cholesterol , pp. 121-145
    • Yeagle, P.L.1
  • 108
    • 0026774957 scopus 로고
    • Na pump and plasma membrane structure in L-cell fibroblasts expressing rat liver fatty acid binding protein
    • Incerpi S, Jefferson JR, Wood WG, Ball WJ, Schroeder F. Na pump and plasma membrane structure in L-cell fibroblasts expressing rat liver fatty acid binding protein. Arch Biochem Biophys 298:35-42, 1992.
    • (1992) Arch Biochem Biophys , vol.298 , pp. 35-42
    • Incerpi, S.1    Jefferson, J.R.2    Wood, W.G.3    Ball, W.J.4    Schroeder, F.5
  • 110
    • 0025334722 scopus 로고
    • Altered membrane structure in transfected mouse L-cell fibroblasts expressing rat liver fatty acid-binding protein
    • Jefferson JR, Powell DM, Rymaszewski Z, Kukowska-Latallo J, Schroeder F. Altered membrane structure in transfected mouse L-cell fibroblasts expressing rat liver fatty acid-binding protein. J Biol Chem 265:11062-11068, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 11062-11068
    • Jefferson, J.R.1    Powell, D.M.2    Rymaszewski, Z.3    Kukowska-Latallo, J.4    Schroeder, F.5
  • 111
    • 0025945569 scopus 로고
    • Intracellular sterol distribution in transfected mouse L-cell fibroblasts expressing rat liver fatty acid binding protein
    • Jefferson JR, Slotte JP, Nemecz G, Pastuszyn A, Scallen TJ, Schroeder F. Intracellular sterol distribution in transfected mouse L-cell fibroblasts expressing rat liver fatty acid binding protein. J Biol Chem 266:5486-5496, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 5486-5496
    • Jefferson, J.R.1    Slotte, J.P.2    Nemecz, G.3    Pastuszyn, A.4    Scallen, T.J.5    Schroeder, F.6
  • 113
    • 0025283040 scopus 로고
    • Pharmacological inhibition of the intracellular transport of low-density lipoprotein-derived cholesterol in Chinese hamster ovary cells
    • Liscum L. Pharmacological inhibition of the intracellular transport of low-density lipoprotein-derived cholesterol in Chinese hamster ovary cells. Biochim Biophys Acta 1045:40-48, 1990.
    • (1990) Biochim Biophys Acta , vol.1045 , pp. 40-48
    • Liscum, L.1
  • 114
    • 0030338965 scopus 로고    scopus 로고
    • Metabolite efflux and influx across the lysosome membrane
    • Lloyd JB, Mason RW, Eds. Kluwer Academic Publishers, New York
    • Boyd JB. Metabolite efflux and influx across the lysosome membrane. In: Lloyd JB, Mason RW, Eds. Biology of the Lysosome. Kluwer Academic Publishers, New York: pp361-386, 1996.
    • (1996) Biology of the Lysosome , pp. 361-386
    • Boyd, J.B.1
  • 118
    • 0030666672 scopus 로고    scopus 로고
    • Altered expression of caveolin-1 and increased cholesterol in detergent insoluble membrane fractions from liver in mice with Niemann-Pick disease type C
    • Garver WS, Erickson RP, Wilson JM, Colton TL, Hossain GS, Kozloski MA, Heidenreich RA. Altered expression of caveolin-1 and increased cholesterol in detergent insoluble membrane fractions from liver in mice with Niemann-Pick disease type C. Biochim Biophys Acta 1361:272-280, 1997.
    • (1997) Biochim Biophys Acta , vol.1361 , pp. 272-280
    • Garver, W.S.1    Erickson, R.P.2    Wilson, J.M.3    Colton, T.L.4    Hossain, G.S.5    Kozloski, M.A.6    Heidenreich, R.A.7
  • 120
    • 0026659920 scopus 로고
    • Deficiencies in sex-regulated expres sion and levels of two hepatic sterol carrier proteins in a murine model of Niemann-Pick type C disease
    • Roff CF, Pastuszyn A, Strauss JFI, Billheimer JT, Vanier MT, Brady RO, Scallen TJ, Pentchev PG. Deficiencies in sex-regulated expres sion and levels of two hepatic sterol carrier proteins in a murine model of Niemann-Pick type C disease. J Biol Chem 267:15902-15908, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 15902-15908
    • Roff, C.F.1    Pastuszyn, A.2    Strauss, J.F.I.3    Billheimer, J.T.4    Vanier, M.T.5    Brady, R.O.6    Scallen, T.J.7    Pentchev, P.G.8
  • 121
    • 0032533544 scopus 로고    scopus 로고
    • Sterol carrier protein-2 participates in hypersecretion of biliary cholesterol during cholesterol gallstone formation in genetically gallstone susceptible mice
    • Fuchs M, Lammert F, Wang DQH, Paigen B, Carey MC, Cohen DE. Sterol carrier protein-2 participates in hypersecretion of biliary cholesterol during cholesterol gallstone formation in genetically gallstone susceptible mice. Biochem J 336:33-37, 1998.
    • (1998) Biochem J , vol.336 , pp. 33-37
    • Fuchs, M.1    Lammert, F.2    Wang, D.Q.H.3    Paigen, B.4    Carey, M.C.5    Cohen, D.E.6
  • 122
    • 33750157660 scopus 로고    scopus 로고
    • Lith genes induce overexpression of sterol carrier protein 2 during cholesterol gallstone formation
    • Fuchs M, Lammert F, Wang DQH, Paigen B, Carey MC, Cohen DE. Lith genes induce overexpression of sterol carrier protein 2 during cholesterol gallstone formation. FASEB J 11:A1060, 1997.
    • (1997) FASEB J , vol.11
    • Fuchs, M.1    Lammert, F.2    Wang, D.Q.H.3    Paigen, B.4    Carey, M.C.5    Cohen, D.E.6
  • 123
    • 0031710550 scopus 로고    scopus 로고
    • Submicellar bile salts stimulate phosphatidylcholine transfer activity of sterol carrier protein 2
    • Leonard AN, Cohen DE. Submicellar bile salts stimulate phosphatidylcholine transfer activity of sterol carrier protein 2. J Lipid Res 39:1981-1988, 1998.
    • (1998) J Lipid Res , vol.39 , pp. 1981-1988
    • Leonard, A.N.1    Cohen, D.E.2
  • 125
    • 0021867669 scopus 로고
    • Fluorescence of delta 5,7,9(11),22-ergostatetraen-3β-ol in micelles, sterol carrier protein complexes, and plasma membranes
    • Fischer RT, Cowlen MS, Dempsey ME, Schroeder F. Fluorescence of delta 5,7,9(11),22-ergostatetraen-3β-ol in micelles, sterol carrier protein complexes, and plasma membranes. Biochemistry 24:3322-3331, 1985.
    • (1985) Biochemistry , vol.24 , pp. 3322-3331
    • Fischer, R.T.1    Cowlen, M.S.2    Dempsey, M.E.3    Schroeder, F.4
  • 126
    • 0021923008 scopus 로고
    • Sterol and squalene carrier protein interactions with fluorescent delta 5,7,9(11)-cholestatrien-3βol
    • Schroeder F, Dempsey ME, Fischer RT. Sterol and squalene carrier protein interactions with fluorescent delta 5,7,9(11)-cholestatrien-3βol. J Biol Chem 260:2904-2911, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 2904-2911
    • Schroeder, F.1    Dempsey, M.E.2    Fischer, R.T.3
  • 127
    • 0000298395 scopus 로고    scopus 로고
    • Relevance of the sterol carrier protein-2 gene for bile acid synthesis and gallstone formation in genetically susceptible mice
    • Muench C, Hafer A, Katzberg N, Scheibner J, Stange EF, Seedorf U, Fuchs M. Relevance of the sterol carrier protein-2 gene for bile acid synthesis and gallstone formation in genetically susceptible mice. Gastroenterology 118:1167, 2000.
    • (2000) Gastroenterology , vol.118 , pp. 1167
    • Muench, C.1    Hafer, A.2    Katzberg, N.3    Scheibner, J.4    Stange, E.F.5    Seedorf, U.6    Fuchs, M.7
  • 128
    • 0001606162 scopus 로고    scopus 로고
    • Studies with sterol carrier protein-2 (SCP-2) gene knockout mice identify liver fatty acid binding protein (FABP1) as intracellular cholesterol transporter contributing to biliary cholesterol hypersecretion and gallstone formation
    • Hafer A, Katzberg N, Muench C, Scheibner J, Stange EF, Seedorf U, Fuchs M. Studies with sterol carrier protein-2 (SCP-2) gene knockout mice identify liver fatty acid binding protein (FABP1) as intracellular cholesterol transporter contributing to biliary cholesterol hypersecretion and gallstone formation. Gastroenterology 118:135, 2000.
    • (2000) Gastroenterology , vol.118 , pp. 135
    • Hafer, A.1    Katzberg, N.2    Muench, C.3    Scheibner, J.4    Stange, E.F.5    Seedorf, U.6    Fuchs, M.7
  • 129
    • 0025041653 scopus 로고
    • The occurrence of soluble and membrane-bound non-specific lipid transfer protein (sterol carrier protein 2) in rat tissues
    • van Heusden GPH, Bos K, Wirtz KWA. The occurrence of soluble and membrane-bound non-specific lipid transfer protein (sterol carrier protein 2) in rat tissues. Biochim Biophys Acta 1046:315-321, 1990.
    • (1990) Biochim Biophys Acta , vol.1046 , pp. 315-321
    • Van Heusden, G.P.H.1    Bos, K.2    Wirtz, K.W.A.3
  • 131
    • 0024596796 scopus 로고
    • Subcellular localization of sterol carrier protein-2 in rat hepatocytes: Its primary localization to peroxisomes
    • Keller GA, Scallen TJ, Clarke D, Maher PA, Krisans SK, Singer SJ. Subcellular localization of sterol carrier protein-2 in rat hepatocytes: its primary localization to peroxisomes. J Cell Biol 108:1353-1361, 1989.
    • (1989) J Cell Biol , vol.108 , pp. 1353-1361
    • Keller, G.A.1    Scallen, T.J.2    Clarke, D.3    Maher, P.A.4    Krisans, S.K.5    Singer, S.J.6
  • 132
    • 0027359198 scopus 로고
    • The presence and subcellular distribution of sterol carrier protein-2 in embyonic chick tissue
    • Reinhart MP, Avart SJ, Dobson TO, Foglia TA. The presence and subcellular distribution of sterol carrier protein-2 in embyonic chick tissue. Biochem J 295:787-792, 1993.
    • (1993) Biochem J , vol.295 , pp. 787-792
    • Reinhart, M.P.1    Avart, S.J.2    Dobson, T.O.3    Foglia, T.A.4
  • 133
    • 0021917233 scopus 로고
    • Ultrastructural localization of a peroxisomal protein in rat liver using the specific antibody against the nonspecific lipid transfer protein (sterol carrier protein-2)
    • Van der Krift TP, Leunissen J, Teerlink T, van Heusden GPH, Verklij AJ. Wirtz KWA. Ultrastructural localization of a peroxisomal protein in rat liver using the specific antibody against the nonspecific lipid transfer protein (sterol carrier protein-2). Biochim Biophys Acta 812:387-392, 1985.
    • (1985) Biochim Biophys Acta , vol.812 , pp. 387-392
    • Van der Krift, T.P.1    Leunissen, J.2    Teerlink, T.3    Van Heusden, G.P.H.4    Verklij, A.J.5    Wirtz, K.W.A.6
  • 134
    • 0028123083 scopus 로고
    • Sterol carrier protein X is peroxisomal 3-oxoacyl coenzyme A thiolase with intrinsic sterol carrier and lipid transfer activity
    • Seedorf U, Brysch P, Engel T, Schrage K, Assmann G. Sterol carrier protein X is peroxisomal 3-oxoacyl coenzyme A thiolase with intrinsic sterol carrier and lipid transfer activity. J Biol Chem 269:21277-21283, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 21277-21283
    • Seedorf, U.1    Brysch, P.2    Engel, T.3    Schrage, K.4    Assmann, G.5
  • 135
    • 0028823706 scopus 로고
    • Peroxisomes and sterol carrier protein-2 in luteal cell steroido-genesis: A possible role in cholesterol transport from lipid droplets to mitochondria
    • Mendis-Handagama SM, Aten RF, Watkins PA, Scallen TJ, Berhman HR. Peroxisomes and sterol carrier protein-2 in luteal cell steroido-genesis: A possible role in cholesterol transport from lipid droplets to mitochondria. Tissue Cell 27:483-490, 1995.
    • (1995) Tissue Cell , vol.27 , pp. 483-490
    • Mendis-Handagama, S.M.1    Aten, R.F.2    Watkins, P.A.3    Scallen, T.J.4    Berhman, H.R.5
  • 136
    • 0026480212 scopus 로고
    • Leydig cell peroxisomes and sterol carrier protein-2 in luteinizing hormone-deprived rats
    • Mendis-Handagama SM, Watkins PA, Gelber SJ, Scallen TJ. Leydig cell peroxisomes and sterol carrier protein-2 in luteinizing hormone-deprived rats. Endocrinology 131:2839-2845, 1992.
    • (1992) Endocrinology , vol.131 , pp. 2839-2845
    • Mendis-Handagama, S.M.1    Watkins, P.A.2    Gelber, S.J.3    Scallen, T.J.4
  • 137
    • 0025695327 scopus 로고
    • Luteinizing hormone causes rapid and transient changes in rat Leydig cell peroxisome volume and intraperoxisomal sterol carrier protein-2 content
    • Mendis-Handagama SM, Watkins PA, Gelber SJ, Scallen TJ, Zirkin BR, Ewing LL. Luteinizing hormone causes rapid and transient changes in rat Leydig cell peroxisome volume and intraperoxisomal sterol carrier protein-2 content. Endocrinology 127:2947-2954, 1990.
    • (1990) Endocrinology , vol.127 , pp. 2947-2954
    • Mendis-Handagama, S.M.1    Watkins, P.A.2    Gelber, S.J.3    Scallen, T.J.4    Zirkin, B.R.5    Ewing, L.L.6
  • 138
    • 0030972973 scopus 로고    scopus 로고
    • Sterol carrier protein-2 overexpression enhances sterol cycling and inhibits cholesterol ester synthesis and high density lipoprotein cholesterol secretion
    • Baum CL, Reschly EJ, Gayen AK, Groh ME, Schadick K. Sterol carrier protein-2 overexpression enhances sterol cycling and inhibits cholesterol ester synthesis and high density lipoprotein cholesterol secretion. J Biol Chem 272:6490-6498, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 6490-6498
    • Baum, C.L.1    Reschly, E.J.2    Gayen, A.K.3    Groh, M.E.4    Schadick, K.5
  • 139
    • 0032964431 scopus 로고    scopus 로고
    • Expression and intracellular processing of the 58-kDa sterol carrier protein 2/3-oxoacyl-CoA thiolase in transfected mouse L-cell fibroblasts
    • Atshaves BP, Petrescu A, Starodub O, Roths J, Kier AB, Schroeder F. Expression and intracellular processing of the 58-kDa sterol carrier protein 2/3-oxoacyl-CoA thiolase in transfected mouse L-cell fibroblasts. J Lipid Res 40:610-622, 1999.
    • (1999) J Lipid Res , vol.40 , pp. 610-622
    • Atshaves, B.P.1    Petrescu, A.2    Starodub, O.3    Roths, J.4    Kier, A.B.5    Schroeder, F.6
  • 142
    • 0032880514 scopus 로고    scopus 로고
    • The sterol carrier protein-2 amino terminus: A membrane interaction domain
    • Huang H, Ball JA, Billheimer JT, Schroeder F. The sterol carrier protein-2 amino terminus: a membrane interaction domain. Biochemistry 38:13231-13243, 1999.
    • (1999) Biochemistry , vol.38 , pp. 13231-13243
    • Huang, H.1    Ball, J.A.2    Billheimer, J.T.3    Schroeder, F.4
  • 143
    • 0033429205 scopus 로고    scopus 로고
    • Interaction of the N terminus of sterol carrier protein-2 with membranes: Role of membrane curvature
    • Huang H, Ball JA, Billheimer JT, Schroeder F. Interaction of the N terminus of sterol carrier protein-2 with membranes: Role of membrane curvature. Biochem J 344:593-603, 1999.
    • (1999) Biochem J , vol.344 , pp. 593-603
    • Huang, H.1    Ball, J.A.2    Billheimer, J.T.3    Schroeder, F.4
  • 145
    • 0026739685 scopus 로고
    • Intracellular cholesterol transport
    • Liscum L, Dahl NK. Intracellular cholesterol transport. J Lipid Res 33:1239-1254, 1992.
    • (1992) J Lipid Res , vol.33 , pp. 1239-1254
    • Liscum, L.1    Dahl, N.K.2
  • 146
    • 0034717894 scopus 로고    scopus 로고
    • Intracellular cholesterol trafficking: Role of the NPC1 protein
    • Blanchette-Mackie EJ. Intracellular cholesterol trafficking: role of the NPC1 protein. Biochim Biophys Acta 1486:171-183, 2000.
    • (2000) Biochim Biophys Acta , vol.1486 , pp. 171-183
    • Blanchette-Mackie, E.J.1
  • 148
    • 0032887393 scopus 로고    scopus 로고
    • Niemann-Pick C1 is a late endosome resident protein that transiently associates with lysosomes and the trans-Golgi network
    • Higgins ME, Davies JP, Chen FW, Ioannou YA. Niemann-Pick C1 is a late endosome resident protein that transiently associates with lysosomes and the trans-Golgi network. Mol Gen Metab 68:1-13, 1999.
    • (1999) Mol Gen Metab , vol.68 , pp. 1-13
    • Higgins, M.E.1    Davies, J.P.2    Chen, F.W.3    Ioannou, Y.A.4
  • 149
    • 0032512758 scopus 로고    scopus 로고
    • Evidence for a cholesterol transport pathway from lysosomes to endoplasmic reticulum that is independent of the plasma membrane
    • Underwood KW, Jacobs NL, Howley A, Liscum L. Evidence for a cholesterol transport pathway from lysosomes to endoplasmic reticulum that is independent of the plasma membrane. J Biol Chem 273:4266-4274, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 4266-4274
    • Underwood, K.W.1    Jacobs, N.L.2    Howley, A.3    Liscum, L.4
  • 151
    • 0029101538 scopus 로고
    • Sterol carrier protein-2 is involved in cholesterol transfer from the endoplasmic reticulum to the plasma membrane in human fibroblasts
    • Puglielli L, Rigotti A, Greco AV, Santos MJ, Nervi F. Sterol carrier protein-2 is involved in cholesterol transfer from the endoplasmic reticulum to the plasma membrane in human fibroblasts. J Biol Chem 270:18723-18726, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 18723-18726
    • Puglielli, L.1    Rigotti, A.2    Greco, A.V.3    Santos, M.J.4    Nervi, F.5
  • 152
    • 0023656457 scopus 로고
    • Binding of fluorescent-labeled phosphatidylcholine to rat liver non-specific lipid transfer protein
    • Nichols JW. Binding of fluorescent-labeled phosphatidylcholine to rat liver non-specific lipid transfer protein. J Biol Chem 29:14172-14177, 1987.
    • (1987) J Biol Chem , vol.29 , pp. 14172-14177
    • Nichols, J.W.1
  • 153
    • 0025997233 scopus 로고
    • The low-affinity lipid binding site of the non-specific lipid transfer protein: Implications for its mode of action
    • Gadella TW Jr., Wirtz KW. The low-affinity lipid binding site of the non-specific lipid transfer protein: Implications for its mode of action. Biochim Biophys Acta 1070:237-245, 1991.
    • (1991) Biochim Biophys Acta , vol.1070 , pp. 237-245
    • Gadella T.W., Jr.1    Wirtz, K.W.2
  • 155
    • 0029082055 scopus 로고
    • Probing the ligand binding sites of fatty acid and sterol carrier proteins: Effects of ethanol
    • Schroeder F, Myers-Payne SC, Billheimer JT, Wood WG. Probing the ligand binding sites of fatty acid and sterol carrier proteins: effects of ethanol. Biochemistry 34:11919-11927, 1995.
    • (1995) Biochemistry , vol.34 , pp. 11919-11927
    • Schroeder, F.1    Myers-Payne, S.C.2    Billheimer, J.T.3    Wood, W.G.4
  • 158
    • 0020288488 scopus 로고
    • Heterogeneity of rabbit intestine brush border plasma membrane cholesterol
    • Bloj B, Zilversmit DB. Heterogeneity of rabbit intestine brush border plasma membrane cholesterol. J Biol Chem 257:7608-7614, 1982.
    • (1982) J Biol Chem , vol.257 , pp. 7608-7614
    • Bloj, B.1    Zilversmit, D.B.2
  • 161
    • 0032772624 scopus 로고    scopus 로고
    • Microsomal long chain fatty acyl CoA transacylation: Differential effect of SCP-2
    • Chao H, Billheimer JT, Kier AB, Schroeder F. Microsomal long chain fatty acyl CoA transacylation: Differential effect of SCP-2. Biochim Biophys Acta 1439:371-383, 1999.
    • (1999) Biochim Biophys Acta , vol.1439 , pp. 371-383
    • Chao, H.1    Billheimer, J.T.2    Kier, A.B.3    Schroeder, F.4
  • 162
    • 0025681619 scopus 로고
    • Role of acidic phospholipids in intermembrane sterol transfer
    • Hapala I, Butko P, Schroeder F. Role of acidic phospholipids in intermembrane sterol transfer. Chem Phys Lipids 56:37-47, 1990.
    • (1990) Chem Phys Lipids , vol.56 , pp. 37-47
    • Hapala, I.1    Butko, P.2    Schroeder, F.3
  • 163
    • 0025049350 scopus 로고
    • Intermembrane cholesterol transfer: Role of sterol carrier proteins and phosphatidylserine
    • Schroeder F, Butko P, Hapala I, Scallen TJ. Intermembrane cholesterol transfer: Role of sterol carrier proteins and phosphatidylserine. Lipids 25:669-674, 1990.
    • (1990) Lipids , vol.25 , pp. 669-674
    • Schroeder, F.1    Butko, P.2    Hapala, I.3    Scallen, T.J.4
  • 164
    • 0025041610 scopus 로고
    • Effect of lipid composition on the transfer of sterols mediated by non-specific lipid transfer protein (sterol carrier protein2)
    • Billheimer JT, Gaylor JL. Effect of lipid composition on the transfer of sterols mediated by non-specific lipid transfer protein (sterol carrier protein2). Biochim Biophys Acta 1046:136-143, 1990.
    • (1990) Biochim Biophys Acta , vol.1046 , pp. 136-143
    • Billheimer, J.T.1    Gaylor, J.L.2
  • 165
    • 0018086864 scopus 로고
    • Differences in fluidity between bilayer halves of tumour cell plasma membranes
    • Schroeder F. Differences in fluidity between bilayer halves of tumour cell plasma membranes. Nature 275:528-530, 1978.
    • (1978) Nature , vol.275 , pp. 528-530
    • Schroeder, F.1
  • 166
    • 0019328160 scopus 로고
    • Differences in fluidity between bilayer halves of plasma cell membranes
    • Schroeder F, Kinden DA. Differences in fluidity between bilayer halves of plasma cell membranes. Nature 287:255-256, 1980.
    • (1980) Nature , vol.287 , pp. 255-256
    • Schroeder, F.1    Kinden, D.A.2
  • 167
    • 0019891679 scopus 로고
    • Use of a fluorescent sterol to probe the transbilayer distribution of sterols in biological membranes
    • Schroeder F. Use of a fluorescent sterol to probe the transbilayer distribution of sterols in biological membranes. FEBS Lett 135:127-130, 1981.
    • (1981) FEBS Lett , vol.135 , pp. 127-130
    • Schroeder, F.1
  • 168
    • 0020104195 scopus 로고
    • Asymmetric transbilayer distribution of sterol across plasma membranes determined by fluorescence quenching of dehydroergosterol
    • Hale JE, Schroeder F. Asymmetric transbilayer distribution of sterol across plasma membranes determined by fluorescence quenching of dehydroergosterol. Eur J Biochem 122:649-661, 1982.
    • (1982) Eur J Biochem , vol.122 , pp. 649-661
    • Hale, J.E.1    Schroeder, F.2
  • 169
    • 0021775991 scopus 로고
    • Fluorescence probes unravel asymmetric structure of membranes
    • Roodyn DB, Ed. Plenum Publishing, New York
    • Schroeder F. Fluorescence probes unravel asymmetric structure of membranes. In: Roodyn DB, Ed. Subcellular Biochemistry. Plenum Publishing, New York: pp51-101, 1985.
    • (1985) Subcellular Biochemistry , pp. 51-101
    • Schroeder, F.1
  • 170
    • 0022470306 scopus 로고
    • Regulation of transbilayer distribution of a fluorescent sterol in tumor cell plasma membranes
    • Kier AB, Sweet WD, Cowlen MS, Schroeder F. Regulation of transbilayer distribution of a fluorescent sterol in tumor cell plasma membranes. Biochim Biophys Acta 861:287-301, 1986.
    • (1986) Biochim Biophys Acta , vol.861 , pp. 287-301
    • Kier, A.B.1    Sweet, W.D.2    Cowlen, M.S.3    Schroeder, F.4
  • 171
    • 0023947429 scopus 로고
    • Transbilayer movement of cholesterol in the human erythrocyte membrane
    • Brasaemle DL, Robertson RD, Attie AD. Transbilayer movement of cholesterol in the human erythrocyte membrane. J Lipid Res 29:481-489, 1988.
    • (1988) J Lipid Res , vol.29 , pp. 481-489
    • Brasaemle, D.L.1    Robertson, R.D.2    Attie, A.D.3
  • 173
    • 0025291728 scopus 로고
    • Asymmetric distribution of a fluorescent sterol in synaptic plasma membranes: Effects of chronic ethanol consumption
    • Wood WG, Schroeder F, Hogy L, Rao AM, Nemecz G. Asymmetric distribution of a fluorescent sterol in synaptic plasma membranes: Effects of chronic ethanol consumption. Biochim Biophys Acta 1025:243-246, 1990.
    • (1990) Biochim Biophys Acta , vol.1025 , pp. 243-246
    • Wood, W.G.1    Schroeder, F.2    Hogy, L.3    Rao, A.M.4    Nemecz, G.5
  • 174
    • 0029935694 scopus 로고    scopus 로고
    • Increasing age alters transbilayer fluidity and cholesterol asymmetry in synaptic plasma membranes of mice
    • Igbavboa U, Avdulov NA, Schroeder F, Wood WG. Increasing age alters transbilayer fluidity and cholesterol asymmetry in synaptic plasma membranes of mice. J Neurochem 66:1717-1725, 1996.
    • (1996) J Neurochem , vol.66 , pp. 1717-1725
    • Igbavboa, U.1    Avdulov, N.A.2    Schroeder, F.3    Wood, W.G.4
  • 175
    • 0024473840 scopus 로고
    • Interaction of sphingomyelins and phosphatidylcholines with fluorescent dehydroergosterol
    • Schroeder F, Nemecz G. Interaction of sphingomyelins and phosphatidylcholines with fluorescent dehydroergosterol. Biochemistry 28:5992-6000, 1989.
    • (1989) Biochemistry , vol.28 , pp. 5992-6000
    • Schroeder, F.1    Nemecz, G.2
  • 178
    • 0020000348 scopus 로고
    • Sterol carrier protein 2: Delivery of cholesterol from adrenal lipid droplets to mitochondria for pregnenolone synthesis
    • Chanderbhan R, Noland BJ, Scallen TJ, Vahouny GV. Sterol carrier protein 2: Delivery of cholesterol from adrenal lipid droplets to mitochondria for pregnenolone synthesis. J Biol Chem 257:8928-8934, 1982.
    • (1982) J Biol Chem , vol.257 , pp. 8928-8934
    • Chanderbhan, R.1    Noland, B.J.2    Scallen, T.J.3    Vahouny, G.V.4
  • 180
    • 0034717943 scopus 로고    scopus 로고
    • Intramitochondrial cholesterol transfer
    • Stocco DM. Intramitochondrial cholesterol transfer. Biochim Biophys Acta 1486:184-197, 2000.
    • (2000) Biochim Biophys Acta , vol.1486 , pp. 184-197
    • Stocco, D.M.1
  • 183
    • 0030848810 scopus 로고    scopus 로고
    • Targeted disruption of the mouse gene encoding steroidogenic acute regulatory protein provides insights into congenital lipoid adrenal hyperplasia
    • Caron KM, Soo SC, Wetsel WC, Stocco DM, Clark BJ, Parker KL. Targeted disruption of the mouse gene encoding steroidogenic acute regulatory protein provides insights into congenital lipoid adrenal hyperplasia. Proc Natl Acad Sci U S A 94:11540-11545, 1997.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 11540-11545
    • Caron, K.M.1    Soo, S.C.2    Wetsel, W.C.3    Stocco, D.M.4    Clark, B.J.5    Parker, K.L.6
  • 185
    • 0026075821 scopus 로고
    • Reverse cholesterol transport
    • Fielding CJ. Reverse cholesterol transport. Curr Opin Lipidol 2:376-378, 1991.
    • (1991) Curr Opin Lipidol , vol.2 , pp. 376-378
    • Fielding, C.J.1
  • 186
    • 0031013536 scopus 로고    scopus 로고
    • Role of multidrug resistance P-glycoproteins in choelsterol esterification
    • Debry P, Nash EA, Neklason DW, Metherall JE. Role of multidrug resistance P-glycoproteins in choelsterol esterification. J Biol Chem 272:1026-1031, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 1026-1031
    • Debry, P.1    Nash, E.A.2    Neklason, D.W.3    Metherall, J.E.4
  • 187
    • 0030459196 scopus 로고    scopus 로고
    • Intracellular transport of low-density lipo protein-derived free cholesterol begins at clathrin-coated pits and terminates at cell surface caveolae
    • Fielding PE, Fielding CJ. Intracellular transport of low-density lipo protein-derived free cholesterol begins at clathrin-coated pits and terminates at cell surface caveolae. Biochemistry 35:14932-14938, 1996.
    • (1996) Biochemistry , vol.35 , pp. 14932-14938
    • Fielding, P.E.1    Fielding, C.J.2
  • 188
    • 0029817701 scopus 로고    scopus 로고
    • Modulation on introhepatic cholesterol trafficking: Evidence by in vivo antisense treatment for the involvement of sterol carrier protein-2 in newly synthesized cholesterol transfer into bile
    • Puglielli L, Rigotti A, Amigo L, Nunez L, Greco AV, Santos MJ, Nervi F. Modulation on introhepatic cholesterol trafficking: Evidence by in vivo antisense treatment for the involvement of sterol carrier protein-2 in newly synthesized cholesterol transfer into bile. Biochem J 317:681-687, 1996.
    • (1996) Biochem J , vol.317 , pp. 681-687
    • Puglielli, L.1    Rigotti, A.2    Amigo, L.3    Nunez, L.4    Greco, A.V.5    Santos, M.J.6    Nervi, F.7
  • 191
    • 0010069306 scopus 로고
    • Effects of membrane lipids and fluidity on acetylcholine receptor function
    • Aloia RC, Curtain CC, Gordon LM, Eds. John Wiley & Sons, Inc., New York
    • McNamee MG, Fong TM. Effects of membrane lipids and fluidity on acetylcholine receptor function. In: Aloia RC, Curtain CC, Gordon LM, Eds. Advancess in Membrane Fluidity: Lipid Domains and the Relationship to Membrane Function. John Wiley & Sons, Inc., New York: pp43-62, 1988.
    • (1988) Advancess in Membrane Fluidity: Lipid Domains and the Relationship to Membrane Function , pp. 43-62
    • McNamee, M.G.1    Fong, T.M.2
  • 192
    • 0030734157 scopus 로고    scopus 로고
    • The cholesterol dependence of activation and fast desensitization of the nicotinic acetylcholine receptor
    • Rankin SE, Addona GH, Kloczewiak MA, Bugge B, Miller KW. The cholesterol dependence of activation and fast desensitization of the nicotinic acetylcholine receptor. Biophys J 73:2446-2455, 1997.
    • (1997) Biophys J , vol.73 , pp. 2446-2455
    • Rankin, S.E.1    Addona, G.H.2    Kloczewiak, M.A.3    Bugge, B.4    Miller, K.W.5
  • 193
    • 0030774729 scopus 로고    scopus 로고
    • Cholesterol as modulator of receptor function
    • Gimpl G, Burger K, Fahrenholz F. Cholesterol as modulator of receptor function. Biochemistry 36:10959-10974, 1997.
    • (1997) Biochemistry , vol.36 , pp. 10959-10974
    • Gimpl, G.1    Burger, K.2    Fahrenholz, F.3
  • 194
    • 0029080687 scopus 로고
    • Formation of membrane domains created during the budding of vesicular stomatitis virus: A model for selective lipid and protein sorting in biological membranes
    • Luan P, Yang L, Glaser M. Formation of membrane domains created during the budding of vesicular stomatitis virus: A model for selective lipid and protein sorting in biological membranes. Biochemistry 34:9874-9883, 1995.
    • (1995) Biochemistry , vol.34 , pp. 9874-9883
    • Luan, P.1    Yang, L.2    Glaser, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.