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Volumn 76, Issue 3, 2011, Pages 216-231

Probes for studying cholesterol binding and cell biology

Author keywords

Cholesterol probes; Cyclodextrins; Cytolysins; Fluorescent and photoreactive sterols; Photoaffinity labeling; Polyenes

Indexed keywords

AZIDE; BENZOPHENONE; BILE ACID; BORON DERIVATIVE; CHOLESTATRIENOL; CHOLESTEROL; CHOLESTEROL DERIVATIVE; CHOLESTEROL OXIDASE; CYCLODEXTRIN; CYTOLYSIN; DANSYL CHLORIDE; DEHYDROERGOSTEROL; ERGOSTEROL; FILIPIN; LIPID BINDING PROTEIN; MACROGOL; MEMBRANE PROTEIN; STEROID HORMONE; UNCLASSIFIED DRUG;

EID: 78751646831     PISSN: 0039128X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.steroids.2010.11.001     Document Type: Review
Times cited : (70)

References (215)
  • 1
    • 0033793871 scopus 로고    scopus 로고
    • Regulation of receptor function by cholesterol
    • K. Burger, G. Gimpl, and F. Fahrenholz Regulation of receptor function by cholesterol Cell Mol Life Sci 57 2000 1577 1592
    • (2000) Cell Mol Life Sci , vol.57 , pp. 1577-1592
    • Burger, K.1    Gimpl, G.2    Fahrenholz, F.3
  • 2
    • 33744543610 scopus 로고    scopus 로고
    • Role of cholesterol in the function and organization of G-protein coupled receptors
    • T.J. Pucadyil, and A. Chattopadhyay Role of cholesterol in the function and organization of G-protein coupled receptors Prog Lipid Res 45 2006 295 333
    • (2006) Prog Lipid Res , vol.45 , pp. 295-333
    • Pucadyil, T.J.1    Chattopadhyay, A.2
  • 3
    • 0030949124 scopus 로고    scopus 로고
    • Functional rafts in cell membranes
    • K. Simons, and E. Ikonen Functional rafts in cell membranes Nature 387 1997 569 572
    • (1997) Nature , vol.387 , pp. 569-572
    • Simons, K.1    Ikonen, E.2
  • 4
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • K. Simons, and D. Toomre Lipid rafts and signal transduction Nat Rev Mol Cell Biol 1 2000 31 39
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 5
    • 0022389171 scopus 로고
    • Cholesterol and the cell membrane
    • P.L. Yeagle Cholesterol and the cell membrane Biochim Biophys Acta 822 1985 267 287
    • (1985) Biochim Biophys Acta , vol.822 , pp. 267-287
    • Yeagle, P.L.1
  • 7
    • 33644871685 scopus 로고    scopus 로고
    • Significance of sterol structural specificity Desmosterol cannot replace cholesterol in lipid rafts
    • S. Vainio, M. Jansen, M. Koivusalo, T. Rog, M. Karttunen, and I. Vattulainen Significance of sterol structural specificity Desmosterol cannot replace cholesterol in lipid rafts J Biol Chem 281 2006 348 355
    • (2006) J Biol Chem , vol.281 , pp. 348-355
    • Vainio, S.1    Jansen, M.2    Koivusalo, M.3    Rog, T.4    Karttunen, M.5    Vattulainen, I.6
  • 8
    • 33746855864 scopus 로고    scopus 로고
    • Cholesterol precursors stabilize ordinary and ceramide-rich ordered lipid domains (lipid rafts) to different degrees Implications for the Bloch hypothesis and sterol biosynthesis disorders
    • Megha, O. Bakht, and E. London Cholesterol precursors stabilize ordinary and ceramide-rich ordered lipid domains (lipid rafts) to different degrees Implications for the Bloch hypothesis and sterol biosynthesis disorders J Biol Chem 281 2006 21903 21913
    • (2006) J Biol Chem , vol.281 , pp. 21903-21913
    • Megha1    Bakht, O.2    London, E.3
  • 9
    • 0021119947 scopus 로고
    • Fluorescent sterols: Probe molecules of membrane structure and function
    • F. Schroeder Fluorescent sterols: probe molecules of membrane structure and function Prog Lipid Res 23 1984 97 113
    • (1984) Prog Lipid Res , vol.23 , pp. 97-113
    • Schroeder, F.1
  • 10
    • 34248365632 scopus 로고    scopus 로고
    • Assess the nature of cholesterol-lipid interactions through the chemical potential of cholesterol in phosphatidylcholine bilayers
    • M.R. Ali, K.H. Cheng, and J. Huang Assess the nature of cholesterol-lipid interactions through the chemical potential of cholesterol in phosphatidylcholine bilayers Proc Natl Acad Sci U S A 104 2007 5372 5377
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 5372-5377
    • Ali, M.R.1    Cheng, K.H.2    Huang, J.3
  • 11
    • 0037429735 scopus 로고    scopus 로고
    • Role of cholesterol in lipid raft formation: Lessons from lipid model systems
    • J.R. Silvius Role of cholesterol in lipid raft formation: lessons from lipid model systems Biochim Biophys Acta 1610 2003 174 183
    • (2003) Biochim Biophys Acta , vol.1610 , pp. 174-183
    • Silvius, J.R.1
  • 12
    • 61349094652 scopus 로고    scopus 로고
    • Direct observation of the nanoscale dynamics of membrane lipids in a living cell
    • C. Eggeling, C. Ringemann, R. Medda, G. Schwarzmann, K. Sandhoff, and S. Polyakova Direct observation of the nanoscale dynamics of membrane lipids in a living cell Nature 457 2009 1159 1162
    • (2009) Nature , vol.457 , pp. 1159-1162
    • Eggeling, C.1    Ringemann, C.2    Medda, R.3    Schwarzmann, G.4    Sandhoff, K.5    Polyakova, S.6
  • 13
    • 0344585437 scopus 로고    scopus 로고
    • Lipid rafts: Elusive or illusive?
    • S. Munro Lipid rafts: elusive or illusive? Cell 115 2003 377 388
    • (2003) Cell , vol.115 , pp. 377-388
    • Munro, S.1
  • 14
    • 33750130964 scopus 로고    scopus 로고
    • Lipid rafts: Now you see them, now you don't
    • A.S. Shaw Lipid rafts: now you see them, now you don't Nat Immunol 7 2006 1139 1142
    • (2006) Nat Immunol , vol.7 , pp. 1139-1142
    • Shaw, A.S.1
  • 15
    • 44649160533 scopus 로고    scopus 로고
    • Have we become overly reliant on lipid rafts? Talking Point on the involvement of lipid rafts in T-cell activation
    • A.K. Kenworthy Have we become overly reliant on lipid rafts? Talking Point on the involvement of lipid rafts in T-cell activation EMBO Rep 9 2008 531 535
    • (2008) EMBO Rep , vol.9 , pp. 531-535
    • Kenworthy, A.K.1
  • 16
    • 69449093833 scopus 로고    scopus 로고
    • Steric and not structure-specific factors dictate the endocytic mechanism of glycosylphosphatidylinositol-anchored proteins
    • P. Bhagatji, R. Leventis, J. Comeau, M. Refaei, and J.R. Silvius Steric and not structure-specific factors dictate the endocytic mechanism of glycosylphosphatidylinositol-anchored proteins J Cell Biol 186 2009 615 628
    • (2009) J Cell Biol , vol.186 , pp. 615-628
    • Bhagatji, P.1    Leventis, R.2    Comeau, J.3    Refaei, M.4    Silvius, J.R.5
  • 17
    • 20444404267 scopus 로고    scopus 로고
    • Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells
    • A.D. Douglass, and R.D. Vale Single-molecule microscopy reveals plasma membrane microdomains created by protein-protein networks that exclude or trap signaling molecules in T cells Cell 121 2005 937 950
    • (2005) Cell , vol.121 , pp. 937-950
    • Douglass, A.D.1    Vale, R.D.2
  • 19
    • 36448929114 scopus 로고    scopus 로고
    • Cholesterol reporter molecules
    • G. Gimpl, and K. Gehrig-Burger Cholesterol reporter molecules Biosci Rep 27 2007 335 358
    • (2007) Biosci Rep , vol.27 , pp. 335-358
    • Gimpl, G.1    Gehrig-Burger, K.2
  • 20
    • 77952313405 scopus 로고    scopus 로고
    • Cholesterol-protein interaction: Methods and cholesterol reporter molecules
    • G. Gimpl Cholesterol-protein interaction: methods and cholesterol reporter molecules Subcell Biochem 51 2010 1 45
    • (2010) Subcell Biochem , vol.51 , pp. 1-45
    • Gimpl, G.1
  • 21
    • 0024806367 scopus 로고
    • Differential effects of alpha-, beta- and gamma-cyclodextrins on human erythrocytes
    • Y. Ohtani, T. Irie, K. Uekama, K. Fukunaga, and J. Pitha Differential effects of alpha-, beta- and gamma-cyclodextrins on human erythrocytes Eur J Biochem 186 1989 17 22
    • (1989) Eur J Biochem , vol.186 , pp. 17-22
    • Ohtani, Y.1    Irie, T.2    Uekama, K.3    Fukunaga, K.4    Pitha, J.5
  • 22
    • 0026646703 scopus 로고
    • Hydroxypropylcyclodextrins in parenteral use I: Lipid dissolution and effects on lipid transfers in vitro
    • T. Irie, K. Fukunaga, and J. Pitha Hydroxypropylcyclodextrins in parenteral use I: Lipid dissolution and effects on lipid transfers in vitro J Pharm Sci 81 1992 521 523
    • (1992) J Pharm Sci , vol.81 , pp. 521-523
    • Irie, T.1    Fukunaga, K.2    Pitha, J.3
  • 23
    • 0028812541 scopus 로고
    • Alteration of the myometrial plasma membrane cholesterol content with beta-cyclodextrin modulates the binding affinity of the oxytocin receptor
    • U. Klein, G. Gimpl, and F. Fahrenholz Alteration of the myometrial plasma membrane cholesterol content with beta-cyclodextrin modulates the binding affinity of the oxytocin receptor Biochemistry 34 1995 13784 13793
    • (1995) Biochemistry , vol.34 , pp. 13784-13793
    • Klein, U.1    Gimpl, G.2    Fahrenholz, F.3
  • 24
    • 0028879530 scopus 로고
    • Expression of the human oxytocin receptor in baculovirus-infected insect cells: High-affinity binding is induced by a cholesterol-cyclodextrin complex
    • G. Gimpl, U. Klein, H. Reilander, and F. Fahrenholz Expression of the human oxytocin receptor in baculovirus-infected insect cells: high-affinity binding is induced by a cholesterol-cyclodextrin complex Biochemistry 34 1995 13794 13801
    • (1995) Biochemistry , vol.34 , pp. 13794-13801
    • Gimpl, G.1    Klein, U.2    Reilander, H.3    Fahrenholz, F.4
  • 26
    • 0030774729 scopus 로고    scopus 로고
    • Cholesterol as modulator of receptor function
    • G. Gimpl, K. Burger, and F. Fahrenholz Cholesterol as modulator of receptor function Biochemistry 36 1997 10959 10974
    • (1997) Biochemistry , vol.36 , pp. 10959-10974
    • Gimpl, G.1    Burger, K.2    Fahrenholz, F.3
  • 27
    • 34249064912 scopus 로고    scopus 로고
    • Use of cyclodextrins to manipulate plasma membrane cholesterol content: Evidence, misconceptions and control strategies
    • R. Zidovetzki, and I. Levitan Use of cyclodextrins to manipulate plasma membrane cholesterol content: evidence, misconceptions and control strategies Biochim Biophys Acta 1768 2007 1311 1324
    • (2007) Biochim Biophys Acta , vol.1768 , pp. 1311-1324
    • Zidovetzki, R.1    Levitan, I.2
  • 28
    • 0035818530 scopus 로고    scopus 로고
    • Cholesterol depletion induces large scale domain segregation in living cell membranes
    • M. Hao, S. Mukherjee, and F.R. Maxfield Cholesterol depletion induces large scale domain segregation in living cell membranes Proc Natl Acad Sci U S A 98 2001 13072 13077
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 13072-13077
    • Hao, M.1    Mukherjee, S.2    Maxfield, F.R.3
  • 29
    • 77950600389 scopus 로고    scopus 로고
    • Limited cholesterol depletion causes aggregation of plasma membrane lipid rafts inducing T cell activation
    • S. Mahammad, J. Dinic, J. Adler, and I. Parmryd Limited cholesterol depletion causes aggregation of plasma membrane lipid rafts inducing T cell activation Biochim Biophys Acta 1801 2010 625 634
    • (2010) Biochim Biophys Acta , vol.1801 , pp. 625-634
    • Mahammad, S.1    Dinic, J.2    Adler, J.3    Parmryd, I.4
  • 30
    • 0036671360 scopus 로고    scopus 로고
    • Cholesterol addition to ER membranes alters conformation of SCAP, the SREBP escort protein that regulates cholesterol metabolism
    • A.J. Brown, L. Sun, J. Feramisco, M.S. Brown, and J.L. Goldstein Cholesterol addition to ER membranes alters conformation of SCAP, the SREBP escort protein that regulates cholesterol metabolism Mol Cell 10 2002 237 245
    • (2002) Mol Cell , vol.10 , pp. 237-245
    • Brown, A.J.1    Sun, L.2    Feramisco, J.3    Brown, M.S.4    Goldstein, J.L.5
  • 31
    • 60549084168 scopus 로고    scopus 로고
    • Reversal of defective lysosomal transport in NPC disease ameliorates liver dysfunction and neurodegeneration in the npc1-/- mouse
    • B. Liu, S.D. Turley, D.K. Burns, A.M. Miller, J.J. Repa, and J.M. Dietschy Reversal of defective lysosomal transport in NPC disease ameliorates liver dysfunction and neurodegeneration in the npc1-/- mouse Proc Natl Acad Sci U S A 106 2009 2377 2382
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 2377-2382
    • Liu, B.1    Turley, S.D.2    Burns, D.K.3    Miller, A.M.4    Repa, J.J.5    Dietschy, J.M.6
  • 32
    • 73349138621 scopus 로고    scopus 로고
    • Cyclodextrin overcomes deficient lysosome-to-endoplasmic reticulum transport of cholesterol in Niemann-Pick type C cells
    • L. Abi-Mosleh, R.E. Infante, A. Radhakrishnan, J.L. Goldstein, and M.S. Brown Cyclodextrin overcomes deficient lysosome-to-endoplasmic reticulum transport of cholesterol in Niemann-Pick type C cells Proc Natl Acad Sci U S A 106 2009 19316 19321
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 19316-19321
    • Abi-Mosleh, L.1    Infante, R.E.2    Radhakrishnan, A.3    Goldstein, J.L.4    Brown, M.S.5
  • 33
    • 77950402392 scopus 로고    scopus 로고
    • Endocytosis of beta-cyclodextrins is responsible for cholesterol reduction in Niemann-Pick type C mutant cells
    • A.I. Rosenbaum, G. Zhang, J.D. Warren, and F.R. Maxfield Endocytosis of beta-cyclodextrins is responsible for cholesterol reduction in Niemann-Pick type C mutant cells Proc Natl Acad Sci U S A 107 2010 5477 5482
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 5477-5482
    • Rosenbaum, A.I.1    Zhang, G.2    Warren, J.D.3    Maxfield, F.R.4
  • 34
    • 0032532271 scopus 로고    scopus 로고
    • Effects of cholesterol depletion by cyclodextrin on the sphingolipid microdomains of the plasma membrane
    • S. Ilangumaran, and D.C. Hoessli Effects of cholesterol depletion by cyclodextrin on the sphingolipid microdomains of the plasma membrane Biochem J 335 Pt 2 1998 433 440
    • (1998) Biochem J , vol.335 , Issue.PART 2 , pp. 433-440
    • Ilangumaran, S.1    Hoessli, D.C.2
  • 35
    • 0345098359 scopus 로고    scopus 로고
    • Dynamics of membrane lipid domains in neuronal cells differentiated in culture
    • E. Ottico, A. Prinetti, S. Prioni, C. Giannotta, L. Basso, and V. Chigorno Dynamics of membrane lipid domains in neuronal cells differentiated in culture J Lipid Res 44 2003 2142 2151
    • (2003) J Lipid Res , vol.44 , pp. 2142-2151
    • Ottico, E.1    Prinetti, A.2    Prioni, S.3    Giannotta, C.4    Basso, L.5    Chigorno, V.6
  • 36
    • 3342957194 scopus 로고    scopus 로고
    • Behavior of alpha-, beta-, and gamma-cyclodextrins and their derivatives on an in vitro model of blood-brain barrier
    • V. Monnaert, S. Tilloy, H. Bricout, L. Fenart, R. Cecchelli, and E. Monflier Behavior of alpha-, beta-, and gamma-cyclodextrins and their derivatives on an in vitro model of blood-brain barrier J Pharmacol Exp Ther 310 2004 745 751
    • (2004) J Pharmacol Exp Ther , vol.310 , pp. 745-751
    • Monnaert, V.1    Tilloy, S.2    Bricout, H.3    Fenart, L.4    Cecchelli, R.5    Monflier, E.6
  • 37
    • 0033577805 scopus 로고    scopus 로고
    • Critical role for cholesterol in Lyn-mediated tyrosine phosphorylation of FcepsilonRI and their association with detergent-resistant membranes
    • E.D. Sheets, D. Holowka, and B. Baird Critical role for cholesterol in Lyn-mediated tyrosine phosphorylation of FcepsilonRI and their association with detergent-resistant membranes J Cell Biol 145 1999 877 887
    • (1999) J Cell Biol , vol.145 , pp. 877-887
    • Sheets, E.D.1    Holowka, D.2    Baird, B.3
  • 39
    • 27144473330 scopus 로고    scopus 로고
    • Clathrin-independent internalization of the human histamine H1-receptor in CHO-K1 cells
    • T.J. Self, S.M. Oakley, and S.J. Hill Clathrin-independent internalization of the human histamine H1-receptor in CHO-K1 cells Br J Pharmacol 146 2005 612 624
    • (2005) Br J Pharmacol , vol.146 , pp. 612-624
    • Self, T.J.1    Oakley, S.M.2    Hill, S.J.3
  • 40
    • 77951991606 scopus 로고    scopus 로고
    • T cell signal regulation by the actin cytoskeleton
    • G.R. Chichili, A.D. Westmuckett, and W. Rodgers T cell signal regulation by the actin cytoskeleton J Biol Chem 285 2010 14737 14746
    • (2010) J Biol Chem , vol.285 , pp. 14737-14746
    • Chichili, G.R.1    Westmuckett, A.D.2    Rodgers, W.3
  • 41
    • 0033554397 scopus 로고    scopus 로고
    • Membrane cholesterol modulates galanin-GalR2 interaction
    • L. Pang, M. Graziano, and S. Wang Membrane cholesterol modulates galanin-GalR2 interaction Biochemistry 38 1999 12003 12011
    • (1999) Biochemistry , vol.38 , pp. 12003-12011
    • Pang, L.1    Graziano, M.2    Wang, S.3
  • 42
    • 0021685522 scopus 로고
    • Filipin as a cholesterol probe. II. Filipin-cholesterol interaction in red blood cell membranes
    • O. Behnke, J. Tranum-Jensen, and D.B. van Filipin as a cholesterol probe II. Filipin-cholesterol interaction in red blood cell membranes Eur J Cell Biol 35 1984 200 215 (Pubitemid 15192791)
    • (1984) European Journal of Cell Biology , vol.35 , Issue.2 , pp. 200-215
    • Behnke, O.1    Tranum-Jensen, J.2    Van Deurs, B.3
  • 43
    • 0028138908 scopus 로고
    • Filipin vs enzymatic localization of cholesterol in guinea pig, mink, and mallard duck testicular cells
    • R.M. Pelletier, and M.L. Vitale Filipin vs enzymatic localization of cholesterol in guinea pig, mink, and mallard duck testicular cells J Histochem Cytochem 42 1994 1539 1554
    • (1994) J Histochem Cytochem , vol.42 , pp. 1539-1554
    • Pelletier, R.M.1    Vitale, M.L.2
  • 44
    • 0021272476 scopus 로고
    • Detection of membrane cholesterol by filipin in isolated rat liver coated vesicles is dependent upon removal of the clathrin coat
    • C.J. Steer, M. Bisher, R. Blumenthal, and A.C. Steven Detection of membrane cholesterol by filipin in isolated rat liver coated vesicles is dependent upon removal of the clathrin coat J Cell Biol 99 1984 315 319
    • (1984) J Cell Biol , vol.99 , pp. 315-319
    • Steer, C.J.1    Bisher, M.2    Blumenthal, R.3    Steven, A.C.4
  • 45
    • 0021106131 scopus 로고
    • Failure of filipin to detect cholesterol-rich domains in smooth muscle plasma membrane
    • N.J. Severs, and H.L. Simons Failure of filipin to detect cholesterol-rich domains in smooth muscle plasma membrane Nature 303 1983 637 638
    • (1983) Nature , vol.303 , pp. 637-638
    • Severs, N.J.1    Simons, H.L.2
  • 46
    • 77952302993 scopus 로고    scopus 로고
    • The cholesterol-dependent cytolysin family of gram-positive bacterial toxins
    • A.P. Heuck, P.C. Moe, and B.B. Johnson The cholesterol-dependent cytolysin family of gram-positive bacterial toxins Subcell Biochem 51 2010 551 577
    • (2010) Subcell Biochem , vol.51 , pp. 551-577
    • Heuck, A.P.1    Moe, P.C.2    Johnson, B.B.3
  • 47
    • 77952316285 scopus 로고    scopus 로고
    • Cholesterol-binding toxins and anti-cholesterol antibodies as structural probes for cholesterol localization
    • Y. Ohno-Iwashita, Y. Shimada, M. Hayashi, M. Iwamoto, S. Iwashita, and M. Inomata Cholesterol-binding toxins and anti-cholesterol antibodies as structural probes for cholesterol localization Subcell Biochem 51 2010 597 621
    • (2010) Subcell Biochem , vol.51 , pp. 597-621
    • Ohno-Iwashita, Y.1    Shimada, Y.2    Hayashi, M.3    Iwamoto, M.4    Iwashita, S.5    Inomata, M.6
  • 48
    • 0016045876 scopus 로고
    • Sterol structural requirements for inhibition of streptolysin O activity
    • K.C. Watson, and E.J. Kerr Sterol structural requirements for inhibition of streptolysin O activity Biochem J 140 1974 95 98
    • (1974) Biochem J , vol.140 , pp. 95-98
    • Watson, K.C.1    Kerr, E.J.2
  • 49
    • 0017100862 scopus 로고
    • Interaction of steptolysin O with sterols
    • D. Prigent, and J.E. Alouf Interaction of steptolysin O with sterols Biochim Biophys Acta 443 1976 288 300
    • (1976) Biochim Biophys Acta , vol.443 , pp. 288-300
    • Prigent, D.1    Alouf, J.E.2
  • 50
    • 41949085510 scopus 로고    scopus 로고
    • How interaction of perfringolysin O with membranes is controlled by sterol structure, lipid structure, and physiological low pH: Insights into the origin of perfringolysin O-lipid raft interaction
    • L.D. Nelson, A.E. Johnson, and E. London How interaction of perfringolysin O with membranes is controlled by sterol structure, lipid structure, and physiological low pH: insights into the origin of perfringolysin O-lipid raft interaction J Biol Chem 283 2008 4632 4642
    • (2008) J Biol Chem , vol.283 , pp. 4632-4642
    • Nelson, L.D.1    Johnson, A.E.2    London, E.3
  • 51
    • 0030666371 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
    • J. Rossjohn, S.C. Feil, W.J. McKinstry, R.K. Tweten, and M.W. Parker Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form Cell 89 1997 685 692
    • (1997) Cell , vol.89 , pp. 685-692
    • Rossjohn, J.1    Feil, S.C.2    McKinstry, W.J.3    Tweten, R.K.4    Parker, M.W.5
  • 52
    • 66149142747 scopus 로고    scopus 로고
    • Cholesterol exposure at the membrane surface is necessary and sufficient to trigger perfringolysin O binding
    • J.J. Flanagan, R.K. Tweten, A.E. Johnson, and A.P. Heuck Cholesterol exposure at the membrane surface is necessary and sufficient to trigger perfringolysin O binding Biochemistry 48 2009 3977 3987
    • (2009) Biochemistry , vol.48 , pp. 3977-3987
    • Flanagan, J.J.1    Tweten, R.K.2    Johnson, A.E.3    Heuck, A.P.4
  • 53
    • 77749292162 scopus 로고    scopus 로고
    • Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface
    • A.J. Farrand, S. LaChapelle, E.M. Hotze, A.E. Johnson, and R.K. Tweten Only two amino acids are essential for cytolytic toxin recognition of cholesterol at the membrane surface Proc Natl Acad Sci U S A 107 2010 4341 4346
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 4341-4346
    • Farrand, A.J.1    Lachapelle, S.2    Hotze, E.M.3    Johnson, A.E.4    Tweten, R.K.5
  • 54
    • 0030865913 scopus 로고    scopus 로고
    • Crosslinked plasmalemmal cholesterol is sequestered to caveolae: Analysis with a new cytochemical probe
    • T. Fujimoto, M. Hayashi, M. Iwamoto, and Y. Ohno-Iwashita Crosslinked plasmalemmal cholesterol is sequestered to caveolae: analysis with a new cytochemical probe J Histochem Cytochem 45 1997 1197 1205
    • (1997) J Histochem Cytochem , vol.45 , pp. 1197-1205
    • Fujimoto, T.1    Hayashi, M.2    Iwamoto, M.3    Ohno-Iwashita, Y.4
  • 55
    • 0030746612 scopus 로고    scopus 로고
    • A biotinylated perfringolysin O derivative: A new probe for detection of cell surface cholesterol
    • M. Iwamoto, I. Morita, M. Fukuda, S. Murota, S. Ando, and Y. Ohno-Iwashita A biotinylated perfringolysin O derivative: a new probe for detection of cell surface cholesterol Biochim Biophys Acta 1327 1997 222 230
    • (1997) Biochim Biophys Acta , vol.1327 , pp. 222-230
    • Iwamoto, M.1    Morita, I.2    Fukuda, M.3    Murota, S.4    Ando, S.5    Ohno-Iwashita, Y.6
  • 58
    • 0141590704 scopus 로고    scopus 로고
    • Biotinylated theta toxin derivative as a probe to examine intracellular cholesterol-rich domains in normal and Niemann-pick type C1 cells
    • S. Sugii, P.C. Reid, N. Ohgami, Y. Shimada, R.A. Maue, and H. Ninomiya Biotinylated theta toxin derivative as a probe to examine intracellular cholesterol-rich domains in normal and Niemann-pick type C1 cells J Lipid Res 2003
    • (2003) J Lipid Res
    • Sugii, S.1    Reid, P.C.2    Ohgami, N.3    Shimada, Y.4    Maue, R.A.5    Ninomiya, H.6
  • 59
    • 1542513994 scopus 로고    scopus 로고
    • A novel cholesterol stain reveals early neuronal cholesterol accumulation in the Niemann-Pick type C1 mouse brain
    • P.C. Reid, N. Sakashita, S. Sugii, Y. Ohno-Iwashita, Y. Shimada, and W.F. Hickey A novel cholesterol stain reveals early neuronal cholesterol accumulation in the Niemann-Pick type C1 mouse brain J Lipid Res 45 2004 582 591
    • (2004) J Lipid Res , vol.45 , pp. 582-591
    • Reid, P.C.1    Sakashita, N.2    Sugii, S.3    Ohno-Iwashita, Y.4    Shimada, Y.5    Hickey, W.F.6
  • 60
    • 4944244476 scopus 로고    scopus 로고
    • Axon-dominant localization of cell-surface cholesterol in cultured hippocampal neurons and its disappearance in Niemann-Pick type C model cells
    • Y. Tashiro, T. Yamazaki, Y. Shimada, Y. Ohno-Iwashita, and K. Okamoto Axon-dominant localization of cell-surface cholesterol in cultured hippocampal neurons and its disappearance in Niemann-Pick type C model cells Eur J Neurosci 20 2004 2015 2021
    • (2004) Eur J Neurosci , vol.20 , pp. 2015-2021
    • Tashiro, Y.1    Yamazaki, T.2    Shimada, Y.3    Ohno-Iwashita, Y.4    Okamoto, K.5
  • 61
    • 0026785987 scopus 로고
    • Effect of lipidic factors on membrane cholesterol topology - Mode of binding of theta-toxin to cholesterol in liposomes
    • Y. Ohno-Iwashita, M. Iwamoto, S. Ando, and S. Iwashita Effect of lipidic factors on membrane cholesterol topology - mode of binding of theta-toxin to cholesterol in liposomes Biochim Biophys Acta 1109 1992 81 90
    • (1992) Biochim Biophys Acta , vol.1109 , pp. 81-90
    • Ohno-Iwashita, Y.1    Iwamoto, M.2    Ando, S.3    Iwashita, S.4
  • 62
    • 18744391355 scopus 로고    scopus 로고
    • The C-terminal domain of perfringolysin O is an essential cholesterol-binding unit targeting to cholesterol-rich microdomains
    • Y. Shimada, M. Maruya, S. Iwashita, and Y. Ohno-Iwashita The C-terminal domain of perfringolysin O is an essential cholesterol-binding unit targeting to cholesterol-rich microdomains Eur J Biochem 269 2002 6195 6203
    • (2002) Eur J Biochem , vol.269 , pp. 6195-6203
    • Shimada, Y.1    Maruya, M.2    Iwashita, S.3    Ohno-Iwashita, Y.4
  • 63
    • 0029556088 scopus 로고
    • Dissecting the molecular mechanisms of polarized membrane traffic: Reconstitution of three transport steps in epithelial cells using streptolysin-O permeabilization
    • F. Lafont, K. Simons, and E. Ikonen Dissecting the molecular mechanisms of polarized membrane traffic: reconstitution of three transport steps in epithelial cells using streptolysin-O permeabilization Cold Spring Harb Symp Quant Biol 60 1995 753 762
    • (1995) Cold Spring Harb Symp Quant Biol , vol.60 , pp. 753-762
    • Lafont, F.1    Simons, K.2    Ikonen, E.3
  • 64
    • 0242582327 scopus 로고    scopus 로고
    • Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3′-phosphoadenosine 5′-phosphate Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms
    • K.A. Lee, H. Fuda, Y.C. Lee, M. Negishi, C.A. Strott, and L.C. Pedersen Crystal structure of human cholesterol sulfotransferase (SULT2B1b) in the presence of pregnenolone and 3′-phosphoadenosine 5′-phosphate Rationale for specificity differences between prototypical SULT2A1 and the SULT2BG1 isoforms J Biol Chem 278 2003 44593 44599
    • (2003) J Biol Chem , vol.278 , pp. 44593-44599
    • Lee, K.A.1    Fuda, H.2    Lee, Y.C.3    Negishi, M.4    Strott, C.A.5    Pedersen, L.C.6
  • 65
    • 47749117627 scopus 로고    scopus 로고
    • Crystal structures of substrate-bound and substrate-free cytochrome P450 46A1, the principal cholesterol hydroxylase in the brain
    • N. Mast, M.A. White, I. Bjorkhem, E.F. Johnson, C.D. Stout, and I.A. Pikuleva Crystal structures of substrate-bound and substrate-free cytochrome P450 46A1, the principal cholesterol hydroxylase in the brain Proc Natl Acad Sci U S A 105 2008 9546 9551
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 9546-9551
    • Mast, N.1    White, M.A.2    Bjorkhem, I.3    Johnson, E.F.4    Stout, C.D.5    Pikuleva, I.A.6
  • 67
    • 70449709431 scopus 로고    scopus 로고
    • Cholesterol oxidase: Biochemistry and structural features
    • A. Vrielink, and S. Ghisla Cholesterol oxidase: biochemistry and structural features FEBS J 276 2009 6826 6843
    • (2009) FEBS J , vol.276 , pp. 6826-6843
    • Vrielink, A.1    Ghisla, S.2
  • 68
    • 0024400234 scopus 로고
    • Spontaneous transfer between phospholipid bilayers of dehydroergosterol, a fluorescent cholesterol analog
    • L.K. Bar, P.L. Chong, Y. Barenholz, and T.E. Thompson Spontaneous transfer between phospholipid bilayers of dehydroergosterol, a fluorescent cholesterol analog Biochim Biophys Acta 983 1989 109 112
    • (1989) Biochim Biophys Acta , vol.983 , pp. 109-112
    • Bar, L.K.1    Chong, P.L.2    Barenholz, Y.3    Thompson, T.E.4
  • 69
    • 1642494863 scopus 로고    scopus 로고
    • Cholesterol oxidase senses subtle changes in lipid bilayer structure
    • K.W. Ahn, and N.S. Sampson Cholesterol oxidase senses subtle changes in lipid bilayer structure Biochemistry 43 2004 827 836
    • (2004) Biochemistry , vol.43 , pp. 827-836
    • Ahn, K.W.1    Sampson, N.S.2
  • 70
    • 0024509922 scopus 로고
    • Plasma membranes contain half the phospholipid and 90% of the cholesterol and sphingomyelin in cultured human fibroblasts
    • Y. Lange, M.H. Swaisgood, B.V. Ramos, and T.L. Steck Plasma membranes contain half the phospholipid and 90% of the cholesterol and sphingomyelin in cultured human fibroblasts J Biol Chem 264 1989 3786 3793
    • (1989) J Biol Chem , vol.264 , pp. 3786-3793
    • Lange, Y.1    Swaisgood, M.H.2    Ramos, B.V.3    Steck, T.L.4
  • 71
    • 0025975875 scopus 로고
    • Disposition of intracellular cholesterol in human fibroblasts
    • Y. Lange Disposition of intracellular cholesterol in human fibroblasts J Lipid Res 32 1991 329 339
    • (1991) J Lipid Res , vol.32 , pp. 329-339
    • Lange, Y.1
  • 72
    • 0026596115 scopus 로고
    • Tracking cell cholesterol with cholesterol oxidase
    • Y. Lange Tracking cell cholesterol with cholesterol oxidase J Lipid Res 33 1992 315 321
    • (1992) J Lipid Res , vol.33 , pp. 315-321
    • Lange, Y.1
  • 73
    • 70149124526 scopus 로고    scopus 로고
    • Activation of membrane cholesterol by 63 amphipaths
    • Y. Lange, J. Ye, M.E. Duban, and T.L. Steck Activation of membrane cholesterol by 63 amphipaths Biochemistry 48 2009 8505 8515
    • (2009) Biochemistry , vol.48 , pp. 8505-8515
    • Lange, Y.1    Ye, J.2    Duban, M.E.3    Steck, T.L.4
  • 74
    • 0021341798 scopus 로고
    • Cholesterol oxidase susceptibility of the red cell membrane
    • Y. Lange, H. Matthies, and T.L. Steck Cholesterol oxidase susceptibility of the red cell membrane Biochim Biophys Acta 769 1984 551 562
    • (1984) Biochim Biophys Acta , vol.769 , pp. 551-562
    • Lange, Y.1    Matthies, H.2    Steck, T.L.3
  • 75
    • 0024419722 scopus 로고
    • Effects of sphingomyelin degradation on cell cholesterol oxidizability and steady-state distribution between the cell surface and the cell interior
    • J.P. Slotte, G. Hedstrom, S. Rannstrom, and S. Ekman Effects of sphingomyelin degradation on cell cholesterol oxidizability and steady-state distribution between the cell surface and the cell interior Biochim Biophys Acta 985 1989 90 96
    • (1989) Biochim Biophys Acta , vol.985 , pp. 90-96
    • Slotte, J.P.1    Hedstrom, G.2    Rannstrom, S.3    Ekman, S.4
  • 76
    • 27744514250 scopus 로고    scopus 로고
    • Activation of membrane cholesterol by displacement from phospholipids
    • Y. Lange, J. Ye, and T.L. Steck Activation of membrane cholesterol by displacement from phospholipids J Biol Chem 280 2005 36126 36131
    • (2005) J Biol Chem , vol.280 , pp. 36126-36131
    • Lange, Y.1    Ye, J.2    Steck, T.L.3
  • 77
    • 0034682556 scopus 로고    scopus 로고
    • Chemical activity of cholesterol in membranes
    • A. Radhakrishnan, and H.M. McConnell Chemical activity of cholesterol in membranes Biochemistry 39 2000 8119 8124
    • (2000) Biochemistry , vol.39 , pp. 8119-8124
    • Radhakrishnan, A.1    McConnell, H.M.2
  • 78
    • 4143069270 scopus 로고    scopus 로고
    • How cholesterol homeostasis is regulated by plasma membrane cholesterol in excess of phospholipids
    • Y. Lange, J. Ye, and T.L. Steck How cholesterol homeostasis is regulated by plasma membrane cholesterol in excess of phospholipids Proc Natl Acad Sci U S A 101 2004 11664 11667
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 11664-11667
    • Lange, Y.1    Ye, J.2    Steck, T.L.3
  • 79
    • 24044483233 scopus 로고    scopus 로고
    • ABCG1 redistributes cell cholesterol to domains removable by high density lipoprotein but not by lipid-depleted apolipoproteins
    • A.M. Vaughan, and J.F. Oram ABCG1 redistributes cell cholesterol to domains removable by high density lipoprotein but not by lipid-depleted apolipoproteins J Biol Chem 280 2005 30150 30157
    • (2005) J Biol Chem , vol.280 , pp. 30150-30157
    • Vaughan, A.M.1    Oram, J.F.2
  • 80
    • 0028125208 scopus 로고
    • Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation
    • E.J. Smart, Y.S. Ying, P.A. Conrad, and R.G. Anderson Caveolin moves from caveolae to the Golgi apparatus in response to cholesterol oxidation J Cell Biol 127 1994 1185 1197
    • (1994) J Cell Biol , vol.127 , pp. 1185-1197
    • Smart, E.J.1    Ying, Y.S.2    Conrad, P.A.3    Anderson, R.G.4
  • 81
    • 0034097133 scopus 로고    scopus 로고
    • Cholesterol oxidation switches the internalization pathway of endothelin receptor type A from caveolae to clathrin-coated pits in Chinese hamster ovary cells
    • Y. Okamoto, H. Ninomiya, S. Miwa, and T. Masaki Cholesterol oxidation switches the internalization pathway of endothelin receptor type A from caveolae to clathrin-coated pits in Chinese hamster ovary cells J Biol Chem 275 2000 6439 6446
    • (2000) J Biol Chem , vol.275 , pp. 6439-6446
    • Okamoto, Y.1    Ninomiya, H.2    Miwa, S.3    Masaki, T.4
  • 82
    • 0025268384 scopus 로고
    • Cholesterol oxidase catalyzed oxidation of cholesterol in mixed lipid monolayers: Effects of surface pressure and phospholipid composition on catalytic activity
    • L. Gronberg, and J.P. Slotte Cholesterol oxidase catalyzed oxidation of cholesterol in mixed lipid monolayers: effects of surface pressure and phospholipid composition on catalytic activity Biochemistry 29 1990 3173 3178
    • (1990) Biochemistry , vol.29 , pp. 3173-3178
    • Gronberg, L.1    Slotte, J.P.2
  • 83
    • 0034620610 scopus 로고    scopus 로고
    • The effect of sterol structure on membrane lipid domains reveals how cholesterol can induce lipid domain formation
    • X. Xu, and E. London The effect of sterol structure on membrane lipid domains reveals how cholesterol can induce lipid domain formation Biochemistry 39 2000 843 849
    • (2000) Biochemistry , vol.39 , pp. 843-849
    • Xu, X.1    London, E.2
  • 84
    • 1842848068 scopus 로고    scopus 로고
    • X-ray structure of the hRORalpha LBD at 1.63 A: Structural and functional data that cholesterol or a cholesterol derivative is the natural ligand of RORalpha
    • J.A. Kallen, J.M. Schlaeppi, F. Bitsch, S. Geisse, M. Geiser, and I. Delhon X-ray structure of the hRORalpha LBD at 1.63 A: structural and functional data that cholesterol or a cholesterol derivative is the natural ligand of RORalpha Structure 10 2002 1697 1707
    • (2002) Structure , vol.10 , pp. 1697-1707
    • Kallen, J.A.1    Schlaeppi, J.M.2    Bitsch, F.3    Geisse, S.4    Geiser, M.5    Delhon, I.6
  • 85
    • 43249129470 scopus 로고    scopus 로고
    • The binding and release of oxygen and hydrogen peroxide are directed by a hydrophobic tunnel in cholesterol oxidase
    • L. Chen, A.Y. Lyubimov, L. Brammer, A. Vrielink, and N.S. Sampson The binding and release of oxygen and hydrogen peroxide are directed by a hydrophobic tunnel in cholesterol oxidase Biochemistry 47 2008 5368 5377
    • (2008) Biochemistry , vol.47 , pp. 5368-5377
    • Chen, L.1    Lyubimov, A.Y.2    Brammer, L.3    Vrielink, A.4    Sampson, N.S.5
  • 86
    • 24344455560 scopus 로고    scopus 로고
    • Structural mechanism for sterol sensing and transport by OSBP-related proteins
    • Y.J. Im, S. Raychaudhuri, W.A. Prinz, and J.H. Hurley Structural mechanism for sterol sensing and transport by OSBP-related proteins Nature 437 2005 154 158
    • (2005) Nature , vol.437 , pp. 154-158
    • Im, Y.J.1    Raychaudhuri, S.2    Prinz, W.A.3    Hurley, J.H.4
  • 87
    • 0033542422 scopus 로고    scopus 로고
    • A porcine homolog of the major secretory protein of human epididymis HE1, specifically binds cholesterol
    • N. Okamura, S. Kiuchi, M. Tamba, T. Kashima, S. Hiramoto, and T. Baba A porcine homolog of the major secretory protein of human epididymis HE1, specifically binds cholesterol Biochim Biophys Acta 1438 1999 377 387
    • (1999) Biochim Biophys Acta , vol.1438 , pp. 377-387
    • Okamura, N.1    Kiuchi, S.2    Tamba, M.3    Kashima, T.4    Hiramoto, S.5    Baba, T.6
  • 88
    • 0344838432 scopus 로고    scopus 로고
    • The integrity of a cholesterol-binding pocket in Niemann-Pick C2 protein is necessary to control lysosome cholesterol levels
    • D.C. Ko, J. Binkley, A. Sidow, and M.P. Scott The integrity of a cholesterol-binding pocket in Niemann-Pick C2 protein is necessary to control lysosome cholesterol levels Proc Natl Acad Sci U S A 2003
    • (2003) Proc Natl Acad Sci U S A
    • Ko, D.C.1    Binkley, J.2    Sidow, A.3    Scott, M.P.4
  • 89
    • 55749083068 scopus 로고    scopus 로고
    • NPC2 facilitates bidirectional transfer of cholesterol between NPC1 and lipid bilayers, a step in cholesterol egress from lysosomes
    • R.E. Infante, M.L. Wang, A. Radhakrishnan, H.J. Kwon, M.S. Brown, and J.L. Goldstein NPC2 facilitates bidirectional transfer of cholesterol between NPC1 and lipid bilayers, a step in cholesterol egress from lysosomes Proc Natl Acad Sci U S A 105 2008 15287 15292
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 15287-15292
    • Infante, R.E.1    Wang, M.L.2    Radhakrishnan, A.3    Kwon, H.J.4    Brown, M.S.5    Goldstein, J.L.6
  • 90
    • 0037418188 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding protein deficient in Niemann-Pick type C2 disease
    • N. Friedland, H.L. Liou, P. Lobel, and A.M. Stock Structure of a cholesterol-binding protein deficient in Niemann-Pick type C2 disease Proc Natl Acad Sci U S A 100 2003 2512 2517
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 2512-2517
    • Friedland, N.1    Liou, H.L.2    Lobel, P.3    Stock, A.M.4
  • 91
    • 33845994402 scopus 로고    scopus 로고
    • NPC2, the protein deficient in Niemann-Pick C2 disease, consists of multiple glycoforms that bind a variety of sterols
    • H.L. Liou, S.S. Dixit, S. Xu, G.S. Tint, A.M. Stock, and P. Lobel NPC2, the protein deficient in Niemann-Pick C2 disease, consists of multiple glycoforms that bind a variety of sterols J Biol Chem 281 2006 36710 36723
    • (2006) J Biol Chem , vol.281 , pp. 36710-36723
    • Liou, H.L.1    Dixit, S.S.2    Xu, S.3    Tint, G.S.4    Stock, A.M.5    Lobel, P.6
  • 92
    • 33750318425 scopus 로고    scopus 로고
    • Mechanism of cholesterol transfer from the Niemann-Pick type C2 protein to model membranes supports a role in lysosomal cholesterol transport
    • S.R. Cheruku, Z. Xu, R. Dutia, P. Lobel, and J. Storch Mechanism of cholesterol transfer from the Niemann-Pick type C2 protein to model membranes supports a role in lysosomal cholesterol transport J Biol Chem 281 2006 31594 31604
    • (2006) J Biol Chem , vol.281 , pp. 31594-31604
    • Cheruku, S.R.1    Xu, Z.2    Dutia, R.3    Lobel, P.4    Storch, J.5
  • 93
    • 0036534286 scopus 로고    scopus 로고
    • The sterol-sensing domain: Multiple families, a unique role?
    • P.E. Kuwabara, and M. Labouesse The sterol-sensing domain: multiple families, a unique role? Trends Genet 18 2002 193 201
    • (2002) Trends Genet , vol.18 , pp. 193-201
    • Kuwabara, P.E.1    Labouesse, M.2
  • 94
    • 4344637102 scopus 로고    scopus 로고
    • Binding between the Niemann-Pick C1 protein and a photoactivatable cholesterol analog requires a functional sterol-sensing domain
    • N. Ohgami, D.C. Ko, M. Thomas, M.P. Scott, C.C. Chang, and T.Y. Chang Binding between the Niemann-Pick C1 protein and a photoactivatable cholesterol analog requires a functional sterol-sensing domain Proc Natl Acad Sci U S A 101 2004 12473 12478
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 12473-12478
    • Ohgami, N.1    Ko, D.C.2    Thomas, M.3    Scott, M.P.4    Chang, C.C.5    Chang, T.Y.6
  • 96
    • 67549105629 scopus 로고    scopus 로고
    • Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol
    • H.J. Kwon, L. Abi-Mosleh, M.L. Wang, J. Deisenhofer, J.L. Goldstein, and M.S. Brown Structure of N-terminal domain of NPC1 reveals distinct subdomains for binding and transfer of cholesterol Cell 137 2009 1213 1224
    • (2009) Cell , vol.137 , pp. 1213-1224
    • Kwon, H.J.1    Abi-Mosleh, L.2    Wang, M.L.3    Deisenhofer, J.4    Goldstein, J.L.5    Brown, M.S.6
  • 97
    • 0034064138 scopus 로고    scopus 로고
    • Structure and lipid transport mechanism of a StAR-related domain
    • Y. Tsujishita, and J.H. Hurley Structure and lipid transport mechanism of a StAR-related domain Nat Struct Biol 7 2000 408 414
    • (2000) Nat Struct Biol , vol.7 , pp. 408-414
    • Tsujishita, Y.1    Hurley, J.H.2
  • 98
    • 0035970108 scopus 로고    scopus 로고
    • Cholesterol binding at the cholesterol recognition/interaction amino acid consensus (CRAC) of the peripheral-type benzodiazepine receptor and inhibition of steroidogenesis by an HIV TAT-CRAC peptide
    • H. Li, Z. Yao, B. Degenhardt, G. Teper, and V. Papadopoulos Cholesterol binding at the cholesterol recognition/interaction amino acid consensus (CRAC) of the peripheral-type benzodiazepine receptor and inhibition of steroidogenesis by an HIV TAT-CRAC peptide Proc Natl Acad Sci U S A 98 2001 1267 1272
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 1267-1272
    • Li, H.1    Yao, Z.2    Degenhardt, B.3    Teper, G.4    Papadopoulos, V.5
  • 99
    • 77952305288 scopus 로고    scopus 로고
    • Cholesterol interaction with proteins that partition into membrane domains: An overview
    • R.M. Epand, A. Thomas, R. Brasseur, and R.F. Epand Cholesterol interaction with proteins that partition into membrane domains: an overview Subcell Biochem 51 2010 253 278
    • (2010) Subcell Biochem , vol.51 , pp. 253-278
    • Epand, R.M.1    Thomas, A.2    Brasseur, R.3    Epand, R.F.4
  • 100
    • 44649172481 scopus 로고    scopus 로고
    • A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor
    • M.A. Hanson, V. Cherezov, M.T. Griffith, C.B. Roth, V.P. Jaakola, and E.Y. Chien A specific cholesterol binding site is established by the 2.8 A structure of the human beta2-adrenergic receptor Structure 16 2008 897 905
    • (2008) Structure , vol.16 , pp. 897-905
    • Hanson, M.A.1    Cherezov, V.2    Griffith, M.T.3    Roth, C.B.4    Jaakola, V.P.5    Chien, E.Y.6
  • 101
    • 38149069055 scopus 로고    scopus 로고
    • Purified NPC1 protein I. Binding of cholesterol and oxysterols to a 1278-amino acid membrane protein
    • R.E. Infante, L. Abi-Mosleh, A. Radhakrishnan, J.D. Dale, M.S. Brown, and J.L. Goldstein Purified NPC1 protein I. Binding of cholesterol and oxysterols to a 1278-amino acid membrane protein J Biol Chem 283 2008 1052 1063
    • (2008) J Biol Chem , vol.283 , pp. 1052-1063
    • Infante, R.E.1    Abi-Mosleh, L.2    Radhakrishnan, A.3    Dale, J.D.4    Brown, M.S.5    Goldstein, J.L.6
  • 102
    • 0037164705 scopus 로고    scopus 로고
    • Identification of a conserved domain of the HIV-1 transmembrane protein gp41 which interacts with cholesteryl groups
    • N. Vincent, C. Genin, and E. Malvoisin Identification of a conserved domain of the HIV-1 transmembrane protein gp41 which interacts with cholesteryl groups Biochim Biophys Acta 1567 2002 157 164
    • (2002) Biochim Biophys Acta , vol.1567 , pp. 157-164
    • Vincent, N.1    Genin, C.2    Malvoisin, E.3
  • 103
    • 37049016678 scopus 로고    scopus 로고
    • Sigma-1 receptors bind cholesterol and remodel lipid rafts in breast cancer cell lines
    • C.P. Palmer, R. Mahen, E. Schnell, M.B. Djamgoz, and E. Aydar Sigma-1 receptors bind cholesterol and remodel lipid rafts in breast cancer cell lines Cancer Res 67 2007 11166 11175
    • (2007) Cancer Res , vol.67 , pp. 11166-11175
    • Palmer, C.P.1    Mahen, R.2    Schnell, E.3    Djamgoz, M.B.4    Aydar, E.5
  • 105
    • 50949123980 scopus 로고    scopus 로고
    • Intracellular cholesterol transporter StarD4 binds free cholesterol and increases cholesteryl ester formation
    • D. Rodriguez-Agudo, S. Ren, E. Wong, D. Marques, K. Redford, and G. Gil Intracellular cholesterol transporter StarD4 binds free cholesterol and increases cholesteryl ester formation J Lipid Res 49 2008 1409 1419
    • (2008) J Lipid Res , vol.49 , pp. 1409-1419
    • Rodriguez-Agudo, D.1    Ren, S.2    Wong, E.3    Marques, D.4    Redford, K.5    Gil, G.6
  • 106
    • 3242668095 scopus 로고    scopus 로고
    • Direct binding of cholesterol to the purified membrane region of SCAP: Mechanism for a sterol-sensing domain
    • A. Radhakrishnan, L.P. Sun, H.J. Kwon, M.S. Brown, and J.L. Goldstein Direct binding of cholesterol to the purified membrane region of SCAP: mechanism for a sterol-sensing domain Mol Cell 15 2004 259 268
    • (2004) Mol Cell , vol.15 , pp. 259-268
    • Radhakrishnan, A.1    Sun, L.P.2    Kwon, H.J.3    Brown, M.S.4    Goldstein, J.L.5
  • 107
    • 0022999003 scopus 로고
    • Physical properties of the fluorescent sterol probe dehydroergosterol
    • G. Smutzer, B.F. Crawford, and P.L. Yeagle Physical properties of the fluorescent sterol probe dehydroergosterol Biochim Biophys Acta 862 1986 361 371
    • (1986) Biochim Biophys Acta , vol.862 , pp. 361-371
    • Smutzer, G.1    Crawford, B.F.2    Yeagle, P.L.3
  • 109
    • 0030037450 scopus 로고    scopus 로고
    • Spontaneous and protein-mediated sterol transfer between intracellular membranes
    • A. Frolov, J.K. Woodford, E.J. Murphy, J.T. Billheimer, and F. Schroeder Spontaneous and protein-mediated sterol transfer between intracellular membranes J Biol Chem 271 1996 16075 16083
    • (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
  • 110
    • 67349204082 scopus 로고    scopus 로고
    • The fluorescent cholesterol analog dehydroergosterol induces liquid-ordered domains in model membranes
    • O. Garvik, P. Benediktson, A.C. Simonsen, J.H. Ipsen, and D. Wustner The fluorescent cholesterol analog dehydroergosterol induces liquid-ordered domains in model membranes Chem Phys Lipids 159 2009 114 118
    • (2009) Chem Phys Lipids , vol.159 , pp. 114-118
    • Garvik, O.1    Benediktson, P.2    Simonsen, A.C.3    Ipsen, J.H.4    Wustner, D.5
  • 111
    • 0034724682 scopus 로고    scopus 로고
    • High density lipoprotein-mediated cholesterol uptake and targeting to lipid droplets in intact L-cell fibroblasts A single- and multiphoton fluorescence approach
    • A. Frolov, A. Petrescu, B.P. Atshaves, P.T. So, E. Gratton, and G. Serrero High density lipoprotein-mediated cholesterol uptake and targeting to lipid droplets in intact L-cell fibroblasts A single- and multiphoton fluorescence approach J Biol Chem 275 2000 12769 12780
    • (2000) J Biol Chem , vol.275 , pp. 12769-12780
    • Frolov, A.1    Petrescu, A.2    Atshaves, B.P.3    So, P.T.4    Gratton, E.5    Serrero, G.6
  • 112
    • 0031687965 scopus 로고    scopus 로고
    • Cholesterol distribution in living cells: Fluorescence imaging using dehydroergosterol as a fluorescent cholesterol analog
    • S. Mukherjee, X. Zha, I. Tabas, and F.R. Maxfield Cholesterol distribution in living cells: fluorescence imaging using dehydroergosterol as a fluorescent cholesterol analog Biophys J 75 1998 1915 1925
    • (1998) Biophys J , vol.75 , pp. 1915-1925
    • Mukherjee, S.1    Zha, X.2    Tabas, I.3    Maxfield, F.R.4
  • 113
    • 0037016677 scopus 로고    scopus 로고
    • Vesicular and non-vesicular sterol transport in living cells the endocytic recycling compartment is a major sterol storage organelle
    • M. Hao, S.X. Lin, O.J. Karylowski, D. Wustner, T.E. McGraw, and F.R. Maxfield Vesicular and non-vesicular sterol transport in living cells The endocytic recycling compartment is a major sterol storage organelle J Biol Chem 277 2002 609 617
    • (2002) J Biol Chem , vol.277 , pp. 609-617
    • Hao, M.1    Lin, S.X.2    Karylowski, O.J.3    Wustner, D.4    McGraw, T.E.5    Maxfield, F.R.6
  • 114
    • 0037119406 scopus 로고    scopus 로고
    • Rapid nonvesicular transport of sterol between the plasma membrane domains of polarized hepatic cells
    • D. Wustner, A. Herrmann, M. Hao, and F.R. Maxfield Rapid nonvesicular transport of sterol between the plasma membrane domains of polarized hepatic cells J Biol Chem 277 2002 30325 30336
    • (2002) J Biol Chem , vol.277 , pp. 30325-30336
    • Wustner, D.1    Herrmann, A.2    Hao, M.3    Maxfield, F.R.4
  • 115
    • 0037458554 scopus 로고    scopus 로고
    • Fluorescence and multiphoton imaging resolve unique structural forms of sterol in membranes of living cells
    • A.L. McIntosh, A.M. Gallegos, B.P. Atshaves, S.M. Storey, D. Kannoju, and F. Schroeder Fluorescence and multiphoton imaging resolve unique structural forms of sterol in membranes of living cells J Biol Chem 278 2003 6384 6403
    • (2003) J Biol Chem , vol.278 , pp. 6384-6403
    • McIntosh, A.L.1    Gallegos, A.M.2    Atshaves, B.P.3    Storey, S.M.4    Kannoju, D.5    Schroeder, F.6
  • 116
    • 12144286290 scopus 로고    scopus 로고
    • Different transport routes for high density lipoprotein and its associated free sterol in polarized hepatic cells
    • D. Wustner, M. Mondal, A. Huang, and F.R. Maxfield Different transport routes for high density lipoprotein and its associated free sterol in polarized hepatic cells J Lipid Res 45 2004 427 437
    • (2004) J Lipid Res , vol.45 , pp. 427-437
    • Wustner, D.1    Mondal, M.2    Huang, A.3    Maxfield, F.R.4
  • 117
    • 14344265621 scopus 로고    scopus 로고
    • Structural analysis of sterol distributions in the plasma membrane of living cells
    • W. Zhang, A.L. McIntosh, H. Xu, D. Wu, T. Gruninger, and B. Atshaves Structural analysis of sterol distributions in the plasma membrane of living cells Biochemistry 44 2005 2864 2884
    • (2005) Biochemistry , vol.44 , pp. 2864-2884
    • Zhang, W.1    McIntosh, A.L.2    Xu, H.3    Wu, D.4    Gruninger, T.5    Atshaves, B.6
  • 118
    • 33846056461 scopus 로고    scopus 로고
    • Plasma membrane sterol distribution resembles the surface topography of living cells
    • D. Wustner Plasma membrane sterol distribution resembles the surface topography of living cells Mol Biol Cell 18 2007 211 228
    • (2007) Mol Biol Cell , vol.18 , pp. 211-228
    • Wustner, D.1
  • 119
    • 33846224732 scopus 로고    scopus 로고
    • Sterol, protein and lipid trafficking in chinese hamster ovary cells with niemann-pick type C1 defect
    • N.H. Pipalia, M. Hao, S. Mukherjee, and F.R. Maxfield Sterol, protein and lipid trafficking in chinese hamster ovary cells with niemann-pick type C1 defect Traffic 8 2007 130 141
    • (2007) Traffic , vol.8 , pp. 130-141
    • Pipalia, N.H.1    Hao, M.2    Mukherjee, S.3    Maxfield, F.R.4
  • 120
    • 61949446361 scopus 로고    scopus 로고
    • Sterols are mainly in the cytoplasmic leaflet of the plasma membrane and the endocytic recycling compartment in CHO cells
    • M. Mondal, B. Mesmin, S. Mukherjee, and F.R. Maxfield Sterols are mainly in the cytoplasmic leaflet of the plasma membrane and the endocytic recycling compartment in CHO cells Mol Biol Cell 20 2009 581 588
    • (2009) Mol Biol Cell , vol.20 , pp. 581-588
    • Mondal, M.1    Mesmin, B.2    Mukherjee, S.3    Maxfield, F.R.4
  • 121
    • 77951780747 scopus 로고    scopus 로고
    • Selective visualization of fluorescent sterols in Caenorhabditis elegans by bleach-rate-based image segmentation
    • D. Wustner, L.A. Landt, N.J. Faergeman, J.R. Brewer, and D. Sage Selective visualization of fluorescent sterols in Caenorhabditis elegans by bleach-rate-based image segmentation Traffic 11 2010 440 454
    • (2010) Traffic , vol.11 , pp. 440-454
    • Wustner, D.1    Landt, L.A.2    Faergeman, N.J.3    Brewer, J.R.4    Sage, D.5
  • 122
    • 0026077765 scopus 로고
    • Selective binding of cholesterol by recombinant fatty acid binding proteins
    • G. Nemecz, and F. Schroeder Selective binding of cholesterol by recombinant fatty acid binding proteins J Biol Chem 266 1991 17180 17186
    • (1991) J Biol Chem , vol.266 , pp. 17180-17186
    • Nemecz, G.1    Schroeder, F.2
  • 123
    • 0025129177 scopus 로고
    • Interaction of fluorescent delta 5,7,9(11),22-ergostatetraen-3 beta-ol with sterol carrier protein-2
    • F. Schroeder, P. Butko, G. Nemecz, and T.J. Scallen Interaction of fluorescent delta 5,7,9(11),22-ergostatetraen-3 beta-ol with sterol carrier protein-2 J Biol Chem 265 1990 151 157
    • (1990) J Biol Chem , vol.265 , pp. 151-157
    • Schroeder, F.1    Butko, P.2    Nemecz, G.3    Scallen, T.J.4
  • 124
    • 59449095489 scopus 로고    scopus 로고
    • Characterization of fluorescent sterol binding to purified human NPC1
    • R. Liu, P. Lu, J.W. Chu, and F.J. Sharom Characterization of fluorescent sterol binding to purified human NPC1 J Biol Chem 284 2009 1840 1852
    • (2009) J Biol Chem , vol.284 , pp. 1840-1852
    • Liu, R.1    Lu, P.2    Chu, J.W.3    Sharom, F.J.4
  • 125
    • 0020110451 scopus 로고
    • Cholestatriene and ergostatetraene as in vivo and in vitro membrane and lipoprotein probes
    • R.J. Bergeron, and J. Scott Cholestatriene and ergostatetraene as in vivo and in vitro membrane and lipoprotein probes J Lipid Res 23 1982 391 404
    • (1982) J Lipid Res , vol.23 , pp. 391-404
    • Bergeron, R.J.1    Scott, J.2
  • 126
    • 0021923008 scopus 로고
    • Sterol and squalene carrier protein interactions with fluorescent delta 5,7,9(11)-cholestatrien-3 beta-ol
    • F. Schroeder, M.E. Dempsey, and R.T. Fischer Sterol and squalene carrier protein interactions with fluorescent delta 5,7,9(11)-cholestatrien-3 beta-ol J Biol Chem 260 1985 2904 2911
    • (1985) J Biol Chem , vol.260 , pp. 2904-2911
    • Schroeder, F.1    Dempsey, M.E.2    Fischer, R.T.3
  • 127
    • 0023794590 scopus 로고
    • A fluorescence and radiolabel study of sterol exchange between membranes
    • G. Nemecz, R.N. Fontaine, and F. Schroeder A fluorescence and radiolabel study of sterol exchange between membranes Biochim Biophys Acta 943 1988 511 521
    • (1988) Biochim Biophys Acta , vol.943 , pp. 511-521
    • Nemecz, G.1    Fontaine, R.N.2    Schroeder, F.3
  • 128
    • 0242580832 scopus 로고    scopus 로고
    • The potential of fluorescent and spin-labeled steroid analogs to mimic natural cholesterol
    • H.A. Scheidt, P. Muller, A. Herrmann, and D. Huster The potential of fluorescent and spin-labeled steroid analogs to mimic natural cholesterol J Biol Chem 278 2003 45563 45569
    • (2003) J Biol Chem , vol.278 , pp. 45563-45569
    • Scheidt, H.A.1    Muller, P.2    Herrmann, A.3    Huster, D.4
  • 129
    • 0021527179 scopus 로고
    • Delta 5,7,9(11)-Cholestatrien-3 beta-ol: A fluorescent cholesterol analogue
    • R.T. Fischer, F.A. Stephenson, and A. Shafiee Schroeder F. delta 5,7,9(11)-Cholestatrien-3 beta-ol: a fluorescent cholesterol analogue Chem Phys Lipids 36 1984 1 14
    • (1984) Chem Phys Lipids , vol.36 , pp. 1-14
    • Fischer, R.T.1    Stephenson, F.A.2    Shafiee, A.3    Schroeder, F.4
  • 130
    • 0024103191 scopus 로고
    • Fluorescence properties of cholestatrienol in phosphatidylcholine bilayer vesicles
    • F. Schroeder, G. Nemecz, E. Gratton, Y. Barenholz, and T.E. Thompson Fluorescence properties of cholestatrienol in phosphatidylcholine bilayer vesicles Biophys Chem 32 1988 57 72
    • (1988) Biophys Chem , vol.32 , pp. 57-72
    • Schroeder, F.1    Nemecz, G.2    Gratton, E.3    Barenholz, Y.4    Thompson, T.E.5
  • 131
    • 0025017861 scopus 로고
    • Organization and interaction of cholesterol and phosphatidylcholine in model bilayer membranes
    • P.A. Hyslop, B. Morel, and R.D. Sauerheber Organization and interaction of cholesterol and phosphatidylcholine in model bilayer membranes Biochemistry 29 1990 1025 1038
    • (1990) Biochemistry , vol.29 , pp. 1025-1038
    • Hyslop, P.A.1    Morel, B.2    Sauerheber, R.D.3
  • 133
    • 22244441444 scopus 로고    scopus 로고
    • Domain formation and stability in complex lipid bilayers as reported by cholestatrienol
    • Y.J. Bjorkqvist, T.K. Nyholm, J.P. Slotte, and B. Ramstedt Domain formation and stability in complex lipid bilayers as reported by cholestatrienol Biophys J 88 2005 4054 4063
    • (2005) Biophys J , vol.88 , pp. 4054-4063
    • Bjorkqvist, Y.J.1    Nyholm, T.K.2    Slotte, J.P.3    Ramstedt, B.4
  • 134
    • 77649253111 scopus 로고    scopus 로고
    • Sterol affinity for bilayer membranes is affected by their ceramide content and the ceramide chain length
    • T.K. Nyholm, P.M. Grandell, B. Westerlund, and J.P. Slotte Sterol affinity for bilayer membranes is affected by their ceramide content and the ceramide chain length Biochim Biophys Acta 1798 2010 1008 1013
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 1008-1013
    • Nyholm, T.K.1    Grandell, P.M.2    Westerlund, B.3    Slotte, J.P.4
  • 135
    • 33646083929 scopus 로고    scopus 로고
    • Effect of anti-tumor ether lipids on ordered domains in model membranes
    • B. Heczkova, and J.P. Slotte Effect of anti-tumor ether lipids on ordered domains in model membranes FEBS Lett 580 2006 2471 2476
    • (2006) FEBS Lett , vol.580 , pp. 2471-2476
    • Heczkova, B.1    Slotte, J.P.2
  • 136
    • 33750605418 scopus 로고    scopus 로고
    • Uptake of cholesterol by the retina occurs primarily via a low density lipoprotein receptor-mediated process
    • N. Tserentsoodol, J. Sztein, M. Campos, N.V. Gordiyenko, R.N. Fariss, and J.W. Lee Uptake of cholesterol by the retina occurs primarily via a low density lipoprotein receptor-mediated process Mol Vis 12 2006 1306 1318
    • (2006) Mol Vis , vol.12 , pp. 1306-1318
    • Tserentsoodol, N.1    Sztein, J.2    Campos, M.3    Gordiyenko, N.V.4    Fariss, R.N.5    Lee, J.W.6
  • 137
    • 0025366661 scopus 로고
    • Chemistry and biology of N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)-labeled lipids: Fluorescent probes of biological and model membranes
    • A. Chattopadhyay Chemistry and biology of N-(7-nitrobenz-2-oxa-1,3- diazol-4-yl)-labeled lipids: fluorescent probes of biological and model membranes Chem Phys Lipids 53 1990 1 15
    • (1990) Chem Phys Lipids , vol.53 , pp. 1-15
    • Chattopadhyay, A.1
  • 138
    • 0035795019 scopus 로고    scopus 로고
    • Exclusion of a cholesterol analog from the cholesterol-rich phase in model membranes
    • L.M. Loura, A. Fedorov, and M. Prieto Exclusion of a cholesterol analog from the cholesterol-rich phase in model membranes Biochim Biophys Acta 1511 2001 236 243
    • (2001) Biochim Biophys Acta , vol.1511 , pp. 236-243
    • Loura, L.M.1    Fedorov, A.2    Prieto, M.3
  • 139
    • 0023652259 scopus 로고
    • Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids
    • A. Chattopadhyay, and E. London Parallax method for direct measurement of membrane penetration depth utilizing fluorescence quenching by spin-labeled phospholipids Biochemistry 26 1987 39 45
    • (1987) Biochemistry , vol.26 , pp. 39-45
    • Chattopadhyay, A.1    London, E.2
  • 140
    • 0024281192 scopus 로고
    • Spectroscopic and ionization properties of N-(7-nitrobenz-2-oxa-1,3- diazol-4-yl)-labeled lipids in model membranes
    • A. Chattopadhyay, and E. London Spectroscopic and ionization properties of N-(7-nitrobenz-2-oxa-1,3-diazol-4-yl)-labeled lipids in model membranes Biochim Biophys Acta 938 1988 24 34
    • (1988) Biochim Biophys Acta , vol.938 , pp. 24-34
    • Chattopadhyay, A.1    London, E.2
  • 141
    • 0030071622 scopus 로고    scopus 로고
    • Membrane organization at low cholesterol concentrations: A study using 7-nitrobenz-2-oxa-1,3-diazol-4-yl-labeled cholesterol
    • S. Mukherjee, and A. Chattopadhyay Membrane organization at low cholesterol concentrations: a study using 7-nitrobenz-2-oxa-1,3-diazol-4-yl- labeled cholesterol Biochemistry 35 1996 1311 1322
    • (1996) Biochemistry , vol.35 , pp. 1311-1322
    • Mukherjee, S.1    Chattopadhyay, A.2
  • 142
    • 0034810547 scopus 로고    scopus 로고
    • Cholesterol organization in membranes at low concentrations: Effects of curvature stress and membrane thickness
    • R. Rukmini, S.S. Rawat, S.C. Biswas, and A. Chattopadhyay Cholesterol organization in membranes at low concentrations: effects of curvature stress and membrane thickness Biophys J 81 2001 2122 2134
    • (2001) Biophys J , vol.81 , pp. 2122-2134
    • Rukmini, R.1    Rawat, S.S.2    Biswas, S.C.3    Chattopadhyay, A.4
  • 144
    • 0026328559 scopus 로고
    • Fluorescence assay for phospholipid membrane asymmetry
    • J.C. McIntyre, and R.G. Sleight Fluorescence assay for phospholipid membrane asymmetry Biochemistry 30 1991 11819 11827
    • (1991) Biochemistry , vol.30 , pp. 11819-11827
    • McIntyre, J.C.1    Sleight, R.G.2
  • 145
    • 0037089350 scopus 로고    scopus 로고
    • Protein-disulfide isomerase is a component of an NBD-cholesterol monomerizing protein complex from hamster small intestine
    • T.Q. Cai, Q. Guo, B. Wong, D. Milot, L. Zhang, and S.D. Wright Protein-disulfide isomerase is a component of an NBD-cholesterol monomerizing protein complex from hamster small intestine Biochim Biophys Acta 1581 2002 100 108
    • (2002) Biochim Biophys Acta , vol.1581 , pp. 100-108
    • Cai, T.Q.1    Guo, Q.2    Wong, B.3    Milot, D.4    Zhang, L.5    Wright, S.D.6
  • 146
    • 0027533511 scopus 로고
    • Cholesterol deprivation affects the fluorescence properties of a ceramide analog at the Golgi apparatus of living cells
    • O.C. Martin, M.E. Comly, E.J. Blanchette-Mackie, P.G. Pentchev, and R.E. Pagano Cholesterol deprivation affects the fluorescence properties of a ceramide analog at the Golgi apparatus of living cells Proc Natl Acad Sci U S A 90 1993 2661 2665
    • (1993) Proc Natl Acad Sci U S A , vol.90 , pp. 2661-2665
    • Martin, O.C.1    Comly, M.E.2    Blanchette-Mackie, E.J.3    Pentchev, P.G.4    Pagano, R.E.5
  • 148
    • 0035813102 scopus 로고    scopus 로고
    • Steroidogenic acute regulatory protein binds cholesterol and modulates mitochondrial membrane sterol domain dynamics
    • A.D. Petrescu, A.M. Gallegos, Y. Okamura, J.F. Strauss III, and F. Schroeder Steroidogenic acute regulatory protein binds cholesterol and modulates mitochondrial membrane sterol domain dynamics J Biol Chem 276 2001 36970 36982
    • (2001) J Biol Chem , vol.276 , pp. 36970-36982
    • Petrescu, A.D.1    Gallegos, A.M.2    Okamura, Y.3    Strauss III, J.F.4    Schroeder, F.5
  • 149
    • 0034711303 scopus 로고    scopus 로고
    • Sterol carrier protein-2 alters high density lipoprotein-mediated cholesterol efflux
    • B.P. Atshaves, O. Starodub, A. McIntosh, A. Petrescu, J.B. Roths, and A.B. Kier Sterol carrier protein-2 alters high density lipoprotein-mediated cholesterol efflux J Biol Chem 275 2000 36852 36861
    • (2000) J Biol Chem , vol.275 , pp. 36852-36861
    • Atshaves, B.P.1    Starodub, O.2    McIntosh, A.3    Petrescu, A.4    Roths, J.B.5    Kier, A.B.6
  • 150
    • 0032832985 scopus 로고    scopus 로고
    • A fluorescent cholesterol analog traces cholesterol absorption in hamsters and is esterified in vivo and in vitro
    • C.P. Sparrow, S. Patel, J. Baffic, Y.S. Chao, M. Hernandez, and M.H. Lam A fluorescent cholesterol analog traces cholesterol absorption in hamsters and is esterified in vivo and in vitro J Lipid Res 40 1999 1747 1757
    • (1999) J Lipid Res , vol.40 , pp. 1747-1757
    • Sparrow, C.P.1    Patel, S.2    Baffic, J.3    Chao, Y.S.4    Hernandez, M.5    Lam, M.H.6
  • 151
    • 1242274634 scopus 로고    scopus 로고
    • Identification of ACAT1- and ACAT2-specific inhibitors using a novel, cell based fluorescence assay: Individual ACAT uniqueness
    • A.T. Lada, M. Davis, C. Kent, J. Chapman, H. Tomoda, and S. Omura Identification of ACAT1- and ACAT2-specific inhibitors using a novel, cell based fluorescence assay: individual ACAT uniqueness J Lipid Res 45 2004 378 386
    • (2004) J Lipid Res , vol.45 , pp. 378-386
    • Lada, A.T.1    Davis, M.2    Kent, C.3    Chapman, J.4    Tomoda, H.5    Omura, S.6
  • 152
    • 0242290835 scopus 로고    scopus 로고
    • HDL-mediated cholesterol uptake and targeting to lipid droplets in adipocytes
    • G. Dagher, N. Donne, C. Klein, P. Ferre, and I. Dugail HDL-mediated cholesterol uptake and targeting to lipid droplets in adipocytes J Lipid Res 44 2003 1811 1820
    • (2003) J Lipid Res , vol.44 , pp. 1811-1820
    • Dagher, G.1    Donne, N.2    Klein, C.3    Ferre, P.4    Dugail, I.5
  • 153
    • 76749149630 scopus 로고    scopus 로고
    • NBD-cholesterol probes to track cholesterol distribution in model membranes
    • D.M. Ramirez, W.W. Ogilvie, and L.J. Johnston NBD-cholesterol probes to track cholesterol distribution in model membranes Biochim Biophys Acta 1798 2010 558 568
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 558-568
    • Ramirez, D.M.1    Ogilvie, W.W.2    Johnston, L.J.3
  • 154
    • 0025744372 scopus 로고
    • A novel fluorescent ceramide analogue for studying membrane traffic in animal cells: Accumulation at the Golgi apparatus results in altered spectral properties of the sphingolipid precursor
    • R.E. Pagano, O.C. Martin, H.C. Kang, and R.P. Haugland A novel fluorescent ceramide analogue for studying membrane traffic in animal cells: accumulation at the Golgi apparatus results in altered spectral properties of the sphingolipid precursor J Cell Biol 113 1991 1267 1279
    • (1991) J Cell Biol , vol.113 , pp. 1267-1279
    • Pagano, R.E.1    Martin, O.C.2    Kang, H.C.3    Haugland, R.P.4
  • 155
    • 54049110711 scopus 로고    scopus 로고
    • Use of Bodipy-labeled sphingolipid and cholesterol analogs to examine membrane microdomains in cells
    • D.L. Marks, R. Bittman, and R.E. Pagano Use of Bodipy-labeled sphingolipid and cholesterol analogs to examine membrane microdomains in cells Histochem Cell Biol 130 2008 819 832
    • (2008) Histochem Cell Biol , vol.130 , pp. 819-832
    • Marks, D.L.1    Bittman, R.2    Pagano, R.E.3
  • 156
    • 33644554780 scopus 로고    scopus 로고
    • First synthesis of free cholesterol-BODIPY conjugates
    • Z. Li, E. Mintzer, and R. Bittman First synthesis of free cholesterol-BODIPY conjugates J Org Chem 71 2006 1718 1721
    • (2006) J Org Chem , vol.71 , pp. 1718-1721
    • Li, Z.1    Mintzer, E.2    Bittman, R.3
  • 157
    • 33645967519 scopus 로고    scopus 로고
    • Correlated fluorescence-atomic force microscopy of membrane domains: Structure of fluorescence probes determines lipid localization
    • J.E. Shaw, R.F. Epand, R.M. Epand, Z. Li, R. Bittman, and C.M. Yip Correlated fluorescence-atomic force microscopy of membrane domains: structure of fluorescence probes determines lipid localization Biophys J 90 2006 2170 2178
    • (2006) Biophys J , vol.90 , pp. 2170-2178
    • Shaw, J.E.1    Epand, R.F.2    Epand, R.M.3    Li, Z.4    Bittman, R.5    Yip, C.M.6
  • 158
    • 35548939515 scopus 로고    scopus 로고
    • Synthesis and spectral properties of cholesterol- and FTY720-containing boron dipyrromethene dyes
    • Z. Li, and R. Bittman Synthesis and spectral properties of cholesterol- and FTY720-containing boron dipyrromethene dyes J Org Chem 72 2007 8376 8382
    • (2007) J Org Chem , vol.72 , pp. 8376-8382
    • Li, Z.1    Bittman, R.2
  • 159
    • 67649352970 scopus 로고    scopus 로고
    • Membrane fluidity and lipid order in ternary giant unilamellar vesicles using a new bodipy-cholesterol derivative
    • F.S. Ariola, Z. Li, C. Cornejo, R. Bittman, and A.A. Heikal Membrane fluidity and lipid order in ternary giant unilamellar vesicles using a new bodipy-cholesterol derivative Biophys J 96 2009 2696 2708
    • (2009) Biophys J , vol.96 , pp. 2696-2708
    • Ariola, F.S.1    Li, Z.2    Cornejo, C.3    Bittman, R.4    Heikal, A.A.5
  • 160
    • 53849130991 scopus 로고    scopus 로고
    • BODIPY-cholesterol: A new tool to visualize sterol trafficking in living cells and organisms
    • M. Holtta-Vuori, R.L. Uronen, J. Repakova, E. Salonen, I. Vattulainen, and P. Panula BODIPY-cholesterol: a new tool to visualize sterol trafficking in living cells and organisms Traffic 9 2008 1839 1849
    • (2008) Traffic , vol.9 , pp. 1839-1849
    • Holtta-Vuori, M.1    Uronen, R.L.2    Repakova, J.3    Salonen, E.4    Vattulainen, I.5    Panula, P.6
  • 161
    • 0037389276 scopus 로고    scopus 로고
    • Transport of plasma membrane-derived cholesterol and the function of Niemann-Pick C1 Protein
    • V. Wiegand, T.Y. Chang, J.F. Strauss III, F. Fahrenholz, and G. Gimpl Transport of plasma membrane-derived cholesterol and the function of Niemann-Pick C1 Protein FASEB J 17 2003 782 784
    • (2003) FASEB J , vol.17 , pp. 782-784
    • Wiegand, V.1    Chang, T.Y.2    Strauss III, J.F.3    Fahrenholz, F.4    Gimpl, G.5
  • 162
    • 0037116591 scopus 로고    scopus 로고
    • Behavior of a photoactivatable analog of cholesterol, 6-photocholesterol, in model membranes
    • E.A. Mintzer, B.L. Waarts, J. Wilschut, and R. Bittman Behavior of a photoactivatable analog of cholesterol, 6-photocholesterol, in model membranes FEBS Lett 510 2002 181 184
    • (2002) FEBS Lett , vol.510 , pp. 181-184
    • Mintzer, E.A.1    Waarts, B.L.2    Wilschut, J.3    Bittman, R.4
  • 163
    • 65249112817 scopus 로고    scopus 로고
    • Orientation and dynamics of a novel fluorescent cholesterol analogue in membranes of varying phase
    • S. Shrivastava, S. Haldar, G. Gimpl, and A. Chattopadhyay Orientation and dynamics of a novel fluorescent cholesterol analogue in membranes of varying phase J Phys Chem B 113 2009 4475 4481
    • (2009) J Phys Chem B , vol.113 , pp. 4475-4481
    • Shrivastava, S.1    Haldar, S.2    Gimpl, G.3    Chattopadhyay, A.4
  • 164
    • 0027322412 scopus 로고
    • Role of the plasma membrane in cholesterol esterification in rat hepatoma cells
    • Y. Lange, F. Strebel, and T.L. Steck Role of the plasma membrane in cholesterol esterification in rat hepatoma cells J Biol Chem 268 1993 13838 13843
    • (1993) J Biol Chem , vol.268 , pp. 13838-13843
    • Lange, Y.1    Strebel, F.2    Steck, T.L.3
  • 165
    • 0033583562 scopus 로고    scopus 로고
    • Intracellular cholesterol transport
    • L. Liscum, and N.J. Munn Intracellular cholesterol transport Biochim Biophys Acta 1438 1999 19 37
    • (1999) Biochim Biophys Acta , vol.1438 , pp. 19-37
    • Liscum, L.1    Munn, N.J.2
  • 166
    • 59249091104 scopus 로고    scopus 로고
    • Fluorescent sterols monitor cell penetrating peptide Pep-1 mediated uptake and intracellular targeting of cargo protein in living cells
    • A.D. Petrescu, A. Vespa, H. Huang, A.L. McIntosh, F. Schroeder, and A.B. Kier Fluorescent sterols monitor cell penetrating peptide Pep-1 mediated uptake and intracellular targeting of cargo protein in living cells Biochim Biophys Acta 1788 2009 425 441
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 425-441
    • Petrescu, A.D.1    Vespa, A.2    Huang, H.3    McIntosh, A.L.4    Schroeder, F.5    Kier, A.B.6
  • 168
    • 0030688948 scopus 로고    scopus 로고
    • Cholesterol derivative of poly(ethylene glycol) inhibits clathrin-independent, but not clathrin-dependent endocytosis
    • H. Ishiwata, S.B. Sato, A. Vertut-Doi, Y. Hamashima, and K. Miyajima Cholesterol derivative of poly(ethylene glycol) inhibits clathrin-independent, but not clathrin-dependent endocytosis Biochim Biophys Acta 1359 1997 123 135
    • (1997) Biochim Biophys Acta , vol.1359 , pp. 123-135
    • Ishiwata, H.1    Sato, S.B.2    Vertut-Doi, A.3    Hamashima, Y.4    Miyajima, K.5
  • 169
    • 2542493177 scopus 로고    scopus 로고
    • Distribution and transport of cholesterol-rich membrane domains monitored by a membrane-impermeant fluorescent polyethylene glycol-derivatized cholesterol
    • S.B. Sato, K. Ishii, A. Makino, K. Iwabuchi, A. Yamaji-Hasegawa, and Y. Senoh Distribution and transport of cholesterol-rich membrane domains monitored by a membrane-impermeant fluorescent polyethylene glycol-derivatized cholesterol J Biol Chem 279 2004 23790 23796
    • (2004) J Biol Chem , vol.279 , pp. 23790-23796
    • Sato, S.B.1    Ishii, K.2    Makino, A.3    Iwabuchi, K.4    Yamaji-Hasegawa, A.5    Senoh, Y.6
  • 171
    • 0036296762 scopus 로고    scopus 로고
    • Investigation on lipid asymmetry using lipid probes: Comparison between spin-labeled lipids and fluorescent lipids
    • P.F. Devaux, P. Fellmann, and P. Herve Investigation on lipid asymmetry using lipid probes: Comparison between spin-labeled lipids and fluorescent lipids Chem Phys Lipids 116 2002 115 134
    • (2002) Chem Phys Lipids , vol.116 , pp. 115-134
    • Devaux, P.F.1    Fellmann, P.2    Herve, P.3
  • 173
    • 0018256329 scopus 로고
    • Inhibition of cholesterol synthesis in cultured cells by 25-azidonorcholesterol
    • W. Stoffel, and R. Klotzbucher Inhibition of cholesterol synthesis in cultured cells by 25-azidonorcholesterol Hoppe Seylers Z Physiol Chem 359 1978 199 209
    • (1978) Hoppe Seylers Z Physiol Chem , vol.359 , pp. 199-209
    • Stoffel, W.1    Klotzbucher, R.2
  • 174
    • 0018459174 scopus 로고
    • Interactions of a photosensitive analog of cholesterol with hydroxymethyglutaryl-CoA reductase (NADPH) and acyl-CoA:cholesterol acyltransferase
    • R.A. Heller, R. Klotzbucher, and W. Stoffel Interactions of a photosensitive analog of cholesterol with hydroxymethyglutaryl-CoA reductase (NADPH) and acyl-CoA:cholesterol acyltransferase Proc Natl Acad Sci U S A 76 1979 1721 1725
    • (1979) Proc Natl Acad Sci U S A , vol.76 , pp. 1721-1725
    • Heller, R.A.1    Klotzbucher, R.2    Stoffel, W.3
  • 175
    • 0001723110 scopus 로고
    • Photolysis of alkyl azides. Evidence for a nonnitrene mechanism
    • E.P. Kyba, and R.A. Abramovitch Photolysis of alkyl azides. Evidence for a nonnitrene mechanism J Am Chem Soc 102 1980 735 740
    • (1980) J Am Chem Soc , vol.102 , pp. 735-740
    • Kyba, E.P.1    Abramovitch, R.A.2
  • 176
    • 0020023310 scopus 로고
    • Chemical studies on the structure of human serum high-density lipoprotein (HDL) Photochemical crosslinking of azido-labelled lipids in HDL
    • W. Stoffel, and P. Metz Chemical studies on the structure of human serum high-density lipoprotein (HDL) Photochemical crosslinking of azido-labelled lipids in HDL Hoppe Seylers Z Physiol Chem 363 1982 19 31
    • (1982) Hoppe Seylers Z Physiol Chem , vol.363 , pp. 19-31
    • Stoffel, W.1    Metz, P.2
  • 177
    • 0020017025 scopus 로고
    • Syntheses of phosphatidylcholines, sphingomyelins and cholesterol substituted with azido fatty acids Photocrosslinking with nearest neighbouring lipids in liposomes chemical and mass spectroscopic proof
    • W. Stoffel, K.P. Salm, and M. Muller Syntheses of phosphatidylcholines, sphingomyelins and cholesterol substituted with azido fatty acids Photocrosslinking with nearest neighbouring lipids in liposomes chemical and mass spectroscopic proof Hoppe Seylers Z Physiol Chem 363 1982 1 18
    • (1982) Hoppe Seylers Z Physiol Chem , vol.363 , pp. 1-18
    • Stoffel, W.1    Salm, K.P.2    Muller, M.3
  • 178
    • 33845550896 scopus 로고
    • Synthesis and photoreactivity of cholesteryl diazoacetate: A novel photolabeling reagent
    • S.A. Keilbaugh, and E.R. Thornton Synthesis and photoreactivity of cholesteryl diazoacetate: a novel photolabeling reagent J Am Chem Soc 105 1983 3283 3286
    • (1983) J Am Chem Soc , vol.105 , pp. 3283-3286
    • Keilbaugh, S.A.1    Thornton, E.R.2
  • 179
    • 0022621319 scopus 로고
    • Syntheses of cholesterol analogs with a carbene-generating substituent on the side chain
    • T. Terasawa, N. Ikekawa, and M. Morisaki Syntheses of cholesterol analogs with a carbene-generating substituent on the side chain Chem Pharm Bull 34 1986 931 934 (Pubitemid 16124664)
    • (1986) Chemical and Pharmaceutical Bulletin , vol.34 , Issue.2 , pp. 931-934
    • Terasawa, T.1    Ikekawa, N.2    Morisaki, M.3
  • 180
    • 33645481359 scopus 로고
    • Photolysis of cholesteryl diazoacetate in small unilamellar vesicles
    • S.A. Keilbaugh, and E.R. Thornton Photolysis of cholesteryl diazoacetate in small unilamellar vesicles Biochemistry 22 1983 5063 5068
    • (1983) Biochemistry , vol.22 , pp. 5063-5068
    • Keilbaugh, S.A.1    Thornton, E.R.2
  • 181
    • 0023124272 scopus 로고
    • Identification of subunits of acetylcholine receptor that interact with a cholesterol photoaffinity probe
    • D.S. Middlemas, and M.A. Raftery Identification of subunits of acetylcholine receptor that interact with a cholesterol photoaffinity probe Biochemistry 26 1987 1219 1223
    • (1987) Biochemistry , vol.26 , pp. 1219-1223
    • Middlemas, D.S.1    Raftery, M.A.2
  • 182
    • 0026597885 scopus 로고
    • Rates of spontaneous exchange of synthetic radiolabeled sterols between lipid vesicles
    • C.C. Kan, J. Yan, and R. Bittman Rates of spontaneous exchange of synthetic radiolabeled sterols between lipid vesicles Biochemistry 31 1992 1866 1874
    • (1992) Biochemistry , vol.31 , pp. 1866-1874
    • Kan, C.C.1    Yan, J.2    Bittman, R.3
  • 183
    • 0020376564 scopus 로고
    • Effects of lipids on acetylcholine receptor Essential need of cholesterol for maintenance of agonist-induced state transitions in lipid vesicles
    • M. Criado, H. Eibl, and F.J. Barrantes Effects of lipids on acetylcholine receptor Essential need of cholesterol for maintenance of agonist-induced state transitions in lipid vesicles Biochemistry 21 1982 3622 3629
    • (1982) Biochemistry , vol.21 , pp. 3622-3629
    • Criado, M.1    Eibl, H.2    Barrantes, F.J.3
  • 184
    • 0027273911 scopus 로고
    • Labeling of the nicotinic acetylcholine receptor by a photoactivatable steroid probe: Effects of cholesterol and cholinergic ligands
    • A.M. Fernandez, G. Fernandez-Ballester, J.A. Ferragut, and J.M. Gonzalez-Ros Labeling of the nicotinic acetylcholine receptor by a photoactivatable steroid probe: effects of cholesterol and cholinergic ligands Biochim Biophys Acta 1149 1993 135 144
    • (1993) Biochim Biophys Acta , vol.1149 , pp. 135-144
    • Fernandez, A.M.1    Fernandez-Ballester, G.2    Ferragut, J.A.3    Gonzalez-Ros, J.M.4
  • 185
    • 0032508916 scopus 로고    scopus 로고
    • Identifying the cholesterol binding domain in the nicotinic acetylcholine receptor with [125I]azido-cholesterol
    • J. Corbin, H.H. Wang, and M.P. Blanton Identifying the cholesterol binding domain in the nicotinic acetylcholine receptor with [125I]azido- cholesterol Biochim Biophys Acta 1414 1998 65 74
    • (1998) Biochim Biophys Acta , vol.1414 , pp. 65-74
    • Corbin, J.1    Wang, H.H.2    Blanton, M.P.3
  • 187
    • 0001485853 scopus 로고
    • Some observations on the scope of the ammonia-hydroxylamine-O-sulfonic acid diaziridine synthesis. The preparation of certain steroid diaziridines and diazirines
    • R.F.R. Church, A.S. Kende, M.J. Weiss, and I. Diazirines Some observations on the scope of the ammonia-hydroxylamine-O-sulfonic acid diaziridine synthesis. The preparation of certain steroid diaziridines and diazirines J Am Chem Soc 87 1965 2665 2671
    • (1965) J Am Chem Soc , vol.87 , pp. 2665-2671
    • Church, R.F.R.1    Kende, A.S.2    Weiss, M.J.3    Diazirines, I.4
  • 188
    • 0020789485 scopus 로고
    • Photolabile derivatives of bile salts. Synthesis and suitability for photoaffinity labeling
    • W. Kramer, and G. Kurz Photolabile derivatives of bile salts. Synthesis and suitability for photoaffinity labeling J Lipid Res 24 1983 910 923
    • (1983) J Lipid Res , vol.24 , pp. 910-923
    • Kramer, W.1    Kurz, G.2
  • 189
    • 0024322421 scopus 로고
    • 3-Diazirine-derivatives of bile salts for photoaffinity labeling
    • W. Kramer, and S. Schneider 3-Diazirine-derivatives of bile salts for photoaffinity labeling J Lipid Res 30 1989 1281 1288
    • (1989) J Lipid Res , vol.30 , pp. 1281-1288
    • Kramer, W.1    Schneider, S.2
  • 191
    • 0033792318 scopus 로고    scopus 로고
    • Cholesterol binds to synaptophysin and is required for biogenesis of synaptic vesicles
    • C. Thiele, M.J. Hannah, F. Fahrenholz, and W.B. Huttner Cholesterol binds to synaptophysin and is required for biogenesis of synaptic vesicles Nat Cell Biol 2 2000 42 49
    • (2000) Nat Cell Biol , vol.2 , pp. 42-49
    • Thiele, C.1    Hannah, M.J.2    Fahrenholz, F.3    Huttner, W.B.4
  • 194
    • 0034597142 scopus 로고    scopus 로고
    • Assembly of myelin by association of proteolipid protein with cholesterol- and galactosylceramide-rich membrane domains
    • M. Simons, E.M. Kramer, C. Thiele, W. Stoffel, and J. Trotter Assembly of myelin by association of proteolipid protein with cholesterol- and galactosylceramide-rich membrane domains J Cell Biol 151 2000 143 154
    • (2000) J Cell Biol , vol.151 , pp. 143-154
    • Simons, M.1    Kramer, E.M.2    Thiele, C.3    Stoffel, W.4    Trotter, J.5
  • 195
    • 33751108519 scopus 로고    scopus 로고
    • Perturbed interactions of mutant proteolipid protein/DM20 with cholesterol and lipid rafts in oligodendroglia: Implications for dysmyelination in spastic paraplegia
    • E.M. Kramer-Albers, K. Gehrig-Burger, C. Thiele, J. Trotter, and K.A. Nave Perturbed interactions of mutant proteolipid protein/DM20 with cholesterol and lipid rafts in oligodendroglia: implications for dysmyelination in spastic paraplegia J Neurosci 26 2006 11743 11752
    • (2006) J Neurosci , vol.26 , pp. 11743-11752
    • Kramer-Albers, E.M.1    Gehrig-Burger, K.2    Thiele, C.3    Trotter, J.4    Nave, K.A.5
  • 197
    • 0037783980 scopus 로고    scopus 로고
    • Intestinal cholesterol absorption: Identification of different binding proteins for cholesterol and cholesterol absorption inhibitors in the enterocyte brush border membrane
    • W. Kramer, F. Girbig, D. Corsiero, K. Burger, F. Fahrenholz, and C. Jung Intestinal cholesterol absorption: identification of different binding proteins for cholesterol and cholesterol absorption inhibitors in the enterocyte brush border membrane Biochim Biophys Acta 1633 2003 13 26
    • (2003) Biochim Biophys Acta , vol.1633 , pp. 13-26
    • Kramer, W.1    Girbig, F.2    Corsiero, D.3    Burger, K.4    Fahrenholz, F.5    Jung, C.6
  • 198
    • 10644239801 scopus 로고    scopus 로고
    • Cholesterol and 25-hydroxycholesterol inhibit activation of SREBPs by different mechanisms, both involving SCAP and Insigs
    • C.M. Adams, J. Reitz, J.K. De Brabander, J.D. Feramisco, L. Li, and M.S. Brown Cholesterol and 25-hydroxycholesterol inhibit activation of SREBPs by different mechanisms, both involving SCAP and Insigs J Biol Chem 279 2004 52772 52780
    • (2004) J Biol Chem , vol.279 , pp. 52772-52780
    • Adams, C.M.1    Reitz, J.2    De Brabander, J.K.3    Feramisco, J.D.4    Li, L.5    Brown, M.S.6
  • 199
    • 41549132149 scopus 로고    scopus 로고
    • Cholesterol interaction with the related steroidogenic acute regulatory lipid-transfer (START) domains of StAR (STARD1) and MLN64 (STARD3)
    • J. Reitz, K. Gehrig-Burger, J.F. Strauss III, and G. Gimpl Cholesterol interaction with the related steroidogenic acute regulatory lipid-transfer (START) domains of StAR (STARD1) and MLN64 (STARD3) FEBS J 275 2008 1790 1802
    • (2008) FEBS J , vol.275 , pp. 1790-1802
    • Reitz, J.1    Gehrig-Burger, K.2    Strauss III, J.F.3    Gimpl, G.4
  • 200
    • 50949095260 scopus 로고    scopus 로고
    • Differential cholesterol binding by class II fusion proteins determines membrane fusion properties
    • M. Umashankar, M.C. Sanchez-San, M. Liao, B. Reilly, A. Guo, and G. Taylor Differential cholesterol binding by class II fusion proteins determines membrane fusion properties J Virol 82 2008 9245 9253
    • (2008) J Virol , vol.82 , pp. 9245-9253
    • Umashankar, M.1    Sanchez-San, M.C.2    Liao, M.3    Reilly, B.4    Guo, A.5    Taylor, G.6
  • 201
    • 31044432386 scopus 로고    scopus 로고
    • Cholesterol interacts with transmembrane alpha-helices M1, M3, and M4 of the Torpedo nicotinic acetylcholine receptor: Photolabeling studies using [3H]Azicholesterol
    • A.K. Hamouda, D.C. Chiara, D. Sauls, J.B. Cohen, and M.P. Blanton Cholesterol interacts with transmembrane alpha-helices M1, M3, and M4 of the Torpedo nicotinic acetylcholine receptor: photolabeling studies using [3H]Azicholesterol Biochemistry 45 2006 976 986
    • (2006) Biochemistry , vol.45 , pp. 976-986
    • Hamouda, A.K.1    Chiara, D.C.2    Sauls, D.3    Cohen, J.B.4    Blanton, M.P.5
  • 202
    • 0036691226 scopus 로고    scopus 로고
    • Synthesis and biochemical properties of a new photoactivatable cholesterol analog 7,7-azocholestanol and its linoleate ester in Chinese hamster ovary cell lines
    • J.C. Cruz, M. Thomas, E. Wong, N. Ohgami, S. Sugii, and T. Curphey Synthesis and biochemical properties of a new photoactivatable cholesterol analog 7,7-azocholestanol and its linoleate ester in Chinese hamster ovary cell lines J Lipid Res 43 2002 1341 1347
    • (2002) J Lipid Res , vol.43 , pp. 1341-1347
    • Cruz, J.C.1    Thomas, M.2    Wong, E.3    Ohgami, N.4    Sugii, S.5    Curphey, T.6
  • 203
    • 33845977384 scopus 로고    scopus 로고
    • Protein-protein interactions mediate mitochondrial cholesterol transport and steroid biosynthesis
    • J. Liu, M.B. Rone, and V. Papadopoulos Protein-protein interactions mediate mitochondrial cholesterol transport and steroid biosynthesis J Biol Chem 281 2006 38879 38893
    • (2006) J Biol Chem , vol.281 , pp. 38879-38893
    • Liu, J.1    Rone, M.B.2    Papadopoulos, V.3
  • 204
    • 0033824922 scopus 로고    scopus 로고
    • One-step synthesis of biotinyl photoprobes from unprotected carbohydrates
    • Y. Hatanaka, U. Kempin, and P. Jong-Jip One-step synthesis of biotinyl photoprobes from unprotected carbohydrates J Org Chem 65 2000 5639 5643
    • (2000) J Org Chem , vol.65 , pp. 5639-5643
    • Hatanaka, Y.1    Kempin, U.2    Jong-Jip, P.3
  • 205
    • 12144289185 scopus 로고    scopus 로고
    • Novel bifunctional probe for radioisotope-free photoaffinity labeling: Compact structure comprised of photospecific ligand ligation and detectable tag anchoring units
    • T. Hosoya, T. Hiramatsu, T. Ikemoto, M. Nakanishi, H. Aoyama, and A. Hosoya Novel bifunctional probe for radioisotope-free photoaffinity labeling: compact structure comprised of photospecific ligand ligation and detectable tag anchoring units Org Biomol Chem 2 2004 637 641
    • (2004) Org Biomol Chem , vol.2 , pp. 637-641
    • Hosoya, T.1    Hiramatsu, T.2    Ikemoto, T.3    Nakanishi, M.4    Aoyama, H.5    Hosoya, A.6
  • 206
    • 58549118993 scopus 로고    scopus 로고
    • Photocrosslinking and click chemistry enable the specific detection of proteins interacting with phospholipids at the membrane interface
    • J. Gubbens, E. Ruijter, L.E. de Fays, J.M. Damen, K.B. de, and M. Slijper Photocrosslinking and click chemistry enable the specific detection of proteins interacting with phospholipids at the membrane interface Chem Biol 16 2009 3 14
    • (2009) Chem Biol , vol.16 , pp. 3-14
    • Gubbens, J.1    Ruijter, E.2    De Fays, L.E.3    Damen, J.M.4    De, K.B.5    Slijper, M.6
  • 207
    • 70349440924 scopus 로고    scopus 로고
    • Protein-lipid interactions: Paparazzi hunting for snap-shots
    • P. Haberkant, and M.G. van Protein-lipid interactions: paparazzi hunting for snap-shots Biol Chem 390 2009 795 803
    • (2009) Biol Chem , vol.390 , pp. 795-803
    • Haberkant, P.1    Van, M.G.2
  • 208
    • 0016240087 scopus 로고
    • Photoaffinity labeling of peptide hormone binding sites
    • R.E. Galardy, L.C. Craig, J.D. Jamieson, and M.P. Printz Photoaffinity labeling of peptide hormone binding sites J Biol Chem 249 1974 3510 3518
    • (1974) J Biol Chem , vol.249 , pp. 3510-3518
    • Galardy, R.E.1    Craig, L.C.2    Jamieson, J.D.3    Printz, M.P.4
  • 209
    • 33644886015 scopus 로고    scopus 로고
    • Methionine acts as a "magnet" in photoaffinity crosslinking experiments
    • A. Wittelsberger, B.E. Thomas, D.F. Mierke, and M. Rosenblatt Methionine acts as a "magnet" in photoaffinity crosslinking experiments FEBS Lett 580 2006 1872 1876
    • (2006) FEBS Lett , vol.580 , pp. 1872-1876
    • Wittelsberger, A.1    Thomas, B.E.2    Mierke, D.F.3    Rosenblatt, M.4
  • 210
    • 3442875823 scopus 로고    scopus 로고
    • Benzophenone-containing cholesterol surrogates: Synthesis and biological evaluation
    • T.A. Spencer, P. Wang, D. Li, J.S. Russel, D.H. Blank, and J. Huuskonen Benzophenone-containing cholesterol surrogates: synthesis and biological evaluation J Lipid Res 45 2004 1510 1518
    • (2004) J Lipid Res , vol.45 , pp. 1510-1518
    • Spencer, T.A.1    Wang, P.2    Li, D.3    Russel, J.S.4    Blank, D.H.5    Huuskonen, J.6
  • 211
    • 0037117697 scopus 로고    scopus 로고
    • Sterol efflux to apolipoprotein A-I originates from caveolin-rich microdomains and potentiates PDGF-dependent protein kinase activity
    • P.E. Fielding, J.S. Russel, T.A. Spencer, H. Hakamata, K. Nagao, and C.J. Fielding Sterol efflux to apolipoprotein A-I originates from caveolin-rich microdomains and potentiates PDGF-dependent protein kinase activity Biochemistry 41 2002 4929 4937
    • (2002) Biochemistry , vol.41 , pp. 4929-4937
    • Fielding, P.E.1    Russel, J.S.2    Spencer, T.A.3    Hakamata, H.4    Nagao, K.5    Fielding, C.J.6
  • 213
    • 34249811452 scopus 로고    scopus 로고
    • Cholesterol binding does not predict activity of the steroidogenic acute regulatory protein StAR
    • B.Y. Baker, R.F. Epand, R.M. Epand, and W.L. Miller Cholesterol binding does not predict activity of the steroidogenic acute regulatory protein StAR J Biol Chem 282 2007 10223 10232
    • (2007) J Biol Chem , vol.282 , pp. 10223-10232
    • Baker, B.Y.1    Epand, R.F.2    Epand, R.M.3    Miller, W.L.4
  • 215
    • 20044376658 scopus 로고    scopus 로고
    • Characterization of the cholesterol recognition amino acid consensus sequence of the peripheral-type benzodiazepine receptor
    • N. Jamin, J.M. Neumann, M.A. Ostuni, T.K. Vu, Z.X. Yao, and S. Murail Characterization of the cholesterol recognition amino acid consensus sequence of the peripheral-type benzodiazepine receptor Mol Endocrinol 19 2005 588 594
    • (2005) Mol Endocrinol , vol.19 , pp. 588-594
    • Jamin, N.1    Neumann, J.M.2    Ostuni, M.A.3    Vu, T.K.4    Yao, Z.X.5    Murail, S.6


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