메뉴 건너뛰기




Volumn 3, Issue 3, 2011, Pages 269-280

Protein-membrane interactions: The virtue of minimal systems in systems biology

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 79960339327     PISSN: 19395094     EISSN: 1939005X     Source Type: Journal    
DOI: 10.1002/wsbm.119     Document Type: Review
Times cited : (22)

References (92)
  • 1
    • 0036500993 scopus 로고    scopus 로고
    • Systems biology: a brief overview
    • Kitano H. Systems biology: a brief overview. Science 2002, 295:1662-1664.
    • (2002) Science , vol.295 , pp. 1662-1664
    • Kitano, H.1
  • 2
  • 4
    • 65549152467 scopus 로고    scopus 로고
    • Accurate determination of membrane dynamics with line-scan FCS
    • Ries J, Chiantia S, Schwille P. Accurate determination of membrane dynamics with line-scan FCS. Biophys J 2009, 96:1999-2008.
    • (2009) Biophys J , vol.96 , pp. 1999-2008
    • Ries, J.1    Chiantia, S.2    Schwille, P.3
  • 5
    • 33751233871 scopus 로고    scopus 로고
    • CombinedAFM and two-focus SFCS study of raft-exhibiting model membranes
    • Chiantia S, Ries J, KahyaN, Schwille P. CombinedAFM and two-focus SFCS study of raft-exhibiting model membranes. Chemphyschem 2006, 7:2409-2418.
    • (2006) Chemphyschem , vol.7 , pp. 2409-2418
    • Chiantia, S.1    Ries, J.2    Kahya, N.3    Schwille, P.4
  • 6
    • 43049122464 scopus 로고    scopus 로고
    • Tip-enhanced Raman scattering
    • Bailo E, Deckert V. Tip-enhanced Raman scattering. Chem Soc Rev 2008, 37:921-930.
    • (2008) Chem Soc Rev , vol.37 , pp. 921-930
    • Bailo, E.1    Deckert, V.2
  • 7
    • 72849145168 scopus 로고    scopus 로고
    • Development of tipenhanced optical spectroscopy for biological applications: a review
    • Elfick AP, Downes AR,Mouras R. Development of tipenhanced optical spectroscopy for biological applications: a review. Anal Bioanal Chem 2010, 396:45-52.
    • (2010) Anal Bioanal Chem , vol.396 , pp. 45-52
    • Elfick, A.P.1    Downes, A.R.2    Mouras, R.3
  • 9
    • 67650076514 scopus 로고    scopus 로고
    • Topography and recognition imaging of protein-patterned surfaces generated by AFM nanolithography
    • Zhu R, Ebner A, Kastner M, Preiner J, Howorka S, Hinterdorfer P. Topography and recognition imaging of protein-patterned surfaces generated by AFM nanolithography. Chemphyschem 2009, 10:1478-1481.
    • (2009) Chemphyschem , vol.10 , pp. 1478-1481
    • Zhu, R.1    Ebner, A.2    Kastner, M.3    Preiner, J.4    Howorka, S.5    Hinterdorfer, P.6
  • 10
    • 33745752076 scopus 로고    scopus 로고
    • Curvaturemodulated phase separation in lipid bilayermembranes
    • Parthasarathy R, Yu CH, Groves JT. Curvaturemodulated phase separation in lipid bilayermembranes. Langmuir 2006, 22:5095-5099.
    • (2006) Langmuir , vol.22 , pp. 5095-5099
    • Parthasarathy, R.1    Yu, C.H.2    Groves, J.T.3
  • 11
    • 28444476999 scopus 로고    scopus 로고
    • Membrane curvature and mechanisms of dynamic cell membrane remodelling
    • McMahon HT, Gallop JL. Membrane curvature and mechanisms of dynamic cell membrane remodelling. Nature 2005, 438:590-596.
    • (2005) Nature , vol.438 , pp. 590-596
    • McMahon, H.T.1    Gallop, J.L.2
  • 12
    • 14744278787 scopus 로고    scopus 로고
    • Sterol structure determines the separation of phases and the curvature of the liquid-ordered phase in model membranes
    • Bacia K, Schwille P, Kurzchalia T. Sterol structure determines the separation of phases and the curvature of the liquid-ordered phase in model membranes. Proc Natl Acad Sci U S A 2005, 102:3272-3277.
    • (2005) Proc Natl Acad Sci U S A , vol.102 , pp. 3272-3277
    • Bacia, K.1    Schwille, P.2    Kurzchalia, T.3
  • 13
    • 70349624358 scopus 로고    scopus 로고
    • Lipid domains in giant unilamellar vesicles and their correspondence with equilibrium thermodynamic phases: a quantitative fluorescence microscopy imaging approach
    • Fidorra M, Garcia A, Ipsen JH, Hartel S, Bagatolli LA. Lipid domains in giant unilamellar vesicles and their correspondence with equilibrium thermodynamic phases: a quantitative fluorescence microscopy imaging approach. Biochim Biophys Acta 2009, 1788:2142-2149.
    • (2009) Biochim Biophys Acta , vol.1788 , pp. 2142-2149
    • Fidorra, M.1    Garcia, A.2    Ipsen, J.H.3    Hartel, S.4    Bagatolli, L.A.5
  • 14
    • 0036208278 scopus 로고    scopus 로고
    • A two-photon view of an enzyme at work: Crotalusatrox venom PLA2 interaction with single-lipid and mixed-lipid giant unilamellar vesicles
    • Sanchez SA, Bagatolli LA, Gratton E, Hazlett TL. A two-photon view of an enzyme at work: Crotalusatrox venom PLA2 interaction with single-lipid and mixed-lipid giant unilamellar vesicles. Biophys J 2002, 82:2232-2243.
    • (2002) Biophys J , vol.82 , pp. 2232-2243
    • Sanchez, S.A.1    Bagatolli, L.A.2    Gratton, E.3    Hazlett, T.L.4
  • 16
    • 70350783743 scopus 로고    scopus 로고
    • Amphipathic motifs in BAR domains are essential for membrane curvature sensing
    • Bhatia VK, Madsen KL, Bolinger PY, Kunding A, Hedegard P, et al. Amphipathic motifs in BAR domains are essential for membrane curvature sensing. EMBO J 2009, 28:3303-3314.
    • (2009) EMBO J , vol.28 , pp. 3303-3314
    • Bhatia, V.K.1    Madsen, K.L.2    Bolinger, P.Y.3    Kunding, A.4    Hedegard, P.5
  • 18
    • 77951936995 scopus 로고    scopus 로고
    • BAR domains, amphipathic helices and membrane-anchored proteins use the same mechanism to sense membrane curvature
    • Madsen KL, Bhatia VK, Gether U, Stamou D. BAR domains, amphipathic helices and membrane-anchored proteins use the same mechanism to sense membrane curvature. FEBS Lett 2010, 584:1848-1855.
    • (2010) FEBS Lett , vol.584 , pp. 1848-1855
    • Madsen, K.L.1    Bhatia, V.K.2    Gether, U.3    Stamou, D.4
  • 20
    • 33646540414 scopus 로고    scopus 로고
    • Controlled microfluidic encapsulation of cells, proteins, and microbeads in lipid vesicles
    • Tan YC, Hettiarachchi K, Siu M, Pan YR, Lee AP. Controlled microfluidic encapsulation of cells, proteins, and microbeads in lipid vesicles. J Am Chem Soc 2006, 128:5656-5658.
    • (2006) J Am Chem Soc , vol.128 , pp. 5656-5658
    • Tan, Y.C.1    Hettiarachchi, K.2    Siu, M.3    Pan, Y.R.4    Lee, A.P.5
  • 21
    • 57649215874 scopus 로고    scopus 로고
    • GTPase cycle of dynamin is coupled to membrane squeeze and release, leading to spontaneous fission
    • Bashkirov PV, Akimov SA, Evseev AI, Schmid SL, Zimmerberg J, Frolov VA. GTPase cycle of dynamin is coupled to membrane squeeze and release, leading to spontaneous fission. Cell 2008, 135:1276-1286.
    • (2008) Cell , vol.135 , pp. 1276-1286
    • Bashkirov, P.V.1    Akimov, S.A.2    Evseev, A.I.3    Schmid, S.L.4    Zimmerberg, J.5    Frolov, V.A.6
  • 22
    • 0037015002 scopus 로고    scopus 로고
    • Formation of geometrically complex lipid nanotube-vesicle networks of higher-order topologies
    • Karlsson M, Sott K, Davidson M, Cans AS, Linderholm P, et al. Formation of geometrically complex lipid nanotube-vesicle networks of higher-order topologies. Proc Natl Acad Sci U S A 2002, 99:11573-11578.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 11573-11578
    • Karlsson, M.1    Sott, K.2    Davidson, M.3    Cans, A.S.4    Linderholm, P.5
  • 23
    • 71549166025 scopus 로고    scopus 로고
    • Chapter 15-Complex nanotube-liposome networks
    • Jesorka A, Orwar O. Chapter 15-Complex nanotube-liposome networks. Meth Enzymol 2009, 464: 309-325.
    • (2009) Meth Enzymol , vol.464 , pp. 309-325
    • Jesorka, A.1    Orwar, O.2
  • 24
    • 57649238675 scopus 로고    scopus 로고
    • Real-time visualization of dynamin-catalyzed membrane fission and vesicle release
    • Pucadyil TJ, Schmid SL. Real-time visualization of dynamin-catalyzed membrane fission and vesicle release. Cell 2008, 135:1263-1275.
    • (2008) Cell , vol.135 , pp. 1263-1275
    • Pucadyil, T.J.1    Schmid, S.L.2
  • 25
    • 21644472900 scopus 로고    scopus 로고
    • Cell-adhesion assays: fabrication of an E-cadherin substratum and isolation of lateral and Basal membrane patches
    • Drees F, Reilein A, Nelson WJ. Cell-adhesion assays: fabrication of an E-cadherin substratum and isolation of lateral and Basal membrane patches. Methods Mol Biol 2005, 294:303-320.
    • (2005) Methods Mol Biol , vol.294 , pp. 303-320
    • Drees, F.1    Reilein, A.2    Nelson, W.J.3
  • 26
    • 0034231383 scopus 로고    scopus 로고
    • The production of 'cell cortices' for light and electron microscopy
    • Heuser J. The production of 'cell cortices' for light and electron microscopy. Traffic 2000, 1:545-552.
    • (2000) Traffic , vol.1 , pp. 545-552
    • Heuser, J.1
  • 27
    • 0025874718 scopus 로고
    • Reconstitution of clathrin-coated pit budding from plasma membranes
    • Lin HC, Moore MS, Sanan DA, Anderson RG. Reconstitution of clathrin-coated pit budding from plasma membranes. J Cell Biol 1991, 114:881-891.
    • (1991) J Cell Biol , vol.114 , pp. 881-891
    • Lin, H.C.1    Moore, M.S.2    Sanan, D.A.3    Anderson, R.G.4
  • 28
    • 0025799606 scopus 로고
    • Simultaneous visualization of LDL receptor distribution and clathrin lattices on membranes torn from the upper surface of cultured cells
    • Sanan DA, Anderson RG. Simultaneous visualization of LDL receptor distribution and clathrin lattices on membranes torn from the upper surface of cultured cells. J Histochem Cytochem 1991, 39:1017-1024.
    • (1991) J Histochem Cytochem , vol.39 , pp. 1017-1024
    • Sanan, D.A.1    Anderson, R.G.2
  • 29
    • 0035794706 scopus 로고    scopus 로고
    • Dynamic localization cycle of the cell division regulator MinE in Escherichia coli
    • Hale CA, Meinhardt H, de Boer PA. Dynamic localization cycle of the cell division regulator MinE in Escherichia coli. EMBO J 2001, 20:1563-1572.
    • (2001) EMBO J , vol.20 , pp. 1563-1572
    • Hale, C.A.1    Meinhardt, H.2    de Boer, P.A.3
  • 30
    • 0035196036 scopus 로고    scopus 로고
    • Spatial regulation of cytokinesis in bacteria
    • Margolin W. Spatial regulation of cytokinesis in bacteria. Curr Opin Microbiol 2001, 4:647-652.
    • (2001) Curr Opin Microbiol , vol.4 , pp. 647-652
    • Margolin, W.1
  • 31
    • 0141925615 scopus 로고    scopus 로고
    • The MinD membrane targeting sequence is a transplantable lipid-binding helix
    • Szeto TH, Rowland SL, Habrukowich CL, King GF. The MinD membrane targeting sequence is a transplantable lipid-binding helix. J Biol Chem 2003, 278:40050-40056.
    • (2003) J Biol Chem , vol.278 , pp. 40050-40056
    • Szeto, T.H.1    Rowland, S.L.2    Habrukowich, C.L.3    King, G.F.4
  • 32
    • 0342420593 scopus 로고    scopus 로고
    • Bacterial cell division: a moving MinE sweeper boggles the MinD
    • Margolin W. Bacterial cell division: a moving MinE sweeper boggles the MinD. Curr Biol 2001, 11:R395-398.
    • (2001) Curr Biol , vol.11
    • Margolin, W.1
  • 35
    • 44049091101 scopus 로고    scopus 로고
    • Spatial regulators for bacterial cell division self-organize into surface waves in vitro
    • Loose M, Fischer-Friedrich E, Ries J, Kruse K, Schwille P. Spatial regulators for bacterial cell division self-organize into surface waves in vitro. Science 2008, 320:789-792.
    • (2008) Science , vol.320 , pp. 789-792
    • Loose, M.1    Fischer-Friedrich, E.2    Ries, J.3    Kruse, K.4    Schwille, P.5
  • 36
    • 33846951488 scopus 로고    scopus 로고
    • An experimentalist's guide to computational modelling of the Min system
    • Kruse K, Howard M, Margolin W. An experimentalist's guide to computational modelling of the Min system. Mol Microbiol 2007, 63:1279-1284.
    • (2007) Mol Microbiol , vol.63 , pp. 1279-1284
    • Kruse, K.1    Howard, M.2    Margolin, W.3
  • 37
    • 74349123957 scopus 로고    scopus 로고
    • Direct MinE-membrane interaction contributes to the proper localization of MinDE in E. coli
    • Hsieh CW, Lin TY, Lai HM, Lin CC, Hsieh TS, Shih YL. Direct MinE-membrane interaction contributes to the proper localization of MinDE in E. coli. Mol Microbiol 2010, 75:499-512.
    • (2010) Mol Microbiol , vol.75 , pp. 499-512
    • Hsieh, C.W.1    Lin, T.Y.2    Lai, H.M.3    Lin, C.C.4    Hsieh, T.S.5    Shih, Y.L.6
  • 38
    • 4644298002 scopus 로고    scopus 로고
    • Actin filaments align into hollow comets for rapid VASP-mediated propulsion
    • Plastino J, Olivier S, Sykes C. Actin filaments align into hollow comets for rapid VASP-mediated propulsion. Curr Biol 2004, 14:1766-1771.
    • (2004) Curr Biol , vol.14 , pp. 1766-1771
    • Plastino, J.1    Olivier, S.2    Sykes, C.3
  • 40
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard TD, Borisy GG. Cellular motility driven by assembly and disassembly of actin filaments. Cell 2003, 112:453-465.
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 41
    • 66349133039 scopus 로고    scopus 로고
    • New players in actin polymerization-WH2-domain-containing actin nucleators
    • Qualmann B, Kessels MM. New players in actin polymerization-WH2-domain-containing actin nucleators. Trends Cell Biol 2009, 19:276-285.
    • (2009) Trends Cell Biol , vol.19 , pp. 276-285
    • Qualmann, B.1    Kessels, M.M.2
  • 42
    • 77649187115 scopus 로고    scopus 로고
    • A "primer"-basedmechanism underlies branched actin filament network formation and motility
    • Achard V, Martiel JL, Michelot A, Guerin C, Reymann AC, et al. A "primer"-basedmechanism underlies branched actin filament network formation and motility. Curr Biol 2010, 20:423-428.
    • (2010) Curr Biol , vol.20 , pp. 423-428
    • Achard, V.1    Martiel, J.L.2    Michelot, A.3    Guerin, C.4    Reymann, A.C.5
  • 44
    • 0024332117 scopus 로고
    • Gamma interferon limits access of Listeria monocytogenes to the macrophage cytoplasm
    • Portnoy DA, Schreiber RD, Connelly P, Tilney LG. Gamma interferon limits access of Listeria monocytogenes to the macrophage cytoplasm. J Exp Med 1989, 170:2141-2146.
    • (1989) J Exp Med , vol.170 , pp. 2141-2146
    • Portnoy, D.A.1    Schreiber, R.D.2    Connelly, P.3    Tilney, L.G.4
  • 46
    • 0032407404 scopus 로고    scopus 로고
    • Intracellular pathogens and the actin cytoskeleton
    • Dramsi S, Cossart P. Intracellular pathogens and the actin cytoskeleton. Annu Rev Cell Dev Biol 1998, 14: 137-166.
    • (1998) Annu Rev Cell Dev Biol , vol.14 , pp. 137-166
    • Dramsi, S.1    Cossart, P.2
  • 47
    • 0024741693 scopus 로고
    • Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes
    • Tilney LG, Portnoy DA. Actin filaments and the growth, movement, and spread of the intracellular bacterial parasite, Listeria monocytogenes. J Cell Biol 1989, 109(4 Pt 1):1597-1608.
    • (1989) J Cell Biol , vol.109 , Issue.4 PART 1 , pp. 1597-1608
    • Tilney, L.G.1    Portnoy, D.A.2
  • 49
    • 36749027680 scopus 로고    scopus 로고
    • ARF1-mediated actin polymerization produces movement of artificial vesicles
    • Heuvingh J, Franco M, Chavrier P, Sykes C. ARF1-mediated actin polymerization produces movement of artificial vesicles. Proc Natl Acad Sci U S A 2007, 104:16928-16933.
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 16928-16933
    • Heuvingh, J.1    Franco, M.2    Chavrier, P.3    Sykes, C.4
  • 50
    • 0038652046 scopus 로고    scopus 로고
    • Compression forces generated by actin comet tails on lipid vesicles
    • Giardini PA, Fletcher DA, Theriot JA. Compression forces generated by actin comet tails on lipid vesicles. Proc Natl Acad Sci U S A 2003, 100:6493-6498.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 6493-6498
    • Giardini, P.A.1    Fletcher, D.A.2    Theriot, J.A.3
  • 52
    • 0141838877 scopus 로고    scopus 로고
    • Biomimetic systems for studying actin-based motility
    • Upadhyaya A, van Oudenaarden A. Biomimetic systems for studying actin-based motility. Curr Biol 2003, 13:R734-744.
    • (2003) Curr Biol , vol.13
    • Upadhyaya, A.1    van Oudenaarden, A.2
  • 53
    • 0035094485 scopus 로고    scopus 로고
    • The Arp2/3 complex nucleates actin filament branches from the sides of pre-existing filaments
    • Amann KJ, Pollard TD. The Arp2/3 complex nucleates actin filament branches from the sides of pre-existing filaments. Nat Cell Biol 2001, 3:306-310.
    • (2001) Nat Cell Biol , vol.3 , pp. 306-310
    • Amann, K.J.1    Pollard, T.D.2
  • 54
    • 0035964794 scopus 로고    scopus 로고
    • Structure of Arp2/3 complex in its activated state and in actin filament branch junctions
    • Volkmann N, Amann KJ, Stoilova-McPhie S, Egile C, Winter DC, et al. Structure of Arp2/3 complex in its activated state and in actin filament branch junctions. Science 2001, 293:2456-2459.
    • (2001) Science , vol.293 , pp. 2456-2459
    • Volkmann, N.1    Amann, K.J.2    Stoilova-McPhie, S.3    Egile, C.4    Winter, D.C.5
  • 55
    • 0018651717 scopus 로고
    • Yolk transport in the ovarian follicle of the hen (Gallus domesticus): lipoprotein-like particles at the periphery of the oocyte in the rapid growth phase
    • Perry MM, Gilbert AB. Yolk transport in the ovarian follicle of the hen (Gallus domesticus): lipoprotein-like particles at the periphery of the oocyte in the rapid growth phase. J Cell Sci 1979, 39:257-272.
    • (1979) J Cell Sci , vol.39 , pp. 257-272
    • Perry, M.M.1    Gilbert, A.B.2
  • 56
    • 32944473016 scopus 로고    scopus 로고
    • Virus entry: open sesame
    • Marsh M, Helenius A. Virus entry: open sesame. Cell 2006, 124:729-740.
    • (2006) Cell , vol.124 , pp. 729-740
    • Marsh, M.1    Helenius, A.2
  • 57
    • 34548176765 scopus 로고    scopus 로고
    • Integrating molecular and network biology to decode endocytosis
    • Schmid EM, McMahon HT. Integrating molecular and network biology to decode endocytosis. Nature 2007, 448:883-888.
    • (2007) Nature , vol.448 , pp. 883-888
    • Schmid, E.M.1    McMahon, H.T.2
  • 58
    • 48249134102 scopus 로고    scopus 로고
    • Mediation, modulation, and consequences of membrane-cytoskeleton interactions
    • Doherty GJ, McMahon HT. Mediation, modulation, and consequences of membrane-cytoskeleton interactions. Annu Rev Biophys 2008, 37:65-95.
    • (2008) Annu Rev Biophys , vol.37 , pp. 65-95
    • Doherty, G.J.1    McMahon, H.T.2
  • 59
    • 3142583466 scopus 로고    scopus 로고
    • Cargo recognition during clathrin-mediated endocytosis: a team effort
    • Sorkin A. Cargo recognition during clathrin-mediated endocytosis: a team effort. Curr Opin Cell Biol 2004, 16:392-399.
    • (2004) Curr Opin Cell Biol , vol.16 , pp. 392-399
    • Sorkin, A.1
  • 60
    • 33748626246 scopus 로고    scopus 로고
    • Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly
    • Schmid EM, Ford MG, Burtey A, Praefcke GJ, Peak-Chew SY, et al. Role of the AP2 beta-appendage hub in recruiting partners for clathrin-coated vesicle assembly. PLoS Biol 2006, 4:e262.
    • (2006) PLoS Biol , vol.4
    • Schmid, E.M.1    Ford, M.G.2    Burtey, A.3    Praefcke, G.J.4    Peak-Chew, S.Y.5
  • 61
    • 33749487743 scopus 로고    scopus 로고
    • The adaptor protein Dab2 sorts LDL receptors into coated pits independently of AP-2 and ARH
    • Maurer ME, Cooper JA. The adaptor protein Dab2 sorts LDL receptors into coated pits independently of AP-2 and ARH. J Cell Sci 2006, 119(Pt 20):4235-4246.
    • (2006) J Cell Sci , vol.119 , Issue.PART 20 , pp. 4235-4246
    • Maurer, M.E.1    Cooper, J.A.2
  • 63
    • 0032167614 scopus 로고    scopus 로고
    • Clathrin coats at 21 A resolution: a cellular assembly designed to recycle multiple membrane receptors
    • Smith CJ, Grigorieff N, Pearse BM. Clathrin coats at 21 A resolution: a cellular assembly designed to recycle multiple membrane receptors. EMBO J 1998, 17:4943-4953.
    • (1998) EMBO J , vol.17 , pp. 4943-4953
    • Smith, C.J.1    Grigorieff, N.2    Pearse, B.M.3
  • 64
    • 0032511190 scopus 로고    scopus 로고
    • Dynamin undergoes a GTPdependent conformational change causing vesiculation
    • Sweitzer SM, Hinshaw JE. Dynamin undergoes a GTPdependent conformational change causing vesiculation. Cell 1998, 93:1021-1029.
    • (1998) Cell , vol.93 , pp. 1021-1029
    • Sweitzer, S.M.1    Hinshaw, J.E.2
  • 65
    • 0028026793 scopus 로고
    • The role of clathrin, adaptors and dynamin in endocytosis
    • Robinson MS. The role of clathrin, adaptors and dynamin in endocytosis. Curr Opin Cell Biol 1994, 6:538-544.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 538-544
    • Robinson, M.S.1
  • 66
    • 0034573212 scopus 로고    scopus 로고
    • Accessory factors in clathrindependent synaptic vesicle endocytosis
    • Slepnev VI, De Camilli P. Accessory factors in clathrindependent synaptic vesicle endocytosis. Nat Rev Neurosci 2000, 1:161-172.
    • (2000) Nat Rev Neurosci , vol.1 , pp. 161-172
    • Slepnev, V.I.1    De Camilli, P.2
  • 67
    • 0029826531 scopus 로고    scopus 로고
    • Eps15 is a component of clathrin-coated pits and vesicles and is located at the rim of coated pits
    • Tebar F, Sorkina T, Sorkin A, Ericsson M, Kirchhausen T. Eps15 is a component of clathrin-coated pits and vesicles and is located at the rim of coated pits. J Biol Chem1996, 271:28727-28730.
    • (1996) J Biol Chem , vol.271 , pp. 28727-28730
    • Tebar, F.1    Sorkina, T.2    Sorkin, A.3    Ericsson, M.4    Kirchhausen, T.5
  • 68
    • 0032552056 scopus 로고    scopus 로고
    • Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis
    • Chen H, Fre S, Slepnev VI, Capua MR, Takei K, et al. Epsin is an EH-domain-binding protein implicated in clathrin-mediated endocytosis. Nature 1998, 394:793-797.
    • (1998) Nature , vol.394 , pp. 793-797
    • Chen, H.1    Fre, S.2    Slepnev, V.I.3    Capua, M.R.4    Takei, K.5
  • 69
    • 0033130119 scopus 로고    scopus 로고
    • Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis
    • Takei K, Slepnev VI, Haucke V, De Camilli P. Functional partnership between amphiphysin and dynamin in clathrin-mediated endocytosis. Nat Cell Biol 1999, 1:33-39.
    • (1999) Nat Cell Biol , vol.1 , pp. 33-39
    • Takei, K.1    Slepnev, V.I.2    Haucke, V.3    De Camilli, P.4
  • 70
    • 4644280545 scopus 로고    scopus 로고
    • The stimulatory action of amphiphysin on dynamin function is dependent on lipid bilayer curvature
    • Yoshida Y, Kinuta M, Abe T, Liang S, Araki K, et al. The stimulatory action of amphiphysin on dynamin function is dependent on lipid bilayer curvature. EMBO J 2004, 23:3483-3491.
    • (2004) EMBO J , vol.23 , pp. 3483-3491
    • Yoshida, Y.1    Kinuta, M.2    Abe, T.3    Liang, S.4    Araki, K.5
  • 72
    • 33745026786 scopus 로고    scopus 로고
    • GTPdependent twisting of dynamin implicates constriction and tension in membrane fission
    • Roux A, Uyhazi K, Frost A, De Camilli P. GTPdependent twisting of dynamin implicates constriction and tension in membrane fission. Nature 2006, 441:528-531.
    • (2006) Nature , vol.441 , pp. 528-531
    • Roux, A.1    Uyhazi, K.2    Frost, A.3    De Camilli, P.4
  • 73
    • 0035889088 scopus 로고    scopus 로고
    • Generation of high curvature membranes mediated by direct endophilin bilayer interactions
    • Farsad K, Ringstad N, Takei K, Floyd SR, Rose K, De Camilli P. Generation of high curvature membranes mediated by direct endophilin bilayer interactions. J Cell Biol 2001, 155:193-200.
    • (2001) J Cell Biol , vol.155 , pp. 193-200
    • Farsad, K.1    Ringstad, N.2    Takei, K.3    Floyd, S.R.4    Rose, K.5    De Camilli, P.6
  • 74
    • 0035135419 scopus 로고    scopus 로고
    • Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes
    • Ford MG, Pearse BM, Higgins MK, Vallis Y,Owen DJ, et al. Simultaneous binding of PtdIns(4,5)P2 and clathrin by AP180 in the nucleation of clathrin lattices on membranes. Science 2001, 291:1051-1055.
    • (2001) Science , vol.291 , pp. 1051-1055
    • Ford, M.G.1    Pearse, B.M.2    Higgins, M.K.3    Vallis, Y.4    Owen, D.J.5
  • 75
    • 70349764506 scopus 로고    scopus 로고
    • Distinct dynamics of endocytic clathrin-coated pits and coated plaques
    • Saffarian S, Cocucci E, Kirchhausen T. Distinct dynamics of endocytic clathrin-coated pits and coated plaques. PLoS Biol 2009, 7:e1000191.
    • (2009) PLoS Biol , vol.7
    • Saffarian, S.1    Cocucci, E.2    Kirchhausen, T.3
  • 76
    • 77950520993 scopus 로고    scopus 로고
    • Protein complexes containing CYFIP/Sra/PIR121 coordinate Arf1 and Rac1 signalling during clathrin-AP-1-coated carrier biogenesis at the TGN
    • Anitei M, Stange C, Parshina I, Baust T, Schenck A, et al. Protein complexes containing CYFIP/Sra/PIR121 coordinate Arf1 and Rac1 signalling during clathrin-AP-1-coated carrier biogenesis at the TGN. Nat Cell Biol 2010, 12:330-340.
    • (2010) Nat Cell Biol , vol.12 , pp. 330-340
    • Anitei, M.1    Stange, C.2    Parshina, I.3    Baust, T.4    Schenck, A.5
  • 77
    • 65249149251 scopus 로고    scopus 로고
    • Effect of high surface curvature on the main phase transition of supported phospholipid bilayers on SiO2 nanoparticles
    • Ahmed S, Wunder SL. Effect of high surface curvature on the main phase transition of supported phospholipid bilayers on SiO2 nanoparticles. Langmuir 2009, 25:3682-3691.
    • (2009) Langmuir , vol.25 , pp. 3682-3691
    • Ahmed, S.1    Wunder, S.L.2
  • 81
    • 68949143189 scopus 로고    scopus 로고
    • Diffusion and partitioning of fluorescent lipid probes in phospholipid monolayers
    • Gudmand M, Fidorra M, Bjornholm T, Heimburg T. Diffusion and partitioning of fluorescent lipid probes in phospholipid monolayers. Biophys J 2009, 96:4598-4609.
    • (2009) Biophys J , vol.96 , pp. 4598-4609
    • Gudmand, M.1    Fidorra, M.2    Bjornholm, T.3    Heimburg, T.4
  • 82
    • 36749044799 scopus 로고    scopus 로고
    • Formation, stability, and mobility of one-dimensional lipid bilayers on polysilicon nanowires
    • Huang SC, Artyukhin AB, Martinez JA, Sirbuly DJ, Wang Y, et al. Formation, stability, and mobility of one-dimensional lipid bilayers on polysilicon nanowires. Nano Lett 2007, 7:3355-3359.
    • (2007) Nano Lett , vol.7 , pp. 3355-3359
    • Huang, S.C.1    Artyukhin, A.B.2    Martinez, J.A.3    Sirbuly, D.J.4    Wang, Y.5
  • 83
    • 77749319350 scopus 로고    scopus 로고
    • Effect of a polymer cushion on the electrical properties and stability of surface-supported lipid bilayers
    • Lin J, Szymanski J, Searson PC, Hristova K. Effect of a polymer cushion on the electrical properties and stability of surface-supported lipid bilayers. Langmuir 2010, 26:3544-3548.
    • (2010) Langmuir , vol.26 , pp. 3544-3548
    • Lin, J.1    Szymanski, J.2    Searson, P.C.3    Hristova, K.4
  • 86
    • 77749306487 scopus 로고    scopus 로고
    • Peptide-induced domain formation in supported lipid bilayers: direct evidence by combined atomic force and polarized total internal reflection fluorescence microscopy
    • Oreopoulos J, Epand RF, Epand RM, Yip CM. Peptide-induced domain formation in supported lipid bilayers: direct evidence by combined atomic force and polarized total internal reflection fluorescence microscopy. Biophys J 2010, 98:815-823.
    • (2010) Biophys J , vol.98 , pp. 815-823
    • Oreopoulos, J.1    Epand, R.F.2    Epand, R.M.3    Yip, C.M.4
  • 88
    • 77950961951 scopus 로고    scopus 로고
    • Plasma oxidized polyhydroxymethylsiloxanea new smooth surface for supported lipid bilayer formation
    • Satriano C, Edvardsson M, Ohlsson G, Wang G, Svedhem S, Kasemo B. Plasma oxidized polyhydroxymethylsiloxanea new smooth surface for supported lipid bilayer formation. Langmuir 2010, 26:5715-5725.
    • (2010) Langmuir , vol.26 , pp. 5715-5725
    • Satriano, C.1    Edvardsson, M.2    Ohlsson, G.3    Wang, G.4    Svedhem, S.5    Kasemo, B.6
  • 90
    • 77951688243 scopus 로고    scopus 로고
    • Preparation of monodisperse block copolymer vesicles via flow focusing in microfluidics
    • Thiele J, Steinhauser D, Pfohl T, Forster S. Preparation of monodisperse block copolymer vesicles via flow focusing in microfluidics. Langmuir 2010, 26:6860-6863.
    • (2010) Langmuir , vol.26 , pp. 6860-6863
    • Thiele, J.1    Steinhauser, D.2    Pfohl, T.3    Forster, S.4
  • 91
    • 77649235243 scopus 로고    scopus 로고
    • A simple method for the reconstitution of membrane proteins into giant unilamellar vesicles
    • Varnier A, Kermarrec F, Blesneac I,Moreau C, Liguori L, et al. A simple method for the reconstitution of membrane proteins into giant unilamellar vesicles. J Membr Biol 2010, 233:85-92.
    • (2010) J Membr Biol , vol.233 , pp. 85-92
    • Varnier, A.1    Kermarrec, F.2    Blesneac, I.3    Moreau, C.4    Liguori, L.5
  • 92
    • 77950549492 scopus 로고    scopus 로고
    • Quantification of the Layer of Hydration of a Supported Lipid Bilayer
    • Zwang TJ, Fletcher WR, Lane TJ, Johal MS. Quantification of the Layer of Hydration of a Supported Lipid Bilayer. Langmuir 2010, 26:4598-4601.
    • (2010) Langmuir , vol.26 , pp. 4598-4601
    • Zwang, T.J.1    Fletcher, W.R.2    Lane, T.J.3    Johal, M.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.