메뉴 건너뛰기




Volumn 103, Issue 11, 2012, Pages 2295-2303

Coiled-coil formation on lipid bilayers - Implications for docking and fusion efficiency

Author keywords

[No Author keywords available]

Indexed keywords

PHOSPHOLIPID;

EID: 84870538185     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2012.08.053     Document Type: Article
Times cited : (25)

References (42)
  • 1
  • 2
    • 0041428123 scopus 로고    scopus 로고
    • Membrane fusion: A structural perspective on the interplay of lipids and proteins
    • L.K. Tamm, J. Crane, and V. Kiessling Membrane fusion: a structural perspective on the interplay of lipids and proteins Curr. Opin. Struct. Biol. 13 2003 453 466
    • (2003) Curr. Opin. Struct. Biol. , vol.13 , pp. 453-466
    • Tamm, L.K.1    Crane, J.2    Kiessling, V.3
  • 3
    • 77951146397 scopus 로고    scopus 로고
    • Self-assembly of coiled coils in synthetic biology: Inspiration and progress
    • H. Robson Marsden, and A. Kros Self-assembly of coiled coils in synthetic biology: inspiration and progress Angew. Chem. Int. Ed. Engl. 49 2010 2988 3005
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 2988-3005
    • Robson Marsden, H.1    Kros, A.2
  • 4
    • 34948875856 scopus 로고    scopus 로고
    • Energetics and dynamics of SNAREpin folding across lipid bilayers
    • F. Li, and F. Pincet D. Tareste Energetics and dynamics of SNAREpin folding across lipid bilayers Nat. Struct. Mol. Biol. 14 2007 890 896
    • (2007) Nat. Struct. Mol. Biol. , vol.14 , pp. 890-896
    • Li, F.1    Pincet, F.2    Tareste, D.3
  • 7
    • 58849092285 scopus 로고    scopus 로고
    • Membrane fusion: Grappling with SNARE and SM proteins
    • T.C. Südhof, and J.E. Rothman Membrane fusion: grappling with SNARE and SM proteins Science 323 2009 474 477
    • (2009) Science , vol.323 , pp. 474-477
    • Südhof, T.C.1    Rothman, J.E.2
  • 9
    • 79959729394 scopus 로고    scopus 로고
    • Docking, not fusion, as the rate-limiting step in a SNARE-driven vesicle fusion assay
    • E.A. Smith, and J.C. Weisshaar Docking, not fusion, as the rate-limiting step in a SNARE-driven vesicle fusion assay Biophys. J. 100 2011 2141 2150
    • (2011) Biophys. J. , vol.100 , pp. 2141-2150
    • Smith, E.A.1    Weisshaar, J.C.2
  • 10
    • 0036158070 scopus 로고    scopus 로고
    • Membrane fusion: Stalk model revisited
    • V.S. Markin, and J.P. Albanesi Membrane fusion: stalk model revisited Biophys. J. 82 2002 693 712
    • (2002) Biophys. J. , vol.82 , pp. 693-712
    • Markin, V.S.1    Albanesi, J.P.2
  • 11
    • 2942635759 scopus 로고    scopus 로고
    • The energetics of membrane fusion from binding, through hemifusion, pore formation, and pore enlargement
    • F.S. Cohen, and G.B. Melikyan The energetics of membrane fusion from binding, through hemifusion, pore formation, and pore enlargement J. Membr. Biol. 199 2004 1 14
    • (2004) J. Membr. Biol. , vol.199 , pp. 1-14
    • Cohen, F.S.1    Melikyan, G.B.2
  • 14
    • 0037020082 scopus 로고    scopus 로고
    • Designing heterodimeric two-stranded α-helical coiled-coils. Effects of hydrophobicity and α-helical propensity on protein folding, stability, and specificity
    • J.R. Litowski, and R.S. Hodges Designing heterodimeric two-stranded α-helical coiled-coils. Effects of hydrophobicity and α-helical propensity on protein folding, stability, and specificity J. Biol. Chem. 277 2002 37272 37279
    • (2002) J. Biol. Chem. , vol.277 , pp. 37272-37279
    • Litowski, J.R.1    Hodges, R.S.2
  • 15
    • 48249090434 scopus 로고    scopus 로고
    • In situ synthesis of lipopeptides as versatile receptors for the specific binding of nanoparticles and liposomes to solid-supported membranes
    • S. Schuy, and B. Treutlein A. Janshoff In situ synthesis of lipopeptides as versatile receptors for the specific binding of nanoparticles and liposomes to solid-supported membranes Small 4 2008 970 981
    • (2008) Small , vol.4 , pp. 970-981
    • Schuy, S.1    Treutlein, B.2    Janshoff, A.3
  • 16
    • 0028330850 scopus 로고
    • Electrostatic interactions control the parallel and antiparallel orientation of α-helical chains in two-stranded α-helical coiled-coils
    • O.D. Monera, C.M. Kay, and R.S. Hodges Electrostatic interactions control the parallel and antiparallel orientation of α-helical chains in two-stranded α-helical coiled-coils Biochemistry 33 1994 3862 3871
    • (1994) Biochemistry , vol.33 , pp. 3862-3871
    • Monera, O.D.1    Kay, C.M.2    Hodges, R.S.3
  • 17
    • 80052441337 scopus 로고    scopus 로고
    • Transmembrane domain peptide/peptide nucleic acid hybrid as a model of a SNARE protein in vesicle fusion
    • A.S. Lygina, and K. Meyenberg U. Diederichsen Transmembrane domain peptide/peptide nucleic acid hybrid as a model of a SNARE protein in vesicle fusion Angew. Chem. Int. Ed. Engl. 50 2011 8597 8601
    • (2011) Angew. Chem. Int. Ed. Engl. , vol.50 , pp. 8597-8601
    • Lygina, A.S.1    Meyenberg, K.2    Diederichsen, U.3
  • 18
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • WEB SERVER ISSUE W668-673
    • L. Whitmore, and B.A. Wallace DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data Nucleic Acids Res. 32 Web Server issue 2004 W668-673
    • (2004) Nucleic Acids Res. , vol.32
    • Whitmore, L.1    Wallace, B.A.2
  • 19
    • 45849096536 scopus 로고    scopus 로고
    • Protein secondary structure analyses from circular dichroism spectroscopy: Methods and reference databases
    • L. Whitmore, and B.A. Wallace Protein secondary structure analyses from circular dichroism spectroscopy: methods and reference databases Biopolymers 89 2008 392 400
    • (2008) Biopolymers , vol.89 , pp. 392-400
    • Whitmore, L.1    Wallace, B.A.2
  • 20
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • C.N. Pace, and F. Vajdos T. Gray How to measure and predict the molar absorption coefficient of a protein Protein Sci. 4 1995 2411 2423
    • (1995) Protein Sci. , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Gray, T.3
  • 21
    • 0026650710 scopus 로고
    • Synthetic model proteins: The relative contribution of leucine residues at the nonequivalent positions of the 3-4 hydrophobic repeat to the stability of the two-stranded α-helical coiled-coil
    • N.E. Zhou, C.M. Kay, and R.S. Hodges Synthetic model proteins: the relative contribution of leucine residues at the nonequivalent positions of the 3-4 hydrophobic repeat to the stability of the two-stranded α-helical coiled-coil Biochemistry 31 1992 5739 5746
    • (1992) Biochemistry , vol.31 , pp. 5739-5746
    • Zhou, N.E.1    Kay, C.M.2    Hodges, R.S.3
  • 22
    • 0029812117 scopus 로고    scopus 로고
    • Kinetic study on the formation of a de novo designed heterodimeric coiled-coil: Use of surface plasmon resonance to monitor the association and dissociation of polypeptide chains
    • H. Chao, and M.E.J. Houston Jr. R.S. Hodges Kinetic study on the formation of a de novo designed heterodimeric coiled-coil: use of surface plasmon resonance to monitor the association and dissociation of polypeptide chains Biochemistry 35 1996 12175 12185
    • (1996) Biochemistry , vol.35 , pp. 12175-12185
    • Chao, H.1    Houston, Jr.M.E.J.2    Hodges, R.S.3
  • 23
    • 57049111581 scopus 로고    scopus 로고
    • PH-sensitivity of the E3/K3 heterodimeric coiled coil
    • B. Apostolovic, and H.-A. Klok pH-sensitivity of the E3/K3 heterodimeric coiled coil Biomacromolecules 9 2008 3173 3180
    • (2008) Biomacromolecules , vol.9 , pp. 3173-3180
    • Apostolovic, B.1    Klok, H.-A.2
  • 24
    • 0031014046 scopus 로고    scopus 로고
    • Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors
    • D.G. Myszka Kinetic analysis of macromolecular interactions using surface plasmon resonance biosensors Curr. Opin. Biotechnol. 8 1997 50 57
    • (1997) Curr. Opin. Biotechnol. , vol.8 , pp. 50-57
    • Myszka, D.G.1
  • 25
    • 0036228119 scopus 로고    scopus 로고
    • Direct comparison of binding equilibrium, thermodynamic, and rate constants determined by surface- and solution-based biophysical methods
    • Y.S.N. Day, and C.L. Baird D.G. Myszka Direct comparison of binding equilibrium, thermodynamic, and rate constants determined by surface- and solution-based biophysical methods Protein Sci. 11 2002 1017 1025
    • (2002) Protein Sci. , vol.11 , pp. 1017-1025
    • Day, Y.S.N.1    Baird, C.L.2    Myszka, D.G.3
  • 26
    • 0010345821 scopus 로고
    • Kinetic and concentration analysis using BIA technology
    • R. Karlsson, and H.k. Roos B. Persson Kinetic and concentration analysis using BIA technology Methods 6 1994 99 110
    • (1994) Methods , vol.6 , pp. 99-110
    • Karlsson, R.1    Roos, H.K.2    Persson, B.3
  • 27
    • 0032968077 scopus 로고    scopus 로고
    • Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes
    • E. Goormaghtigh, V. Raussens, and J.-M. Ruysschaert Attenuated total reflection infrared spectroscopy of proteins and lipids in biological membranes Biochim. Biophys. Acta 1422 1999 105 185
    • (1999) Biochim. Biophys. Acta , vol.1422 , pp. 105-185
    • Goormaghtigh, E.1    Raussens, V.2    Ruysschaert, J.-M.3
  • 28
    • 0039182128 scopus 로고    scopus 로고
    • FTIR-spectroscopy of multistranded coiled coil proteins
    • T. Heimburg, and J. Schünemann N. Geisler FTIR-spectroscopy of multistranded coiled coil proteins Biochemistry 38 1999 12727 12734
    • (1999) Biochemistry , vol.38 , pp. 12727-12734
    • Heimburg, T.1    Schünemann, J.2    Geisler, N.3
  • 29
    • 38149125407 scopus 로고    scopus 로고
    • Phase transition of individually addressable microstructured membranes visualized by imaging ellipsometry
    • S. Faiss, and S. Schuy A. Janshoff Phase transition of individually addressable microstructured membranes visualized by imaging ellipsometry J. Phys. Chem. B 111 2007 13979 13986
    • (2007) J. Phys. Chem. B , vol.111 , pp. 13979-13986
    • Faiss, S.1    Schuy, S.2    Janshoff, A.3
  • 30
    • 69249227554 scopus 로고    scopus 로고
    • Coiled-coil lipopeptides mimicking the prehairpin intermediate of glycoprotein gp41
    • S. Schuy, and E. Schäfer A. Janshoff Coiled-coil lipopeptides mimicking the prehairpin intermediate of glycoprotein gp41 Angew. Chem. Int. Ed. Engl. 121 2009 765 768
    • (2009) Angew. Chem. Int. Ed. Engl. , vol.121 , pp. 765-768
    • Schuy, S.1    Schäfer, E.2    Janshoff, A.3
  • 31
    • 33745601739 scopus 로고    scopus 로고
    • Cooperative adsorption of proteins onto lipid membranes
    • A. Hinderliter, and S. May Cooperative adsorption of proteins onto lipid membranes J. Phys. Condens. Matter 18 2006 S1257 S1270
    • (2006) J. Phys. Condens. Matter , vol.18
    • Hinderliter, A.1    May, S.2
  • 32
    • 0033860639 scopus 로고    scopus 로고
    • Association entropy in adsorption processes
    • N. Ben-Tal, and B. Honig A. Ben-Shaul Association entropy in adsorption processes Biophys. J. 79 2000 1180 1187
    • (2000) Biophys. J. , vol.79 , pp. 1180-1187
    • Ben-Tal, N.1    Honig, B.2    Ben-Shaul, A.3
  • 33
    • 77953725374 scopus 로고    scopus 로고
    • Colloidal probe microscopy of membrane-membrane interactions: From ligand-receptor recognition to fusion events
    • B. Lorenz, and R. Keller A. Janshoff Colloidal probe microscopy of membrane-membrane interactions: from ligand-receptor recognition to fusion events Biophys. Chem. 150 2010 54 63
    • (2010) Biophys. Chem. , vol.150 , pp. 54-63
    • Lorenz, B.1    Keller, R.2    Janshoff, A.3
  • 34
    • 0025045387 scopus 로고
    • Characteristics of self-quenching of the fluorescence of lipid-conjugated rhodamine in membranes
    • R.I. MacDonald Characteristics of self-quenching of the fluorescence of lipid-conjugated rhodamine in membranes J. Biol. Chem. 265 1990 13533 13539
    • (1990) J. Biol. Chem. , vol.265 , pp. 13533-13539
    • MacDonald, R.I.1
  • 35
    • 0022798145 scopus 로고
    • Mechanism of concentration quenching of a xanthene dye encapsulated in phospholipid vesicles
    • A.L. Plant Mechanism of concentration quenching of a xanthene dye encapsulated in phospholipid vesicles Photochem. Photobiol. 44 1986 453 459
    • (1986) Photochem. Photobiol. , vol.44 , pp. 453-459
    • Plant, A.L.1
  • 36
    • 77950346996 scopus 로고    scopus 로고
    • Site-specific DNA-controlled fusion of single lipid vesicles to supported lipid bilayers
    • L. Simonsson, and P. Jönsson F. Höök Site-specific DNA-controlled fusion of single lipid vesicles to supported lipid bilayers ChemPhysChem 11 2010 1011 1017
    • (2010) ChemPhysChem , vol.11 , pp. 1011-1017
    • Simonsson, L.1    Jönsson, P.2    Höök, F.3
  • 37
    • 0033607279 scopus 로고    scopus 로고
    • Rapid and efficient fusion of phospholipid vesicles by the α-helical core of a SNARE complex in the absence of an N-terminal regulatory domain
    • F. Parlati, and T. Weber J.E. Rothman Rapid and efficient fusion of phospholipid vesicles by the α-helical core of a SNARE complex in the absence of an N-terminal regulatory domain Proc. Natl. Acad. Sci. USA 96 1999 12565 12570
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 12565-12570
    • Parlati, F.1    Weber, T.2    Rothman, J.E.3
  • 39
    • 33846680089 scopus 로고    scopus 로고
    • Optimization of the hydrochloric acid concentration used for trifluoroacetate removal from synthetic peptides
    • V.V. Andrushchenko, H.J. Vogel, and E.J. Prenner Optimization of the hydrochloric acid concentration used for trifluoroacetate removal from synthetic peptides J. Pept. Sci. 13 2007 37 43
    • (2007) J. Pept. Sci. , vol.13 , pp. 37-43
    • Andrushchenko, V.V.1    Vogel, H.J.2    Prenner, E.J.3
  • 40
    • 0017192686 scopus 로고
    • Mobility measurement by analysis of fluorescence photobleaching recovery kinetics
    • D. Axelrod, and D.E. Koppel W.W. Webb Mobility measurement by analysis of fluorescence photobleaching recovery kinetics Biophys. J. 16 1976 1055 1069
    • (1976) Biophys. J. , vol.16 , pp. 1055-1069
    • Axelrod, D.1    Koppel, D.E.2    Webb, W.W.3
  • 41
    • 0020568317 scopus 로고
    • Theoretical analysis of fluorescence photobleaching recovery experiments
    • D.M. Soumpasis Theoretical analysis of fluorescence photobleaching recovery experiments Biophys. J. 41 1983 95 97
    • (1983) Biophys. J. , vol.41 , pp. 95-97
    • Soumpasis, D.M.1
  • 42
    • 2942668382 scopus 로고    scopus 로고
    • Investigation of temperature-induced phase transitions in DOPC and DPPC phospholipid bilayers using temperature-controlled scanning force microscopy
    • Z.V. Leonenko, and E. Finot D.T. Cramb Investigation of temperature-induced phase transitions in DOPC and DPPC phospholipid bilayers using temperature-controlled scanning force microscopy Biophys. J. 86 2004 3783 3793
    • (2004) Biophys. J. , vol.86 , pp. 3783-3793
    • Leonenko, Z.V.1    Finot, E.2    Cramb, D.T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.