메뉴 건너뛰기




Volumn 6, Issue 4, 2012, Pages

Mechanical properties of lipid bilayers and regulation of mechanosensitive function: From biological to biomimetic channels

Author keywords

Hydrophobic mismatch; Lipid interdigitation; Membrane tension; MscL and mscs channels; Peptide tilting; Peptidic pores; Periplasmic loop; Phospholipid membranes; Pore forming peptides; Snorkeling effect; Transmembrane helices

Indexed keywords

ALAMETHICIN; AZOLECTIN; DIPALMITOYLPHOSPHATIDYLCHOLINE; LYSOPHOSPHATIDYLCHOLINE; MELITTIN; PHOSPHOLIPID; POLYPEPTIDE ANTIBIOTIC AGENT; POLYUNSATURATED FATTY ACID; BIOMIMETIC MATERIAL; ESCHERICHIA COLI PROTEIN; ION CHANNEL; MSCL PROTEIN, E COLI; MSCS PROTEIN, E COLI; PEPTIDE;

EID: 84865305388     PISSN: 19336950     EISSN: 19336969     Source Type: Journal    
DOI: 10.4161/chan.21085     Document Type: Review
Times cited : (22)

References (150)
  • 1
    • 34047118100 scopus 로고    scopus 로고
    • 3.5 Billion years of mechanosensory transduction: Structure and function of mechanosensitive channels in prokaryotes
    • Martinac B. 3.5 Billion years of mechanosensory transduction: structure and function of mechanosensitive channels in prokaryotes. Current Topics Membr 2007; 58:25-57; http://dx.doi.org/10.1016/S1063-5823(06)58002-0.
    • (2007) Current Topics Membr , vol.58 , pp. 25-57
    • Martinac, B.1
  • 2
    • 0036280794 scopus 로고    scopus 로고
    • Purification of the small mechanosensitive channel of Escherichia coli (MscS): The subunit structure, conduction, and gating characteristics in liposomes
    • PMID:12080120
    • Sukharev S. Purification of the small mechanosensitive channel of Escherichia coli (MscS): the subunit structure, conduction, and gating characteristics in liposomes. Biophys J 2002; 83:290-8; PMID:12080120; http://dx.doi.org/10.1016/S0006-3495(02)75169-2.
    • (2002) Biophys J , vol.83 , pp. 290-298
    • Sukharev, S.1
  • 3
    • 77957942877 scopus 로고    scopus 로고
    • Mechanosensitive channels in microbes
    • PMID:20825352
    • Kung C, Martinac B, Sukharev S. Mechanosensitive channels in microbes. Annu Rev Microbiol 2010; 64:313-29; PMID:20825352; http://dx.doi.org/10.1146/ annurev.micro.112408.134106.
    • (2010) Annu Rev Microbiol , vol.64 , pp. 313-329
    • Kung, C.1    Martinac, B.2    Sukharev, S.3
  • 4
    • 0345196593 scopus 로고    scopus 로고
    • Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: Identification of genes required for MscS activity
    • PMID:10202137
    • Levina N, Tötemeyer S, Stokes NR, Louis P, Jones MA, Booth IR. Protection of Escherichia coli cells against extreme turgor by activation of MscS and MscL mechanosensitive channels: identification of genes required for MscS activity. EMBO J 1999; 18:1730-7; PMID:10202137; http://dx.doi.org/10.1093/ emboj/18.7.1730.
    • (1999) EMBO J , vol.18 , pp. 1730-1737
    • Levina, N.1    Tötemeyer, S.2    Stokes, N.R.3    Louis, P.4    Jones, M.A.5    Booth, I.R.6
  • 5
    • 84857769134 scopus 로고    scopus 로고
    • Three routes to modulate the pore size of the MscL channel/nanovalve
    • PMID:22206349
    • Yang LM, Wray R, Parker J, Wilson D, Duran RS, Blount P. Three routes to modulate the pore size of the MscL channel/nanovalve. ACS Nano 2012; 6:1134-41; PMID:22206349; http://dx.doi.org/10.1021/nn203703j.
    • (2012) ACS Nano , vol.6 , pp. 1134-1141
    • Yang, L.M.1    Wray, R.2    Parker, J.3    Wilson, D.4    Duran, R.S.5    Blount, P.6
  • 6
    • 69949160755 scopus 로고    scopus 로고
    • Structure of a tetrameric MscL in an expanded intermediate state
    • PMID:19701184
    • Liu Z, Gandhi CS, Rees DC. Structure of a tetrameric MscL in an expanded intermediate state. Nature 2009; 461:120-4; PMID:19701184; http://dx.doi.org/10. 1038/nature08277.
    • (2009) Nature , vol.461 , pp. 120-124
    • Liu, Z.1    Gandhi, C.S.2    Rees, D.C.3
  • 7
    • 79251582837 scopus 로고    scopus 로고
    • OCAM: A new tool for studying the oligomeric diversity of MscL channels
    • PMID:21280123
    • Gandhi CS, Walton TA, Rees DC. OCAM: a new tool for studying the oligomeric diversity of MscL channels. Protein Sci 2011; 20:313-26; PMID:21280123; http://dx.doi.org/10.1002/pro.562.
    • (2011) Protein Sci , vol.20 , pp. 313-326
    • Gandhi, C.S.1    Walton, T.A.2    Rees, D.C.3
  • 8
    • 69049103033 scopus 로고    scopus 로고
    • Conserved motifs in mechanosensitive channels MscL and MscS
    • PMID:19424690
    • Balleza D, Gómez-Lagunas F. Conserved motifs in mechanosensitive channels MscL and MscS. Eur Biophys J 2009; 38:1013-27; PMID:19424690; http://dx.doi.org/10.1007/s00249-009-0460-y.
    • (2009) Eur Biophys J , vol.38 , pp. 1013-1027
    • Balleza, D.1    Gómez-Lagunas, F.2
  • 9
    • 34047126893 scopus 로고    scopus 로고
    • Structures of the prokaryotic mechanosensitive channels MscL and MscS
    • Steinbacher S, Bass R, Strop P, Rees DC. Structures of the prokaryotic mechanosensitive channels MscL and MscS. Current Topics Membr 2007; 58:1-24; http://dx.doi.org/10.1016/S1063-5823(06)58001-9.
    • (2007) Current Topics Membr , vol.58 , pp. 1-24
    • Steinbacher, S.1    Bass, R.2    Strop, P.3    Rees, D.C.4
  • 10
    • 34247849390 scopus 로고    scopus 로고
    • Penetration of lipid chains into transmembrane surfaces of membrane proteins: Studies with MscL
    • PMID:17307828
    • Carney J, East JM, Lee AG. Penetration of lipid chains into transmembrane surfaces of membrane proteins: studies with MscL. Biophys J 2007; 92:3556-63; PMID:17307828; http://dx.doi.org/10.1529/biophysj.106.102210.
    • (2007) Biophys J , vol.92 , pp. 3556-3563
    • Carney, J.1    East, J.M.2    Lee, A.G.3
  • 11
    • 7144257172 scopus 로고    scopus 로고
    • Functional and structural conservation in the mechanosensitive channel MscL implicates elements crucial for mechanosensation
    • PMID:9632260
    • Moe PC, Blount P, Kung C. Functional and structural conservation in the mechanosensitive channel MscL implicates elements crucial for mechanosensation. Mol Microbiol 1998; 28:583-92; PMID:9632260; http://dx.doi.org/10.1046/j.1365- 2958.1998.00821.x.
    • (1998) Mol Microbiol , vol.28 , pp. 583-592
    • Moe, P.C.1    Blount, P.2    Kung, C.3
  • 12
    • 0034613258 scopus 로고    scopus 로고
    • Correlating a protein structure with function of a bacterial mechanosensitive channel
    • PMID:10846181
    • Moe PC, Levin G, Blount P. Correlating a protein structure with function of a bacterial mechanosensitive channel. J Biol Chem 2000; 275:31121-7; PMID:10846181; http://dx.doi.org/10.1074/jbc.M002971200.
    • (2000) J Biol Chem , vol.275 , pp. 31121-31127
    • Moe, P.C.1    Levin, G.2    Blount, P.3
  • 13
    • 33947662068 scopus 로고    scopus 로고
    • Versatile polyketide enzymatic machinery for the biosynthesis of complex mycobacterial lipids
    • PMID:17389997
    • Gokhale RS, Saxena P, Chopra T, Mohanty D. Versatile polyketide enzymatic machinery for the biosynthesis of complex mycobacterial lipids. Nat Prod Rep 2007; 24:267-77; PMID:17389997; http://dx.doi.org/10.1039/b616817p.
    • (2007) Nat Prod Rep , vol.24 , pp. 267-277
    • Gokhale, R.S.1    Saxena, P.2    Chopra, T.3    Mohanty, D.4
  • 14
    • 0033957169 scopus 로고    scopus 로고
    • Contributions of the different extramembranous domains of the mechanosensitive ion channel MscL to its response to membrane tension
    • PMID:10625640
    • Ajouz B, Berrier C, Besnard M, Martinac B, Ghazi A. Contributions of the different extramembranous domains of the mechanosensitive ion channel MscL to its response to membrane tension. J Biol Chem 2000; 275:1015-22; PMID:10625640; http://dx.doi.org/10.1074/jbc.275.2.1015.
    • (2000) J Biol Chem , vol.275 , pp. 1015-1022
    • Ajouz, B.1    Berrier, C.2    Besnard, M.3    Martinac, B.4    Ghazi, A.5
  • 15
    • 1942487703 scopus 로고    scopus 로고
    • Purification and functional reconstitution of N- and C-halves of the MscL channel
    • PMID:15041653
    • Park KH, Berrier C, Martinac B, Ghazi A. Purification and functional reconstitution of N- and C-halves of the MscL channel. Biophys J 2004; 86:2129-36; PMID:15041653; http://dx.doi.org/10.1016/S0006-3495(04)74272-1.
    • (2004) Biophys J , vol.86 , pp. 2129-2136
    • Park, K.H.1    Berrier, C.2    Martinac, B.3    Ghazi, A.4
  • 16
    • 22844452065 scopus 로고    scopus 로고
    • The role of the periplasmic loop residue glutamine 65 for MscL mechanosensitivity
    • PMID:15812636
    • Tsai IJ, Liu ZW, Rayment J, Norman C, McKinley A, Martinac B. The role of the periplasmic loop residue glutamine 65 for MscL mechanosensitivity. Eur Biophys J 2005; 34:403-12; PMID:15812636; http://dx.doi.org/10.1007/s00249-005- 0476-x.
    • (2005) Eur Biophys J , vol.34 , pp. 403-412
    • Tsai, I.J.1    Liu, Z.W.2    Rayment, J.3    Norman, C.4    McKinley, A.5    Martinac, B.6
  • 17
    • 84855996441 scopus 로고    scopus 로고
    • Mechanosensitive behavior of bacterial cyclic nucleotide gated (bCNG) ion channels: Insights into the mechanism of channel gating in the mechanosensitive channel of small conductance superfamily
    • PMID:22206667
    • Malcolm HR, Elmore DE, Maurer JA. Mechanosensitive behavior of bacterial cyclic nucleotide gated (bCNG) ion channels: Insights into the mechanism of channel gating in the mechanosensitive channel of small conductance superfamily. Biochem Biophys Res Commun 2012; 417:972-6; PMID:22206667; http://dx.doi.org/ 10.1016/j.bbrc.2011.12.049.
    • (2012) Biochem Biophys Res Commun , vol.417 , pp. 972-976
    • Malcolm, H.R.1    Elmore, D.E.2    Maurer, J.A.3
  • 18
    • 1842738226 scopus 로고    scopus 로고
    • Total chemical synthesis and electrophysiological characterization of mechanosensitive channels from Escherichia coli and Mycobacterium tuberculosis
    • PMID:15041744
    • Clayton D, Shapovalov G, Maurer JA, Dougherty DA, Lester HA, Kochendoerfer GG. Total chemical synthesis and electrophysiological characterization of mechanosensitive channels from Escherichia coli and Mycobacterium tuberculosis. Proc Natl Acad Sci U S A 2004; 101:4764-9; PMID:15041744; http://dx.doi.org/10.1073/pnas.0305693101.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 4764-4769
    • Clayton, D.1    Shapovalov, G.2    Maurer, J.A.3    Dougherty, D.A.4    Lester, H.A.5    Kochendoerfer, G.G.6
  • 19
    • 78649764518 scopus 로고    scopus 로고
    • Coupled cell-free synthesis and lipid vesicle insertion of a functional oligomeric channel MscL MscL does not need the insertase YidC for insertion in vitro
    • PMID:20888317
    • Berrier C, Guilvout I, Bayan N, Park KH, Mesneau A, Chami M, et al. Coupled cell-free synthesis and lipid vesicle insertion of a functional oligomeric channel MscL MscL does not need the insertase YidC for insertion in vitro. Biochim Biophys Acta 2011; 1808:41-6; PMID:20888317; http://dx.doi.org/ 10.1016/j.bbamem.2010.09.018.
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 41-46
    • Berrier, C.1    Guilvout, I.2    Bayan, N.3    Park, K.H.4    Mesneau, A.5    Chami, M.6
  • 20
    • 78650921227 scopus 로고    scopus 로고
    • In vitro synthesis and oligomerization of the mechanosensitive channel of large conductance, MscL, into a functional ion channel
    • PMID:21134371
    • Price CE, Kocer A, Kol S, van der Berg JP, Driessen AJM. In vitro synthesis and oligomerization of the mechanosensitive channel of large conductance, MscL, into a functional ion channel. FEBS Lett 2011; 585:249-54; PMID:21134371; http://dx.doi.org/10.1016/j.febslet.2010.11.057.
    • (2011) FEBS Lett , vol.585 , pp. 249-254
    • Price, C.E.1    Kocer, A.2    Kol, S.3    Van Der Berg, J.P.4    Driessen, A.J.M.5
  • 21
    • 1642359643 scopus 로고    scopus 로고
    • Energetics of pore formation induced by membrane active peptides
    • PMID:15035629
    • Lee MT, Chen FY, Huang HW. Energetics of pore formation induced by membrane active peptides. Biochemistry 2004; 43:3590-9; PMID:15035629; http://dx.doi.org/10.1021/bi036153r.
    • (2004) Biochemistry , vol.43 , pp. 3590-3599
    • Lee, M.T.1    Chen, F.Y.2    Huang, H.W.3
  • 22
    • 42449116949 scopus 로고    scopus 로고
    • Mechanism and kinetics of pore formation in membranes by water-soluble amphipathic peptides
    • PMID:18375755
    • Lee MT, Hung WC, Chen FY, Huang HW. Mechanism and kinetics of pore formation in membranes by water-soluble amphipathic peptides. Proc Natl Acad Sci U S A 2008; 105:5087-92; PMID:18375755; http://dx.doi.org/10.1073/pnas. 0710625105.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 5087-5092
    • Lee, M.T.1    Hung, W.C.2    Chen, F.Y.3    Huang, H.W.4
  • 23
    • 77956906517 scopus 로고    scopus 로고
    • Mechanosensitivity of ion channels based on protein-lipid interactions
    • PMID:20356872
    • Yoshimura K, Sokabe M. Mechanosensitivity of ion channels based on protein-lipid interactions. J R Soc Interface 2010; 7(Suppl 3):S307-20; PMID:20356872; http://dx.doi.org/10.1098/rsif.2010.0095.focus.
    • (2010) J R Soc Interface , vol.7 , Issue.SUPPL. 3
    • Yoshimura, K.1    Sokabe, M.2
  • 24
    • 80054068982 scopus 로고    scopus 로고
    • Mechanosensitive channels: What can they do and how do they do it?
    • PMID:22000509
    • Haswell ES, Phillips R, Rees DC. Mechanosensitive channels: what can they do and how do they do it? Structure 2011; 19:1356-69; PMID:22000509; http://dx.doi.org/10.1016/j.str.2011.09.005.
    • (2011) Structure , vol.19 , pp. 1356-1369
    • Haswell, E.S.1    Phillips, R.2    Rees, D.C.3
  • 25
    • 83755186704 scopus 로고    scopus 로고
    • Bacterial mechanosensitive channels as a paradigm for mechanosensory transduction
    • PMID:22178995
    • Martinac B. Bacterial mechanosensitive channels as a paradigm for mechanosensory transduction. Cell Physiol Biochem 2011; 28:1051-60; PMID:22178995; http://dx.doi.org/10.1159/000335842.
    • (2011) Cell Physiol Biochem , vol.28 , pp. 1051-1060
    • Martinac, B.1
  • 26
    • 84861365324 scopus 로고    scopus 로고
    • Bacterial mechanosensitive channels-MscS: Evolution's solution to creating sensitivity in function
    • PMID:22404681
    • Naismith JH, Booth IR. Bacterial mechanosensitive channels-MscS: Evolution's solution to creating sensitivity in function. Annu Rev Biophys 2012; 41:157-77; PMID:22404681; http://dx.doi.org/10.1146/annurev-biophys-101211- 113227.
    • (2012) Annu Rev Biophys , vol.41 , pp. 157-177
    • Naismith, J.H.1    Booth, I.R.2
  • 27
    • 0346422375 scopus 로고    scopus 로고
    • Lipid bilayers: Thermodynamics, structure, fluctuations, and interactions
    • PMID:14706737
    • Tristram-Nagle S, Nagle JF. Lipid bilayers: thermodynamics, structure, fluctuations, and interactions. Chem Phys Lipids 2004; 127:3-14; PMID:14706737; http://dx.doi.org/10.1016/j.chemphyslip.2003.09.002.
    • (2004) Chem Phys Lipids , vol.127 , pp. 3-14
    • Tristram-Nagle, S.1    Nagle, J.F.2
  • 28
    • 84856762196 scopus 로고    scopus 로고
    • Phase behavior of lipid bilayers under tension
    • PMID:22325274
    • Uline MJ, Schick M, Szleifer I. Phase behavior of lipid bilayers under tension. Biophys J 2012; 102:517-22; PMID:22325274; http://dx.doi.org/10.1016/j. bpj.2011.12.050.
    • (2012) Biophys J , vol.102 , pp. 517-522
    • Uline, M.J.1    Schick, M.2    Szleifer, I.3
  • 30
    • 77949661963 scopus 로고    scopus 로고
    • Coarse-grained simulations of membranes under tension
    • PMID:20331316
    • Neder J, West B, Nielaba P, Schmid F. Coarse-grained simulations of membranes under tension. J Chem Phys 2010; 132:115101; PMID:20331316; http://dx.doi.org/10.1063/1.3352583.
    • (2010) J Chem Phys , vol.132 , pp. 115101
    • Neder, J.1    West, B.2    Nielaba, P.3    Schmid, F.4
  • 31
    • 78651270968 scopus 로고    scopus 로고
    • Atomistic simulation of lipid and DiI dynamics in membrane bilayers under tension
    • PMID:21152516
    • Muddana HS, Gullapalli RR, Manias E, Butler PJ. Atomistic simulation of lipid and DiI dynamics in membrane bilayers under tension. Phys Chem Chem Phys 2011; 13:1368-78; PMID:21152516; http://dx.doi.org/10.1039/c0cp00430h.
    • (2011) Phys Chem Chem Phys , vol.13 , pp. 1368-1378
    • Muddana, H.S.1    Gullapalli, R.R.2    Manias, E.3    Butler, P.J.4
  • 32
    • 0036226098 scopus 로고    scopus 로고
    • Size distribution of barrel-stave aggregates of membrane peptides: Influence of the bilayer lateral pressure profile
    • PMID:11964240
    • Cantor RS. Size distribution of barrel-stave aggregates of membrane peptides: influence of the bilayer lateral pressure profile. Biophys J 2002; 82:2520-5; PMID:11964240; http://dx.doi.org/10.1016/S0006-3495(02)75595-1.
    • (2002) Biophys J , vol.82 , pp. 2520-2525
    • Cantor, R.S.1
  • 33
    • 33745041479 scopus 로고    scopus 로고
    • Roles of bilayer material properties in function and distribution of membrane proteins
    • PMID:16689633
    • McIntosh TJ, Simon SA. Roles of bilayer material properties in function and distribution of membrane proteins. Annu Rev Biophys Biomol Struct 2006; 35:177-98; PMID:16689633; http://dx.doi.org/10.1146/annurev.biophys.35.040405. 102022.
    • (2006) Annu Rev Biophys Biomol Struct , vol.35 , pp. 177-198
    • McIntosh, T.J.1    Simon, S.A.2
  • 34
    • 34347262391 scopus 로고    scopus 로고
    • Bilayer thickness and membrane protein function: An energetic perspective
    • PMID:17263662
    • Andersen OS, Koeppe RE 2nd. Bilayer thickness and membrane protein function: an energetic perspective. Annu Rev Biophys Biomol Struct 2007; 36:107-30; PMID:17263662; http://dx.doi.org/10.1146/annurev.biophys.36.040306. 132643.
    • (2007) Annu Rev Biophys Biomol Struct , vol.36 , pp. 107-130
    • Andersen, O.S.1    Koeppe II, R.E.2
  • 35
    • 78649809259 scopus 로고    scopus 로고
    • Changes in single K(+) channel behavior induced by a lipid phase transition
    • PMID:21112292
    • Seeger HM, Aldrovandi L, Alessandrini A, Facci P. Changes in single K(+) channel behavior induced by a lipid phase transition. Biophys J 2010; 99:3675-83; PMID:21112292; http://dx.doi.org/10.1016/j.bpj.2010.10.042.
    • (2010) Biophys J , vol.99 , pp. 3675-3683
    • Seeger, H.M.1    Aldrovandi, L.2    Alessandrini, A.3    Facci, P.4
  • 36
    • 58049194119 scopus 로고    scopus 로고
    • Voltage-dependent K+ channel gating and voltage sensor toxin sensitivity depend on the mechanical state of the lipid membrane
    • PMID:19050073
    • Schmidt D, MacKinnon R. Voltage-dependent K+ channel gating and voltage sensor toxin sensitivity depend on the mechanical state of the lipid membrane. Proc Natl Acad Sci U S A 2008; 105:19276-81; PMID:19050073; http://dx.doi.org/ 10.1073/pnas.0810187105.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 19276-19281
    • Schmidt, D.1    MacKinnon, R.2
  • 37
    • 77949590752 scopus 로고    scopus 로고
    • Gadolinium ions block mechanosensitive channels by altering the packing and lateral pressure of anionic lipids
    • PMID:20303859
    • Ermakov YA, Kamaraju K, Sengupta K, Sukharev S. Gadolinium ions block mechanosensitive channels by altering the packing and lateral pressure of anionic lipids. Biophys J 2010; 98:1018-27; PMID:20303859; http://dx.doi.org/10. 1016/j.bpj.2009.11.044.
    • (2010) Biophys J , vol.98 , pp. 1018-1027
    • Ermakov, Y.A.1    Kamaraju, K.2    Sengupta, K.3    Sukharev, S.4
  • 38
    • 33846578173 scopus 로고    scopus 로고
    • Modulation of channel activity and gadolinium block of MscL by static magnetic fields
    • PMID:17089151
    • Petrov E, Martinac B. Modulation of channel activity and gadolinium block of MscL by static magnetic fields. Eur Biophys J 2007; 36:95-105; PMID:17089151; http://dx.doi.org/10.1007/s00249-006-0109-z.
    • (2007) Eur Biophys J , vol.36 , pp. 95-105
    • Petrov, E.1    Martinac, B.2
  • 39
    • 0034951046 scopus 로고    scopus 로고
    • The influence of lysolipids on the spontaneous curvature and bending elasticity of phospholipid membranes
    • PMID:11423410
    • Fuller N, Rand RP. The influence of lysolipids on the spontaneous curvature and bending elasticity of phospholipid membranes. Biophys J 2001; 81:243-54; PMID:11423410; http://dx.doi.org/10.1016/S0006-3495(01)75695-0.
    • (2001) Biophys J , vol.81 , pp. 243-254
    • Fuller, N.1    Rand, R.P.2
  • 40
    • 77952674796 scopus 로고    scopus 로고
    • Phospholipid demixing and the birth of a lipid droplet
    • PMID:20184900
    • Zanghellini J, Wodlei F, von Grünberg HH. Phospholipid demixing and the birth of a lipid droplet. J Theor Biol 2010; 264:952-61; PMID:20184900; http://dx.doi.org/10.1016/j.jtbi.2010.02.025.
    • (2010) J Theor Biol , vol.264 , pp. 952-961
    • Zanghellini, J.1    Wodlei, F.2    Von Grünberg, H.H.3
  • 41
    • 0018882371 scopus 로고
    • Differential miscibility properties of various phosphatidylcholine/ lysophosphatidylcholine mixtures
    • PMID:7349884
    • Van Echteld CJ, de Kruijff B, de Gier J. Differential miscibility properties of various phosphatidylcholine/lysophosphatidylcholine mixtures. Biochim Biophys Acta 1980; 595:71-81; PMID:7349884; http://dx.doi.org/10.1016/ 0005-2736(80)90249-7.
    • (1980) Biochim Biophys Acta , vol.595 , pp. 71-81
    • Van Echteld, C.J.1    De Kruijff, B.2    De Gier, J.3
  • 42
    • 0004683285 scopus 로고    scopus 로고
    • Effect of lysophosphatidylcholine on behavior and structure of phosphatidylcholine liposomes
    • PMID:18726286
    • Lu J, Xu Y, Chen J, Huang F. Effect of lysophosphatidylcholine on behavior and structure of phosphatidylcholine liposomes. Sci China C Life Sci 1997; 40:622-9; PMID:18726286; http://dx.doi.org/10.1007/BF02882692.
    • (1997) Sci China C Life Sci , vol.40 , pp. 622-629
    • Lu, J.1    Xu, Y.2    Chen, J.3    Huang, F.4
  • 43
    • 0036725152 scopus 로고    scopus 로고
    • Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating
    • PMID:12172537
    • Perozo E, Kloda A, Cortes DM, Martinac B. Physical principles underlying the transduction of bilayer deformation forces during mechanosensitive channel gating. Nat Struct Biol 2002; 9:696-703; PMID:12172537; http://dx.doi.org/10. 1038/nsb827.
    • (2002) Nat Struct Biol , vol.9 , pp. 696-703
    • Perozo, E.1    Kloda, A.2    Cortes, D.M.3    Martinac, B.4
  • 44
    • 50649109171 scopus 로고    scopus 로고
    • A structural mechanism for MscS gating in lipid bilayers
    • PMID:18755978
    • Vásquez V, Sotomayor M, Cordero-Morales J, Schulten K, Perozo E. A structural mechanism for MscS gating in lipid bilayers. Science 2008; 321:1210-4; PMID:18755978; http://dx.doi.org/10.1126/science.1159674.
    • (2008) Science , vol.321 , pp. 1210-1214
    • Vásquez, V.1    Sotomayor, M.2    Cordero-Morales, J.3    Schulten, K.4    Perozo, E.5
  • 45
    • 36849039435 scopus 로고    scopus 로고
    • Lateral pressure profile, spontaneous curvature frustration, and the incorporation and conformation of proteins in membranes
    • PMID:17704167
    • Marsh D. Lateral pressure profile, spontaneous curvature frustration, and the incorporation and conformation of proteins in membranes. Biophys J 2007; 93:3884-99; PMID:17704167; http://dx.doi.org/10.1529/biophysj.107.107938.
    • (2007) Biophys J , vol.93 , pp. 3884-3899
    • Marsh, D.1
  • 46
    • 70449096451 scopus 로고    scopus 로고
    • Curvature generation and pressure profile modulation in membrane by lysolipids: Insights from coarse-grained simulations
    • PMID:19843459
    • Yoo J, Cui Q. Curvature generation and pressure profile modulation in membrane by lysolipids: insights from coarse-grained simulations. Biophys J 2009; 97:2267-76; PMID:19843459; http://dx.doi.org/10.1016/j.bpj.2009.07.051.
    • (2009) Biophys J , vol.97 , pp. 2267-2276
    • Yoo, J.1    Cui, Q.2
  • 47
    • 67349231331 scopus 로고    scopus 로고
    • The interactions between phosphatidylglycerol and phosphatidylethanolamines in model bacterial membranes: The effect of the acyl chain length and saturation
    • PMID:19380216
    • Wydro P, Witkowska K. The interactions between phosphatidylglycerol and phosphatidylethanolamines in model bacterial membranes: the effect of the acyl chain length and saturation. Colloids Surf B Biointerfaces 2009; 72:32-9; PMID:19380216; http://dx.doi.org/10.1016/j.colsurfb.2009.03.011.
    • (2009) Colloids Surf B Biointerfaces , vol.72 , pp. 32-39
    • Wydro, P.1    Witkowska, K.2
  • 48
    • 0037116518 scopus 로고    scopus 로고
    • Polyunsaturated fatty acids in lipid bilayers: Intrinsic and environmental contributions to their unique physical properties
    • PMID:11782184
    • Feller SE, Gawrisch K, MacKerell AD Jr. Polyunsaturated fatty acids in lipid bilayers: intrinsic and environmental contributions to their unique physical properties. J Am Chem Soc 2002; 124:318-26; PMID:11782184; http://dx.doi.org/10.1021/ja0118340.
    • (2002) J Am Chem Soc , vol.124 , pp. 318-326
    • Feller, S.E.1    Gawrisch, K.2    MacKerell Jr., A.D.3
  • 49
    • 79954996866 scopus 로고    scopus 로고
    • Shear rheology of lipid monolayers and insights on membrane fluidity
    • PMID:21444777
    • Espinosa G, López-Montero I, Monroy F, Langevin D. Shear rheology of lipid monolayers and insights on membrane fluidity. Proc Natl Acad Sci U S A 2011; 108:6008-13; PMID:21444777; http://dx.doi.org/10.1073/pnas.1018572108.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 6008-6013
    • Espinosa, G.1    López-Montero, I.2    Monroy, F.3    Langevin, D.4
  • 50
    • 69349095079 scopus 로고    scopus 로고
    • Structural changes in the cytoplasmic domain of the mechanosensitive channel MscS during opening
    • PMID:19686652
    • Machiyama H, Tatsumi H, Sokabe M. Structural changes in the cytoplasmic domain of the mechanosensitive channel MscS during opening. Biophys J 2009; 97:1048-57; PMID:19686652; http://dx.doi.org/10.1016/j.bpj.2009.05.021.
    • (2009) Biophys J , vol.97 , pp. 1048-1057
    • Machiyama, H.1    Tatsumi, H.2    Sokabe, M.3
  • 51
    • 84861901984 scopus 로고    scopus 로고
    • Differential effects of lipids and lyso-lipids on the mechanosensitivity of the mechanosensitive channels MscL and MscS
    • PMID:22586095
    • Nomura T, Cranfield CG, Deplazes E, Owen DM, Macmillan A, Battle AR, et al. Differential effects of lipids and lyso-lipids on the mechanosensitivity of the mechanosensitive channels MscL and MscS. Proc Natl Acad Sci U S A 2012; 109:8770-5; PMID:22586095; http://dx.doi.org/10.1073/pnas.1200051109.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 8770-8775
    • Nomura, T.1    Cranfield, C.G.2    Deplazes, E.3    Owen, D.M.4    Macmillan, A.5    Battle, A.R.6
  • 52
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • PMID:19458714
    • Phillips R, Ursell T, Wiggins P, Sens P. Emerging roles for lipids in shaping membrane-protein function. Nature 2009; 459:379-85; PMID:19458714; http://dx.doi.org/10.1038/nature08147.
    • (2009) Nature , vol.459 , pp. 379-385
    • Phillips, R.1    Ursell, T.2    Wiggins, P.3    Sens, P.4
  • 53
    • 84859351412 scopus 로고    scopus 로고
    • Engineering de novo membrane-mediated protein-protein communication networks
    • PMID:22428921
    • Charalambous K, Booth PJ, Woscholski R, Seddon JM, Templer RH, Law RV, et al. Engineering de novo membrane-mediated protein-protein communication networks. J Am Chem Soc 2012; 134:5746-9; PMID:22428921; http://dx.doi.org/10. 1021/ja300523q.
    • (2012) J Am Chem Soc , vol.134 , pp. 5746-5749
    • Charalambous, K.1    Booth, P.J.2    Woscholski, R.3    Seddon, J.M.4    Templer, R.H.5    Law, R.V.6
  • 54
    • 69449086544 scopus 로고    scopus 로고
    • Morphology and interaction between lipid domains
    • PMID:19620730
    • Ursell TS, Klug WS, Phillips R. Morphology and interaction between lipid domains. Proc Natl Acad Sci U S A 2009; 106:13301-6; PMID:19620730; http://dx.doi.org/10.1073/pnas.0903825106.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 13301-13306
    • Ursell, T.S.1    Klug, W.S.2    Phillips, R.3
  • 55
    • 73349128115 scopus 로고    scopus 로고
    • Phase-transition-induced protein redistribution in lipid bilayers
    • PMID:19928819
    • Seeger HM, Bortolotti CA, Alessandrini A, Facci P. Phase-transition- induced protein redistribution in lipid bilayers. J Phys Chem B 2009; 113:16654-9; PMID:19928819; http://dx.doi.org/10.1021/jp907505m.
    • (2009) J Phys Chem B , vol.113 , pp. 16654-16659
    • Seeger, H.M.1    Bortolotti, C.A.2    Alessandrini, A.3    Facci, P.4
  • 56
    • 79952153989 scopus 로고    scopus 로고
    • Lipid packing drives the segregation of transmembrane helices into disordered lipid domains in model membranes
    • PMID:21205902
    • Schäfer LV, de Jong DH, Holt A, Rzepiela AJ, de Vries AH, Poolman B, et al. Lipid packing drives the segregation of transmembrane helices into disordered lipid domains in model membranes. Proc Natl Acad Sci U S A 2011; 108:1343-8; PMID:21205902; http://dx.doi.org/10.1073/pnas.1009362108.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 1343-1348
    • Schäfer, L.V.1    De Jong, D.H.2    Holt, A.3    Rzepiela, A.J.4    De Vries, A.H.5    Poolman, B.6
  • 57
    • 34249651256 scopus 로고    scopus 로고
    • Cooperative gating and spatial organization of membrane proteins through elastic interactions
    • PMID:17480116
    • Ursell TS, Huang KC, Peterson E, Phillips R. Cooperative gating and spatial organization of membrane proteins through elastic interactions. PLoS Comput Biol 2007; 3:e81; PMID:17480116; http://dx.doi.org/10.1371/journal.pcbi. 0030081.
    • (2007) PLoS Comput Biol , vol.3
    • Ursell, T.S.1    Huang, K.C.2    Peterson, E.3    Phillips, R.4
  • 58
    • 79953857432 scopus 로고    scopus 로고
    • Bilayer-mediated clustering and functional interaction of MscL channels
    • PMID:21354398
    • Grage SL, Keleshian AM, Turdzeladze T, Battle AR, Tay WC, May RP, et al. Bilayer-mediated clustering and functional interaction of MscL channels. Biophys J 2011; 100:1252-60; PMID:21354398; http://dx.doi.org/10.1016/j.bpj.2011.01. 023.
    • (2011) Biophys J , vol.100 , pp. 1252-1260
    • Grage, S.L.1    Keleshian, A.M.2    Turdzeladze, T.3    Battle, A.R.4    Tay, W.C.5    May, R.P.6
  • 59
    • 0036728233 scopus 로고    scopus 로고
    • A large iris-like expansion of a mechanosensitive channel protein induced by membrane tension
    • PMID:12172538
    • Betanzos M, Chiang CS, Guy HR, Sukharev S. A large iris-like expansion of a mechanosensitive channel protein induced by membrane tension. Nat Struct Biol 2002; 9:704-10; PMID:12172538; http://dx.doi.org/10.1038/nsb828.
    • (2002) Nat Struct Biol , vol.9 , pp. 704-710
    • Betanzos, M.1    Chiang, C.S.2    Guy, H.R.3    Sukharev, S.4
  • 60
    • 0037194760 scopus 로고    scopus 로고
    • Open channel structure of MscL and the gating mechanism of mechanosensitive channels
    • PMID:12198539
    • Perozo E, Cortes DM, Sompornpisut P, Kloda A, Martinac B. Open channel structure of MscL and the gating mechanism of mechanosensitive channels. Nature 2002; 418:942-8; PMID:12198539; http://dx.doi.org/10.1038/nature00992.
    • (2002) Nature , vol.418 , pp. 942-948
    • Perozo, E.1    Cortes, D.M.2    Sompornpisut, P.3    Kloda, A.4    Martinac, B.5
  • 61
    • 50649125767 scopus 로고    scopus 로고
    • The structure of an open form of an E. coli mechanosensitive channel at 3.45 A resolution
    • PMID:18755969
    • Wang W, Black SS, Edwards MD, Miller S, Morrison EL, Bartlett W, et al. The structure of an open form of an E. coli mechanosensitive channel at 3.45 A resolution. Science 2008; 321:1179-83; PMID:18755969; http://dx.doi.org/10.1126/ science.1159262.
    • (2008) Science , vol.321 , pp. 1179-1183
    • Wang, W.1    Black, S.S.2    Edwards, M.D.3    Miller, S.4    Morrison, E.L.5    Bartlett, W.6
  • 62
    • 36348937414 scopus 로고    scopus 로고
    • Effect of line tension on the lateral organization of lipid membranes
    • PMID:17848582
    • García-Sáez AJ, Chiantia S, Schwille P. Effect of line tension on the lateral organization of lipid membranes. J Biol Chem 2007; 282:33537-44; PMID:17848582; http://dx.doi.org/10.1074/jbc.M706162200.
    • (2007) J Biol Chem , vol.282 , pp. 33537-33544
    • García-Sáez, A.J.1    Chiantia, S.2    Schwille, P.3
  • 63
    • 77954760821 scopus 로고    scopus 로고
    • Protein-protein and protein-lipid interactions in domain-assembly: Lessons from giant unilamellar vesicles
    • PMID:20211599
    • Kahya N. Protein-protein and protein-lipid interactions in domain-assembly: lessons from giant unilamellar vesicles. Biochim Biophys Acta 2010; 1798:1392-8; PMID:20211599; http://dx.doi.org/10.1016/j.bbamem.2010.02. 028.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 1392-1398
    • Kahya, N.1
  • 64
    • 79959343843 scopus 로고    scopus 로고
    • Forming giant vesicles with controlled membrane composition, asymmetry, and contents
    • PMID:21593410
    • Richmond DL, Schmid EM, Martens S, Stachowiak JC, Liska N, Fletcher DA. Forming giant vesicles with controlled membrane composition, asymmetry, and contents. Proc Natl Acad Sci U S A 2011; 108:9431-6; PMID:21593410; http://dx.doi.org/10.1073/pnas.1016410108.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 9431-9436
    • Richmond, D.L.1    Schmid, E.M.2    Martens, S.3    Stachowiak, J.C.4    Liska, N.5    Fletcher, D.A.6
  • 65
    • 79952926357 scopus 로고    scopus 로고
    • Targeting proteins to liquid-ordered domains in lipid membranes
    • PMID:21155607
    • Stachowiak JC, Hayden CC, Sanchez MAA, Wang J, Bunker BC, Voigt JA, et al. Targeting proteins to liquid-ordered domains in lipid membranes. Langmuir 2011; 27:1457-62; PMID:21155607; http://dx.doi.org/10.1021/la1041458.
    • (2011) Langmuir , vol.27 , pp. 1457-1462
    • Stachowiak, J.C.1    Hayden, C.C.2    Sanchez, M.A.A.3    Wang, J.4    Bunker, B.C.5    Voigt, J.A.6
  • 66
    • 21244447355 scopus 로고    scopus 로고
    • Distribution, lateral mobility and function of membrane proteins incorporated into giant unilamellar vesicles
    • PMID:15574707
    • Doeven MK, Folgering JH, Krasnikov V, Geertsma ER, van den Bogaart G, Poolman B. Distribution, lateral mobility and function of membrane proteins incorporated into giant unilamellar vesicles. Biophys J 2005; 88:1134-42; PMID:15574707; http://dx.doi.org/10.1529/biophysj.104.053413.
    • (2005) Biophys J , vol.88 , pp. 1134-1142
    • Doeven, M.K.1    Folgering, J.H.2    Krasnikov, V.3    Geertsma, E.R.4    Van Den Bogaart, G.5    Poolman, B.6
  • 67
    • 55649097956 scopus 로고    scopus 로고
    • Dual-color fluores-cence- burst analysis to study pore formation and protein-protein interactions
    • PMID:18667165
    • van den Bogaart G, Kusters I, Velásquez J, Mika JT, Krasnikov V, Driessen AJ, et al. Dual-color fluores-cence- burst analysis to study pore formation and protein-protein interactions. Methods 2008; 46:123-30; PMID:18667165; http://dx.doi.org/10.1016/j.ymeth.2008.06.016.
    • (2008) Methods , vol.46 , pp. 123-130
    • Van Den Bogaart, G.1    Kusters, I.2    Velásquez, J.3    Mika, J.T.4    Krasnikov, V.5    Driessen, A.J.6
  • 68
    • 77649235243 scopus 로고    scopus 로고
    • A simple method for the reconstitution of membrane proteins into giant unilamellar vesicles
    • PMID:20135103
    • Varnier A, Kermarrec F, Blesneac I, Moreau C, Liguori L, Lenormand JL, et al. A simple method for the reconstitution of membrane proteins into giant unilamellar vesicles. J Membr Biol 2010; 233:85-92; PMID:20135103; http://dx.doi.org/10.1007/s00232-010-9227-8.
    • (2010) J Membr Biol , vol.233 , pp. 85-92
    • Varnier, A.1    Kermarrec, F.2    Blesneac, I.3    Moreau, C.4    Liguori, L.5    Lenormand, J.L.6
  • 69
    • 58149503739 scopus 로고    scopus 로고
    • Rapid and improved reconstitution of bacterial mechanosensitive ion channel proteins MscS and MscL into liposomes using a modified sucrose method
    • PMID:19111548
    • Battle AR, Petrov E, Pal P, Martinac B. Rapid and improved reconstitution of bacterial mechanosensitive ion channel proteins MscS and MscL into liposomes using a modified sucrose method. FEBS Lett 2009; 583:407-12; PMID:19111548; http://dx.doi.org/10.1016/j.febslet.2008.12.033.
    • (2009) FEBS Lett , vol.583 , pp. 407-412
    • Battle, A.R.1    Petrov, E.2    Pal, P.3    Martinac, B.4
  • 70
    • 84855499182 scopus 로고    scopus 로고
    • Expression and characterization of the bacterial mechanosensitive channel MscS in Xenopus laevis oocytes
    • PMID:22084416
    • Maksaev G, Haswell ES. Expression and characterization of the bacterial mechanosensitive channel MscS in Xenopus laevis oocytes. J Gen Physiol 2011; 138:641-9; PMID:22084416; http://dx.doi.org/10.1085/jgp.201110723.
    • (2011) J Gen Physiol , vol.138 , pp. 641-649
    • Maksaev, G.1    Haswell, E.S.2
  • 71
    • 7044224839 scopus 로고    scopus 로고
    • The protein-lipid interface: Perspectives from magnetic resonance and crystal structures
    • PMID:15519312
    • Marsh D, Páli T. The protein-lipid interface: perspectives from magnetic resonance and crystal structures. Biochim Biophys Acta 2004; 1666:118-41; PMID:15519312; http://dx.doi.org/10.1016/j.bbamem.2004.08.006.
    • (2004) Biochim Biophys Acta , vol.1666 , pp. 118-141
    • Marsh, D.1    Páli, T.2
  • 72
    • 79957470462 scopus 로고    scopus 로고
    • Lipid-protein interactions
    • PMID:21599646
    • Lee AG. Lipid-protein interactions. Biochem Soc Trans 2011; 39:761-6; PMID:21599646.
    • (2011) Biochem Soc Trans , vol.39 , pp. 761-766
    • Lee, A.G.1
  • 73
    • 33746647787 scopus 로고    scopus 로고
    • Peptides in lipid bilayers: The power of simple models
    • PMID:16828281
    • Killian JA, Nyholm TK. Peptides in lipid bilayers: the power of simple models. Curr Opin Struct Biol 2006; 16:473-9; PMID:16828281; http://dx.doi.org/10.1016/j.sbi.2006.06.007.
    • (2006) Curr Opin Struct Biol , vol.16 , pp. 473-479
    • Killian, J.A.1    Nyholm, T.K.2
  • 74
    • 33646198955 scopus 로고    scopus 로고
    • Molecular dynamics simulations of model trans-membrane peptides in lipid bilayers: A systematic investigation of hydrophobic mismatch
    • PMID:16428278
    • Kandasamy SK, Larson RG. Molecular dynamics simulations of model trans-membrane peptides in lipid bilayers: a systematic investigation of hydrophobic mismatch. Biophys J 2006; 90:2326-43; PMID:16428278; http://dx.doi.org/10.1529/biophysj.105.073395.
    • (2006) Biophys J , vol.90 , pp. 2326-2343
    • Kandasamy, S.K.1    Larson, R.G.2
  • 75
    • 33846963172 scopus 로고    scopus 로고
    • How protein transmembrane segments sense the lipid environment
    • PMID:17279611
    • Nyholm TK, Ozdirekcan S, Killian JA. How protein transmembrane segments sense the lipid environment. Biochemistry 2007; 46:1457-65; PMID:17279611; http://dx.doi.org/10.1021/bi061941c.
    • (2007) Biochemistry , vol.46 , pp. 1457-1465
    • Nyholm, T.K.1    Ozdirekcan, S.2    Killian, J.A.3
  • 76
    • 0038694994 scopus 로고    scopus 로고
    • Snorkeling of lysine side chains in transmembrane helices: How easy can it get?
    • PMID:12782292
    • Strandberg E, Killian JA. Snorkeling of lysine side chains in transmembrane helices: how easy can it get? FEBS Lett 2003; 544:69-73; PMID:12782292; http://dx.doi.org/10.1016/S0014-5793(03)00475-7.
    • (2003) FEBS Lett , vol.544 , pp. 69-73
    • Strandberg, E.1    Killian, J.A.2
  • 77
    • 0034910316 scopus 로고    scopus 로고
    • Structural models of the MscL gating mechanism
    • PMID:11463635
    • Sukharev S, Durell SR, Guy HR. Structural models of the MscL gating mechanism. Biophys J 2001; 81:917-36; PMID:11463635; http://dx.doi.org/10.1016/ S0006-3495(01)75751-7.
    • (2001) Biophys J , vol.81 , pp. 917-936
    • Sukharev, S.1    Durell, S.R.2    Guy, H.R.3
  • 78
    • 3242889840 scopus 로고    scopus 로고
    • Intragenic suppression of gain-of-function mutations in the Escherichia coli mechanosensitive channel, MscL
    • PMID:15228529
    • Li Y, Wray R, Blount P. Intragenic suppression of gain-of-function mutations in the Escherichia coli mechanosensitive channel, MscL. Mol Microbiol 2004; 53:485-95; PMID:15228529; http://dx.doi.org/10.1111/j.1365-2958.2004. 04150.x.
    • (2004) Mol Microbiol , vol.53 , pp. 485-495
    • Li, Y.1    Wray, R.2    Blount, P.3
  • 79
    • 24944467312 scopus 로고    scopus 로고
    • Capping transmembrane helices of MscL with aromatic residues changes channel response to membrane stretch
    • PMID:16156671
    • Chiang CS, Shirinian L, Sukharev S. Capping transmembrane helices of MscL with aromatic residues changes channel response to membrane stretch. Biochemistry 2005; 44:12589-97; PMID:16156671; http://dx.doi.org/10.1021/ bi050750r.
    • (2005) Biochemistry , vol.44 , pp. 12589-12597
    • Chiang, C.S.1    Shirinian, L.2    Sukharev, S.3
  • 80
    • 33746828240 scopus 로고    scopus 로고
    • A finite element framework for studying the mechanical response of macromolecules: Application to the gating of the mechanosensitive channel MscL
    • PMID:16731564
    • Tang Y, Cao G, Chen X, Yoo J, Yethiraj A, Cui Q. A finite element framework for studying the mechanical response of macromolecules: application to the gating of the mechanosensitive channel MscL. Biophys J 2006; 91:1248-63; PMID:16731564; http://dx.doi.org/10.1529/biophysj.106.085985.
    • (2006) Biophys J , vol.91 , pp. 1248-1263
    • Tang, Y.1    Cao, G.2    Chen, X.3    Yoo, J.4    Yethiraj, A.5    Cui, Q.6
  • 81
    • 47749128439 scopus 로고    scopus 로고
    • Gating mechanisms of mechanosensitive channels of large conductance, II: Systematic study of conformational transitions
    • PMID:18390625
    • Tang Y, Yoo J, Yethiraj A, Cui Q, Chen X. Gating mechanisms of mechanosensitive channels of large conductance, II: systematic study of conformational transitions. Biophys J 2008; 95:581-96; PMID:18390625; http://dx.doi.org/10.1529/biophysj.107.128496.
    • (2008) Biophys J , vol.95 , pp. 581-596
    • Tang, Y.1    Yoo, J.2    Yethiraj, A.3    Cui, Q.4    Chen, X.5
  • 82
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • PMID:7108955
    • Kyte J, Doolittle RF. A simple method for displaying the hydropathic character of a protein. J Mol Biol 1982; 157:105-32; PMID:7108955; http://dx.doi.org/10.1016/0022-2836(82)90515-0.
    • (1982) J Mol Biol , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 83
    • 51649115608 scopus 로고    scopus 로고
    • On the structure of the N-terminal domain of the MscL channel: Helical bundle or membrane interface
    • Iscla I, Wray R, Blount P. On the structure of the N-terminal domain of the MscL channel: helical bundle or membrane interface. Biophys J 2008; 95(5):2283-2291.
    • (2008) Biophys J , vol.95 , Issue.5 , pp. 2283-2291
    • Iscla, I.1    Wray, R.2    Blount, P.3
  • 84
    • 42449087270 scopus 로고    scopus 로고
    • New insights of membrane environment effects on MscL channel mechanics from theoretical approaches
    • PMID:18004782
    • Debret G, Valadié H, Stadler AM, Etchebest C. New insights of membrane environment effects on MscL channel mechanics from theoretical approaches. Proteins 2008; 71:1183-96; PMID:18004782; http://dx.doi.org/10.1002/ prot.21810.
    • (2008) Proteins , vol.71 , pp. 1183-1196
    • Debret, G.1    Valadié, H.2    Stadler, A.M.3    Etchebest, C.4
  • 85
    • 2142708147 scopus 로고    scopus 로고
    • Cysteine scanning of MscL transmembrane domains reveals residues critical for mechanosensitive channel gating
    • PMID:15111403
    • Levin G, Blount P. Cysteine scanning of MscL transmembrane domains reveals residues critical for mechanosensitive channel gating. Biophys J 2004; 86:2862-70; PMID:15111403; http://dx.doi.org/10.1016/S0006-3495(04)74338-6.
    • (2004) Biophys J , vol.86 , pp. 2862-2870
    • Levin, G.1    Blount, P.2
  • 86
    • 0038080063 scopus 로고    scopus 로고
    • Generation and evaluation of a large mutational library from the Escherichia coli mechanosensitive channel of large conductance, MscL: Implications for channel gating and evolutionary design
    • PMID:12670944
    • Maurer JA, Dougherty DA. Generation and evaluation of a large mutational library from the Escherichia coli mechanosensitive channel of large conductance, MscL: implications for channel gating and evolutionary design. J Biol Chem 2003; 278:21076-82; PMID:12670944; http://dx.doi.org/10.1074/jbc.M302892200.
    • (2003) J Biol Chem , vol.278 , pp. 21076-21082
    • Maurer, J.A.1    Dougherty, D.A.2
  • 87
    • 43649090741 scopus 로고    scopus 로고
    • Gating of the mechanosensitive channel protein MscL: The interplay of membrane and protein
    • PMID:18212020
    • Jeon J, Voth GA. Gating of the mechanosensitive channel protein MscL: the interplay of membrane and protein. Biophys J 2008; 94:3497-511; PMID:18212020; http://dx.doi.org/10.1529/biophysj.107.109850.
    • (2008) Biophys J , vol.94 , pp. 3497-3511
    • Jeon, J.1    Voth, G.A.2
  • 88
    • 84857737028 scopus 로고    scopus 로고
    • Hydrophobic mismatch of mobile transmembrane helices: Merging theory and experiments
    • PMID:22326890
    • Strandberg E, Esteban-Martín S, Ulrich AS, Salgado J. Hydrophobic mismatch of mobile transmembrane helices: Merging theory and experiments. Biochim Biophys Acta 2012; 1818:1242-9; PMID:22326890; http://dx.doi.org/10. 1016/j.bbamem.2012.01.023.
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 1242-1249
    • Strandberg, E.1    Esteban-Martín, S.2    Ulrich, A.S.3    Salgado, J.4
  • 89
    • 41449090448 scopus 로고    scopus 로고
    • Binding of anionic lipids to at least three nonannular sites on the potassium channel KcsA is required for channel opening
    • PMID:18024500
    • Marius P, Zagnoni M, Sandison ME, East JM, Morgan H, Lee AG. Binding of anionic lipids to at least three nonannular sites on the potassium channel KcsA is required for channel opening. Biophys J 2008; 94:1689-98; PMID:18024500; http://dx.doi.org/10.1529/biophysj.107.117507.
    • (2008) Biophys J , vol.94 , pp. 1689-1698
    • Marius, P.1    Zagnoni, M.2    Sandison, M.E.3    East, J.M.4    Morgan, H.5    Lee, A.G.6
  • 90
    • 56249140425 scopus 로고    scopus 로고
    • Importance of direct interactions with lipids for the function of the mechanosensitive channel MscL
    • PMID:18950196
    • Powl AM, East JM, Lee AG. Importance of direct interactions with lipids for the function of the mechanosensitive channel MscL. Biochemistry 2008; 47:12175-84; PMID:18950196; http://dx.doi.org/10.1021/bi801352a.
    • (2008) Biochemistry , vol.47 , pp. 12175-12184
    • Powl, A.M.1    East, J.M.2    Lee, A.G.3
  • 91
    • 27844504698 scopus 로고    scopus 로고
    • Lipid interactions with bacterial channels: Fluorescence studies
    • PMID:16246007
    • Powl AM, Carney J, Marius P, East JM, Lee AG. Lipid interactions with bacterial channels: fluorescence studies. Biochem Soc Trans 2005; 33:905-9; PMID:16246007; http://dx.doi.org/10.1042/BST20050905.
    • (2005) Biochem Soc Trans , vol.33 , pp. 905-909
    • Powl, A.M.1    Carney, J.2    Marius, P.3    East, J.M.4    Lee, A.G.5
  • 92
    • 24644491716 scopus 로고    scopus 로고
    • Assessment of potential stimuli for mechano-dependent gating of MscL: Effects of pressure, tension, and lipid headgroups
    • PMID:16142922
    • Moe PC, Blount P. Assessment of potential stimuli for mechano-dependent gating of MscL: effects of pressure, tension, and lipid headgroups. Biochemistry 2005; 44:12239-44; PMID:16142922; http://dx.doi.org/10.1021/bi0509649.
    • (2005) Biochemistry , vol.44 , pp. 12239-12244
    • Moe, P.C.1    Blount, P.2
  • 93
    • 34447284723 scopus 로고    scopus 로고
    • Different effects of lipid chain length on the two sides of a membrane and the lipid annulus of MscL
    • PMID:17416625
    • Powl AM, East JM, Lee AG. Different effects of lipid chain length on the two sides of a membrane and the lipid annulus of MscL. Biophys J 2007; 93:113-22; PMID:17416625; http://dx.doi.org/10.1529/biophysj.107.105130.
    • (2007) Biophys J , vol.93 , pp. 113-122
    • Powl, A.M.1    East, J.M.2    Lee, A.G.3
  • 94
    • 79551637188 scopus 로고    scopus 로고
    • An in vivo screen reveals protein-lipid interactions crucial for gating a mechanosensitive channel
    • PMID:21068398
    • Iscla I, Wray R, Blount P. An in vivo screen reveals protein-lipid interactions crucial for gating a mechanosensitive channel. FASEB J 2011; 25:694-702; PMID:21068398; http://dx.doi.org/10.1096/fj.10-170878.
    • (2011) FASEB J , vol.25 , pp. 694-702
    • Iscla, I.1    Wray, R.2    Blount, P.3
  • 95
    • 41849136544 scopus 로고    scopus 로고
    • Anionic phospholipids affect the rate and extent of flux through the mechanosensitive channel of large conductance MscL
    • PMID:18341289
    • Powl AM, East JM, Lee AG. Anionic phospholipids affect the rate and extent of flux through the mechanosensitive channel of large conductance MscL. Biochemistry 2008; 47:4317-28; PMID:18341289; http://dx.doi.org/10.1021/ bi702409t.
    • (2008) Biochemistry , vol.47 , pp. 4317-4328
    • Powl, A.M.1    East, J.M.2    Lee, A.G.3
  • 96
    • 77953053747 scopus 로고    scopus 로고
    • Adaptive behavior of bacterial mechanosensitive channels is coupled to membrane mechanics
    • PMID:20513760
    • Belyy V, Kamaraju K, Akitake B, Anishkin A, Sukharev S. Adaptive behavior of bacterial mechanosensitive channels is coupled to membrane mechanics. J Gen Physiol 2010; 135:641-52; PMID:20513760; http://dx.doi.org/10.1085/jgp. 200910371.
    • (2010) J Gen Physiol , vol.135 , pp. 641-652
    • Belyy, V.1    Kamaraju, K.2    Akitake, B.3    Anishkin, A.4    Sukharev, S.5
  • 97
    • 0037450544 scopus 로고    scopus 로고
    • Specific lipid requirements of membrane proteins - A putative bottleneck in heterologous expression
    • PMID:12586375
    • Opekarová M, Tanner W. Specific lipid requirements of membrane proteins - a putative bottleneck in heterologous expression. Biochim Biophys Acta 2003; 1610:11-22; PMID:12586375; http://dx.doi.org/10.1016/S0005-2736(02) 00708-3.
    • (2003) Biochim Biophys Acta , vol.1610 , pp. 11-22
    • Opekarová, M.1    Tanner, W.2
  • 98
    • 44449167975 scopus 로고    scopus 로고
    • Role of phosphatidylglycerols in the stability of bacterial membranes
    • PMID:18373983
    • Zhao W, Róg T, Gurtovenko AA, Vattulainen I, Karttunen M. Role of phosphatidylglycerols in the stability of bacterial membranes. Biochimie 2008; 90:930-8; PMID:18373983; http://dx.doi.org/10.1016/j.biochi.2008.02.025.
    • (2008) Biochimie , vol.90 , pp. 930-938
    • Zhao, W.1    Róg, T.2    Gurtovenko, A.A.3    Vattulainen, I.4    Karttunen, M.5
  • 99
    • 20144372892 scopus 로고    scopus 로고
    • Pivotal role of the glycine-rich TM3 helix in gating the MscS mechanosensitive channel
    • PMID:15665866
    • Edwards MD, Li Y, Kim S, Miller S, Bartlett W, Black S, et al. Pivotal role of the glycine-rich TM3 helix in gating the MscS mechanosensitive channel. Nat Struct Mol Biol 2005; 12:113-9; PMID:15665866; http://dx.doi.org/10.1038/ nsmb895.
    • (2005) Nat Struct Mol Biol , vol.12 , pp. 113-119
    • Edwards, M.D.1    Li, Y.2    Kim, S.3    Miller, S.4    Bartlett, W.5    Black, S.6
  • 100
    • 80052511947 scopus 로고    scopus 로고
    • Cytoplasmic domain filter function in the mechanosensitive channel of small conductance
    • PMID:21723817
    • Gamini R, Sotomayor M, Chipot C, Schulten K. Cytoplasmic domain filter function in the mechanosensitive channel of small conductance. Biophys J 2011; 101:80-9; PMID:21723817; http://dx.doi.org/10.1016/j.bpj.2011.05.042.
    • (2011) Biophys J , vol.101 , pp. 80-89
    • Gamini, R.1    Sotomayor, M.2    Chipot, C.3    Schulten, K.4
  • 102
    • 33749012269 scopus 로고    scopus 로고
    • Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic α-helical antimicrobial peptides
    • PMID:16697975
    • Sato H, Feix JB. Peptide-membrane interactions and mechanisms of membrane destruction by amphipathic α-helical antimicrobial peptides. Biochim Biophys Acta 2006; 1758:1245-56; PMID:16697975; http://dx.doi.org/10.1016/j. bbamem.2006.02.021.
    • (2006) Biochim Biophys Acta , vol.1758 , pp. 1245-1256
    • Sato, H.1    Feix, J.B.2
  • 103
    • 34447322795 scopus 로고    scopus 로고
    • The history of alamethicin: A review of the most extensively studied peptaibol
    • PMID:17589875
    • Leitgeb B, Szekeres A, Manczinger L, Vágvölgyi C, Kredics L. The history of alamethicin: a review of the most extensively studied peptaibol. Chem Biodivers 2007; 4:1027-51; PMID:17589875; http://dx.doi.org/10.1002/cbdv. 200790095.
    • (2007) Chem Biodivers , vol.4 , pp. 1027-1051
    • Leitgeb, B.1    Szekeres, A.2    Manczinger, L.3    Vágvölgyi, C.4    Kredics, L.5
  • 104
    • 77953724763 scopus 로고    scopus 로고
    • Antimicrobial peptides in toroidal and cylindrical pores
    • PMID:20403332
    • Mihajlovic M, Lazaridis T. Antimicrobial peptides in toroidal and cylindrical pores. Biochim Biophys Acta 2010; 1798:1485-93; PMID:20403332; http://dx.doi.org/10.1016/j.bbamem.2010.04.004.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 1485-1493
    • Mihajlovic, M.1    Lazaridis, T.2
  • 105
    • 77953705223 scopus 로고    scopus 로고
    • Antimicrobial peptides bind more strongly to membrane pores
    • PMID:20188066
    • Mihajlovic M, Lazaridis T. Antimicrobial peptides bind more strongly to membrane pores. Biochim Biophys Acta 2010; 1798:1494-502; PMID:20188066; http://dx.doi.org/10.1016/j.bbamem.2010.02.023.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 1494-1502
    • Mihajlovic, M.1    Lazaridis, T.2
  • 106
    • 84855453413 scopus 로고    scopus 로고
    • Mechanism of structural transformations induced by antimicrobial peptides in lipid membranes
    • PMID:22100601
    • Lam KL, Wang H, Siaw TA, Chapman MR, Waring AJ, Kindt JT, et al. Mechanism of structural transformations induced by antimicrobial peptides in lipid membranes. Biochim Biophys Acta 2012; 1818:194-204; PMID:22100601; http://dx.doi.org/10.1016/j.bbamem.2011.11.002.
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 194-204
    • Lam, K.L.1    Wang, H.2    Siaw, T.A.3    Chapman, M.R.4    Waring, A.J.5    Kindt, J.T.6
  • 107
    • 0028157445 scopus 로고
    • Transduction of membrane tension by the ion channel alamethicin
    • PMID:7510531
    • Opsahl LR, Webb WW. Transduction of membrane tension by the ion channel alamethicin. Biophys J 1994; 66:71-4; PMID:7510531; http://dx.doi.org/10.1016/ S0006-3495(94)80751-9.
    • (1994) Biophys J , vol.66 , pp. 71-74
    • Opsahl, L.R.1    Webb, W.W.2
  • 108
    • 0034068919 scopus 로고    scopus 로고
    • Stability of a melittin pore in a lipid bilayer: A molecular dynamics study
    • PMID:10733954
    • Lin JH, Baumgaertner A. Stability of a melittin pore in a lipid bilayer: a molecular dynamics study. Biophys J 2000; 78:1714-24; PMID:10733954; http://dx.doi.org/10.1016/S0006-3495(00)76723-3.
    • (2000) Biophys J , vol.78 , pp. 1714-1724
    • Lin, J.H.1    Baumgaertner, A.2
  • 109
    • 27544458537 scopus 로고    scopus 로고
    • Surface tension effect on transmembrane channel stability in a model membrane
    • PMID:16853516
    • Zhu Q, Vaughn MW. Surface tension effect on transmembrane channel stability in a model membrane. J Phys Chem B 2005; 109:19474-83; PMID:16853516; http://dx.doi.org/10.1021/jp051419k.
    • (2005) J Phys Chem B , vol.109 , pp. 19474-19483
    • Zhu, Q.1    Vaughn, M.W.2
  • 110
    • 0034910318 scopus 로고    scopus 로고
    • Osmotically induced membrane tension modulates membrane permeabilization by class L amphipathic helical peptides: Nucleation model of defect formation
    • PMID:11463637
    • Polozov IV, Anantharamaiah GM, Segrest JP, Epand RM. Osmotically induced membrane tension modulates membrane permeabilization by class L amphipathic helical peptides: nucleation model of defect formation. Biophys J 2001; 81:949-59; PMID:11463637; http://dx.doi.org/10.1016/S0006-3495(01)75753-0.
    • (2001) Biophys J , vol.81 , pp. 949-959
    • Polozov, I.V.1    Anantharamaiah, G.M.2    Segrest, J.P.3    Epand, R.M.4
  • 111
    • 0030030828 scopus 로고    scopus 로고
    • Osmotic and pH transmembrane gradients control the lytic power of melittin
    • PMID:8789100
    • Benachir T, Lafleur M. Osmotic and pH transmembrane gradients control the lytic power of melittin. Biophys J 1996; 70:831-40; PMID:8789100; http://dx.doi.org/10.1016/S0006-3495(96)79622-4.
    • (1996) Biophys J , vol.70 , pp. 831-840
    • Benachir, T.1    Lafleur, M.2
  • 112
    • 2942754299 scopus 로고    scopus 로고
    • Molecular mechanism of Peptide-induced pores in membranes
    • PMID:15169456
    • Huang HW, Chen FY, Lee MT. Molecular mechanism of Peptide-induced pores in membranes. Phys Rev Lett 2004; 92:198304; PMID:15169456; http://dx.doi.org/ 10.1103/PhysRevLett.92.198304.
    • (2004) Phys Rev Lett , vol.92 , pp. 198304
    • Huang, H.W.1    Chen, F.Y.2    Lee, M.T.3
  • 113
    • 60749131043 scopus 로고    scopus 로고
    • Orientation and peptide-lipid interactions of alamethicin incorporated in phospholipid membranes: Polarized infrared and spin-label EPR spectroscopy
    • PMID:19133787
    • Marsh D. Orientation and peptide-lipid interactions of alamethicin incorporated in phospholipid membranes: polarized infrared and spin-label EPR spectroscopy. Biochemistry 2009; 48:729-37; PMID:19133787; http://dx.doi.org/10. 1021/bi801279n.
    • (2009) Biochemistry , vol.48 , pp. 729-737
    • Marsh, D.1
  • 114
    • 0035498468 scopus 로고    scopus 로고
    • Voltage-dependent pore formation and antimicrobial activity by alamethicin and analogues
    • PMID:11687873
    • Duclohier H, Wróblewski H. Voltage-dependent pore formation and antimicrobial activity by alamethicin and analogues. J Membr Biol 2001; 184:1-12; PMID:11687873; http://dx.doi.org/10.1007/s00232-001-0077-2.
    • (2001) J Membr Biol , vol.184 , pp. 1-12
    • Duclohier, H.1    Wróblewski, H.2
  • 115
    • 77749314917 scopus 로고    scopus 로고
    • Interactions of alamethicin with model cell membranes investigated using sum frequency generation vibrational spectroscopy in real time in situ
    • PMID:20163089
    • Ye S, Nguyen KT, Chen Z. Interactions of alamethicin with model cell membranes investigated using sum frequency generation vibrational spectroscopy in real time in situ. J Phys Chem B 2010; 114:3334-40; PMID:20163089; http://dx.doi.org/10.1021/jp911174d.
    • (2010) J Phys Chem B , vol.114 , pp. 3334-3340
    • Ye, S.1    Nguyen, K.T.2    Chen, Z.3
  • 116
    • 25844513230 scopus 로고    scopus 로고
    • Interaction of alamethicin with ether-linked phospholipid bilayers: Oriented circular dichroism, 31P solid-state NMR, and differential scanning calorimetry studies
    • PMID:16055546
    • Dave PC, Billington E, Pan YL, Straus SK. Interaction of alamethicin with ether-linked phospholipid bilayers: oriented circular dichroism, 31P solid-state NMR, and differential scanning calorimetry studies. Biophys J 2005; 89:2434-42; PMID:16055546; http://dx.doi.org/10.1529/biophysj.105.067678.
    • (2005) Biophys J , vol.89 , pp. 2434-2442
    • Dave, P.C.1    Billington, E.2    Pan, Y.L.3    Straus, S.K.4
  • 117
    • 79952000948 scopus 로고    scopus 로고
    • Long-term-stable ether-lipid vs conventional ester-lipid bicelles in oriented solid-state NMR: Altered structural information in studies of antimicrobial peptides
    • PMID:21309516
    • Bertelsen K, Vad B, Nielsen EH, Hansen SK, Skrydstrup T, Otzen DE, et al. Long-term-stable ether-lipid vs conventional ester-lipid bicelles in oriented solid-state NMR: altered structural information in studies of antimicrobial peptides. J Phys Chem B 2011; 115:1767-74; PMID:21309516; http://dx.doi.org/10. 1021/jp110866g.
    • (2011) J Phys Chem B , vol.115 , pp. 1767-1774
    • Bertelsen, K.1    Vad, B.2    Nielsen, E.H.3    Hansen, S.K.4    Skrydstrup, T.5    Otzen, D.E.6
  • 118
    • 15244349709 scopus 로고    scopus 로고
    • Melittin-induced bilayer leakage depends on lipid material properties: Evidence for toroidal pores
    • PMID:15596510
    • Allende D, Simon SA, McIntosh TJ. Melittin-induced bilayer leakage depends on lipid material properties: evidence for toroidal pores. Biophys J 2005; 88:1828-37; PMID:15596510; http://dx.doi.org/10.1529/biophysj.104.049817.
    • (2005) Biophys J , vol.88 , pp. 1828-1837
    • Allende, D.1    Simon, S.A.2    McIntosh, T.J.3
  • 119
    • 0034859096 scopus 로고    scopus 로고
    • Barrel-stave model or toroidal model? A case study on melittin pores
    • PMID:11509361
    • Yang L, Harroun TA, Weiss TM, Ding L, Huang HW. Barrel-stave model or toroidal model? A case study on melittin pores. Biophys J 2001; 81:1475-85; PMID:11509361; http://dx.doi.org/10.1016/S0006-3495(01)75802-X.
    • (2001) Biophys J , vol.81 , pp. 1475-1485
    • Yang, L.1    Harroun, T.A.2    Weiss, T.M.3    Ding, L.4    Huang, H.W.5
  • 120
    • 34447282684 scopus 로고    scopus 로고
    • Melittin: A membrane-active peptide with diverse functions
    • PMID:17139559
    • Raghuraman H, Chattopadhyay A. Melittin: a membrane-active peptide with diverse functions. Biosci Rep 2007; 27:189-223; PMID:17139559; http://dx.doi.org/10.1007/s10540-006-9030-z.
    • (2007) Biosci Rep , vol.27 , pp. 189-223
    • Raghuraman, H.1    Chattopadhyay, A.2
  • 121
    • 1642488938 scopus 로고    scopus 로고
    • Analytic models for mechanotransduction: Gating a mechanosensitive channel
    • PMID:15024097
    • Wiggins P, Phillips R. Analytic models for mechanotransduction: gating a mechanosensitive channel. Proc Natl Acad Sci U S A 2004; 101:4071-6; PMID:15024097; http://dx.doi.org/10.1073/pnas.0307804101.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 4071-4076
    • Wiggins, P.1    Phillips, R.2
  • 122
    • 16344384943 scopus 로고    scopus 로고
    • Dynamic structure of vesicle-bound melittin in a variety of lipid chain lengths by solid-state NMR
    • PMID:15339796
    • Toraya S, Nishimura K, Naito A. Dynamic structure of vesicle-bound melittin in a variety of lipid chain lengths by solid-state NMR. Biophys J 2004; 87:3323-35; PMID:15339796; http://dx.doi.org/10.1529/biophysj.104.046102.
    • (2004) Biophys J , vol.87 , pp. 3323-3335
    • Toraya, S.1    Nishimura, K.2    Naito, A.3
  • 123
    • 13944255096 scopus 로고    scopus 로고
    • Understanding the energetics of helical peptide orientation in membranes
    • PMID:15657932
    • Sengupta D, Meinhold L, Langosch D, Ullmann GM, Smith JC. Understanding the energetics of helical peptide orientation in membranes. Proteins 2005; 58:913-22; PMID:15657932; http://dx.doi.org/10.1002/prot.20383.
    • (2005) Proteins , vol.58 , pp. 913-922
    • Sengupta, D.1    Meinhold, L.2    Langosch, D.3    Ullmann, G.M.4    Smith, J.C.5
  • 124
    • 58849139281 scopus 로고    scopus 로고
    • Structure and alignment of the membrane-associated peptaibols ampullosporin A and alamethicin by oriented 15N and 31P solid-state NMR spectroscopy
    • PMID:18835909
    • Salnikov ES, Friedrich H, Li X, Bertani P, Reissmann S, Hertweck C, et al. Structure and alignment of the membrane-associated peptaibols ampullosporin A and alamethicin by oriented 15N and 31P solid-state NMR spectroscopy. Biophys J 2009; 96:86-100; PMID:18835909; http://dx.doi.org/10.1529/biophysj.108.136242.
    • (2009) Biophys J , vol.96 , pp. 86-100
    • Salnikov, E.S.1    Friedrich, H.2    Li, X.3    Bertani, P.4    Reissmann, S.5    Hertweck, C.6
  • 125
    • 0037147239 scopus 로고    scopus 로고
    • Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature
    • PMID:12381734
    • Basañez G, Sharpe JC, Galanis J, Brandt TB, Hardwick JM, Zimmerberg J. Bax-type apoptotic proteins porate pure lipid bilayers through a mechanism sensitive to intrinsic monolayer curvature. J Biol Chem 2002; 277:49360-5; PMID:12381734; http://dx.doi.org/10.1074/jbc.M206069200.
    • (2002) J Biol Chem , vol.277 , pp. 49360-49365
    • Basañez, G.1    Sharpe, J.C.2    Galanis, J.3    Brandt, T.B.4    Hardwick, J.M.5    Zimmerberg, J.6
  • 126
    • 22244493864 scopus 로고    scopus 로고
    • Peptides derived from apoptotic Bax and Bid reproduce the poration activity of the parent full-length proteins
    • PMID:15778450
    • García-Sáez AJ, Coraiola M, Dalla Serra M, Mingarro I, Menestrina G, Salgado J. Peptides derived from apoptotic Bax and Bid reproduce the poration activity of the parent full-length proteins. Biophys J 2005; 88:3976-90; PMID:15778450; http://dx.doi.org/10.1529/biophysj.104.058008.
    • (2005) Biophys J , vol.88 , pp. 3976-3990
    • García-Sáez, A.J.1    Coraiola, M.2    Dalla Serra, M.3    Mingarro, I.4    Menestrina, G.5    Salgado, J.6
  • 127
    • 33644946679 scopus 로고    scopus 로고
    • Peptides corresponding to helices 5 and 6 of Bax can independently form large lipid pores
    • PMID:16478471
    • García-Sáez AJ, Coraiola M, Serra MD, Mingarro I, Müller P, Salgado J. Peptides corresponding to helices 5 and 6 of Bax can independently form large lipid pores. FEBS J 2006; 273:971-81; PMID:16478471; http://dx.doi.org/10.1111/j.1742-4658.2006.05123.x.
    • (2006) FEBS J , vol.273 , pp. 971-981
    • García-Sáez, A.J.1    Coraiola, M.2    Serra, M.D.3    Mingarro, I.4    Müller, P.5    Salgado, J.6
  • 128
    • 34447255173 scopus 로고    scopus 로고
    • Pore formation by a Bax-derived peptide: Effect on the line tension of the membrane probed by AFM
    • PMID:17416629
    • García-Sáez AJ, Chiantia S, Salgado J, Schwille P. Pore formation by a Bax-derived peptide: effect on the line tension of the membrane probed by AFM. Biophys J 2007; 93:103-12; PMID:17416629; http://dx.doi.org/10. 1529/biophysj.106.100370.
    • (2007) Biophys J , vol.93 , pp. 103-112
    • García-Sáez, A.J.1    Chiantia, S.2    Salgado, J.3    Schwille, P.4
  • 129
    • 4944225045 scopus 로고    scopus 로고
    • Effect of lipids with different spontaneous curvature on the channel activity of colicin E1: Evidence in favor of a toroidal pore
    • PMID:15474038
    • Sobko AA, Kotova EA, Antonenko YN, Zakharov SD, Cramer WA. Effect of lipids with different spontaneous curvature on the channel activity of colicin E1: evidence in favor of a toroidal pore. FEBS Lett 2004; 576:205-10; PMID:15474038; http://dx.doi.org/10.1016/j.febslet.2004.09.016.
    • (2004) FEBS Lett , vol.576 , pp. 205-210
    • Sobko, A.A.1    Kotova, E.A.2    Antonenko, Y.N.3    Zakharov, S.D.4    Cramer, W.A.5
  • 130
    • 33744921915 scopus 로고    scopus 로고
    • Lipid dependence of the channel properties of a colicin E1-lipid toroidal pore
    • PMID:16556601
    • Sobko AA, Kotova EA, Antonenko YN, Zakharov SD, Cramer WA. Lipid dependence of the channel properties of a colicin E1-lipid toroidal pore. J Biol Chem 2006; 281:14408-16; PMID:16556601; http://dx.doi.org/10.1074/jbc. M513634200.
    • (2006) J Biol Chem , vol.281 , pp. 14408-14416
    • Sobko, A.A.1    Kotova, E.A.2    Antonenko, Y.N.3    Zakharov, S.D.4    Cramer, W.A.5
  • 131
    • 48749122220 scopus 로고    scopus 로고
    • Mechanosensitive channel MscS in the open state: Modeling of the transition, explicit simulations, and experimental measurements of conductance
    • PMID:18591417
    • Anishkin A, Kamaraju K, Sukharev S. Mechanosensitive channel MscS in the open state: modeling of the transition, explicit simulations, and experimental measurements of conductance. J Gen Physiol 2008; 132:67-83; PMID:18591417; http://dx.doi.org/10.1085/jgp.200810000.
    • (2008) J Gen Physiol , vol.132 , pp. 67-83
    • Anishkin, A.1    Kamaraju, K.2    Sukharev, S.3
  • 132
    • 0027291942 scopus 로고
    • Probability of alamethicin conductance states varies with nonlamellar tendency of bilayer phospholipids
    • PMID:8369434
    • Keller SL, Bezrukov SM, Gruner SM, Tate MW, Vodyanoy I, Parsegian VA. Probability of alamethicin conductance states varies with nonlamellar tendency of bilayer phospholipids. Biophys J 1993; 65:23-7; PMID:8369434; http://dx.doi.org/10.1016/S0006-3495(93)81040-3.
    • (1993) Biophys J , vol.65 , pp. 23-27
    • Keller, S.L.1    Bezrukov, S.M.2    Gruner, S.M.3    Tate, M.W.4    Vodyanoy, I.5    Parsegian, V.A.6
  • 133
    • 0032227858 scopus 로고    scopus 로고
    • Lipid packing stress and polypeptide aggregation: Alamethicin channel probed by proton titration of lipid charge
    • discussion 225-46; PMID:10822608
    • Bezrukov SM, Rand RP, Vodyanoy I, Parsegian VA. Lipid packing stress and polypeptide aggregation: alamethicin channel probed by proton titration of lipid charge. Faraday Discuss 1998; 111:173-83, discussion 225-46; PMID:10822608; http://dx.doi.org/10.1039/a806579i.
    • (1998) Faraday Discuss , vol.111 , pp. 173-183
    • Bezrukov, S.M.1    Rand, R.P.2    Vodyanoy, I.3    Parsegian, V.A.4
  • 134
    • 0028860483 scopus 로고
    • Two classes of alamethicin transmembrane channels: Molecular models from single-channel properties
    • PMID:8599639
    • Mak DO, Webb WW. Two classes of alamethicin transmembrane channels: molecular models from single-channel properties. Biophys J 1995; 69:2323-36; PMID:8599639; http://dx.doi.org/10.1016/S0006-3495(95)80102-5.
    • (1995) Biophys J , vol.69 , pp. 2323-2336
    • Mak, D.O.1    Webb, W.W.2
  • 135
    • 80052467631 scopus 로고    scopus 로고
    • Defining the role of the tension sensor in the mechanosensitive channel of small conductance
    • PMID:21767486
    • Malcolm HR, Heo YY, Elmore DE, Maurer JA. Defining the role of the tension sensor in the mechanosensitive channel of small conductance. Biophys J 2011; 101:345-52; PMID:21767486; http://dx.doi.org/10.1016/j.bpj.2011.05.058.
    • (2011) Biophys J , vol.101 , pp. 345-352
    • Malcolm, H.R.1    Heo, Y.Y.2    Elmore, D.E.3    Maurer, J.A.4
  • 136
    • 0034698046 scopus 로고    scopus 로고
    • Comparing and contrasting Escherichia coli and Mycobacterium tuberculosis mechanosensitive channels (MscL). New gain of function mutations in the loop region
    • PMID:10801868
    • Maurer JA, Elmore DE, Lester HA, Dougherty DA. Comparing and contrasting Escherichia coli and Mycobacterium tuberculosis mechanosensitive channels (MscL). New gain of function mutations in the loop region. J Biol Chem 2000; 275:22238-44; PMID:10801868; http://dx.doi.org/10.1074/jbc.M003056200.
    • (2000) J Biol Chem , vol.275 , pp. 22238-22244
    • Maurer, J.A.1    Elmore, D.E.2    Lester, H.A.3    Dougherty, D.A.4
  • 137
    • 0037334905 scopus 로고    scopus 로고
    • On the conformation of the COOH-terminal domain of the large mechanosensitive channel MscL
    • PMID:12601086
    • Anishkin A, Gendel V, Sharifi NA, Chiang CS, Shirinian L, Guy HR, et al. On the conformation of the COOH-terminal domain of the large mechanosensitive channel MscL. J Gen Physiol 2003; 121:227-44; PMID:12601086; http://dx.doi.org/10.1085/jgp.20028768.
    • (2003) J Gen Physiol , vol.121 , pp. 227-244
    • Anishkin, A.1    Gendel, V.2    Sharifi, N.A.3    Chiang, C.S.4    Shirinian, L.5    Guy, H.R.6
  • 138
    • 84860390116 scopus 로고    scopus 로고
    • The oligomeric state of the truncated mechanosensitive channel of large conductance shows no variance in vivo
    • PMID:21739498
    • Iscla I, Wray R, Blount P. The oligomeric state of the truncated mechanosensitive channel of large conductance shows no variance in vivo. Protein Sci 2011; 20:1638-42; PMID:21739498; http://dx.doi.org/10.1002/pro.686.
    • (2011) Protein Sci , vol.20 , pp. 1638-1642
    • Iscla, I.1    Wray, R.2    Blount, P.3
  • 139
    • 57749116040 scopus 로고    scopus 로고
    • On the mechanism of pore formation by melittin
    • PMID:18819911
    • van den Bogaart G, Guzmán JV, Mika JT, Poolman B. On the mechanism of pore formation by melittin. J Biol Chem 2008; 283:33854-7; PMID:18819911; http://dx.doi.org/10.1074/jbc.M805171200.
    • (2008) J Biol Chem , vol.283 , pp. 33854-33857
    • Van Den Bogaart, G.1    Guzmán, J.V.2    Mika, J.T.3    Poolman, B.4
  • 140
    • 0028285338 scopus 로고
    • Chemical synthesis and characterization of peptides and oligomeric proteins designed to form transmembrane ion channels
    • PMID:7523324
    • Iwamoto T, Grove A, Montal MO, Montal M, Tomich JM. Chemical synthesis and characterization of peptides and oligomeric proteins designed to form transmembrane ion channels. Int J Pept Protein Res 1994; 43:597-607; PMID:7523324; http://dx.doi.org/10.1111/j.1399-3011.1994.tb00562.x.
    • (1994) Int J Pept Protein Res , vol.43 , pp. 597-607
    • Iwamoto, T.1    Grove, A.2    Montal, M.O.3    Montal, M.4    Tomich, J.M.5
  • 141
    • 0029870676 scopus 로고    scopus 로고
    • Peptide models for membrane channels
    • PMID:8615800
    • Marsh D. Peptide models for membrane channels. Biochem J 1996; 315:345-61; PMID:8615800.
    • (1996) Biochem J , vol.315 , pp. 345-361
    • Marsh, D.1
  • 142
    • 15744405292 scopus 로고    scopus 로고
    • A synthetic peptide forms voltage-gated porin-like ion channels in lipid bilayer membranes
    • PMID:15796923
    • Thundimadathil J, Roeske RW, Guo L. A synthetic peptide forms voltage-gated porin-like ion channels in lipid bilayer membranes. Biochem Biophys Res Commun 2005; 330:585-90; PMID:15796923; http://dx.doi.org/10.1016/j. bbrc.2005.02.184.
    • (2005) Biochem Biophys Res Commun , vol.330 , pp. 585-590
    • Thundimadathil, J.1    Roeske, R.W.2    Guo, L.3
  • 143
    • 33645974334 scopus 로고    scopus 로고
    • Redesigning channel-forming peptides: Amino acid substitutions that enhance rates of supramolecular self-assembly and raise ion transport activity
    • PMID:16387776
    • Shank LP, Broughman JR, Takeguchi W, Cook G, Robbins AS, Hahn L, et al. Redesigning channel-forming peptides: amino acid substitutions that enhance rates of supramolecular self-assembly and raise ion transport activity. Biophys J 2006; 90:2138-50; PMID:16387776; http://dx.doi.org/10.1529/biophysj.105. 070078.
    • (2006) Biophys J , vol.90 , pp. 2138-2150
    • Shank, L.P.1    Broughman, J.R.2    Takeguchi, W.3    Cook, G.4    Robbins, A.S.5    Hahn, L.6
  • 144
    • 79953686194 scopus 로고    scopus 로고
    • Strategies and perspectives in ion-channel engineering
    • PMID:21472911
    • Grosse W, Essen LO, Koert U. Strategies and perspectives in ion-channel engineering. Chembiochem 2011; 12:830-9; PMID:21472911; http://dx.doi.org/10. 1002/cbic.201000793.
    • (2011) Chembiochem , vol.12 , pp. 830-839
    • Grosse, W.1    Essen, L.O.2    Koert, U.3
  • 145
    • 84857200887 scopus 로고    scopus 로고
    • Protein conducting channels-mechanisms, structures and applications
    • PMID:22258412
    • Bonardi F, Nouwen N, Feringa BL, Driessen AJ. Protein conducting channels-mechanisms, structures and applications. Mol Biosyst 2012; 8:709-19; PMID:22258412; http://dx.doi.org/10.1039/c2mb05433g.
    • (2012) Mol Biosyst , vol.8 , pp. 709-719
    • Bonardi, F.1    Nouwen, N.2    Feringa, B.L.3    Driessen, A.J.4
  • 146
    • 0041441177 scopus 로고    scopus 로고
    • Membrane peptides and their role in protobiological evolution
    • PMID:12967266
    • Pohorille A, Wilson MA, Chipot C. Membrane peptides and their role in protobiological evolution. Orig Life Evol Biosph 2003; 33:173-97; PMID:12967266; http://dx.doi.org/10.1023/A:1024627726231.
    • (2003) Orig Life Evol Biosph , vol.33 , pp. 173-197
    • Pohorille, A.1    Wilson, M.A.2    Chipot, C.3
  • 147
    • 0036828867 scopus 로고    scopus 로고
    • How did cells get their size?
    • PMID:12382322
    • Morris CE. How did cells get their size? Anat Rec 2002; 268:239-51; PMID:12382322; http://dx.doi.org/10.1002/ar.10158.
    • (2002) Anat Rec , vol.268 , pp. 239-251
    • Morris, C.E.1
  • 148
    • 0036829555 scopus 로고    scopus 로고
    • Membrane self-assembly processes: Steps toward the first cellular life
    • PMID:12382318
    • Monnard PA, Deamer DW. Membrane self-assembly processes: steps toward the first cellular life. Anat Rec 2002; 268:196-207; PMID:12382318; http://dx.doi.org/10.1002/ar.10154.
    • (2002) Anat Rec , vol.268 , pp. 196-207
    • Monnard, P.A.1    Deamer, D.W.2
  • 149
    • 63549086214 scopus 로고    scopus 로고
    • Co-evolution of primordial membranes and membrane proteins
    • PMID:19303305
    • Mulkidjanian AY, Galperin MY, Koonin EV. Co-evolution of primordial membranes and membrane proteins. Trends Biochem Sci 2009; 34:206-15; PMID:19303305; http://dx.doi.org/10.1016/j.tibs.2009.01.005.
    • (2009) Trends Biochem Sci , vol.34 , pp. 206-215
    • Mulkidjanian, A.Y.1    Galperin, M.Y.2    Koonin, E.V.3
  • 150
    • 78650543009 scopus 로고    scopus 로고
    • Release of content through mechanosensitive gates in pressurized liposomes
    • PMID:21041677
    • Louhivuori M, Risselada HJ, van der Giessen E, Marrink SJ. Release of content through mechanosensitive gates in pressurized liposomes. Proc Natl Acad Sci U S A 2010; 107:19856-60; PMID:21041677; http://dx.doi.org/10.1073/pnas. 1001316107.
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 19856-19860
    • Louhivuori, M.1    Risselada, H.J.2    Van Der Giessen, E.3    Marrink, S.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.