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Volumn 1808, Issue 6, 2011, Pages 1673-1683

On the role of anionic lipids in charged protein interactions with membranes

Author keywords

Anionic lipid; Arginine; Cell penetrating peptide; Membrane binding; Phosphatidylglycerol; Proteinlipid interaction

Indexed keywords

ARGININE; LIPID; PHOSPHATIDYLCHOLINE; PHOSPHATIDYLGLYCEROL;

EID: 79954723199     PISSN: 00052736     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamem.2010.11.009     Document Type: Article
Times cited : (46)

References (108)
  • 3
    • 20544475665 scopus 로고    scopus 로고
    • Membrane-protein interactions in cell signaling and membrane trafficking
    • DOI 10.1146/annurev.biophys.33.110502.133337
    • W.H. Cho, and R.V. Stahelin Membrane-protein interactions in cell signaling and membrane trafficking Annu. Rev. Biophys. Biomol. Struct. 34 2005 119 151 (Pubitemid 40847721)
    • (2005) Annual Review of Biophysics and Biomolecular Structure , vol.34 , pp. 119-151
    • Cho, W.1    Stahelin, R.V.2
  • 5
    • 52949087550 scopus 로고    scopus 로고
    • Disparate proteins use similar architectures to damage membranes
    • G. Anderluh, and J.H. Lakey Disparate proteins use similar architectures to damage membranes Trends Biochem. Sci. 33 2008 482 490
    • (2008) Trends Biochem. Sci. , vol.33 , pp. 482-490
    • Anderluh, G.1    Lakey, J.H.2
  • 6
    • 35448979574 scopus 로고    scopus 로고
    • The role of electrostatic and nonpolar interactions in the association of peripheral proteins with membranes
    • D. Murray, A. Arbuzova, B. Honig, and S. McLaughlin The role of electrostatic and nonpolar interactions in the association of peripheral proteins with membranes Pept. Lipid Interact. 52 2002 277 307
    • (2002) Pept. Lipid Interact. , vol.52 , pp. 277-307
    • Murray, D.1    Arbuzova, A.2    Honig, B.3    McLaughlin, S.4
  • 8
    • 0030754783 scopus 로고    scopus 로고
    • Electrostatic binding of proteins to membranes. Theoretical predictions and experimental results with charybdotoxin and phospholipid vesicles
    • N. Ben-Tal, B. Honig, C. Miller, and S. McLaughlin Electrostatic binding of proteins to membranes. Theoretical predictions and experimental results with charybdotoxin and phospholipid vesicles Biophys. J. 73 1997 1717 1727 (Pubitemid 27425703)
    • (1997) Biophysical Journal , vol.73 , Issue.4 , pp. 1717-1727
    • Ben-Tal, N.1    Honig, B.2    Miller, C.3    McLaughlin, S.4
  • 9
    • 34247211729 scopus 로고    scopus 로고
    • Annexin A4 binding to anionic phospholipid vesicles modulated by pH and calcium
    • DOI 10.1007/s00249-007-0147-1, Klaus Arnold Special Issue
    • O. Zschornig, F. Opitz, and M. Muller Annexin A4 binding to anionic phospholipid vesicles modulated by pH and calcium Eur. Biophys. J. 36 2007 415 424 (Pubitemid 46626219)
    • (2007) European Biophysics Journal , vol.36 , Issue.4-5 , pp. 415-424
    • Zschornig, O.1    Opitz, F.2    Muller, M.3
  • 10
    • 0030957823 scopus 로고    scopus 로고
    • Molecular basis for membrane phospholipid diversity: Why are there so many lipids?
    • DOI 10.1146/annurev.biochem.66.1.199
    • W. Dowhan Molecular basis for membrane phospholipid diversity: why are there so many lipids? Annu. Rev. Biochem. 66 1997 199 232 (Pubitemid 27274656)
    • (1997) Annual Review of Biochemistry , vol.66 , pp. 199-232
    • Dowhan, W.1
  • 14
    • 0037165196 scopus 로고    scopus 로고
    • Antimicrobial peptides of multicellular organisms
    • DOI 10.1038/415389a
    • M. Zasloff Antimicrobial peptides of multicellular organisms Nature 415 2002 389 395 (Pubitemid 34100944)
    • (2002) Nature , vol.415 , Issue.6870 , pp. 389-395
    • Zasloff, M.1
  • 15
    • 28844454642 scopus 로고    scopus 로고
    • Arginine-rich cell penetrating peptides: From endosomal uptake to nuclear delivery
    • DOI 10.1007/s00018-005-5293-y
    • K. Melikov, and L. Chernomordik Arginine-rich cell penetrating peptides: from endosomal uptake to nuclear delivery Cell. Mol. Life Sci. 62 2005 2739 2749 (Pubitemid 41779944)
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.23 , pp. 2739-2749
    • Melikov, K.1    Chernomordik, L.V.2
  • 16
    • 70350040736 scopus 로고    scopus 로고
    • Cell penetrating peptides: How do they do it?
    • H.D. Herce, and A.E. Garcia Cell penetrating peptides: how do they do it? J. Biol. Phys. 33 2007 345 356
    • (2007) J. Biol. Phys. , vol.33 , pp. 345-356
    • Herce, H.D.1    Garcia, A.E.2
  • 17
    • 33646525645 scopus 로고    scopus 로고
    • Protein transduction: Cell penetrating peptides and their therapeutic applications
    • K.M. Wagstaff, and D.A. Jans Protein transduction: cell penetrating peptides and their therapeutic applications Curr. Med. Chem. 13 2006 1371 1387
    • (2006) Curr. Med. Chem. , vol.13 , pp. 1371-1387
    • Wagstaff, K.M.1    Jans, D.A.2
  • 18
    • 1442317538 scopus 로고    scopus 로고
    • BAR Domains as Sensors of Membrane Curvature: The Amphiphysin BAR Structure
    • DOI 10.1126/science.1092586
    • B.J. Peter, H.M. Kent, I.G. Mills, Y. Vallis, P.J.G. Butler, P.R. Evans, and H.T. McMahon BAR domains as sensors of membrane curvature: the amphiphysin BAR structure Science 303 2004 495 499 (Pubitemid 38120842)
    • (2004) Science , vol.303 , Issue.5657 , pp. 495-499
    • Peter, B.J.1    Kent, H.M.2    Mills, I.G.3    Vallis, Y.4    Butler, P.J.G.5    Evans, P.R.6    McMahon, H.T.7
  • 19
    • 0035479424 scopus 로고    scopus 로고
    • 'Detergent-like' permeabilization of anionic lipid vesicles by melittin
    • DOI 10.1016/S0005-2736(01)00382-0, PII S0005273601003820
    • A.S. Ladokhin, and S.H. White 'Detergent-like' permeabilization of anionic lipid vesicles by melittin Biochim. Biophys. Acta 1514 2001 253 260 (Pubitemid 32831013)
    • (2001) Biochimica et Biophysica Acta - Biomembranes , vol.1514 , Issue.2 , pp. 253-260
    • Ladokhin, A.S.1    White, S.H.2
  • 21
    • 17644381598 scopus 로고    scopus 로고
    • Solution structure and lipid membrane partitioning of VSTx1, an inhibitor of the KvAP potassium channel
    • DOI 10.1021/bi0477034
    • H.J. Jung, J.Y. Lee, S.H. Kim, Y.J. Eu, S.Y. Shin, M. Milescu, K.J. Swartz, and J.I. Kim Solution structure and lipid membrane partitioning of VSTx1, an inhibitor of the KvAP potassium channel Biochemistry 44 2005 6015 6023 (Pubitemid 40570695)
    • (2005) Biochemistry , vol.44 , Issue.16 , pp. 6015-6023
    • Hoi, J.J.1    Ju, Y.L.2    Su, H.K.3    Eu, Y.-J.4    Song, Y.S.5    Milescu, M.6    Swartz, K.J.7    Jae, I.K.8
  • 22
    • 0034604029 scopus 로고    scopus 로고
    • A receptor for phosphatidylserine-specific clearance of apoptotic cells
    • DOI 10.1038/35011084
    • V.A. Fadok, D.L. Bratton, D.M. Rose, A. Pearson, R.A.B. Ezekewitz, and P.M. Henson A receptor for phosphatidylserine-specific clearance of apoptotic cells Nature 405 2000 85 90 (Pubitemid 30321820)
    • (2000) Nature , vol.405 , Issue.6782 , pp. 85-90
    • Fadok, V.A.1    Bratton, D.L.2    Rose, D.M.3    Pearson, A.4    Ezekewitz, R.A.B.5    Henson, P.M.6
  • 23
    • 1942420641 scopus 로고    scopus 로고
    • M1 ganglioside
    • DOI 10.1016/j.peptides.2004.01.001, PII S0196978104000038
    • B. Kurganov, M. Doh, and N. Arispe Aggregation of liposomes induced by the toxic peptides Alzheimer's A beta s, human amylin and prion (106-126): facilitation by membrane-bound G(M1) ganglioside Peptides 25 2004 217 232 (Pubitemid 38520052)
    • (2004) Peptides , vol.25 , Issue.2 , pp. 217-232
    • Kurganov, B.1    Doh, M.2    Arispe, N.3
  • 24
    • 59349111854 scopus 로고    scopus 로고
    • Nano-scale imaging and dynamics of amylin-membrane interactions and its implication in type II diabetes mellitus
    • W.J. Cho, B.P. Jena, and A.M. Jeremic Nano-scale imaging and dynamics of amylin-membrane interactions and its implication in type II diabetes mellitus Methods Cell Biol. 90 2008 267 286
    • (2008) Methods Cell Biol. , vol.90 , pp. 267-286
    • Cho, W.J.1    Jena, B.P.2    Jeremic, A.M.3
  • 25
    • 0032540327 scopus 로고    scopus 로고
    • Stabilization of α-Synuclein secondary structure upon binding to synthetic membranes
    • DOI 10.1074/jbc.273.16.9443
    • W.S. Davidson, A. Jonas, D.F. Clayton, and J.M. George Stabilization of alpha-synuclein secondary structure upon binding to synthetic membranes J. Biol. Chem. 273 1998 9443 9449 (Pubitemid 28183026)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.16 , pp. 9443-9449
    • Davidson, W.S.1    Jonas, A.2    Clayton, D.F.3    George, J.M.4
  • 26
    • 77953004116 scopus 로고    scopus 로고
    • The role of the lipid bilayer in tau aggregation
    • S. Elbaum-Garfinkle, T. Ramlall, and E. Rhoades The role of the lipid bilayer in tau aggregation Biophys. J. 98 2010 2722 2730
    • (2010) Biophys. J. , vol.98 , pp. 2722-2730
    • Elbaum-Garfinkle, S.1    Ramlall, T.2    Rhoades, E.3
  • 27
    • 64849109238 scopus 로고    scopus 로고
    • Alpha-synuclein binds large unilamellar vesicles as an extended helix
    • A.J. Trexler, and E. Rhoades Alpha-synuclein binds large unilamellar vesicles as an extended helix Biochemistry 48 2009 2304 2306
    • (2009) Biochemistry , vol.48 , pp. 2304-2306
    • Trexler, A.J.1    Rhoades, E.2
  • 28
    • 4143119891 scopus 로고    scopus 로고
    • DNA release from lipoplexes by anionic lipids: Correlation with lipid mesomorphism, interfacial curvature, and membrane fusion
    • DOI 10.1529/biophysj.104.042895
    • Y.S. Tarahovsky, R. Koynova, and R.C. MacDonald DNA release from lipoplexes by anionic lipids: correlation with lipid mesomorphism, interfacial curvature, and membrane fusion Biophys. J. 87 2004 1054 1064 (Pubitemid 39095084)
    • (2004) Biophysical Journal , vol.87 , Issue.2 , pp. 1054-1064
    • Tarahovsky, Y.S.1    Koynova, R.2    MacDonald, R.C.3
  • 30
    • 0030793215 scopus 로고    scopus 로고
    • The anionic phospholipid-mediated membrane interaction of the Anti- Cancer Drug doxorubicin is enhanced by phosphatidylethanolamine compared to other zwitterionic phospholipids
    • DOI 10.1021/bi963151g
    • G. Speelmans, R.W.H.M. Staffhorst, and B. de Kruijff The anionic phospholipid-mediated membrane interaction of the anti-cancer drug doxorubicin is enhanced by phosphatidylethanolamine compared to other zwitterionic phospholipids Biochemistry 36 1997 8657 8662 (Pubitemid 27305151)
    • (1997) Biochemistry , vol.36 , Issue.28 , pp. 8657-8662
    • Speelmans, G.1    Staffhorst, R.W.H.M.2    De Kruijff, B.3
  • 31
    • 0032932898 scopus 로고    scopus 로고
    • Membrane interaction of an antitumor antibiotic, mithramycin, with anionic phospholipid vesicles
    • DOI 10.1016/S0006-2952(98)00374-8, PII S0006295298003748
    • S. Majee, and A. Chakrabarti Membrane interaction of an antitumor antibiotic, mithramycin, with anionic phospholipid vesicles Biochem. Pharmacol. 57 1999 981 987 (Pubitemid 29168546)
    • (1999) Biochemical Pharmacology , vol.57 , Issue.9 , pp. 981-987
    • Majee, S.1    Chakrabarti, A.2
  • 32
    • 0037151327 scopus 로고    scopus 로고
    • Enhanced transdermal transport by electroporation using anionic lipids
    • DOI 10.1016/S0168-3659(02)00164-5, PII S0168365902001645
    • A. Sen, Y.L. Zhao, L. Zhang, and S.W. Hui Enhanced transdermal transport by electroporation using anionic lipids J. Control. Release 82 2002 399 405 (Pubitemid 34880193)
    • (2002) Journal of Controlled Release , vol.82 , Issue.2-3 , pp. 399-405
    • Sen, A.1    Zhao, Y.2    Zhang, L.3    Hui, S.W.4
  • 33
    • 65549133368 scopus 로고    scopus 로고
    • Delivery of macromolecules using arginine-rich cell-penetrating peptides: Ways to overcome endosomal entrapment
    • A. El-Sayed, S. Futaki, and H. Harashima Delivery of macromolecules using arginine-rich cell-penetrating peptides: ways to overcome endosomal entrapment AAPS J. 11 2009 13 22
    • (2009) AAPS J. , vol.11 , pp. 13-22
    • El-Sayed, A.1    Futaki, S.2    Harashima, H.3
  • 34
    • 0035946613 scopus 로고    scopus 로고
    • Roles of lipid polymorphism in intracellular delivery
    • DOI 10.1016/S0169-409X(01)00103-X, PII S0169409X0100103X
    • I.M. Hafez, and P.R. Cullis Roles of lipid polymorphism in intracellular delivery Adv. Drug Del. Rev. 47 2001 139 148 (Pubitemid 32324111)
    • (2001) Advanced Drug Delivery Reviews , vol.47 , Issue.2-3 , pp. 139-148
    • Hafez, I.M.1    Cullis, P.R.2
  • 35
    • 43749083559 scopus 로고    scopus 로고
    • Quantum dot probes for bacteria distinguish Escherichia coli mutants and permit in vivo imaging
    • DOI 10.1039/b803590c
    • W.M. Leevy, T.N. Lambert, J.R. Johnson, J. Morris, and B.D. Smith Quantum dot probes for bacteria distinguish Escherichia coli mutants and permit in vivo imaging Chem. Commun. 2008 2331 2333 (Pubitemid 351691997)
    • (2008) Chemical Communications , Issue.20 , pp. 2331-2333
    • Leevy, W.M.1    Lambert, T.N.2    Johnson, J.R.3    Morris, J.4    Smith, B.D.5
  • 37
    • 38549083648 scopus 로고    scopus 로고
    • Membrane biosensor platforms using nano- and microporous supports
    • E. Reimhult, and K. Kumar Membrane biosensor platforms using nano- and microporous supports Trends Biotechnol. 26 2008 82 89
    • (2008) Trends Biotechnol. , vol.26 , pp. 82-89
    • Reimhult, E.1    Kumar, K.2
  • 38
    • 0028228949 scopus 로고
    • Anionic phospholipids and protein translocation
    • DOI 10.1016/0014-5793(94)00404-8
    • B. de Kruijff Anionic phospholipids and protein translocation FEBS Lett. 346 1994 78 82 (Pubitemid 24183832)
    • (1994) FEBS Letters , vol.346 , Issue.1 , pp. 78-82
    • De Kruijff, B.1
  • 39
    • 0034986771 scopus 로고    scopus 로고
    • Anionic lipids stimulate sec-independent insertion of a membrane protein lacking charged amino acid side chains
    • A.N.J.A. Ridder, A. Kuhn, J.A. Killian, and B. de Kruijff Anionic lipids stimulate Sec-independent insertion of a membrane protein lacking charged amino acid side chains EMBO Rep. 2 2001 403 408 (Pubitemid 32509956)
    • (2001) EMBO Reports , vol.2 , Issue.5 , pp. 403-408
    • Ridder, A.N.J.A.1    Kuhn, A.2    Killian, J.A.3    De Kruijff, B.4
  • 40
    • 0023878031 scopus 로고
    • Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranes
    • T. de Vrije, R.L. de Swart, W. Dowhan, J. Tommassen, and B. de Kruijff Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranes Nature 334 1988 173 175
    • (1988) Nature , vol.334 , pp. 173-175
    • De Vrije, T.1    De Swart, R.L.2    Dowhan, W.3    Tommassen, J.4    De Kruijff, B.5
  • 41
    • 0026514429 scopus 로고
    • SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: A monolayer study
    • E. Breukink, R.A. Demel, G. de Korte-Kool, and B. de Kruijff SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: a monolayer study Biochemistry 31 1992 1119 1124
    • (1992) Biochemistry , vol.31 , pp. 1119-1124
    • Breukink, E.1    Demel, R.A.2    De Korte-Kool, G.3    De Kruijff, B.4
  • 42
    • 0030791975 scopus 로고    scopus 로고
    • Anionic phospholipids are determinants of membrane protein topology
    • DOI 10.1093/emboj/16.14.4261
    • W. van Klompenburg, I. Nilsson, G. von Heijne, and B. de Kruijff Anionic phospholipids are determinants of membrane protein topology EMBO J. 16 1997 4261 4266 (Pubitemid 27298178)
    • (1997) EMBO Journal , vol.16 , Issue.14 , pp. 4261-4266
    • Van Klompenburg, W.1    Nilsson, I.2    Von Heijne, G.3    De Kruijff, B.4
  • 43
    • 33646168447 scopus 로고    scopus 로고
    • Anionic phospholipid interactions with the potassium channel KcsA: Simulation studies
    • S.S. Deol, C. Domene, P.J. Bond, and M.S.P. Sansom Anionic phospholipid interactions with the potassium channel KcsA: simulation studies Biophys. J. 90 2006 822 830
    • (2006) Biophys. J. , vol.90 , pp. 822-830
    • Deol, S.S.1    Domene, C.2    Bond, P.J.3    Sansom, M.S.P.4
  • 44
    • 0037015161 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1021/bi026215y
    • F.I. Valiyaveetil, Y.F. Zhou, and R. Mackinnon Lipids in the structure, folding, and function of the KcsA K+ channel Biochemistry 41 2002 10771 10777 (Pubitemid 34971053)
    • (2002) Biochemistry , vol.41 , Issue.35 , pp. 10771-10777
    • Valiyaveetil, F.I.1    Zhou, Y.2    MacKinnon, R.3
  • 45
    • 17144372582 scopus 로고    scopus 로고
    • Heterogeneity in the binding of lipid molecules to the surface of a membrane protein: Hot spots for anionic lipids on the mechanosensitive channel of large conductance MscL and effects on conformation
    • DOI 10.1021/bi047439e
    • A.M. Powl, J.M. East, and A.G. Lee Heterogeneity in the binding of lipid molecules to the surface of a membrane protein: hot spots for anionic lipids on the mechanosensitive channel of large conductance MscL and effects on conformation Biochemistry 44 2005 5873 5883 (Pubitemid 40525124)
    • (2005) Biochemistry , vol.44 , Issue.15 , pp. 5873-5883
    • Powl, A.M.1    East, J.M.2    Lee, A.G.3
  • 46
    • 71749098387 scopus 로고    scopus 로고
    • Anionic lipids allosterically modulate multiple nicotinic acetylcholine receptor conformational equilibria
    • C.J. Dacosta, S.A. Medaglia, N. Lavigne, S. Wang, C.L. Carswell, and J.E. Baenziger Anionic lipids allosterically modulate multiple nicotinic acetylcholine receptor conformational equilibria J. Biol. Chem. 284 2009 33841 33849
    • (2009) J. Biol. Chem. , vol.284 , pp. 33841-33849
    • Dacosta, C.J.1    Medaglia, S.A.2    Lavigne, N.3    Wang, S.4    Carswell, C.L.5    Baenziger, J.E.6
  • 47
    • 0029757155 scopus 로고    scopus 로고
    • Binding of small basic peptides to membranes containing acidic lipids: Theoretical models and experimental results
    • N. Ben-Tal, B. Honig, R.M. Peitzsch, G. Denisov, and S. McLaughlin Binding of small basic peptides to membranes containing acidic lipids: theoretical models and experimental results Biophys. J. 71 1996 561 575 (Pubitemid 26289141)
    • (1996) Biophysical Journal , vol.71 , Issue.2 , pp. 561-575
    • Ben-Tal, N.1    Honig, B.2    Peitzsch, R.M.3    Denisov, G.4    McLaughlin, S.5
  • 48
    • 0344589334 scopus 로고    scopus 로고
    • Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling
    • DOI 10.1016/S0304-4157(98)00009-4, PII S0304415798000094
    • D. Marsh, and L.I. Horvath Structure, dynamics and composition of the lipid-protein interface. Perspectives from spin-labelling Biochim. Biophys. Acta 1376 1998 267 296 (Pubitemid 28517881)
    • (1998) Biochimica et Biophysica Acta - Reviews on Biomembranes , vol.1376 , Issue.3 , pp. 267-296
    • Marsh, D.1    Horvath, L.I.2
  • 49
  • 50
    • 0038364008 scopus 로고    scopus 로고
    • Lipid-protein interactions in biological membranes: A structural perspective
    • DOI 10.1016/S0005-2736(03)00056-7
    • A.G. Lee Lipid-protein interactions in biological membranes: a structural perspective Biochim. Biophys. Acta 1612 2003 1 40 (Pubitemid 36555684)
    • (2003) Biochimica et Biophysica Acta - Biomembranes , vol.1612 , Issue.1 , pp. 1-40
    • Lee, A.G.1
  • 52
    • 33845637597 scopus 로고    scopus 로고
    • Phospholipids and the origin of cationic gating charges in voltage sensors
    • DOI 10.1038/nature05416, PII NATURE05416
    • D. Schmidt, Q.X. Jiang, and R. MacKinnon Phospholipids and the origin of cationic gating charges in voltage sensors Nature 444 2006 775 779 (Pubitemid 44949608)
    • (2006) Nature , vol.444 , Issue.7120 , pp. 775-779
    • Schmidt, D.1    Jiang, Q.-X.2    MacKinnon, R.3
  • 53
    • 0018135125 scopus 로고
    • Enzymology, genetics, and regulation of membrane phospholipid synthesis in Escherichia coli
    • C.R.H. Raetz Enzymology, genetics, and regulation of membrane phospholipid synthesis in Escherichia coli Microbiol. Rev. 42 1978 614 659 (Pubitemid 9044056)
    • (1978) Microbiological Reviews , vol.42 , Issue.3 , pp. 614-659
    • Raetz, C.R.H.1
  • 55
    • 34547661911 scopus 로고    scopus 로고
    • The essential role of phosphatidylglycerol in photosynthesis
    • DOI 10.1007/s11120-007-9203-z, A Tribute to Andrew A. Benson
    • H. Wada, and N. Murata The essential role of phosphatidylglycerol in photosynthesis Photosynth. Res. 92 2007 205 215 (Pubitemid 47222263)
    • (2007) Photosynthesis Research , vol.92 , Issue.2 , pp. 205-215
    • Wada, H.1    Murata, N.2
  • 56
    • 34249102563 scopus 로고    scopus 로고
    • Counterion-mediated membrane penetration: Cationic cell-penetrating peptides overcome Born energy barrier by ion-pairing with phospholipids
    • DOI 10.1016/j.bbamem.2007.03.004, PII S0005273607000764
    • E.K. Esbjorner, P. Lincoln, and B. Norden Counterion-mediated membrane penetration: cationic cell-penetrating peptides overcome Born energy barrier by ion-pairing with phospholipids Biochim. Biophys. Acta 1768 2007 1550 1558 (Pubitemid 46782707)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.6 , pp. 1550-1558
    • Esbjorner, E.K.1    Lincoln, P.2    Norden, B.3
  • 57
    • 0014481138 scopus 로고
    • Energy of an ion crossing a low dielectric membrane: Solutions to four relevant electrostatic problems
    • A. Parsegian Energy of an ion crossing a low dielectric membrane: solutions to four relevant electrostatic problems Nature 221 1969 844 846
    • (1969) Nature , vol.221 , pp. 844-846
    • Parsegian, A.1
  • 59
    • 34247626293 scopus 로고    scopus 로고
    • Partitioning of amino acid side chains into lipid bilayers: Results from computer simulations and comparison to experiment
    • DOI 10.1085/jgp.200709745
    • J.L. MacCallum, W.F.D. Bennett, and D.P. Tieleman Partitioning of amino acid side chains into lipid bilayers: results from computer simulations and comparison to experiment J. Gen. Physiol. 129 2007 371 377 (Pubitemid 46686453)
    • (2007) Journal of General Physiology , vol.129 , Issue.5 , pp. 371-377
    • MacCallum, J.L.1    Bennett, W.F.D.2    Tieleman, D.P.3
  • 61
    • 50549097744 scopus 로고    scopus 로고
    • Assessing atomistic and coarse-grained force fields for protein-lipid interactions: The formidable challenge of an ionizable side chain in a membrane
    • I. Vorobyov, L.B. Li, and T.W. Allen Assessing atomistic and coarse-grained force fields for protein-lipid interactions: the formidable challenge of an ionizable side chain in a membrane J. Phys. Chem. B 112 2008 9588 9602
    • (2008) J. Phys. Chem. B , vol.112 , pp. 9588-9602
    • Vorobyov, I.1    Li, L.B.2    Allen, T.W.3
  • 62
    • 66549128460 scopus 로고    scopus 로고
    • The role of lipid composition for insertion and stabilization of amino acids in membranes
    • A.C.V. Johansson, and E. Lindahl The role of lipid composition for insertion and stabilization of amino acids in membranes J. Chem. Phys. 130 2009 185101
    • (2009) J. Chem. Phys. , vol.130 , pp. 185101
    • Johansson, A.C.V.1    Lindahl, E.2
  • 63
    • 34547622288 scopus 로고    scopus 로고
    • Modeling charged protein side chains in lipid membranes [5]
    • DOI 10.1085/jgp.200709850
    • T.W. Allen Modeling charged protein side chains in lipid membranes J. Gen. Physiol. 130 2007 237 240 (Pubitemid 47204916)
    • (2007) Journal of General Physiology , vol.130 , Issue.2 , pp. 237-240
    • Allen, T.W.1
  • 64
    • 50549085702 scopus 로고    scopus 로고
    • Potential of mean force and pK(a) profile calculation for a lipid membrane-exposed arginine side chain
    • L.B. Li, I. Vorobyov, and T.W. Allen Potential of mean force and pK(a) profile calculation for a lipid membrane-exposed arginine side chain J. Phys. Chem. B 112 2008 9574 9587
    • (2008) J. Phys. Chem. B , vol.112 , pp. 9574-9587
    • Li, L.B.1    Vorobyov, I.2    Allen, T.W.3
  • 65
    • 79954639726 scopus 로고    scopus 로고
    • I. Vorobyov, T.E. Olson, J.H. Kim, R.E. Koeppe II, O.S. Andersen, T.W. Allen, (in preparation), 2010
    • I. Vorobyov, T.E. Olson, J.H. Kim, R.E. Koeppe II, O.S. Andersen, T.W. Allen, (in preparation), 2010.
  • 66
    • 0015868742 scopus 로고
    • Currents related to movement of the gating particles of the sodium channels
    • C.M. Armstrong, and F. Bezanilla Currents related to movement of the gating particles of the sodium channels Nature 242 1973 459 461
    • (1973) Nature , vol.242 , pp. 459-461
    • Armstrong, C.M.1    Bezanilla, F.2
  • 67
    • 0025829307 scopus 로고
    • From femtoseconds to biology-mechanism of bacteriorhodopsins light-driven proton pump
    • R.A. Mathies, S.W. Lin, J.B. Ames, and W.T. Pollard From femtoseconds to biology-mechanism of bacteriorhodopsins light-driven proton pump Annu. Rev. Biophys. Biophys. Chem. 20 1991 491 518
    • (1991) Annu. Rev. Biophys. Biophys. Chem. , vol.20 , pp. 491-518
    • Mathies, R.A.1    Lin, S.W.2    Ames, J.B.3    Pollard, W.T.4
  • 68
    • 0039355490 scopus 로고    scopus 로고
    • Specific arginine and threonine residues control anion binding and transport in the light-driven chloride pump halorhodopsin
    • DOI 10.1093/emboj/16.13.3813
    • M. Rudiger, and D. Oesterhelt Specific arginine and threonine residues control anion binding and transport in the light-driven chloride pump halorhodopsin EMBO J. 16 1997 3813 3821 (Pubitemid 27280997)
    • (1997) EMBO Journal , vol.16 , Issue.13 , pp. 3813-3821
    • Rudiger, M.1    Oesterhelt, D.2
  • 69
    • 30044452344 scopus 로고    scopus 로고
    • Cationic host defense (antimicrobial) peptides
    • DOI 10.1016/j.coi.2005.11.004, PII S0952791505001998, Innate Immunity/Antigen Processing and Recognition
    • K.L. Brown, and R.E.W. Hancock Cationic host defense (antimicrobial) peptides Curr. Opin. Immunol. 18 2006 24 30 (Pubitemid 43049644)
    • (2006) Current Opinion in Immunology , vol.18 , Issue.1 , pp. 24-30
    • Brown, K.L.1    Hancock, R.E.W.2
  • 70
    • 27844504698 scopus 로고    scopus 로고
    • Lipid interactions with bacterial channels: Fluorescence studies
    • DOI 10.1042/BST20050905
    • A.M. Powl, J. Carney, P. Marius, J.M. East, and A.G. Lee Lipid interactions with bacterial channels: fluorescence studies Biochem. Soc. Trans. 33 2005 905 909 (Pubitemid 41659075)
    • (2005) Biochemical Society Transactions , vol.33 , Issue.5 , pp. 905-909
    • Powl, A.M.1    Carney, J.2    Marius, P.3    East, J.M.4    Lee, A.G.5
  • 71
    • 77949795332 scopus 로고    scopus 로고
    • Water-protein interactions of an arginine-rich membrane peptide in lipid bilayers investigated by solid-state nuclear magnetic resonance spectroscopy
    • S.H. Li, Y.C. Su, W.B. Luo, and M. Hong Water-protein interactions of an arginine-rich membrane peptide in lipid bilayers investigated by solid-state nuclear magnetic resonance spectroscopy J. Phys. Chem. B 114 2010 4063 4069
    • (2010) J. Phys. Chem. B , vol.114 , pp. 4063-4069
    • Li, S.H.1    Su, Y.C.2    Luo, W.B.3    Hong, M.4
  • 72
    • 77954831684 scopus 로고    scopus 로고
    • Membrane-bound dynamic structure of an arginine-rich cell-penetrating peptide, the protein transduction domain of HIV TAT, from solid-state NMR
    • Y.C. Su, A.J. Waring, P. Ruchala, and M. Hong Membrane-bound dynamic structure of an arginine-rich cell-penetrating peptide, the protein transduction domain of HIV TAT, from solid-state NMR Biochemistry 49 2010 6009 6020
    • (2010) Biochemistry , vol.49 , pp. 6009-6020
    • Su, Y.C.1    Waring, A.J.2    Ruchala, P.3    Hong, M.4
  • 77
    • 0034250744 scopus 로고    scopus 로고
    • An improved empirical potential energy function for molecular simulations of phospholipids
    • S.E. Feller, and A.D. MacKerell An improved empirical potential energy function for molecular simulations of phospholipids J. Phys. Chem. B 104 2000 7510 7515
    • (2000) J. Phys. Chem. B , vol.104 , pp. 7510-7515
    • Feller, S.E.1    MacKerell, A.D.2
  • 78
    • 0000999989 scopus 로고    scopus 로고
    • Combined ab initio empirical approach for optimization of Lennard-Jones parameters
    • D.X. Yin, and A.D. Mackerell Combined ab initio empirical approach for optimization of Lennard-Jones parameters J. Comput. Chem. 19 1998 334 348
    • (1998) J. Comput. Chem. , vol.19 , pp. 334-348
    • Yin, D.X.1    MacKerell, A.D.2
  • 79
    • 0001655657 scopus 로고
    • Finite representation of an infinite bulk system: Solvent boundary potential for computer simulations
    • D. Beglov, and B. Roux Finite representation of an infinite bulk system: solvent boundary potential for computer simulations J. Chem. Phys. 100 1994 9050 9063
    • (1994) J. Chem. Phys. , vol.100 , pp. 9050-9063
    • Beglov, D.1    Roux, B.2
  • 81
    • 15744368593 scopus 로고    scopus 로고
    • An ab initio study on the torsional surface of alkanes and its effect on molecular simulations of alkanes and a DPPC bilayer
    • DOI 10.1021/jp0468096
    • J.B. Klauda, B.R. Brooks, A.D. MacKerell Jr., R.M. Venable, and R.W. Pastor An ab initio study on the torsional surface of alkanes and its effect on molecular simulations of alkanes and a DPPC bilayer J. Phys. Chem. B 109 2005 5300 5311 (Pubitemid 40407752)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.11 , pp. 5300-5311
    • Klauda, J.B.1    Brooks, B.R.2    MacKerell Jr., A.D.3    Venable, R.M.4    Pastor, R.W.5
  • 83
    • 77952680504 scopus 로고    scopus 로고
    • Electrostatics of solvent and membrane interfaces and the role of polarizability
    • I.V. Vorobyov, and T.W. Allen Electrostatics of solvent and membrane interfaces and the role of polarizability J. Chem. Phys. 132 2010 185101
    • (2010) J. Chem. Phys. , vol.132 , pp. 185101
    • Vorobyov, I.V.1    Allen, T.W.2
  • 84
    • 77953589882 scopus 로고    scopus 로고
    • The electrostatics of ions in deformable lipid membranes
    • I.V. Vorobyov, B. Bekker, and T.W. Allen The electrostatics of ions in deformable lipid membranes Biophys. J. 98 2010 2904 2913
    • (2010) Biophys. J. , vol.98 , pp. 2904-2913
    • Vorobyov, I.V.1    Bekker, B.2    Allen, T.W.3
  • 85
    • 0026071516 scopus 로고
    • Monte Carlo simulation studies of lipid order parameter profiles near integral membrane proteins
    • M.M. Sperotto, and O.G. Mouritsen Monte Carlo simulation studies of lipid order parameter profiles near integral membrane proteins Biophys. J. 59 1991 261 270
    • (1991) Biophys. J. , vol.59 , pp. 261-270
    • Sperotto, M.M.1    Mouritsen, O.G.2
  • 86
    • 0035900141 scopus 로고    scopus 로고
    • Comparison of bilayer and monolayer properties of phospholipid systems containing dipalmitoylphosphatidylglycerol and dipalmitoylphosphatidylinositol
    • DOI 10.1021/la0108454
    • H. Mansour, D.-S. Wang, C.-S. Chen, and G. Zografi Comparison of bilayer and monolayer properties of phospholipid systems containing dipalmitoylphosphatidylglycerol and dipalmitoylphosphatidylinositol Langmuir 17 2001 6622 6632 (Pubitemid 35330647)
    • (2001) Langmuir , vol.17 , Issue.21 , pp. 6622-6632
    • Mansour, H.1    Wang, D.-S.2    Chen, C.-S.3    Zografi, G.4
  • 87
    • 33846823909 scopus 로고
    • Particle mesh Ewald-an N.log(N) method for Ewald sums in large systems
    • T. Darden, D. York, and L. Pedersen Particle mesh Ewald-an N.log(N) method for Ewald sums in large systems J. Chem. Phys. 98 1993 10089 10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 88
    • 84986534166 scopus 로고
    • New spherical-cutoff methods for long-range forces in macromolecular simulation
    • P.J. Steinbach, and B.R. Brooks New spherical-cutoff methods for long-range forces in macromolecular simulation J. Comput. Chem. 15 1994 667 683
    • (1994) J. Comput. Chem. , vol.15 , pp. 667-683
    • Steinbach, P.J.1    Brooks, B.R.2
  • 89
    • 33744920795 scopus 로고    scopus 로고
    • Closer look at structure of fully hydrated fluid phase DPPC bilayers
    • N. Kucerka, S. Tristram-Nagle, and J.F. Nagle Closer look at structure of fully hydrated fluid phase DPPC bilayers Biophys. J. 90 2006 L83 L85
    • (2006) Biophys. J. , vol.90
    • Kucerka, N.1    Tristram-Nagle, S.2    Nagle, J.F.3
  • 90
    • 0017871649 scopus 로고
    • Measurement of repulsive forces between charged phospholipid bilayers
    • A.C. Cowley, N.L. Fuller, R.P. Rand, and V.A. Parsegian Measurement of repulsive forces between charged phospholipid bilayers Biochemistry 17 1978 3163 3168 (Pubitemid 8392655)
    • (1978) Biochemistry , vol.17 , Issue.15 , pp. 3163-3168
    • Cowley, A.C.1    Fuller, N.L.2    Rand, R.P.3    Parsegian, V.A.4
  • 91
    • 0342929614 scopus 로고
    • Nonphysical sampling distributions in Monte Carlo free-energy estimation: Umbrella sampling
    • G.M. Torrie, and J.P. Valleau Nonphysical sampling distributions in Monte Carlo free-energy estimation: umbrella sampling J. Comput. Phys. 23 1977 187 199
    • (1977) J. Comput. Phys. , vol.23 , pp. 187-199
    • Torrie, G.M.1    Valleau, J.P.2
  • 92
    • 84986519238 scopus 로고
    • The weighted histogram analysis method for free-energy calculations on biomolecules: I. The method
    • S. Kumar, J.M. Rosenberg, D. Bouzida, R.H. Swendsen, and P.A. Kollman The weighted histogram analysis method for free-energy calculations on biomolecules: I. The method J. Comput. Chem. 13 1992 1011 1021
    • (1992) J. Comput. Chem. , vol.13 , pp. 1011-1021
    • Kumar, S.1    Rosenberg, J.M.2    Bouzida, D.3    Swendsen, R.H.4    Kollman, P.A.5
  • 93
    • 22244445788 scopus 로고    scopus 로고
    • Imaging α-hemolysin with molecular dynamics: Ionic conductance, osmotic permeability, and the electrostatic potential map
    • DOI 10.1529/biophysj.104.058727
    • A. Aksimentiev, and K. Schulten Imaging alpha-hemolysin with molecular dynamics: ionic conductance, osmotic permeability, and the electrostatic potential map Biophys. J. 88 2005 3745 3761 (Pubitemid 40991090)
    • (2005) Biophysical Journal , vol.88 , Issue.6 , pp. 3745-3761
    • Aksimentiev, A.1    Schulten, K.2
  • 96
    • 43049122273 scopus 로고    scopus 로고
    • Water in nonpolar confinement: From nanotubes to proteins and beyond
    • DOI 10.1146/annurev.physchem.59.032607.093815
    • J.C. Rasaiah, S. Garde, and G. Hummer Water in nonpolar confinement: from nanotubes to proteins and beyond Annu. Rev. Phys. Chem. 59 2008 713 740 (Pubitemid 351703402)
    • (2008) Annual Review of Physical Chemistry , vol.59 , pp. 713-740
    • Rasaiah, J.C.1    Garde, S.2    Hummer, G.3
  • 97
    • 0038514127 scopus 로고    scopus 로고
    • Simulation of pore formation in lipid bilayers by mechanical stress and electric fields
    • DOI 10.1021/ja029504i
    • D.P. Tieleman, H. Leontiadou, A.E. Mark, and S.J. Marrink Simulation of pore formation in lipid bilayers by mechanical stress and electric fields J. Am. Chem. Soc. 125 2003 6382 6383 (Pubitemid 36605403)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.21 , pp. 6382-6383
    • Tieleman, D.P.1    Leontiadou, H.2    Mark, A.E.3    Marrink, S.-J.4
  • 98
    • 0035169468 scopus 로고    scopus 로고
    • Leakage and aggregation of phospholipid vesicles induced by the BH3-only Bcl-2 family member, BID
    • DOI 10.1046/j.1432-1327.2001.01841.x
    • D.Y. Zhai, Q. Miao, X.F. Xin, and F.Y. Yang Leakage and aggregation of phospholipid vesicles induced by the BH3-only Bcl-2 family member, BID Eur. J. Biochem. 268 2001 48 55 (Pubitemid 32052246)
    • (2001) European Journal of Biochemistry , vol.268 , Issue.1 , pp. 48-55
    • Zhai, D.1    Miao, Q.2    Xin, X.3    Yang, F.4
  • 99
    • 0028924198 scopus 로고
    • Molecular basis for membrane selectivity of an antimicrobial peptide, magainin 2
    • K. Matsuzaki, K. Sugishita, N. Fujii, and K. Miyajima Molecular basis for membrane selectivity of an antimicrobial peptide, magainin 2 Biochemistry 34 1995 3423 3429
    • (1995) Biochemistry , vol.34 , pp. 3423-3429
    • Matsuzaki, K.1    Sugishita, K.2    Fujii, N.3    Miyajima, K.4
  • 101
    • 0029027974 scopus 로고
    • Mechanism of liposome destabilization by polycationic amino acids
    • R.M. Epand, and W. Lim Mechanism of liposome destabilization by polycationic amino acids Biosci. Rep. 15 1995 151 160
    • (1995) Biosci. Rep. , vol.15 , pp. 151-160
    • Epand, R.M.1    Lim, W.2
  • 102
    • 35048820105 scopus 로고    scopus 로고
    • Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptide from solid-state NMR
    • DOI 10.1021/ja072511s
    • M. Tang, A.J. Waring, and M. Hong Phosphate-mediated arginine insertion into lipid membranes and pore formation by a cationic membrane peptide from solid-state NMR J. Am. Chem. Soc. 129 2007 11438 11446 (Pubitemid 47555563)
    • (2007) Journal of the American Chemical Society , vol.129 , Issue.37 , pp. 11438-11446
    • Tang, M.1    Waring, A.J.2    Hong, M.3
  • 103
    • 0037440938 scopus 로고    scopus 로고
    • Calculation of the dielectric permittivity profile for a nonuniform system: Application to a lipid bilayer simulation
    • H.A. Stern, and S.E. Feller Calculation of the dielectric permittivity profile for a nonuniform system: application to a lipid bilayer simulation J. Chem. Phys. 118 2003 3401 3412
    • (2003) J. Chem. Phys. , vol.118 , pp. 3401-3412
    • Stern, H.A.1    Feller, S.E.2
  • 104
    • 67650079292 scopus 로고    scopus 로고
    • Charge equilibration force fields for lipid environments: Applications to fully hydrated DPPC bilayers and DMPC-embedded gramicidin A
    • J.E. Davis, and S. Patel Charge equilibration force fields for lipid environments: applications to fully hydrated DPPC bilayers and DMPC-embedded gramicidin A J. Phys. Chem. B 113 2009 9183 9196
    • (2009) J. Phys. Chem. B , vol.113 , pp. 9183-9196
    • Davis, J.E.1    Patel, S.2
  • 105
    • 67849105001 scopus 로고    scopus 로고
    • Free energy for the permeation of Na+ and Cl- ions and their ion-pair through a zwitterionic dimyristoyl phosphatidylcholine lipid bilayer by umbrella integration with harmonic Fourier beads
    • I.V. Khavrutskii, A.A. Gorfe, B.Z. Lu, and J.A. McCammon Free energy for the permeation of Na+ and Cl- ions and their ion-pair through a zwitterionic dimyristoyl phosphatidylcholine lipid bilayer by umbrella integration with harmonic Fourier beads J. Am. Chem. Soc. 131 2009 1706 1716
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 1706-1716
    • Khavrutskii, I.V.1    Gorfe, A.A.2    Lu, B.Z.3    McCammon, J.A.4
  • 106
    • 0000123071 scopus 로고    scopus 로고
    • Removal of pressure and free energy artifacts in charged periodic systems via net charge corrections to the Ewald potential
    • S. Bogusz, T.E. Cheatham, and B.R. Brooks Removal of pressure and free energy artifacts in charged periodic systems via net charge corrections to the Ewald potential J. Chem. Phys. 108 1998 7070 7084 (Pubitemid 128594474)
    • (1998) Journal of Chemical Physics , vol.108 , Issue.17 , pp. 7070-7084
    • Bogusz, S.1    Cheatham III, T.E.2    Brooks, B.R.3
  • 107
    • 0030904245 scopus 로고    scopus 로고
    • A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus
    • DOI 10.1074/jbc.272.25.16010
    • E. Vives, P. Brodin, and B. Lebleu A truncated HIV-1 Tat protein basic domain rapidly translocates through the plasma membrane and accumulates in the cell nucleus J. Biol. Chem. 272 1997 16010 16017 (Pubitemid 27265584)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.25 , pp. 16010-16017
    • Vives, E.1    Brodin, P.2    Lebleu, B.3
  • 108
    • 1842483252 scopus 로고    scopus 로고
    • Membrane curvature: How BAR domains bend bilayers
    • J. Zimmerberg, and S. McLaughlin Membrane curvature: how BAR domains bend bilayers Curr. Biol. 14 2004 R250 252
    • (2004) Curr. Biol. , vol.14 , pp. 250-252
    • Zimmerberg, J.1    McLaughlin, S.2


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