메뉴 건너뛰기




Volumn 1828, Issue 8, 2013, Pages 1674-1682

Observing the translocation of a mitochondria-penetrating peptide with solid-state NMR

Author keywords

Electroporation; Mitochondria targeting; Penetrating peptides; Solid state NMR spectroscopy; Translocation mechanism

Indexed keywords

CARBON 13; CELL PENETRATING PEPTIDE; LIPID; MAGNESIUM ION; MITOCHONDRIA PENETRATING PEPTIDE; UNCLASSIFIED DRUG;

EID: 84877076601     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2013.03.027     Document Type: Article
Times cited : (16)

References (103)
  • 1
    • 0031772126 scopus 로고    scopus 로고
    • The mitochondrial permeability transition is required for tumor necrosis factor alpha-mediated apoptosis and cytochrome c release
    • C.A. Bradham, T. Qian, K. Streetz, C. Trautwein, D.A. Brenner, and J.J. Lemasters The mitochondrial permeability transition is required for tumor necrosis factor alpha-mediated apoptosis and cytochrome c release Mol. Cell. Biol. 18 1998 6353 6364 (Pubitemid 28500525)
    • (1998) Molecular and Cellular Biology , vol.18 , Issue.11 , pp. 6353-6364
    • Bradham, C.A.1    Qian, T.2    Streetz, K.3    Trautwein, C.4    Brenner, D.A.5    Lemasters, J.J.6
  • 2
    • 0026671245 scopus 로고
    • Association of mitochondrial DNA damage with aging and coronary atherosclerotic heart disease
    • M. Corral-Debrinski, J.M. Shoffner, M.T. Lott, and D.C. Wallace Association of mitochondrial DNA damage with aging and coronary atherosclerotic heart disease Mutation Research/DNAging 275 1992 169 180
    • (1992) Mutation Research/DNAging , vol.275 , pp. 169-180
    • Corral-Debrinski, M.1    Shoffner, J.M.2    Lott, M.T.3    Wallace, D.C.4
  • 3
    • 0029788601 scopus 로고    scopus 로고
    • The role of mitochondria in ischemic heart disease
    • R. Ferrari The role of mitochondria in ischemic heart disease J. Cardiovasc. Pharmacol. 28 1996 1 10
    • (1996) J. Cardiovasc. Pharmacol. , vol.28 , pp. 1-10
    • Ferrari, R.1
  • 4
    • 0029090167 scopus 로고
    • Direct evidence for tumor necrosis factor-induced mitochondrial reactive oxygen intermediates and their involvement in cytotoxicity
    • V. Goossens, J. Grooten, K. De Vos, and W. Fiers Direct evidence for tumor necrosis factor-induced mitochondrial reactive oxygen intermediates and their involvement in cytotoxicity Proc. Natl. Acad. Sci. U.S.A. 92 1995 8115 8119
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 8115-8119
    • Goossens, V.1    Grooten, J.2    De Vos, K.3    Fiers, W.4
  • 5
    • 0024583049 scopus 로고
    • Hypothyroidism in rats decreases mitochondrial inner membrane cation permeability
    • DOI 10.1016/0014-5793(89)80455-7
    • R.P. Hafner, M.J. Leake, and M.D. Brand Hypothyroidism in rats decreases mitochondrial inner membrane cation permeability FEBS Lett. 248 1989 175 178 (Pubitemid 19129337)
    • (1989) FEBS Letters , vol.248 , Issue.1-2 , pp. 175-178
    • Hafner, R.P.1    Leake, M.J.2    Brand, M.D.3
  • 8
    • 0030929650 scopus 로고    scopus 로고
    • Cardiolipin-dependent decrease of cytochrome c oxidase activity in heart mitochondria from hypothyroid rats
    • DOI 10.1016/S0005-2728(97)00012-1, PII S0005272897000121
    • G. Paradies, G. Petrosillo, and F.M. Ruggiero Cardiolipin-dependent decrease of cytochrome c oxidase activity in heart mitochondria from hypothyroid rats Biochimica et Biophysica Acta (BBA) - Bioenergetics 1319 1997 5 8 (Pubitemid 27138371)
    • (1997) Biochimica et Biophysica Acta - Bioenergetics , vol.1319 , Issue.1 , pp. 5-8
    • Paradies, G.1    Petrosillo, G.2    Ruggiero, F.M.3
  • 9
    • 0021143782 scopus 로고
    • Mitochondrial myopathy, encephalopathy, lactic acidosis, and strokelike episodes: A distinctive clinical syndrome
    • S.G. Pavlakis, P.C. Phillips, S. DiMauro, D.C. De Vivo, and L.P. Rowland Mitochondrial myopathy, encephalopathy, lactic acidosis, and strokelike episodes: a distinctive clinical syndrome Ann. Neurol. 16 1984 481 488 (Pubitemid 14021826)
    • (1984) Annals of Neurology , vol.16 , Issue.4 , pp. 481-488
    • Pavlakis, S.G.1    Phillips, P.C.2    DiMauro, S.3
  • 11
    • 0004235430 scopus 로고    scopus 로고
    • John Wiley & Sons, Inc. Hoboken, New Jersey
    • I.E. Scheffler Mitochondria 2008 John Wiley & Sons, Inc. Hoboken, New Jersey
    • (2008) Mitochondria
    • Scheffler, I.E.1
  • 12
    • 70349554126 scopus 로고    scopus 로고
    • Mitochondria-penetrating peptides: Sequence effects and model cargo transport
    • L.F. Yousif, K.M. Stewart, K.L. Horton, and S.O. Kelley Mitochondria-penetrating peptides: sequence effects and model cargo transport Chembiochem 10 2009 2081 2088
    • (2009) Chembiochem , vol.10 , pp. 2081-2088
    • Yousif, L.F.1    Stewart, K.M.2    Horton, K.L.3    Kelley, S.O.4
  • 13
    • 70349554208 scopus 로고    scopus 로고
    • Targeting mitochondria with organelle-specific compounds: Strategies and applications
    • L.F. Yousif, K.M. Stewart, and S.O. Kelley Targeting mitochondria with organelle-specific compounds: strategies and applications Chembiochem 10 2009 1939 1950
    • (2009) Chembiochem , vol.10 , pp. 1939-1950
    • Yousif, L.F.1    Stewart, K.M.2    Kelley, S.O.3
  • 14
    • 79952578695 scopus 로고    scopus 로고
    • Maximizing the therapeutic window of an antimicrobial drug by imparting mitochondrial sequestration in human cells
    • M.P. Pereira, and S.O. Kelley Maximizing the therapeutic window of an antimicrobial drug by imparting mitochondrial sequestration in human cells J. Am. Chem. Soc. 133 2011 3260 3263
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 3260-3263
    • Pereira, M.P.1    Kelley, S.O.2
  • 15
    • 77955576540 scopus 로고    scopus 로고
    • Magic angle spinning NMR investigation of influenza A M218-60: Support for an allosteric mechanism of inhibition
    • L.B. Andreas, M.T. Eddy, R.M. Pielak, J. Chou, and R.G. Griffin Magic angle spinning NMR investigation of influenza A M218-60: support for an allosteric mechanism of inhibition J. Am. Chem. Soc. 132 2010 10958 10960
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 10958-10960
    • Andreas, L.B.1    Eddy, M.T.2    Pielak, R.M.3    Chou, J.4    Griffin, R.G.5
  • 16
    • 84857980586 scopus 로고    scopus 로고
    • The membrane interactions of antimicrobial peptides revealed by solid-state NMR spectroscopy
    • B. Bechinger, and E.S. Salnikov The membrane interactions of antimicrobial peptides revealed by solid-state NMR spectroscopy Chem. Phys. Lipids 165 2012 282 301
    • (2012) Chem. Phys. Lipids , vol.165 , pp. 282-301
    • Bechinger, B.1    Salnikov, E.S.2
  • 17
    • 33845217043 scopus 로고    scopus 로고
    • Oligomeric Structure, Dynamics, and Orientation of Membrane Proteins from Solid-State NMR
    • DOI 10.1016/j.str.2006.10.002, PII S0969212606004011
    • M. Hong Oligomeric structure, dynamics, and orientation of membrane proteins from solid-state NMR Structure 14 2006 1731 1740 (Pubitemid 44855624)
    • (2006) Structure , vol.14 , Issue.12 , pp. 1731-1740
    • Hong, M.1
  • 18
    • 79953186604 scopus 로고    scopus 로고
    • Structure and dynamics of cationic membrane peptides and proteins: Insights from solid-state NMR
    • M. Hong, and Y. Su Structure and dynamics of cationic membrane peptides and proteins: insights from solid-state NMR Protein Sci. 20 2011 641 655
    • (2011) Protein Sci. , vol.20 , pp. 641-655
    • Hong, M.1    Su, Y.2
  • 19
    • 84859912916 scopus 로고    scopus 로고
    • Membrane protein structure and dynamics from NMR spectroscopy
    • M. Hong, Y. Zhang, and F. Hu Membrane protein structure and dynamics from NMR spectroscopy Annu. Rev. Phys. Chem. 63 2012 1 24
    • (2012) Annu. Rev. Phys. Chem. , vol.63 , pp. 1-24
    • Hong, M.1    Zhang, Y.2    Hu, F.3
  • 20
    • 78651426700 scopus 로고    scopus 로고
    • Role of cationic group structure in membrane binding and disruption by amphiphilic copolymers
    • E.F. Palermo, D.-K. Lee, A. Ramamoorthy, and K. Kuroda Role of cationic group structure in membrane binding and disruption by amphiphilic copolymers J. Phys. Chem. B 115 2010 366 375
    • (2010) J. Phys. Chem. B , vol.115 , pp. 366-375
    • Palermo, E.F.1    Lee, D.-K.2    Ramamoorthy, A.3    Kuroda, K.4
  • 21
    • 67349241519 scopus 로고    scopus 로고
    • Beyond NMR spectra of antimicrobial peptides: Dynamical images at atomic resolution and functional insights
    • A. Ramamoorthy Beyond NMR spectra of antimicrobial peptides: dynamical images at atomic resolution and functional insights Solid State Nucl. Magn. Reson. 35 2009 201 207
    • (2009) Solid State Nucl. Magn. Reson. , vol.35 , pp. 201-207
    • Ramamoorthy, A.1
  • 24
    • 46949096206 scopus 로고    scopus 로고
    • Asymmetric insertion of membrane proteins in lipid bilayers by solid-state NMR paramagnetic relaxation enhancement: A cell-penetrating peptide example
    • DOI 10.1021/ja802383t
    • Y. Su, R. Mani, and M. Hong Asymmetric insertion of membrane proteins in lipid bilayers by solid-state NMR paramagnetic relaxation enhancement: a cell-penetrating peptide example J. Am. Chem. Soc. 130 2008 8856 8864 (Pubitemid 351962521)
    • (2008) Journal of the American Chemical Society , vol.130 , Issue.27 , pp. 8856-8864
    • Su, Y.1    Mani, R.2    Hong, M.3
  • 25
    • 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. 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.1    Waring, A.J.2    Ruchala, P.3    Hong, M.4
  • 26
    • 77955330334 scopus 로고    scopus 로고
    • High-resolution orientation and depth of insertion of the voltage-sensing S4 helix of a potassium channel in lipid bilayers
    • T. Doherty, Y. Su, and M. Hong High-resolution orientation and depth of insertion of the voltage-sensing S4 helix of a potassium channel in lipid bilayers J. Mol. Biol. 401 2010 642 652
    • (2010) J. Mol. Biol. , vol.401 , pp. 642-652
    • Doherty, T.1    Su, Y.2    Hong, M.3
  • 28
    • 84861364500 scopus 로고    scopus 로고
    • Paramagnetic Cu(II) for probing membrane protein structure and function: Inhibition mechanism of the influenza M2 proton channel
    • Y. Su, F. Hu, and M. Hong Paramagnetic Cu(II) for probing membrane protein structure and function: inhibition mechanism of the influenza M2 proton channel J. Am. Chem. Soc. 134 2012 8693 8702
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 8693-8702
    • Su, Y.1    Hu, F.2    Hong, M.3
  • 31
    • 77952362863 scopus 로고    scopus 로고
    • Amphipathic helical cationic antimicrobial peptides promote rapid formation of crystalline states in the presence of phosphatidylglycerol: Lipid clustering in anionic membranes
    • R.F. Epand, L. Maloy, A. Ramamoorthy, and R.M. Epand Amphipathic helical cationic antimicrobial peptides promote rapid formation of crystalline states in the presence of phosphatidylglycerol: lipid clustering in anionic membranes Biophys. J. 98 2010 2564 2573
    • (2010) Biophys. J. , vol.98 , pp. 2564-2573
    • Epand, R.F.1    Maloy, L.2    Ramamoorthy, A.3    Epand, R.M.4
  • 32
    • 71649106004 scopus 로고    scopus 로고
    • Induction of non-lamellar lipid phases by antimicrobial peptides: A potential link to mode of action
    • E.F. Haney, S. Nathoo, H.J. Vogel, and E.J. Prenner Induction of non-lamellar lipid phases by antimicrobial peptides: a potential link to mode of action Chem. Phys. Lipids 163 2010 82 93
    • (2010) Chem. Phys. Lipids , vol.163 , pp. 82-93
    • Haney, E.F.1    Nathoo, S.2    Vogel, H.J.3    Prenner, E.J.4
  • 34
    • 84867091546 scopus 로고    scopus 로고
    • Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation
    • M.F.M. Sciacca, J.R. Brender, D.-K. Lee, and A. Ramamoorthy Phosphatidylethanolamine enhances amyloid fiber-dependent membrane fragmentation Biochemistry 51 2012 7676 7684
    • (2012) Biochemistry , vol.51 , pp. 7676-7684
    • Sciacca, M.F.M.1    Brender, J.R.2    Lee, D.-K.3    Ramamoorthy, A.4
  • 35
    • 3543051871 scopus 로고    scopus 로고
    • Role of membrane potential and hydrogen bonding in the mechanism of translocation of guanidinium-rich peptides into cells
    • DOI 10.1021/ja0482536
    • J.B. Rothbard, T.C. Jessop, R.S. Lewis, B.A. Murray, and P.A. Wender Role of membrane potential and hydrogen bonding in the mechanism of translocation of guanidinium-rich peptides into cells J. Am. Chem. Soc. 126 2004 9506 9507 (Pubitemid 39031015)
    • (2004) Journal of the American Chemical Society , vol.126 , Issue.31 , pp. 9506-9507
    • Rothbard, J.B.1    Jessop, T.C.2    Lewis, R.S.3    Murray, B.A.4    Wender, P.A.5
  • 36
    • 58949093974 scopus 로고    scopus 로고
    • Effect of membrane composition on antimicrobial peptides aurein 2.2 and 2.3 from australian southern bell frogs
    • J.T.J. Cheng, J.D. Hale, M. Elliot, R.E.W. Hancock, and S.K. Straus Effect of membrane composition on antimicrobial peptides aurein 2.2 and 2.3 from australian southern bell frogs Biophys. J. 96 2009 552 565
    • (2009) Biophys. J. , vol.96 , pp. 552-565
    • Cheng, J.T.J.1    Hale, J.D.2    Elliot, M.3    Hancock, R.E.W.4    Straus, S.K.5
  • 37
    • 0032717886 scopus 로고    scopus 로고
    • Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides
    • Y. Shai Mechanism of the binding, insertion and destabilization of phospholipid bilayer membranes by α-helical antimicrobial and cell non-selective membrane-lytic peptides Biochimica et Biophysica Acta (BBA) - Biomembranes 1462 1999 55 70
    • (1999) Biochimica et Biophysica Acta (BBA) - Biomembranes , vol.1462 , pp. 55-70
    • Shai, Y.1
  • 41
    • 0031984072 scopus 로고    scopus 로고
    • Trojan peptides: The penetratin system for intracellular delivery
    • DOI 10.1016/S0962-8924(97)01214-2
    • D. Derossi, G. Chassaing, and A. Prochiantz Trojan peptides: the penetratin system for intracellular delivery Trends Cell Biol. 8 1998 84 87 (Pubitemid 28056816)
    • (1998) Trends in Cell Biology , vol.8 , Issue.2 , pp. 84-87
    • Derossi, D.1    Chassaing, G.2    Prochiantz, A.3
  • 42
    • 0030273590 scopus 로고    scopus 로고
    • Getting hydrophilic compounds into cells: Lessons from homeopeptides. Commentary
    • DOI 10.1016/S0959-4388(96)80095-X
    • A. Prochiantz Getting hydrophilic compounds into cells: lessons from homeopeptides Curr. Opin. Neurobiol. 6 1996 629 634 (Pubitemid 26387717)
    • (1996) Current Opinion in Neurobiology , vol.6 , Issue.5 , pp. 629-634
    • Prochiantz, A.1
  • 43
    • 0041843710 scopus 로고    scopus 로고
    • Charge-dependent translocation of the Trojan peptide penetratin across lipid membranes
    • H. Binder, and G. Lindblom Charge-dependent translocation of the Trojan peptide penetratin across lipid membranes Biophys. J. 85 2003 982 995 (Pubitemid 36909662)
    • (2003) Biophysical Journal , vol.85 , Issue.2 , pp. 982-995
    • Binder, H.1    Lindblom, G.2
  • 44
    • 78149422223 scopus 로고    scopus 로고
    • Cell-penetrating peptides, electroporation and drug delivery
    • K. Cahill Cell-penetrating peptides, electroporation and drug delivery IET Syst. Biol. 4 2010 367 378
    • (2010) IET Syst. Biol. , vol.4 , pp. 367-378
    • Cahill, K.1
  • 46
    • 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
  • 47
    • 23044450818 scopus 로고    scopus 로고
    • Solid-state nuclear magnetic resonance relaxation studies of the interaction mechanism of antimicrobial peptides with phospholipid bilayer membranes
    • DOI 10.1021/bi050730p
    • J.-X. Lu, K. Damodaran, J. Blazyk, and G.A. Lorigan Solid-state nuclear magnetic resonance relaxation studies of the interaction mechanism of antimicrobial peptides with phospholipid bilayer membranes Biochemistry 44 2005 10208 10217 (Pubitemid 41076816)
    • (2005) Biochemistry , vol.44 , Issue.30 , pp. 10208-10217
    • Lu, J.-X.1    Damodaraiv, K.2    Blazyk, J.3    Lorigan, G.A.4
  • 49
    • 80051785173 scopus 로고    scopus 로고
    • The expanding scope of antimicrobial peptide structures and their modes of action
    • L.T. Nguyen, E.F. Haney, and H.J. Vogel The expanding scope of antimicrobial peptide structures and their modes of action Trends Biotechnol. 29 2011 464 472
    • (2011) Trends Biotechnol. , vol.29 , pp. 464-472
    • Nguyen, L.T.1    Haney, E.F.2    Vogel, H.J.3
  • 51
    • 0029802678 scopus 로고    scopus 로고
    • Conformational and associative behaviours of the third helix of antennapedia homeodomain in membrane-mimetic environments
    • J.P. Berlose, O. Convert, D. Derossi, A. Brunissen, and G. Chassaing Conformational and associative behaviours of the third helix of antennapedia homeodomain in membrane-mimetic environments Eur. J. Biochem. 242 1996 372 386 (Pubitemid 26414244)
    • (1996) European Journal of Biochemistry , vol.242 , Issue.2 , pp. 372-386
    • Berlose, J.-P.1    Convert, O.2    Derossi, D.3    Brunissen, A.4    Chassaing, G.5
  • 52
    • 0037139592 scopus 로고    scopus 로고
    • Micelle-induced curvature in a water-insoluble HIV-1 Env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel
    • DOI 10.1021/ja017875d
    • J.J. Chou, J.D. Kaufman, S.J. Stahl, P.T. Wingfield, and A. Bax Micelle-induced curvature in a water-insoluble HIV-1 Env peptide revealed by NMR dipolar coupling measurement in stretched polyacrylamide gel J. Am. Chem. Soc. 124 2002 2450 2451 (Pubitemid 34251754)
    • (2002) Journal of the American Chemical Society , vol.124 , Issue.11 , pp. 2450-2451
    • Chou, J.J.1    Kaufman, J.D.2    Stahl, S.J.3    Wingfield, P.T.4    Bax, A.5
  • 53
    • 0022980372 scopus 로고
    • Molecular details of melittin-induced lysis of phospholipid membranes as revealed by deuterium and phosphorus NMR
    • E.J. Dufourc, I.C.P. Smith, and J. Dufourcq Molecular details of melittin-induced lysis of phospholipid membranes as revealed by deuterium and phosphorus NMR Biochemistry 25 1986 6448 6455 (Pubitemid 17217892)
    • (1986) Biochemistry , vol.25 , Issue.21 , pp. 6448-6455
    • Dufourc, E.J.1    Smith, I.C.P.2    Dufourcq, J.3
  • 54
    • 74249114791 scopus 로고    scopus 로고
    • Membrane interactions and dynamics of a 21-mer cytotoxic peptide: A solid-state NMR study
    • M. Ouellet, N. Voyer, and M. Auger Membrane interactions and dynamics of a 21-mer cytotoxic peptide: a solid-state NMR study Biochim. Biophys. Acta 1798 2010 235 243
    • (2010) Biochim. Biophys. Acta , vol.1798 , pp. 235-243
    • Ouellet, M.1    Voyer, N.2    Auger, M.3
  • 55
    • 80052553690 scopus 로고    scopus 로고
    • Conformational disorder of membrane peptides investigated from solid-state NMR line widths and line shapes
    • Y. Su, and M. Hong Conformational disorder of membrane peptides investigated from solid-state NMR line widths and line shapes J. Phys. Chem. B 115 2011 10758 10767
    • (2011) J. Phys. Chem. B , vol.115 , pp. 10758-10767
    • Su, Y.1    Hong, M.2
  • 56
    • 79959281852 scopus 로고    scopus 로고
    • Probing the interaction of polyphenols with lipid bilayers by solid-state NMR spectroscopy
    • X. Yu, S. Chu, A.E. Hagerman, and G.A. Lorigan Probing the interaction of polyphenols with lipid bilayers by solid-state NMR spectroscopy J. Agr. Food Chem. 59 2011 6783 6789
    • (2011) J. Agr. Food Chem. , vol.59 , pp. 6783-6789
    • Yu, X.1    Chu, S.2    Hagerman, A.E.3    Lorigan, G.A.4
  • 58
    • 33750707584 scopus 로고    scopus 로고
    • 13C solid-state NMR spectroscopic study
    • DOI 10.1021/bi0614028
    • 13C solid-state NMR spectroscopic study Biochemistry 45 2006 13312 13322 (Pubitemid 44707691)
    • (2006) Biochemistry , vol.45 , Issue.44 , pp. 13312-13322
    • Abu-Baker, S.1    Lorigan, G.A.2
  • 59
    • 36549049519 scopus 로고    scopus 로고
    • Investigating the interaction of Saposin C with POPS and POPC phospholipids: A solid-state NMR spectroscopic study
    • DOI 10.1529/biophysj.107.107789
    • S. Abu-Baker, X. Qi, and G.A. Lorigan Investigating the interaction of saposin s with POPS and POPC phospholipids: a solid-state NMR spectroscopic study Biophys. J. 93 2007 3480 3490 (Pubitemid 350190811)
    • (2007) Biophysical Journal , vol.93 , Issue.10 , pp. 3480-3490
    • Abu-Baker, S.1    Qi, X.2    Lorigan, G.A.3
  • 60
    • 36849117843 scopus 로고
    • Proton relaxation times in paramagnetic solutions
    • N. Bloembergen Proton relaxation times in paramagnetic solutions J. Chem. Phys. 27 1957 572 573
    • (1957) J. Chem. Phys. , vol.27 , pp. 572-573
    • Bloembergen, N.1
  • 61
    • 36149008265 scopus 로고
    • Relaxation processes in a system of two spins
    • I. Solomon Relaxation processes in a system of two spins Phys. Rev. 99 1955 559
    • (1955) Phys. Rev. , vol.99 , pp. 559
    • Solomon, I.1
  • 62
    • 0025978021 scopus 로고
    • Lanthanide-induced phosphorus-31 NMR downfield chemical shifts of lysophosphatidylcholines are sensitive to lysophospholipid critical micelle concentration
    • V.V. Kumar, and W.J. Baumann Lanthanide-induced phosphorus-31 NMR downfield chemical shifts of lysophosphatidylcholines are sensitive to lysophospholipid critical micelle concentration Biophys. J. 59 1991 103 107
    • (1991) Biophys. J. , vol.59 , pp. 103-107
    • Kumar, V.V.1    Baumann, W.J.2
  • 63
    • 0024655521 scopus 로고
    • Lysophosphatidylcholine stabilizes small unilamellar phosphatidylcholine vesicles. Phosphorus-31 NMR evidence for the "wedge" effect
    • V.V. Kumar, B. Malewicz, and W.J. Baumann Lysophosphatidylcholine stabilizes small unilamellar phosphatidylcholine vesicles. Phosphorus-31 NMR evidence for the "wedge" effect Biophys. J. 55 1989 789 792
    • (1989) Biophys. J. , vol.55 , pp. 789-792
    • Kumar, V.V.1    Malewicz, B.2    Baumann, W.J.3
  • 64
    • 84861101914 scopus 로고    scopus 로고
    • Solid-state nuclear magnetic resonance structural studies of proteins using paramagnetic probes
    • C.P. Jaroniec Solid-state nuclear magnetic resonance structural studies of proteins using paramagnetic probes Solid State Nucl. Mag. 43-44 2012 1 13
    • (2012) Solid State Nucl. Mag. , vol.43-44 , pp. 1-13
    • Jaroniec, C.P.1
  • 65
    • 80755125957 scopus 로고    scopus 로고
    • 15N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR
    • 15N longitudinal paramagnetic relaxation enhancements in proteins by solid-state NMR J. Biomol. NMR 51 2011 293 302
    • (2011) J. Biomol. NMR , vol.51 , pp. 293-302
    • Nadaud, P.1    Sengupta, I.2    Helmus, J.3    Jaroniec, C.4
  • 66
    • 67650534960 scopus 로고    scopus 로고
    • Paramagnetic ions enable tuning of nuclear relaxation rates and provide long-range structural restraints in solid-state NMR of proteins
    • P.S. Nadaud, J.J. Helmus, S.L. Kall, and C.P. Jaroniec Paramagnetic ions enable tuning of nuclear relaxation rates and provide long-range structural restraints in solid-state NMR of proteins J. Am. Chem. Soc. 131 2009 8108 8120
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 8108-8120
    • Nadaud, P.S.1    Helmus, J.J.2    Kall, S.L.3    Jaroniec, C.P.4
  • 67
    • 77954639411 scopus 로고    scopus 로고
    • Rapid acquisition of multidimensional solid-state NMR spectra of proteins facilitated by covalently bound paramagnetic tags
    • P.S. Nadaud, J.J. Helmus, I. Sengupta, and C.P. Jaroniec Rapid acquisition of multidimensional solid-state NMR spectra of proteins facilitated by covalently bound paramagnetic tags J. Am. Chem. Soc. 132 2010 9561 9563
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 9561-9563
    • Nadaud, P.S.1    Helmus, J.J.2    Sengupta, I.3    Jaroniec, C.P.4
  • 68
    • 84860258939 scopus 로고    scopus 로고
    • Protein fold determined by paramagnetic magic-angle spinning solid-state NMR spectroscopy
    • I. Sengupta, P.S. Nadaud, J.J. Helmus, C.D. Schwieters, and C.P. Jaroniec Protein fold determined by paramagnetic magic-angle spinning solid-state NMR spectroscopy Nat. Chem. 4 2012 410 417
    • (2012) Nat. Chem. , vol.4 , pp. 410-417
    • Sengupta, I.1    Nadaud, P.S.2    Helmus, J.J.3    Schwieters, C.D.4    Jaroniec, C.P.5
  • 70
    • 77952566893 scopus 로고    scopus 로고
    • Use of a copper-chelated lipid speeds up NMR measurements from membrane proteins
    • K. Yamamoto, J. Xu, K.E. Kawulka, J.C. Vederas, and A. Ramamoorthy Use of a copper-chelated lipid speeds up NMR measurements from membrane proteins J. Am. Chem. Soc. 132 2010 6929 6931
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6929-6931
    • Yamamoto, K.1    Xu, J.2    Kawulka, K.E.3    Vederas, J.C.4    Ramamoorthy, A.5
  • 71
    • 0037533875 scopus 로고    scopus 로고
    • EDTA-derivatized deoxythymidine as a tool for rapid determination of protein binding polarity to DNA by intermolecular paramagnetic relaxation enhancement
    • DOI 10.1021/ja034488q
    • J. Iwahara, D.E. Anderson, E.C. Murphy, and G.M. Clore EDTA-derivatized deoxythymidine as a tool for rapid determination of protein binding polarity to DNA by intermolecular paramagnetic relaxation enhancement J. Am. Chem. Soc. 125 2003 6634 6635 (Pubitemid 36667439)
    • (2003) Journal of the American Chemical Society , vol.125 , Issue.22 , pp. 6634-6635
    • Iwahara, J.1    Anderson, D.E.2    Murphy, E.C.3    Clore, G.M.4
  • 72
    • 33646356250 scopus 로고    scopus 로고
    • Detecting transient intermediates in macromolecular binding by paramagnetic NMR
    • J. Iwahara, and G.M. Clore Detecting transient intermediates in macromolecular binding by paramagnetic NMR Nature 440 2006 1227 1230
    • (2006) Nature , vol.440 , pp. 1227-1230
    • Iwahara, J.1    Clore, G.M.2
  • 73
    • 44649202072 scopus 로고    scopus 로고
    • Solid-state NMR spectroscopy of a membrane protein in biphenyl phospholipid bicelles with the bilayer normal parallel to the magnetic field
    • S.H. Park, C. Loudet, F.M. Marassi, E.J. Dufourc, and S.J. Opella Solid-state NMR spectroscopy of a membrane protein in biphenyl phospholipid bicelles with the bilayer normal parallel to the magnetic field J. Magn. Reson. 193 2008 133 138
    • (2008) J. Magn. Reson. , vol.193 , pp. 133-138
    • Park, S.H.1    Loudet, C.2    Marassi, F.M.3    Dufourc, E.J.4    Opella, S.J.5
  • 74
    • 77957964107 scopus 로고    scopus 로고
    • Solid-state NMR paramagnetic relaxation enhancement immersion depth studies in phospholipid bilayers
    • S. Chu, S. Maltsev, A.H. Emwas, and G.A. Lorigan Solid-state NMR paramagnetic relaxation enhancement immersion depth studies in phospholipid bilayers J. Magn. Reson. 207 2010 89 94
    • (2010) J. Magn. Reson. , vol.207 , pp. 89-94
    • Chu, S.1    Maltsev, S.2    Emwas, A.H.3    Lorigan, G.A.4
  • 76
    • 0345275894 scopus 로고    scopus 로고
    • Penetratin and Related Cell-Penetrating Cationic Peptides Can Translocate Across Lipid Bilayers in the Presence of a Transbilayer Potential
    • DOI 10.1021/bi035293y
    • D. Terrone, S.L.W. Sang, L. Roudaia, and J.R. Silvius Penetratin and related cell-penetrating cationic peptides can translocate across lipid bilayers in the presence of a transbilayer potential Biochemistry 42 2003 13787 13799 (Pubitemid 37466604)
    • (2003) Biochemistry , vol.42 , Issue.47 , pp. 13787-13799
    • Terrone, D.1    Sang, S.L.W.2    Roudaia, L.3    Silvius, J.R.4
  • 77
    • 0015499213 scopus 로고
    • The response of fluorescent amines to pH gradients across liposome membranes
    • D.W. Deamer, R.C. Prince, and A.R. Crofts The response of fluorescent amines to pH gradients across liposome membranes Biochim. Biophys. Acta 274 1972 323 335
    • (1972) Biochim. Biophys. Acta , vol.274 , pp. 323-335
    • Deamer, D.W.1    Prince, R.C.2    Crofts, A.R.3
  • 78
    • 0033835604 scopus 로고    scopus 로고
    • Formation of unilamellar vesicles by repetitive freeze-thaw cycles: Characterization by electron microscopy and P-31-nuclear magnetic resonance
    • M. Traikia, D.E. Warschawski, M. Recouvreur, J. Cartaud, and P.F. Devaux Formation of unilamellar vesicles by repetitive freeze-thaw cycles: characterization by electron microscopy and P-31-nuclear magnetic resonance Eur. Biophys. J. Biophys. Lett. 29 2000 184 195
    • (2000) Eur. Biophys. J. Biophys. Lett. , vol.29 , pp. 184-195
    • Traikia, M.1    Warschawski, D.E.2    Recouvreur, M.3    Cartaud, J.4    Devaux, P.F.5
  • 79
    • 23944483437 scopus 로고    scopus 로고
    • Cell-penetrating pep tides: Tools for intracellular delivery of therapeutics
    • DOI 10.1007/s00018-005-5109-0
    • S. Deshayes, M.C. Morris, G. Divita, and F. Heitz Cell-penetrating peptides: tools for intracellular delivery of therapeutics Cell. Mol. Life Sci. 62 2005 1839 1849 (Pubitemid 41188523)
    • (2005) Cellular and Molecular Life Sciences , vol.62 , Issue.16 , pp. 1839-1849
    • Deshayes, S.1    Morris, M.C.2    Divita, G.3    Heitz, F.4
  • 80
    • 38949213664 scopus 로고    scopus 로고
    • Predicting cell-penetrating peptides
    • DOI 10.1016/j.addr.2007.09.003, PII S0169409X07002918
    • M. Hansen, K. Kilk, and Ü. Langel Predicting cell-penetrating peptides Adv. Drug Deliv. Rev. 60 2008 572 579 (Pubitemid 351215574)
    • (2008) Advanced Drug Delivery Reviews , vol.60 , Issue.4-5 , pp. 572-579
    • Hansen, M.1    Kilk, K.2    Langel, U.3
  • 81
    • 13844254266 scopus 로고    scopus 로고
    • Cell-penetrating peptides: Mechanism and kinetics of cargo delivery
    • DOI 10.1016/j.addr.2004.10.010, PII S0169409X04002674
    • M. Zorko, and Ü. Langel Cell-penetrating peptides: mechanism and kinetics of cargo delivery Adv. Drug Deliv. Rev. 57 2005 529 545 (Pubitemid 40255559)
    • (2005) Advanced Drug Delivery Reviews , vol.57 , Issue.4 SPEC.ISS. , pp. 529-545
    • Zorko, M.1    Langel, U.2
  • 83
    • 0027975256 scopus 로고
    • Facile acquisition and assignment of oriented sample NMR spectra for bilayer surface-associated proteins
    • C.R. Sanders, and G.C. Landis Facile acquisition and assignment of oriented sample NMR spectra for bilayer surface-associated proteins J. Am. Chem. Soc. 116 1994 6470 6471
    • (1994) J. Am. Chem. Soc. , vol.116 , pp. 6470-6471
    • Sanders, C.R.1    Landis, G.C.2
  • 84
    • 0028947465 scopus 로고
    • Reconstitution of membrane proteins into lipid-rich bilayered mixed micelles for NMR studies
    • C.R. Sanders, and G.C. Landis Reconstitution of membrane proteins into lipid-rich bilayered mixed micelles for NMR studies Biochemistry 34 1995 4030 4040
    • (1995) Biochemistry , vol.34 , pp. 4030-4040
    • Sanders, C.R.1    Landis, G.C.2
  • 86
    • 58149308564 scopus 로고    scopus 로고
    • Membrane deformation under local pH gradient: Mimicking mitochondrial cristae dynamics
    • N. Khalifat, N. Puff, S. Bonneau, J.-B. Fournier, and M.I. Angelova Membrane deformation under local pH gradient: mimicking mitochondrial cristae dynamics Biophys. J. 95 2008 4924 4933
    • (2008) Biophys. J. , vol.95 , pp. 4924-4933
    • Khalifat, N.1    Puff, N.2    Bonneau, S.3    Fournier, J.-B.4    Angelova, M.I.5
  • 88
    • 68849106030 scopus 로고    scopus 로고
    • Interaction of Poly(l-arginine) with negatively charged dppg membranes: Calorimetric and monolayer studies
    • C. Schwieger, and A. Blume Interaction of Poly(l-arginine) with negatively charged dppg membranes: calorimetric and monolayer studies Biomacromolecules 10 2009 2152 2161
    • (2009) Biomacromolecules , vol.10 , pp. 2152-2161
    • Schwieger, C.1    Blume, A.2
  • 89
    • 20444382011 scopus 로고    scopus 로고
    • Bilayer interaction and localization of cell penetrating peptides with model membranes: A comparative study of a human calcitonin (hCT)-derived peptide with pVEC and pAntp(43-58)
    • DOI 10.1016/j.bbamem.2005.04.006, PII S0005273605001045
    • M.E. Herbig, U. Fromm, J. Leuenberger, U. Krauss, A.G. Beck-Sickinger, and H.P. Merkle Bilayer interaction and localization of cell penetrating peptides with model membranes: a comparative study of a human calcitonin (hCT)-derived peptide with pVEC and pAntp(43-58) Biochim. Biophys. Acta-Biomembr. 1712 2005 197 211 (Pubitemid 40799305)
    • (2005) Biochimica et Biophysica Acta - Biomembranes , vol.1712 , Issue.2 , pp. 197-211
    • Herbig, M.E.1    Fromm, U.2    Leuenberger, J.3    Krauss, U.4    Beck-Sickinger, A.G.5    Merkle, H.P.6
  • 90
    • 84859208261 scopus 로고    scopus 로고
    • Binding of Tat peptides on DOPC and DOPG lipid bilayer membrane studied by molecular dynamics simulations
    • S. Kawamoto, M. Takasu, T. Miyakawa, R. Morikawa, T. Oda, S. Futaki, and H. Nagao Binding of Tat peptides on DOPC and DOPG lipid bilayer membrane studied by molecular dynamics simulations Mol. Simul. 38 2012 366 368
    • (2012) Mol. Simul. , vol.38 , pp. 366-368
    • Kawamoto, S.1    Takasu, M.2    Miyakawa, T.3    Morikawa, R.4    Oda, T.5    Futaki, S.6    Nagao, H.7
  • 91
    • 21244497735 scopus 로고    scopus 로고
    • Penetratin-membrane association: W48/R52/W56 shield the peptide from the aqueous phase
    • DOI 10.1529/biophysj.104.052787
    • M.F. Lensink, B. Christiaens, J. Vandekerckhove, A. Prochiantz, and M. Rosseneu Penetratin-membrane association: W48/R52/W56 shield the peptide from the aqueous phase Biophys. J. 88 2005 939 952 (Pubitemid 40975929)
    • (2005) Biophysical Journal , vol.88 , Issue.2 , pp. 939-952
    • Lensink, M.F.1    Christiaens, B.2    Vandekerckhove, J.3    Prochiantz, A.4    Rosseneu, M.5
  • 92
    • 0037071786 scopus 로고    scopus 로고
    • Conformational states of the cell-penetrating peptide penetratin when interacting with phospholipid vesicles: Effects of surface charge and peptide concentration
    • DOI 10.1016/S0005-2736(02)00373-5, PII S0005273602003735
    • M. Magzoub, L.E.G. Eriksson, and A. Graslund Conformational states of the cell-penetrating peptide penetratin when interacting with phospholipid vesicles: effects of surface charge and peptide concentration Biochim. Biophys. Acta-Biomembr. 1563 2002 53 63 (Pubitemid 34455043)
    • (2002) Biochimica et Biophysica Acta - Biomembranes , vol.1563 , Issue.1-2 , pp. 53-63
    • Magzoub, M.1    Eriksson, L.E.G.2    Graslund, A.3
  • 93
    • 0035795727 scopus 로고    scopus 로고
    • Interaction and structure induction of cell-penetrating peptides in the presence of phospholipid vesicles
    • DOI 10.1016/S0005-2736(01)00304-2, PII S0005273601003042
    • M. Magzoub, K. Kilk, L.E.G. Eriksson, U. Langel, and A. Graslund Interaction and structure induction of cell-penetrating peptides in the presence of phospholipid vesicles BBA - Biomembranes 1512 2001 77 89 (Pubitemid 32378784)
    • (2001) Biochimica et Biophysica Acta - Biomembranes , vol.1512 , Issue.1 , pp. 77-89
    • Magzoub, M.1    Kilk, K.2    Eriksson L.E.Goran3    Langel, U.4    Graslund, A.5
  • 94
    • 82155176225 scopus 로고    scopus 로고
    • Comparative study on the interaction of cell-penetrating polycationic polymers with lipid membranes
    • Y. Takechi, H. Tanaka, H. Kitayama, H. Yoshii, M. Tanaka, and H. Saito Comparative study on the interaction of cell-penetrating polycationic polymers with lipid membranes Chem. Phys. Lipids 165 2012 51 58
    • (2012) Chem. Phys. Lipids , vol.165 , pp. 51-58
    • Takechi, Y.1    Tanaka, H.2    Kitayama, H.3    Yoshii, H.4    Tanaka, M.5    Saito, H.6
  • 96
    • 33746853554 scopus 로고    scopus 로고
    • Real-time transmembrane translocation of penetratin driven by light-generated proton pumping
    • J. Bjorklund, H. Biverstahl, A. Graslund, L. Maler, and P. Brzezinski Real-time transmembrane translocation of penetratin driven by light-generated proton pumping Biophys. J. 91 2006 L29 L31
    • (2006) Biophys. J. , vol.91
    • Bjorklund, J.1    Biverstahl, H.2    Graslund, A.3    Maler, L.4    Brzezinski, P.5
  • 97
    • 70350023192 scopus 로고    scopus 로고
    • Arginine-rich peptides destabilize the plasma membrane, consistent with a pore formation translocation mechanism of cell-penetrating peptides
    • H.D. Herce, A.E. Garcia, J. Litt, R.S. Kane, P. Martin, N. Enrique, A. Rebolledo, and V. Milesi Arginine-rich peptides destabilize the plasma membrane, consistent with a pore formation translocation mechanism of cell-penetrating peptides Biophys. J. 97 2009 1917 1925
    • (2009) Biophys. J. , vol.97 , pp. 1917-1925
    • Herce, H.D.1    Garcia, A.E.2    Litt, J.3    Kane, R.S.4    Martin, P.5    Enrique, N.6    Rebolledo, A.7    Milesi, V.8
  • 98
    • 27744493266 scopus 로고    scopus 로고
    • Modeling the endosomal escape of cell-penetrating peptides: Transmembrane pH gradient driven translocation across phospholipid bilayers
    • DOI 10.1021/bi051356w
    • M. Magzoub, A. Pramanik, and A. Graslund Modeling the endosomal escape of cell-penetrating peptides: transmembrane pH gradient driven translocation across phospholipid bilayers Biochemistry 44 2005 14890 14897 (Pubitemid 41612268)
    • (2005) Biochemistry , vol.44 , Issue.45 , pp. 14890-14897
    • Magzoub, M.1    Pramanik, A.2    Graslund, A.3
  • 99
    • 24944516963 scopus 로고    scopus 로고
    • An experiment-based algorithm for predicting the partitioning of unfolded peptides into phosphatidylcholine bilayer interfaces
    • DOI 10.1021/bi051193b
    • K. Hristova, and S.H. White An experiment-based algorithm for predicting the partitioning of unfolded peptides into phosphatidylcholine bilayer interfaces Biochemistry 44 2005 12614 12619 (Pubitemid 41324352)
    • (2005) Biochemistry , vol.44 , Issue.37 , pp. 12614-12619
    • Hristova, K.1    White, S.H.2
  • 100
    • 0029738872 scopus 로고    scopus 로고
    • Experimentally determined hydrophobicity scale for proteins at membrane interfaces
    • DOI 10.1038/nsb1096-842
    • W. Wimley, and S. White Experimentally determined hydrophobicity scale for proteins at membrane interfaces Nat. Struct. Mol. Biol. 3 1996 842 848 (Pubitemid 26330634)
    • (1996) Nature Structural Biology , vol.3 , Issue.10 , pp. 842-848
    • Wimley, W.C.1    White, S.H.2
  • 101
    • 0030005250 scopus 로고    scopus 로고
    • Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides
    • W.C. Wimley, T.P. Creamer, and S.H. White Solvation energies of amino acid side chains and backbone in a family of host-guest pentapeptides Biochemistry 35 1996 5109 5124
    • (1996) Biochemistry , vol.35 , pp. 5109-5124
    • Wimley, W.C.1    Creamer, T.P.2    White, S.H.3
  • 102
    • 4544370680 scopus 로고    scopus 로고
    • Cell-permeable peptide antioxidants targeted to inner mitochondrial membrane inhibit mitochondrial swelling, oxidative cell death, and reperfusion injury
    • DOI 10.1074/jbc.M402999200
    • K. Zhao, G.-M. Zhao, D. Wu, Y. Soong, A.V. Birk, P.W. Schiller, and H.H. Szeto Cell-permeable peptide antioxidants targeted to inner mitochondrial membrane inhibit mitochondrial swelling, oxidative cell death, and reperfusion injury J. Biol. Chem. 279 2004 34682 34690 (Pubitemid 39318098)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.33 , pp. 34682-34690
    • Zhao, K.1    Zhao, G.-M.2    Wu, D.3    Soong, Y.4    Birk, A.V.5    Schiller, P.W.6    Szeto, H.H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.