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Volumn 6, Issue , 2016, Pages

SARS-CoV fusion peptides induce membrane surface ordering and curvature

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDE; VIRUS FUSION PROTEIN;

EID: 84999663587     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep37131     Document Type: Article
Times cited : (51)

References (102)
  • 1
    • 1642509113 scopus 로고    scopus 로고
    • SARS -Beginning to understand a new virus
    • Stadler, K., et al. SARS -Beginning to understand a new virus. Nat Rev Microbiol 1, 209-218, doi: 10.1038/Nrmicro775 (2003
    • (2003) Nat Rev Microbiol , vol.1 , pp. 209-218
    • Stadler, K.1
  • 2
    • 0037561920 scopus 로고    scopus 로고
    • Characterization of a novel coronavirus associated with severe acute respiratory syndrome
    • Rota, P. A., et al. Characterization of a novel coronavirus associated with severe acute respiratory syndrome. Science 300, 1394-1399, doi: 10.1126/science.108952 (2003
    • (2003) Science , vol.300 , pp. 1394-1399
    • Rota, P.A.1
  • 3
    • 0344395657 scopus 로고    scopus 로고
    • Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus
    • Li, W. H., et al. Angiotensin-converting enzyme 2 is a functional receptor for the SARS coronavirus. Nature 426, 450-454, doi: 10.1038/Nature02145 (2003
    • (2003) Nature , vol.426 , pp. 450-454
    • Li, W.H.1
  • 4
    • 8144221600 scopus 로고    scopus 로고
    • CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome coronavirus
    • Jeffers, S. A., et al. CD209L (L-SIGN) is a receptor for severe acute respiratory syndrome coronavirus. P Natl Acad Sci USA 101, 15748-15753, doi: 10.1073/pnas.0403812101 (2004
    • (2004) P Natl Acad Sci USA , vol.101 , pp. 15748-15753
    • Jeffers, S.A.1
  • 6
    • 38849114449 scopus 로고    scopus 로고
    • SARS coronavirus entry into host cells through a novel clathrin-and caveolae-independent endocytic pathway
    • Wang, H. L., et al. SARS coronavirus entry into host cells through a novel clathrin-and caveolae-independent endocytic pathway. Cell Res 18, 290-301, doi: 10.1038/Cr.2008.15 (2008
    • (2008) Cell Res , vol.18 , pp. 290-301
    • Wang, H.L.1
  • 7
    • 2542444524 scopus 로고    scopus 로고
    • The life cycle of SARS coronavirus in Vero E6 cells
    • Zhang, Q. F., et al. The life cycle of SARS coronavirus in Vero E6 cells. J Med Virol 73, 332-337, doi: 10.1002/Jmv.20095 (2004
    • (2004) J Med Virol , vol.73 , pp. 332-337
    • Zhang, Q.F.1
  • 8
    • 14644403757 scopus 로고    scopus 로고
    • The spike protein of severe acute respiratory syndrome (SARS) is cleaved in virus infected Vero-E6 cells
    • Wu, X. D., et al. The spike protein of severe acute respiratory syndrome (SARS) is cleaved in virus infected Vero-E6 cells. Cell Res 14, 400-406, doi: 10.1038/sj.cr.7290240 (2004
    • (2004) Cell Res , vol.14 , pp. 400-406
    • Wu, X.D.1
  • 9
    • 33745282653 scopus 로고    scopus 로고
    • Furin cleavage of the SARS coronavirus spike glycoprotein enhances cell-cell fusion but does not affect virion entry
    • Follis, K. E., York, J., & Nunberg, J. H. Furin cleavage of the SARS coronavirus spike glycoprotein enhances cell-cell fusion but does not affect virion entry. Virology 350, 358-369, doi: 10.1016/j.virol.2006.02.003 (2006
    • (2006) Virology , vol.350 , pp. 358-369
    • Follis, K.E.1    York, J.2    Nunberg, J.H.3
  • 10
    • 84871868782 scopus 로고    scopus 로고
    • Mechanisms of coronavirus cell entry mediated by the viral spike protein
    • Belouzard, S., Millet, J. K., Licitra, B. N., & Whittaker, G. R. Mechanisms of Coronavirus Cell Entry Mediated by the Viral Spike Protein. Viruses-Basel 4, 1011-1033, doi: 10.3390/V4061011 (2012
    • (2012) Viruses-Basel , vol.4 , pp. 1011-1033
    • Belouzard, S.1    Millet, J.K.2    Licitra, B.N.3    Whittaker, G.R.4
  • 11
    • 11144237311 scopus 로고    scopus 로고
    • Structure of a proteolytically resistant core from the severe acute respiratory syndrome coronavirus S2 fusion protein
    • Supekar, V. M., et al. Structure of a proteolytically resistant core from the severe acute respiratory syndrome coronavirus S2 fusion protein. P Natl Acad Sci USA 101, 17958-17963, doi: 10.1073/pnas.0406128102 (2004
    • (2004) P Natl Acad Sci USA , vol.101 , pp. 17958-17963
    • Supekar, V.M.1
  • 12
    • 0032503238 scopus 로고    scopus 로고
    • Roles in cell-to-cell fusion of two conserved hydrophobic regions in the murine coronavirus spike protein
    • Luo, Z. L., & Weiss, S. R. Roles in cell-to-cell fusion of two conserved hydrophobic regions in the murine coronavirus spike protein. Virology 244, 483-494, doi: 10.1006/viro.1998.9121 (1998
    • (1998) Virology , vol.244 , pp. 483-494
    • Luo, Z.L.1    Weiss, S.R.2
  • 13
    • 26244466757 scopus 로고    scopus 로고
    • Genetic analysis of the SARS-coronavirus spike glycoprotein functional domains involved in cell-surface expression and cell-to-cell fusion
    • Petit, C. M., et al. Genetic analysis of the SARS-coronavirus spike glycoprotein functional domains involved in cell-surface expression and cell-to-cell fusion. Virology 341, 215-230, doi: 10.1016/j.virol.2005.06.046 (2005
    • (2005) Virology , vol.341 , pp. 215-230
    • Petit, C.M.1
  • 14
    • 67650899039 scopus 로고    scopus 로고
    • Characterization of a highly conserved domain within the severe acute respiratory syndrome coronavirus spike protein s2 domain with characteristics of a viral fusion peptide
    • Madu, I. G., Roth, S. L., Belouzard, S., & Whittaker, G. R. Characterization of a Highly Conserved Domain within the Severe Acute Respiratory Syndrome Coronavirus Spike Protein S2 Domain with Characteristics of a Viral Fusion Peptide. J Virol 83, 7411-7421, doi: 10.1128/Jvi.00079-09 (2009
    • (2009) J Virol , vol.83 , pp. 7411-7421
    • Madu, I.G.1    Roth, S.L.2    Belouzard, S.3    Whittaker, G.R.4
  • 15
    • 18744404801 scopus 로고    scopus 로고
    • Identification and characterization of the putative fusion peptide of the severe acute respiratory syndrome-associated coronavirus spike protein
    • Sainz, B., Rausch, J., Gallaher, W., Garry, R., & Wimley, W. Identification and characterization of the putative fusion peptide of the severe acute respiratory syndrome-associated coronavirus spike protein. Journal of Virology 79, 7195-7206, doi: 10.1128/JVI.79.11.7195-7206.2005 (2005
    • (2005) Journal of Virology , vol.79 , pp. 7195-7206
    • Sainz, B.1    Rausch, J.2    Gallaher, W.3    Garry, R.4    Wimley, W.5
  • 17
    • 0037381269 scopus 로고    scopus 로고
    • The structural biology of type i viral membrane fusion
    • Colman, P., & Lawrence, M. The structural biology of type I viral membrane fusion. Nature Reviews Molecular Cell Biology 4, 309-319, doi: 10.1038/nrm1076 (2003
    • (2003) Nature Reviews Molecular Cell Biology , vol.4 , pp. 309-319
    • Colman, P.1    Lawrence, M.2
  • 18
    • 85017019017 scopus 로고    scopus 로고
    • Mechanisms of virus membrane fusion proteins
    • Kielian, M., & Enquist, L. Mechanisms of Virus Membrane Fusion Proteins. Annual Review of Virology, Vol 1 1, 171-189, doi: 10.1146/annurev-virology-031413-085521 (2014
    • (2014) Annual Review of Virology , vol.1 , Issue.1 , pp. 171-189
    • Kielian, M.1    Enquist, L.2
  • 19
    • 31344432402 scopus 로고    scopus 로고
    • Virus membrane-fusion proteins: More than one way to make a hairpin
    • Kielian, M., & Rey, F. Virus membrane-fusion proteins: more than one way to make a hairpin. Nature Reviews Microbiology 4, 67-76, doi: 10.1038/nrmicro1326 (2006
    • (2006) Nature Reviews Microbiology , vol.4 , pp. 67-76
    • Kielian, M.1    Rey, F.2
  • 20
    • 0036948265 scopus 로고    scopus 로고
    • Structure and function of membrane fusion peptides
    • Tamm, L., Han, X., Li, Y., & Lai, A. Structure and function of membrane fusion peptides. Biopolymers 66, 249-260, doi: 10.1002/bip.10261 (2002
    • (2002) Biopolymers , vol.66 , pp. 249-260
    • Tamm, L.1    Han, X.2    Li, Y.3    Lai, A.4
  • 21
    • 0038487379 scopus 로고    scopus 로고
    • Are fusion peptides a good model to study viral cell fusion?
    • Nieva, J., & Agirre, A. Are fusion peptides a good model to study viral cell fusion? Biochimica Et Biophysica Acta-Biomembranes 1614, 104-115, doi: 10.1016/S0005-2736(03)00168-8 (2003
    • (2003) Biochimica et Biophysica Acta-Biomembranes , vol.1614 , pp. 104-115
    • Nieva, J.1    Agirre, A.2
  • 22
    • 48549104349 scopus 로고    scopus 로고
    • And dynamic characterization of the interaction of the putative fusion peptide of the S2 SARS-CoV virus protein with lipid membranes
    • Guillen, J., de Almeida, R., Prieto, M., & Villalain, J. Structural and dynamic characterization of the interaction of the putative fusion peptide of the S2 SARS-CoV virus protein with lipid membranes. Journal of Physical Chemistry B 112, 6997-7007, doi: 10.1021/jp7118229 (2008
    • (2008) Journal of Physical Chemistry B , vol.112 , pp. 6997-7007
    • Guillen, J.1    De Almeida, R.2    Prieto, M.3    Structural, V.J.4
  • 23
    • 48649092280 scopus 로고    scopus 로고
    • A second sars-cov s2 glycoprotein internal membrane-active peptide biophysical characterization and membrane interaction
    • Guillen, J., Perez-Berna, A., Moreno, M., & Villalain, J. A second SARS-CoV S2 glycoprotein internal membrane-active peptide. Biophysical characterization and membrane interaction. Biochemistry 47, 8214-8224, doi: 10.1021/bi800814q (2008
    • (2008) Biochemistry , vol.47 , pp. 8214-8224
    • Guillen, J.1    Perez-Berna, A.2    Moreno, M.3    Villalain, J.4
  • 24
    • 0000326938 scopus 로고    scopus 로고
    • Nonlinear-least-squares analysis of slow-motion epr spectra in one and two dimensions using a modified levenberg-marquardt algorithm
    • Budil, D., Lee, S., Saxena, S., & Freed, J. Nonlinear-least-squares analysis of slow-motion EPR spectra in one and two dimensions using a modified Levenberg-Marquardt algorithm. Journal of Magnetic Resonance Series A 120, 155-189 (1996
    • (1996) Journal of Magnetic Resonance Series A , vol.120 , pp. 155-189
    • Budil, D.1    Lee, S.2    Saxena, S.3    Freed, J.4
  • 25
    • 0023662539 scopus 로고
    • A differential scanning calorimetric study of the thermotropic phase behavior of model membranes composed of phosphatidylcholines containing linear saturated fatty acyl chains
    • Lewis, R., Mak, N., & McElhaney, R. A differential scanning calorimetric study of the thermotropic phase behavior of model membranes composed of phosphatidylcholines containing linear saturated fatty acyl chains. Biochemistry 26, 6118-6126, doi: 10.1021/bi00393a026 (1987
    • (1987) Biochemistry , vol.26 , pp. 6118-6126
    • Lewis, R.1    Mak, N.2    McElhaney, R.3
  • 26
    • 0033803592 scopus 로고    scopus 로고
    • Calorimetric and spectroscopic studies of the thermotropic phase behavior of lipid bilayer model membranes composed of a homologous series of linear saturated phosphatidylserines
    • Lewis, R., & McElhaney, R. Calorimetric and spectroscopic studies of the thermotropic phase behavior of lipid bilayer model membranes composed of a homologous series of linear saturated phosphatidylserines. Biophysical Journal 79, 2043-2055 (2000
    • (2000) Biophysical Journal , vol.79 , pp. 2043-2055
    • Lewis, R.1    McElhaney, R.2
  • 27
    • 68849106030 scopus 로고    scopus 로고
    • Interaction of poly(l-arginine) with negatively charged dppg membranes: Calorimetric and monolayer studies
    • Schwieger, C., & Blume, A. Interaction of Poly(L-arginine) with Negatively Charged DPPG Membranes: Calorimetric and Monolayer Studies. Biomacromolecules 10, 2152-2161, doi: 10.1021/bm9003207 (2009
    • (2009) Biomacromolecules , vol.10 , pp. 2152-2161
    • Schwieger, C.1    Blume, A.2
  • 28
    • 33947424036 scopus 로고    scopus 로고
    • Interaction of the C2 domain from protein kinase C epsilon with model membranes
    • Sanchez-Bautista, S., et al. Interaction of the C2 domain from protein kinase C epsilon with model membranes. Biochemistry 46, 3183-3192, doi: 10.1021/bi0621720 (2007
    • (2007) Biochemistry , vol.46 , pp. 3183-3192
    • Sanchez-Bautista, S.1
  • 30
    • 0001994554 scopus 로고
    • Some aspects of the phase behavior of charged lipids
    • Hauser, H. Some aspects of the phase behavior of charged lipids. Biochimica Et Biophysica Acta 772, 37-50, doi: 10.1016/0005-2736(84)90515-7 (1984
    • (1984) Biochimica et Biophysica Acta , vol.772 , pp. 37-50
    • Hauser, H.1
  • 31
    • 65249177275 scopus 로고    scopus 로고
    • Lipid bilayer pre-transition as the beginning of the melting process
    • Riske, K., et al. Lipid bilayer pre-transition as the beginning of the melting process. Biochimica et Biophysica Acta-Biomembranes 1788, 954-963, doi: 10.1016/j.bbamem.2009.01.007 (2009
    • (2009) Biochimica et Biophysica Acta-Biomembranes , vol.1788 , pp. 954-963
    • Riske, K.1
  • 32
    • 0034841836 scopus 로고    scopus 로고
    • Membrane fusion between liposomes composed of acidic phospholipids and neutral phospholipids induced by melittin: A differential scanning calorimetric study
    • Higashino, Y., Matsui, A., & Ohki, K. Membrane fusion between liposomes composed of acidic phospholipids and neutral phospholipids induced by melittin: A differential scanning calorimetric study. Journal of Biochemistry 130, 393-397 (2001
    • (2001) Journal of Biochemistry , vol.130 , pp. 393-397
    • Higashino, Y.1    Matsui, A.2    Ohki, K.3
  • 33
    • 78649776872 scopus 로고    scopus 로고
    • Effects of the antimalarial drug primaquine on the dynamic structure of lipid model membranes
    • Basso, L. G. M., Rodrigues, R. Z., Naal, R. M. Z. G., & Costa-Filho, A. J. Effects of the antimalarial drug primaquine on the dynamic structure of lipid model membranes. Biochimica Et Biophysica Acta-Biomembranes 1808, 55-64, doi: 10.1016/j. bbamem.2010.08.009 (2011
    • (2011) Biochimica et Biophysica Acta-Biomembranes , vol.1808 , pp. 55-64
    • Basso, L.G.M.1    Rodrigues, R.Z.2    Naal, R.M.Z.G.3    Costa-Filho, A.J.4
  • 34
    • 0028941129 scopus 로고
    • Interaction of a peptide model of a hydrophobic transmembrane alpha-helical segment of a membrane protein with phosphatidylethanolamine bilayers: Differential scanning calorimetric and fourier transform infrared spectroscopic studies
    • Zhang, Y., Lewis, R., Hodges, R., & McElhaney, R. Interaction of a peptide model of a hydrophobic transmembrane alpha-helical segment of a membrane protein with phosphatidylethanolamine bilayers: differential scanning calorimetric and Fourier transform infrared spectroscopic studies. Biophysical Journal 68, 847-857 (1995
    • (1995) Biophysical Journal , vol.68 , pp. 847-857
    • Zhang, Y.1    Lewis, R.2    Hodges, R.3    McElhaney, R.4
  • 35
    • 0017138422 scopus 로고
    • Nature of the thermal pretransition of synthetic phospholipids: Dimyristolyl-and dipalmitoyllecithin
    • Janiak, M., Small, D., & Shipley, G. Nature of the thermal pretransition of synthetic phospholipids: dimyristolyl-and dipalmitoyllecithin. Biochemistry 15, 4575-4580 (1976
    • (1976) Biochemistry , vol.15 , pp. 4575-4580
    • Janiak, M.1    Small, D.2    Shipley, G.3
  • 36
    • 0014645670 scopus 로고
    • Thermal analysis of lipids, proteins and biological membranes a review and summary of some recent studies
    • Ladbrooke, B., & Chapman, D. Thermal analysis of lipids, proteins and biological membranes. A review and summary of some recent studies. Chemistry and Physics of Lipids 3, 304-356 (1969
    • (1969) Chemistry and Physics of Lipids , vol.3 , pp. 304-356
    • Ladbrooke, B.1    Chapman, D.2
  • 37
    • 84856278457 scopus 로고    scopus 로고
    • Molecular view of the role of fusion peptides in promoting positive membrane curvature
    • Fuhrmans, M., & Marrink, S. Molecular View of the Role of Fusion Peptides in Promoting Positive Membrane Curvature. Journal of the American Chemical Society 134, 1543-1552, doi: 10.1021/ja207290b (2012
    • (2012) Journal of the American Chemical Society , vol.134 , pp. 1543-1552
    • Fuhrmans, M.1    Marrink, S.2
  • 38
    • 0038487375 scopus 로고    scopus 로고
    • Fusion peptides and the mechanism of viral fusion
    • Epand, R. Fusion peptides and the mechanism of viral fusion. Biochimica Et Biophysica Acta-Biomembranes 1614, 116-121, doi: 10.1016/S0005-2736(03)00169-X (2003
    • (2003) Biochimica et Biophysica Acta-Biomembranes , vol.1614 , pp. 116-121
    • Epand, R.1
  • 39
    • 0011847313 scopus 로고
    • Stability of lyotropic phases with curved interfaces
    • Gruner, S. Stability of lyotropic phases with curved interfaces. Journal of Physical Chemistry 93, 7562-7570 (1989
    • (1989) Journal of Physical Chemistry , vol.93 , pp. 7562-7570
    • Gruner, S.1
  • 40
    • 0030783371 scopus 로고    scopus 로고
    • The mechanism of lamellar-to-inverted hexagonal phase transitions in phosphatidylethanolamine: Implications for membrane fusion mechanisms
    • Siegel, D., & Epand, R. The mechanism of lamellar-to-inverted hexagonal phase transitions in phosphatidylethanolamine: Implications for membrane fusion mechanisms. Biophysical Journal 73, 3089-3111 (1997
    • (1997) Biophysical Journal , vol.73 , pp. 3089-3111
    • Siegel, D.1    Epand, R.2
  • 41
    • 0027369494 scopus 로고
    • Reciprocal effects of apolipoprotein and lytic peptide analogs on membranes cross-sectional molecular shapes of amphipathic alpha helixes control membrane stability
    • Tytle, R. E., et al. Reciprocal effects of apolipoprotein and lytic peptide analogs on membranes. Cross-sectional molecular shapes of amphipathic alpha helixes control membrane stability. Journal of Biological Chemistry 268, 22112-22118 (1993
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 22112-22118
    • Tytle, R.E.1
  • 42
    • 84921630096 scopus 로고    scopus 로고
    • Interactions of the antimalarial amodiaquine with lipid model membranes
    • Barroso, R., Basso, L., & Costa, A. Interactions of the antimalarial amodiaquine with lipid model membranes. Chemistry and Physics of Lipids 186, 68-78, doi: 10.1016/j.chemphyslip.2014.12.003 (2015
    • (2015) Chemistry and Physics of Lipids , vol.186 , pp. 68-78
    • Barroso, R.1    Basso, L.2    Costa, A.3
  • 43
    • 84971254212 scopus 로고    scopus 로고
    • The two sides of a lipid-protein story
    • Basso, L., Mendes, L., & Costa-Filho, A. The two sides of a lipid-protein story. Biophysical Reviews 8, 179-191, doi: 10.1007/s12551-016-0199-5 (2016
    • (2016) Biophysical Reviews , vol.8 , pp. 179-191
    • Basso, L.1    Mendes, L.2    Costa-Filho, A.3
  • 44
    • 0028281769 scopus 로고
    • 250-GHz electron spin resonance studies of polarity gradients along the aliphatic chains in phospholipid membranes
    • Earle, K., Moscicki, J., Ge, M., Budil, D., & Freed, J. 250-GHz electron spin resonance studies of polarity gradients along the aliphatic chains in phospholipid membranes. Biophysical Journal 66, 1213-1221 (1994
    • (1994) Biophysical Journal , vol.66 , pp. 1213-1221
    • Earle, K.1    Moscicki, J.2    Ge, M.3    Budil, D.4    Freed, J.5
  • 45
    • 0031880099 scopus 로고    scopus 로고
    • Polarity profiles in oriented and dispersed phosphatidylcholine bilayers are different: An electron spin resonance study
    • Ge, M., & Freed, J. Polarity profiles in oriented and dispersed phosphatidylcholine bilayers are different: An electron spin resonance study. Biophysical Journal 74, 910-917 (1998
    • (1998) Biophysical Journal , vol.74 , pp. 910-917
    • Ge, M.1    Freed, J.2
  • 46
    • 68949109991 scopus 로고    scopus 로고
    • Fusion peptide from influenza hemagglutinin increases membrane surface order: An electron-spin resonance study
    • Ge, M., & Freed, J. Fusion Peptide from Influenza Hemagglutinin Increases Membrane Surface Order: An Electron-Spin Resonance Study. Biophysical Journal 96, 4925-4934, doi: 10.1016/j.bpj.2009.04.015 (2009
    • (2009) Biophysical Journal , vol.96 , pp. 4925-4934
    • Ge, M.1    Freed, J.2
  • 47
    • 84891846958 scopus 로고    scopus 로고
    • HIV gp41 fusion peptide increases membrane ordering in a cholesterol-dependent fashion
    • Lai, A., & Freed, J. HIV gp41 Fusion Peptide Increases Membrane Ordering in a Cholesterol-Dependent Fashion. Biophysical Journal 106, 172-181, doi: 10.1016/j.bpj.2013.11.027 (2014
    • (2014) Biophysical Journal , vol.106 , pp. 172-181
    • Lai, A.1    Freed, J.2
  • 48
    • 0024502680 scopus 로고
    • Chain configuration and flexibility gradient in phospholipid membranes-comparison between spin-label electron spin resonance and deuteron nuclear magnetic resonance and identification of new conformations
    • Moser, M., Marsh, D., Meier, P., Wassmer, K., & Kothe, G. Chain configuration and flexibility gradient in phospholipid membranes-Comparison between spin-label electron spin resonance and deuteron nuclear magnetic resonance and identification of new conformations. Biophysical Journal 55, 111-123 (1989
    • (1989) Biophysical Journal , vol.55 , pp. 111-123
    • Moser, M.1    Marsh, D.2    Meier, P.3    Wassmer, K.4    Kothe, G.5
  • 49
    • 0028218958 scopus 로고
    • An electron-spin-resonance study of interactions between phosphatidylcholine and phosphatidylserine in oriented membranes
    • Ge, M., Budil, D., & Freed, J. An Electron-Spin-Resonance Study of Interactions Between Phosphatidylcholine and Phosphatidylserine in Oriented Membranes. Biophysical Journal 66, 1515-1521 (1994
    • (1994) Biophysical Journal , vol.66 , pp. 1515-1521
    • Ge, M.1    Budil, D.2    Freed, J.3
  • 50
    • 0028271679 scopus 로고
    • Inhibition of membrane fusion by lysophosphatidylcholine
    • Yeagle, P., Smith, F., Young, J., & Flanagan, T. Inhibition of membrane fusion by lysophosphatidylcholine. Biochemistry 33, 1820-1827, doi: 10.1021/bi00173a027 (1994
    • (1994) Biochemistry , vol.33 , pp. 1820-1827
    • Yeagle, P.1    Smith, F.2    Young, J.3    Flanagan, T.4
  • 51
    • 0028882377 scopus 로고
    • Lysophosphatidylcholine inhibits vesicles fusion induced by the NH2-terminal extremity of SIV/HIV fusogenic proteins
    • Martin, I., & Ruysschaert, J. Lysophosphatidylcholine inhibits vesicles fusion induced by the NH2-terminal extremity of SIV/HIV fusogenic proteins. Biochimica Et Biophysica Acta-Biomembranes 1240, 95-100, doi: 10.1016/0005-2736(95)00171-4 (1995
    • (1995) Biochimica et Biophysica Acta-Biomembranes , vol.1240 , pp. 95-100
    • Martin, I.1    Ruysschaert, J.2
  • 52
    • 0028969738 scopus 로고
    • Control of baculovirus gp64-induced syncytium formation by membrane lipid composition
    • Chernomordik, L., Leikina, E., Cho, M., & Zimmerberg, J. Control of baculovirus gp64-induced syncytium formation by membrane lipid composition. Journal of Virology 69, 3049-3058 (1995
    • (1995) Journal of Virology , vol.69 , pp. 3049-3058
    • Chernomordik, L.1    Leikina, E.2    Cho, M.3    Zimmerberg, J.4
  • 53
    • 0344981517 scopus 로고    scopus 로고
    • Structure and molecular interactions in the headgroup region of dioleoylphosphatidylcholine bilayers: An electron spin resonance study
    • Ge, M., & Freed, J. Hydration, structure and molecular interactions in the headgroup region of dioleoylphosphatidylcholine bilayers: An electron spin resonance study. Biophysical Journal 85, 4023-4040, doi: 10.1016/S0006-3495(03)74816-4 (2003
    • (2003) Biophysical Journal , vol.85 , pp. 4023-4040
    • Ge, M.1    Hydration, F.J.2
  • 54
    • 22444446673 scopus 로고    scopus 로고
    • Water concentration profiles in membranes measured by ESEEM of spin-labeled lipids
    • Erilov, D., et al. Water concentration profiles in membranes measured by ESEEM of spin-labeled lipids. Journal of Physical Chemistry B 109, 12003-12013, doi: 10.1021/jp050886z (2005
    • (2005) Journal of Physical Chemistry B , vol.109 , pp. 12003-12013
    • Erilov, D.1
  • 55
    • 84885640998 scopus 로고    scopus 로고
    • Glycerol penetration profile in phospholipid bilayers measured by ESEEM of spin-labelled lipids
    • Konov, K., Isaev, N., & Dzuba, S. Glycerol penetration profile in phospholipid bilayers measured by ESEEM of spin-labelled lipids. Molecular Physics 111, 2882-2886, doi: 10.1080/00268976.2013.796416 (2013
    • (2013) Molecular Physics , vol.111 , pp. 2882-2886
    • Konov, K.1    Isaev, N.2    Dzuba, S.3
  • 56
    • 62649120466 scopus 로고    scopus 로고
    • Eseem measurements of local water concentration in d(2) o-containing spin-labeled systems
    • Milov, A., Samoilova, R., Shubin, A., Grishin, Y., & Dzuba, S. ESEEM Measurements of Local Water Concentration in D(2) O-Containing Spin-Labeled Systems. Applied Magnetic Resonance 35, 73-94, doi: 10.1007/s00723-008-0144-2 (2008
    • (2008) Applied Magnetic Resonance , vol.35 , pp. 73-94
    • Milov, A.1    Samoilova, R.2    Shubin, A.3    Grishin, Y.4    Dzuba, S.5
  • 57
    • 84939245868 scopus 로고    scopus 로고
    • Membrane-sugar interactions probed by pulsed electron paramagnetic resonance of spin labels
    • Konov, K., et al. Membrane-Sugar Interactions Probed by Pulsed Electron Paramagnetic Resonance of Spin Labels. Journal of Physical Chemistry B 119, 10261-10266, doi: 10.1021/acs.jpcb.5b06864 (2015
    • (2015) Journal of Physical Chemistry B , vol.119 , pp. 10261-10266
    • Konov, K.1
  • 58
    • 84855853473 scopus 로고    scopus 로고
    • Investigation of model membrane disruption mechanism by melittin using pulse electron paramagnetic resonance spectroscopy and cryogenic transmission electron microscopy
    • Gordon-Grossman, M., Zimmermann, H., Wolf, S., Shai, Y., & Goldfarb, D. Investigation of Model Membrane Disruption Mechanism by Melittin using Pulse Electron Paramagnetic Resonance Spectroscopy and Cryogenic Transmission Electron Microscopy. Journal of Physical Chemistry B 116, 179-188, doi: 10.1021/jp207159z (2012
    • (2012) Journal of Physical Chemistry B , vol.116 , pp. 179-188
    • Gordon-Grossman, M.1    Zimmermann, H.2    Wolf, S.3    Shai, Y.4    Goldfarb, D.5
  • 59
    • 77449151358 scopus 로고    scopus 로고
    • Electron spin-echo envelope modulation (eseem) reveals water and phosphate interactions with the kcsa potassium channel
    • Cieslak, J., Focia, P., & Gross, A. Electron Spin-Echo Envelope Modulation (ESEEM) Reveals Water and Phosphate Interactions with the KcsA Potassium Channel. Biochemistry 49, 1486-1494, doi: 10.1021/bi9016523 (2010
    • (2010) Biochemistry , vol.49 , pp. 1486-1494
    • Cieslak, J.1    Focia, P.2    Gross, A.3
  • 60
    • 84910008002 scopus 로고    scopus 로고
    • Water penetration profile at the protein-lipid interface in na, k-atpase membranes
    • Bartucci, R., Guzzi, R., Esmann, M., & Marsh, D. Water Penetration Profile at the Protein-Lipid Interface in Na, K-ATPase Membranes. Biophysical Journal 107, 1375-1382, doi: 10.1016/j.bpj.2014.07.057 (2014
    • (2014) Biophysical Journal , vol.107 , pp. 1375-1382
    • Bartucci, R.1    Guzzi, R.2    Esmann, M.3    Marsh, D.4
  • 62
    • 61549143693 scopus 로고    scopus 로고
    • Intramembrane water associated with toac spin-labeled alamethicin: Electron spin-echo envelope modulation by d2o
    • Bartucci, R., Guzzi, R., Sportelli, L., & Marsh, D. Intramembrane Water Associated with TOAC Spin-Labeled Alamethicin: Electron Spin-Echo Envelope Modulation by D2O. Biophysical Journal 96, 997-1007, doi: 10.1016/j.bpj.2008.10.024 (2009
    • (2009) Biophysical Journal , vol.96 , pp. 997-1007
    • Bartucci, R.1    Guzzi, R.2    Sportelli, L.3    Marsh, D.4
  • 63
    • 33646446451 scopus 로고    scopus 로고
    • Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains
    • Kucerka, N., Tristram-Nagle, S., & Nagle, J. Structure of fully hydrated fluid phase lipid bilayers with monounsaturated chains. Journal of Membrane Biology 208, 193-202, doi: 10.1007/s00232-005-7006-8 (2005
    • (2005) Journal of Membrane Biology , vol.208 , pp. 193-202
    • Kucerka, N.1    Tristram-Nagle, S.2    Nagle, J.3
  • 64
    • 0037380858 scopus 로고    scopus 로고
    • A 2d-eldor study of the liquid ordered phase in multilamellar vesicle membranes
    • Costa, A., Shimoyama, Y., & Freed, J. A 2D-ELDOR study of the liquid ordered phase in multilamellar vesicle membranes. Biophysical Journal 84, 2619-2633, doi: 10.1016/S0006-3495(03)75067-X (2003
    • (2003) Biophysical Journal , vol.84 , pp. 2619-2633
    • Costa, A.1    Shimoyama, Y.2    Freed, J.3
  • 65
    • 84920668399 scopus 로고    scopus 로고
    • The influenza hemagglutinin fusion domain is an amphipathic helical hairpin that functions by inducing membrane curvature
    • Smrt, S., Draney, A., & Lorieau, J. The Influenza Hemagglutinin Fusion Domain Is an Amphipathic Helical Hairpin That Functions by Inducing Membrane Curvature. Journal of Biological Chemistry 290, 228-238, doi: 10.1074/jbc.M114.611657 (2015
    • (2015) Journal of Biological Chemistry , vol.290 , pp. 228-238
    • Smrt, S.1    Draney, A.2    Lorieau, J.3
  • 66
    • 84930011701 scopus 로고    scopus 로고
    • The atomic structure of the HIV-1 gp41 transmembrane domain and its connection to the immunogenic membrane-proximal external region
    • Apellaniz, B., et al. The Atomic Structure of the HIV-1 gp41 Transmembrane Domain and Its Connection to the Immunogenic Membrane-proximal External Region. Journal of Biological Chemistry 290, 12999-13015, doi: 10.1074/jbc.M115.644351 (2015
    • (2015) Journal of Biological Chemistry , vol.290 , pp. 12999-13015
    • Apellaniz, B.1
  • 67
    • 84906328200 scopus 로고    scopus 로고
    • Order and disorder control the functional rearrangement of influenza hemagglutinin
    • Lin, X., et al. Order and disorder control the functional rearrangement of influenza hemagglutinin. Proceedings of the National Academy of Sciences of the United States of America 111, 12049-12054, doi: 10.1073/pnas.1412849111 (2014
    • (2014) Proceedings of the National Academy of Sciences of the United States of America , vol.111 , pp. 12049-12054
    • Lin, X.1
  • 68
    • 84941010285 scopus 로고    scopus 로고
    • Viral fusion protein transmembrane domain adopts beta-strand structure to facilitate membrane topological changes for virus-cell fusion
    • Yao, H., Lee, M., Waring, A., Wong, G., & Hong, M. Viral fusion protein transmembrane domain adopts beta-strand structure to facilitate membrane topological changes for virus-cell fusion. Proceedings of the National Academy of Sciences of the United States of America 112, 10926-10931, doi: 10.1073/pnas.1501430112 (2015
    • (2015) Proceedings of the National Academy of Sciences of the United States of America , vol.112 , pp. 10926-10931
    • Yao, H.1    Lee, M.2    Waring, A.3    Wong, G.4    Hong, M.5
  • 69
    • 84930226254 scopus 로고    scopus 로고
    • Real-time intermembrane force measurements and imaging of lipid domain morphology during hemifusion
    • Lee, D., et al. Real-time intermembrane force measurements and imaging of lipid domain morphology during hemifusion. Nature Communications 6, doi: 10.1038/ncomms8238 (2015
    • (2015) Nature Communications , vol.6
    • Lee, D.1
  • 70
    • 84929307298 scopus 로고    scopus 로고
    • HIV gp41-mediated membrane fusion occurs at edges of cholesterol-rich lipid domains
    • Yang, S., Kiessling, V., Simmons, J., White, J., & Tamm, L. HIV gp41-mediated membrane fusion occurs at edges of cholesterol-rich lipid domains. Nature Chemical Biology 11, 424, doi: 10.1038/NCHEMBIO.1800 (2015
    • (2015) Nature Chemical Biology , vol.11 , pp. 424
    • Yang, S.1    Kiessling, V.2    Simmons, J.3    White, J.4    Tamm, L.5
  • 71
    • 13744249901 scopus 로고    scopus 로고
    • Identification of the membrane-active regions of the severe acute respiratory syndrome coronavirus spike membrane glycoprotein using a 16/18-mer peptide scan: Implications for the viral fusion mechanism
    • Guillen, J., Perez-Berna, A., Moreno, M., & Villalain, J. Identification of the membrane-active regions of the severe acute respiratory syndrome coronavirus spike membrane glycoprotein using a 16/18-mer peptide scan: Implications for the viral fusion mechanism. Journal of Virology 79, 1743-1752, doi: 10.1128/JVI.79.3.1743-1752.2005 (2005
    • (2005) Journal of Virology , vol.79 , pp. 1743-1752
    • Guillen, J.1    Perez-Berna, A.2    Moreno, M.3    Villalain, J.4
  • 72
    • 38049129569 scopus 로고    scopus 로고
    • Interaction of a peptide from the pre-transmembrane domain of the severe acute respiratory syndrome coronavirus spike protein with phospholipid membranes
    • Guillen, J., Moreno, M., Perez-Berna, A., Bernabeu, A., & Villalain, J. Interaction of a peptide from the pre-transmembrane domain of the severe acute respiratory syndrome coronavirus spike protein with phospholipid membranes. Journal of Physical Chemistry B 111, 13714-13725, doi: 10.1021/jp073675y (2007
    • (2007) Journal of Physical Chemistry B , vol.111 , pp. 13714-13725
    • Guillen, J.1    Moreno, M.2    Perez-Berna, A.3    Bernabeu, A.4    Villalain, J.5
  • 73
    • 55749105699 scopus 로고    scopus 로고
    • Membrane insertion of the three main membranotropic sequences from SARS-CoV S2 glycoprotein
    • Guillen, J., Kinnunen, P., & Villalain, J. Membrane insertion of the three main membranotropic sequences from SARS-CoV S2 glycoprotein. Biochimica Et Biophysica Acta-Biomembranes 1778, 2765-2774, doi: 10.1016/j.bbamem.2008.07.021 (2008
    • (2008) Biochimica et Biophysica Acta-Biomembranes , vol.1778 , pp. 2765-2774
    • Guillen, J.1    Kinnunen, P.2    Villalain, J.3
  • 74
    • 67650317982 scopus 로고    scopus 로고
    • Interaction of a peptide corresponding to the loop domain of the S2 SARSCoV virus protein with model membranes
    • Guillen, J., De Almeida, R., Prieto, M., & Villalain, J. Interaction of a peptide corresponding to the loop domain of the S2 SARSCoV virus protein with model membranes. Molecular Membrane Biology 26, 236-248, doi: 10.1080/09687680902926203 (2009
    • (2009) Molecular Membrane Biology , vol.26 , pp. 236-248
    • Guillen, J.1    De Almeida, R.2    Prieto, M.3    Villalain, J.4
  • 75
    • 0034444121 scopus 로고    scopus 로고
    • Viral fusion peptides: A tool set to disrupt and connect biological membranes
    • Tamm, L., & Han, X. Viral fusion peptides: A tool set to disrupt and connect biological membranes. Bioscience Reports 20, 501-518, doi: 10.1023/A: 1010406920417 (2000
    • (2000) Bioscience Reports , vol.20 , pp. 501-518
    • Tamm, L.1    Han, X.2
  • 78
    • 0024378918 scopus 로고
    • Hydration forces between phospholipid bilayers
    • Rand, R., & Parsegian, V. Hydration forces between phospholipid bilayers. Biochimica Et Biophysica Acta 988, 351-376, doi: 10.1016/0304-4157(89)90010-5 (1989
    • (1989) Biochimica et Biophysica Acta , vol.988 , pp. 351-376
    • Rand, R.1    Parsegian, V.2
  • 80
    • 0026576543 scopus 로고
    • Modulation of poly(ethylene glycol)-induced fusion by membrane hydration: Importance of interbilayer separation
    • Burgess, S., Mcintosh, T., & Lentz, B. Modulation of poly(ethylene glycol)-induced fusion by membrane hydration: importance of interbilayer separation. Biochemistry 31, 2653-2661, doi: 10.1021/bi00125a004 (1992
    • (1992) Biochemistry , vol.31 , pp. 2653-2661
    • Burgess, S.1    Mcintosh, T.2    Lentz, B.3
  • 81
    • 0000295299 scopus 로고
    • Thermodynamic and structural properties of phosphatidylserine bilayer membranes in the presence of lithium ions and protons
    • Cevc, G., Seddon, J., & Marsh, D. Thermodynamic and structural properties of phosphatidylserine bilayer membranes in the presence of lithium ions and protons. Biochimica Et Biophysica Acta 814, 141-150, doi: 10.1016/0005-2736(85)90429-8 (1985
    • (1985) Biochimica et Biophysica Acta , vol.814 , pp. 141-150
    • Cevc, G.1    Seddon, J.2    Marsh, D.3
  • 82
    • 0020482250 scopus 로고
    • A mechanism of divalent ion-induced phosphatidylserine membrane fusion
    • Ohki, S. A mechanism of divalent ion-induced phosphatidylserine membrane fusion. Biochimica Et Biophysica Acta 689, 1-11, doi: 10.1016/0005-2736(82)90182-1 (1982
    • (1982) Biochimica et Biophysica Acta , vol.689 , pp. 1-11
    • Ohki, S.1
  • 83
    • 0002635843 scopus 로고
    • Fluorescence techniques for probing water penetration into lipid bilayers
    • Stubbs, C. D., Ho, C., & Slater, S. J. Fluorescence techniques for probing water penetration into lipid bilayers. Journal of Fluorescence 5, 19-28, doi: 10.1007/bf00718779 (1995
    • (1995) Journal of Fluorescence , vol.5 , pp. 19-28
    • Stubbs, C.D.1    Ho, C.2    Slater, S.J.3
  • 84
    • 0032474434 scopus 로고    scopus 로고
    • Location of diphenylhexatriene (DPH) and its derivatives within membranes: Comparison of different fluorescence quenching analyses of membrane depth
    • Kaiser, R., & London, E. Location of diphenylhexatriene (DPH) and its derivatives within membranes: Comparison of different fluorescence quenching analyses of membrane depth. Biochemistry 37, 8180-8190, doi: 10.1021/bi980064a (1998
    • (1998) Biochemistry , vol.37 , pp. 8180-8190
    • Kaiser, R.1    London, E.2
  • 85
    • 79960821626 scopus 로고    scopus 로고
    • Recent developments in molecular dynamics simulations of fluorescent membrane probes
    • Loura, L., & Ramalho, J. Recent Developments in Molecular Dynamics Simulations of Fluorescent Membrane Probes. Molecules 16, 5437-5452, doi: 10.3390/molecules16075437 (2011
    • (2011) Molecules , vol.16 , pp. 5437-5452
    • Loura, L.1    Ramalho, J.2
  • 86
    • 0040093935 scopus 로고    scopus 로고
    • The origin of the diphenylhexatriene short lifetime component in membranes and solvents
    • Konopasek, I., et al. The origin of the diphenylhexatriene short lifetime component in membranes and solvents. Chemical Physics Letters 293, 429-435, doi: 10.1016/S0009-2614(98)00825-2 (1998
    • (1998) Chemical Physics Letters , vol.293 , pp. 429-435
    • Konopasek, I.1
  • 87
    • 18744429928 scopus 로고    scopus 로고
    • Short-lived fluorescence component of DPH reports on lipid-water interface of biological membranes
    • Konopasek, I., Vecer, J., Strzsalka, K., & Amler, E. Short-lived fluorescence component of DPH reports on lipid-water interface of biological membranes. Chemistry and Physics of Lipids 130, 135-144, doi: 10.1016/j.chemphyslip.2004.02.005 (2004
    • (2004) Chemistry and Physics of Lipids , vol.130 , pp. 135-144
    • Konopasek, I.1    Vecer, J.2    Strzsalka, K.3    Amler, E.4
  • 89
    • 67749097800 scopus 로고    scopus 로고
    • Induction of negative curvature as a mechanism of cell toxicity by amyloidogenic peptides: The case of islet amyloid polypeptide
    • Smith, P., Brender, J., & Ramamoorthy, A. Induction of Negative Curvature as a Mechanism of Cell Toxicity by Amyloidogenic Peptides: The Case of Islet Amyloid Polypeptide. Journal of the American Chemical Society 131, 4470-4478, doi: 10.1021/ja809002a (2009
    • (2009) Journal of the American Chemical Society , vol.131 , pp. 4470-4478
    • Smith, P.1    Brender, J.2    Ramamoorthy, A.3
  • 90
    • 71649106004 scopus 로고    scopus 로고
    • Induction of non-lamellar lipid phases by antimicrobial peptides: A potential link to mode of action
    • Haney, E., Nathoo, S., Vogel, H., & Prenner, E. Induction of non-lamellar lipid phases by antimicrobial peptides: a potential link to mode of action. Chemistry and Physics of Lipids 163, 82-93, doi: 10.1016/j.chemphyslip.2009.09.002 (2010
    • (2010) Chemistry and Physics of Lipids , vol.163 , pp. 82-93
    • Haney, E.1    Nathoo, S.2    Vogel, H.3    Prenner, E.4
  • 92
    • 84889567227 scopus 로고    scopus 로고
    • Wild-type and mutant hemagglutinin fusion peptides alter bilayer structure as well as kinetics and activation thermodynamics of stalk and pore formation differently: Mechanistic implications
    • Chakraborty, H., Tarafdar, P., Klapper, D., & Lentz, B. Wild-Type and Mutant Hemagglutinin Fusion Peptides Alter Bilayer Structure as Well as Kinetics and Activation Thermodynamics of Stalk and Pore Formation Differently: Mechanistic Implications. Biophysical Journal 105, 2495-2506, doi: 10.1016/j.bpj.2013.10.010 (2013
    • (2013) Biophysical Journal , vol.105 , pp. 2495-2506
    • Chakraborty, H.1    Tarafdar, P.2    Klapper, D.3    Lentz, B.4
  • 93
    • 84894157764 scopus 로고    scopus 로고
    • Conformation and lipid interaction of the fusion peptide of the paramyxovirus piv5 in anionic and negative-curvature membranes from solid-state nmr
    • Yao, H., & Hong, M. Conformation and Lipid Interaction of the Fusion Peptide of the Paramyxovirus PIV5 in Anionic and Negative-Curvature Membranes from Solid-State NMR. Journal of the American Chemical Society 136, 2611-2624, doi: 10.1021/ja4121956 (2014
    • (2014) Journal of the American Chemical Society , vol.136 , pp. 2611-2624
    • Yao, H.1    Hong, M.2
  • 94
    • 84915758532 scopus 로고    scopus 로고
    • NMR structures and localization of the potential fusion peptides and the pre-transmembrane region of SARS-CoV: Implications in membrane fusion
    • Mahajan, M., & Bhattacharjya, S. NMR structures and localization of the potential fusion peptides and the pre-transmembrane region of SARS-CoV: Implications in membrane fusion. Biochimica Et Biophysica Acta-Biomembranes 1848, 721-730, doi: 10.1016/j.bbamem.2014.11.025 (2015
    • (2015) Biochimica et Biophysica Acta-Biomembranes , vol.1848 , pp. 721-730
    • Mahajan, M.1    Bhattacharjya, S.2
  • 95
    • 84924388647 scopus 로고    scopus 로고
    • Tryptophan-dependent membrane interaction and heteromerization with the internal fusion peptide by the membrane proximal external region of sars-cov spike protein
    • Liao, Y., Zhang, S., Neo, T., & Tam, J. Tryptophan-Dependent Membrane Interaction and Heteromerization with the Internal Fusion Peptide by the Membrane Proximal External Region of SARS-CoV Spike Protein. Biochemistry 54, 1819-1830, doi: 10.1021/bi501352u (2015
    • (2015) Biochemistry , vol.54 , pp. 1819-1830
    • Liao, Y.1    Zhang, S.2    Neo, T.3    Tam, J.4
  • 96
    • 0038290760 scopus 로고    scopus 로고
    • Protein-lipid interplay in fusion and fission of biological membranes
    • Chernomordik, L., & Kozlov, M. Protein-lipid interplay in fusion and fission of biological membranes. Annual Review of Biochemistry 72, 175-207, doi: 10.1146/annurev.biochem.72.121801.161504 (2003
    • (2003) Annual Review of Biochemistry , vol.72 , pp. 175-207
    • Chernomordik, L.1    Kozlov, M.2
  • 97
    • 33749125215 scopus 로고    scopus 로고
    • Biophysical properties of lipids and dynamic membranes
    • Janmey, P., & Kinnunen, P. Biophysical properties of lipids and dynamic membranes. Trends in Cell Biology 16, 538-546, doi: 10.1016/j.tcb.2006.08.009 (2006
    • (2006) Trends in Cell Biology , vol.16 , pp. 538-546
    • Janmey, P.1    Kinnunen, P.2
  • 98
    • 0020395778 scopus 로고
    • Synthesis of the antibacterial peptide cecropin-A(1-33
    • Merrifield, R., Vizioli, L., & Boman, H. Synthesis of the antibacterial peptide cecropin-A(1-33). Biochemistry 21, 5020-5031, doi: 10.1021/bi00263a028 (1982
    • (1982) Biochemistry , vol.21 , pp. 5020-5031
    • Merrifield, R.1    Vizioli, L.2    Boman, H.3
  • 99
    • 84926465975 scopus 로고    scopus 로고
    • N-terminal microdomain peptide from human dihydroorotate dehydrogenase: Structure and model membrane interactions
    • Vicente, E., et al. N-Terminal Microdomain Peptide from Human Dihydroorotate Dehydrogenase: Structure and Model Membrane Interactions. Protein and Peptide Letters 22, 119-129 (2015
    • (2015) Protein and Peptide Letters , vol.22 , pp. 119-129
    • Vicente, E.1
  • 101
    • 0031880099 scopus 로고    scopus 로고
    • Polarity profiles in oriented and dispersed phosphatidylcholine bilayers are different -an electron spin resonance study
    • Ge, M., & Freed, J. H. Polarity Profiles in Oriented and Dispersed Phosphatidylcholine Bilayers Are Different -An Electron Spin Resonance Study. Biophysical Journal 74, 910-917 (1998
    • (1998) Biophysical Journal , vol.74 , pp. 910-917
    • Ge, M.1    Freed, J.H.2
  • 102
    • 0002214132 scopus 로고
    • Elimination of unwanted echoes and reduction of dead time in three-pulse electron spin-echo spectroscopy
    • Fauth, J., Schweiger, A., Braunschweiler, L., Forrer, J., & Ernst, R. Elimination of unwanted echoes and reduction of dead time in three-pulse electron spin-echo spectroscopy. Journal of Magnetic Resonance 66, 74-85, doi: 10.1016/0022-2364(86)90105-8 (1986
    • (1986) Journal of Magnetic Resonance , vol.66 , pp. 74-85
    • Fauth, J.1    Schweiger, A.2    Braunschweiler, L.3    Forrer, J.4    Ernst, R.5


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