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Volumn 99, Issue 6, 2010, Pages 1773-1782

Lipid Polymorphism Induced by Surfactant Peptide SP-B1.25

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EID: 77957376252     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2010.06.076     Document Type: Article
Times cited : (18)

References (57)
  • 1
    • 0031740674 scopus 로고    scopus 로고
    • Pulmonary surfactant: Functions and molecular composition
    • Goerke, J. 1998. Pulmonary surfactant: functions and molecular composition. Biochim. Biophys. Acta. 1408:79-89.
    • (1998) Biochim. Biophys. Acta. , vol.1408 , pp. 79-89
    • Goerke, J.1
  • 2
    • 0037180829 scopus 로고    scopus 로고
    • Hydrophobic surfactant proteins in lung function and disease
    • Whitsett, J. A., and T. E. Weaver. 2002. Hydrophobic surfactant proteins in lung function and disease. N. Engl. J. Med. 347:2141-2148.
    • (2002) N. Engl. J. Med. , vol.347 , pp. 2141-2148
    • Whitsett, J.A.1    Weaver, T.E.2
  • 3
    • 0036667738 scopus 로고    scopus 로고
    • Pulmonary surfactant: Phase behavior and function
    • Piknova, B., V. Schram, and S. B. Hall. 2002. Pulmonary surfactant: phase behavior and function. Curr. Opin. Struct. Biol. 12:487-494.
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 487-494
    • Piknova, B.1    Schram, V.2    Hall, S.B.3
  • 4
    • 0023575418 scopus 로고
    • Metabolism and turnover of lung surfactant
    • Wright, J. R., and J. A. Clements. 1987. Metabolism and turnover of lung surfactant. Am. Rev. Respir. Dis. 136:426-444.
    • (1987) Am. Rev. Respir. Dis. , vol.136 , pp. 426-444
    • Wright, J.R.1    Clements, J.A.2
  • 6
    • 0035008878 scopus 로고    scopus 로고
    • A comparison of the molecular species compositions of mammalian lung surfactant phospholipids
    • Postle, A. D., E. L. Heeley, and D. C. Wilton. 2001. A comparison of the molecular species compositions of mammalian lung surfactant phospholipids. Comp. Biochem. Physiol. A Mol. Integr. Physiol. 129:65-73.
    • (2001) Comp. Biochem. Physiol. A Mol. Integr. Physiol. , vol.129 , pp. 65-73
    • Postle, A.D.1    Heeley, E.L.2    Wilton, D.C.3
  • 7
    • 0029950675 scopus 로고    scopus 로고
    • Role of lipid polymorphism in pulmonary surfactant
    • Perkins, W. R., R. B. Dause, A. S. Janoff. 1996. Role of lipid polymorphism in pulmonary surfactant. Science. 273:330-332.
    • (1996) Science. , vol.273 , pp. 330-332
    • Perkins, W.R.1    Dause, R.B.2    Janoff, A.S.3
  • 8
    • 0033635798 scopus 로고    scopus 로고
    • The role of surfactant proteins in dppc enrichment of surface films
    • Veldhuizen, E. J. A., J. J. Batenburg, H. P. Haagsman. 2000. The role of surfactant proteins in DPPC enrichment of surface films. Biophys. J. 79:3164-3171.
    • (2000) Biophys. J. , vol.79 , pp. 3164-3171
    • Veldhuizen, E.J.A.1    Batenburg, J.J.2    Haagsman, H.P.3
  • 9
    • 52049111368 scopus 로고    scopus 로고
    • Current perspectives in pulmonary surfactant-inhibition, enhancement and evaluation
    • Zuo, Y. Y., R. A. W. Veldhuizen, F. Possmayer. 2008. Current perspectives in pulmonary surfactant-inhibition, enhancement and evaluation. Biochim. Biophys. Acta. 1778:1947-1977.
    • (2008) Biochim. Biophys. Acta. , vol.1778 , pp. 1947-1977
    • Zuo, Y.Y.1    Veldhuizen, R.A.W.2    Possmayer, F.3
  • 10
    • 50949083025 scopus 로고    scopus 로고
    • Structure of pulmonary surfactant membranes and films: The role of proteins and lipid-protein interactions
    • Pérez-Gil, J. 2008. Structure of pulmonary surfactant membranes and films: the role of proteins and lipid-protein interactions. Biochim. Biophys. Acta. 1778:1676-1695.
    • (2008) Biochim. Biophys. Acta. , vol.1778 , pp. 1676-1695
    • Pérez-Gil, J.1
  • 11
    • 0028875787 scopus 로고
    • Human surfactant protein b: Structure, function, regulation, and genetic disease
    • Whitsett, J. A., L. M. Nogee, A. D. Horowitz. 1995. Human surfactant protein B: structure, function, regulation, and genetic disease.Physiol. Rev. 75:749-757.
    • (1995) Physiol. Rev. , vol.75 , pp. 749-757
    • Whitsett, J.A.1    Nogee, L.M.2    Horowitz, A.D.3
  • 12
    • 0029096591 scopus 로고
    • Targeted disruption of the surfactant protein b gene disrupts surfactant homeostasis, causing respiratory failure in newborn mice
    • Clark, J. C., S. E. Wert, J. A. Whitsett. 1995. Targeted disruption of the surfactant protein B gene disrupts surfactant homeostasis, causing respiratory failure in newborn mice. Proc. Natl. Acad. Sci. USA. 92:7794-7798.
    • (1995) Proc. Natl. Acad. Sci. USA. , vol.92 , pp. 7794-7798
    • Clark, J.C.1    Wert, S.E.2    Whitsett, J.A.3
  • 13
    • 0242301636 scopus 로고    scopus 로고
    • Surfactant protein profile of pulmonary surfactant in premature infants
    • Ballard, P. L., J. D. Merrill, R. A. Ballard. 2003. Surfactant protein profile of pulmonary surfactant in premature infants. Am. J. Respir. Crit. Care Med. 168:1123-1128.
    • (2003) Am. J. Respir. Crit. Care Med. , vol.168 , pp. 1123-1128
    • Ballard, P.L.1    Merrill, J.D.2    Ballard, R.A.3
  • 14
    • 0030942158 scopus 로고    scopus 로고
    • Molecular structures and interactions of pulmonary surfactant components
    • Johansson, J., and T. Curstedt. 1997. Molecular structures and interactions of pulmonary surfactant components. Eur. J. Biochem. 244: 675-693.
    • (1997) Eur. J. Biochem. , vol.244 , pp. 675-693
    • Johansson, J.1    Curstedt, T.2
  • 15
    • 0026059522 scopus 로고
    • Immunogenicity of surfactant. Ii. Porcine and bovine surfactants
    • Strayer, D. S., M. Hallman, and T. A. Merritt. 1991. Immunogenicity of surfactant. II. Porcine and bovine surfactants. Clin. Exp. Immunol. 83:41-46.
    • (1991) Clin. Exp. Immunol. , vol.83 , pp. 41-46
    • Strayer, D.S.1    Hallman, M.2    Merritt, T.A.3
  • 16
    • 0025727587 scopus 로고
    • The use of synthetic peptides in the formation of biophysically and biologically active pulmonary surfactants
    • Revak, S. D., T. A. Merritt, C. G. Cochrane. 1991. The use of synthetic peptides in the formation of biophysically and biologically active pulmonary surfactants. Pediatr. Res. 29:460-465.
    • (1991) Pediatr. Res. , vol.29 , pp. 460-465
    • Revak, S.D.1    Merritt, T.A.2    Cochrane, C.G.3
  • 18
    • 12344310107 scopus 로고    scopus 로고
    • Mapping and analysis of the lytic and fusogenic domains of surfactant protein b
    • Ryan, M. A., X. Y. Qi, T. E. Weaver. 2005. Mapping and analysis of the lytic and fusogenic domains of surfactant protein B. Biochemistry. 44:861-872.
    • (2005) Biochemistry. , vol.44 , pp. 861-872
    • Ryan, M.A.1    Qi, X.Y.2    Weaver, T.E.3
  • 19
    • 33646147571 scopus 로고    scopus 로고
    • Critical structure-function determinants within the N-terminal region of pulmonary surfactant protein sp-b
    • Serrano, A. G., M. Ryan, .,J. Perez-Gil. 2006. Critical structure-function determinants within the N-terminal region of pulmonary surfactant protein SP-B. Biophys. J. 90:238-249.
    • (2006) Biophys. J. , vol.90 , pp. 238-249
    • Serrano, A.G.1    Ryan, M.2    Perez-Gil, J.3
  • 20
    • 23244442451 scopus 로고    scopus 로고
    • A multicenter, randomized, controlled trial of lucinactant versus poractant alfa among very premature infants at high risk for respiratory distress syndrome
    • Surfaxin Therapy Against Respiratory Distress Syndrome Collaborative Group
    • Sinha, S. K., T. Lacaze-Masmonteil, R. d'Agostino; Surfaxin Therapy Against Respiratory Distress Syndrome Collaborative Group. 2005. A multicenter, randomized, controlled trial of lucinactant versus poractant alfa among very premature infants at high risk for respiratory distress syndrome. Pediatrics. 115:1030-1038.
    • (2005) Pediatrics. , vol.115 , pp. 1030-1038
    • Sinha, S.K.1    Lacaze-Masmonteil, R.T.2    D'Agostino3
  • 21
    • 12344251969 scopus 로고    scopus 로고
    • Simple, helical peptoid analogs of lung surfactant protein b
    • Seurynck, S. L., J. A. Patch, and A. E. Barron. 2005. Simple, helical peptoid analogs of lung surfactant protein B. Chem. Biol. 12:77-88.
    • (2005) Chem. Biol. , vol.12 , pp. 77-88
    • Seurynck, S.L.1    Patch, J.A.2    Barron, A.E.3
  • 22
    • 0034477405 scopus 로고    scopus 로고
    • Comparison of functional efficacy of surfactant protein B analogues in lavaged rats
    • Gupta, M., J. M. Hernández-Juviel, F. J. Walther. 2000. Comparison of functional efficacy of surfactant protein B analogues in lavaged rats. Eur. Respir. J. 16:1129-1133.
    • (2000) Eur. Respir. J. , vol.16 , pp. 1129-1133
    • Gupta, M.1    Hernández-Juviel, J.M.2    Walther, F.J.3
  • 23
    • 28944446005 scopus 로고    scopus 로고
    • The role of charged amphipathic helices in the structure and function of surfactant protein b
    • Waring, A. J., F. J. Walther, J. A. Zasadzinski. 2005. The role of charged amphipathic helices in the structure and function of surfactant protein B. J. Pept. Res. 66:364-374.
    • (2005) J. Pept. Res. , vol.66 , pp. 364-374
    • Waring, A.J.1    Walther, F.J.2    Zasadzinski, J.A.3
  • 24
    • 54049146845 scopus 로고    scopus 로고
    • Interactions of the c-terminus of lung surfactant protein b with lipid bilayers are modulated by acyl chain saturation
    • Antharam, V. C., R. S. Farver, J. R. Long. 2008. Interactions of the C-terminus of lung surfactant protein B with lipid bilayers are modulated by acyl chain saturation. Biochim. Biophys. Acta. 1778:2544-2554.
    • (2008) Biochim. Biophys. Acta. , vol.1778 , pp. 2544-2554
    • Antharam, V.C.1    Farver, R.S.2    Long, J.R.3
  • 26
    • 0030018339 scopus 로고    scopus 로고
    • Conformation and molecular topography of the n-terminal segment of surfactant protein B in structure-promoting environments
    • Gordon, L. M., S. Horvath, A. J. Waring. 1996. Conformation and molecular topography of the N-terminal segment of surfactant protein B in structure-promoting environments. Protein Sci. 5:1662-1675.
    • (1996) Protein Sci. , vol.5 , pp. 1662-1675
    • Gordon, L.M.1    Horvath, S.2    Waring, A.J.3
  • 29
    • 33745747109 scopus 로고    scopus 로고
    • Solid-state nmr investigation of the membrane-disrupting mechanism of antimicrobial peptides msi-78 and msi-594 derived from magainin 2 and melittin
    • Ramamoorthy, A., S. Thennarasu, L. Maloy. 2006. Solid-state NMR investigation of the membrane-disrupting mechanism of antimicrobial peptides MSI-78 and MSI-594 derived from magainin 2 and melittin. Biophys. J. 91:206-216.
    • (2006) Biophys. J. , vol.91 , pp. 206-216
    • Ramamoorthy, A.1    Thennarasu, S.2    Maloy, L.3
  • 30
    • 0035743686 scopus 로고    scopus 로고
    • Simultaneous determination of orientational and order parameter distributions from nmr spectra of partially oriented model membranes
    • Sternin, E., H. Schafer, K. Gawrisch. 2001. Simultaneous determination of orientational and order parameter distributions from NMR spectra of partially oriented model membranes. J. Magn. Reson. 149:110-113.
    • (2001) J. Magn. Reson. , vol.149 , pp. 110-113
    • Sternin, E.1    Schafer, H.2    Gawrisch, K.3
  • 32
    • 0027190754 scopus 로고
    • Evaluation of secondary structure of proteins from uv circular dichroism spectra using an unsupervised learning neural network
    • Andrade, M. A., P. Chacón, F. Morán. 1993. Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng. 6: 383-390.
    • (1993) Protein Eng. , vol.6 , pp. 383-390
    • Andrade, M.A.1    Chacón, P.2    Morán, F.3
  • 34
    • 67349153137 scopus 로고    scopus 로고
    • Perturbation of dppc/popg bilayers by the n-terminal helix of lung surfactant protein sp-b: A 2h nmr study
    • Russell-Schulz, B., V. Booth, and M. R. Morrow. 2009. Perturbation of DPPC/POPG bilayers by the N-terminal helix of lung surfactant protein SP-B: a 2H NMR study. Eur. Biophys. J. 38:613-624.
    • (2009) Eur. Biophys. J. , vol.38 , pp. 613-624
    • Russell-Schulz, B.1    Booth, V.2    Morrow, M.R.3
  • 35
    • 0037162409 scopus 로고    scopus 로고
    • Effect of variations in the structure of a polyleucine-based α-helical transmembrane peptide on its interaction with phosphatidylcholine bilayers
    • Liu, F., R. N. A. H. Lewis, R. N. McElhaney. 2002. Effect of variations in the structure of a polyleucine-based α-helical transmembrane peptide on its interaction with phosphatidylcholine bilayers. Biochemistry. 41:9197-9207.
    • (2002) Biochemistry. , vol.41 , pp. 9197-9207
    • Liu, F.1    Lewis, R.N.A.H.2    McElhaney, R.N.3
  • 37
    • 0031795752 scopus 로고    scopus 로고
    • Lipid polymorphism and protein-lipid interactions
    • Epand, R. M. 1998. Lipid polymorphism and protein-lipid interactions. Biochim. Biophys. Acta. 1376:353-368.
    • (1998) Biochim. Biophys. Acta. , vol.1376 , pp. 353-368
    • Epand, R.M.1
  • 38
    • 0018797519 scopus 로고
    • Lipid polymorphism and the functional roles of lipids in biological membranes
    • Cullis, P. R., and B. de Kruijff. 1979. Lipid polymorphism and the functional roles of lipids in biological membranes. Biochim. Biophys. Acta. 559:399-420.
    • (1979) Biochim. Biophys. Acta. , vol.559 , pp. 399-420
    • Cullis, P.R.1    De Kruijff, B.2
  • 39
    • 3142543171 scopus 로고    scopus 로고
    • Perturbation of the hydrophobic core of lipid bilayers by the human antimicrobial peptide LL-37
    • Henzler-Wildman, K. A., G. V. Martinez, A. Ramamoorthy. 2004. Perturbation of the hydrophobic core of lipid bilayers by the human antimicrobial peptide LL-37. Biochemistry. 43:8459-8469.
    • (2004) Biochemistry. , vol.43 , pp. 8459-8469
    • Henzler-Wildman, K.A.1    Martinez, G.V.2    Ramamoorthy, A.3
  • 40
    • 7744229375 scopus 로고    scopus 로고
    • Structure and orientation of pardaxin determined by nmr experiments in model membranes
    • Porcelli, F., B. Buck, G. Veglia. 2004. Structure and orientation of pardaxin determined by NMR experiments in model membranes. J. Biol. Chem. 279:45815-45823.
    • (2004) J. Biol. Chem. , vol.279 , pp. 45815-45823
    • Porcelli, F.1    Buck, B.2    Veglia, G.3
  • 41
    • 0025770286 scopus 로고
    • Surfactant protein b: Lipid interactions of synthetic peptides representing the amino-terminal amphipathic domain
    • Bruni, R., H. W. Taeusch, and A. J. Waring. 1991. Surfactant protein B: lipid interactions of synthetic peptides representing the amino-terminal amphipathic domain. Proc. Natl. Acad. Sci. USA. 88:7451-7455.
    • (1991) Proc. Natl. Acad. Sci. USA. , vol.88 , pp. 7451-7455
    • Bruni, R.1    Taeusch, H.W.2    Waring, A.J.3
  • 42
    • 0027209909 scopus 로고
    • A function of lung surfactant protein SP-B
    • Longo, M. L., A. M. Bisagno, A. J. Waring. 1993. A function of lung surfactant protein SP-B. Science. 261:453-456.
    • (1993) Science. , vol.261 , pp. 453-456
    • Longo, M.L.1    Bisagno, A.M.2    Waring, A.J.3
  • 43
    • 0031215004 scopus 로고    scopus 로고
    • Effects of lung surfactant specific protein sp-b and model sp-b peptide on lipid monolayers at the air-water interface
    • Lee, K. Y. C., M. M. Lipp, A. J. Waring. 1997. Effects of lung surfactant specific protein SP-B and model SP-B peptide on lipid monolayers at the air-water interface. Colloid Surface A. 128:225-242.
    • (1997) Colloid Surface A. , vol.128 , pp. 225-242
    • Lee, K.Y.C.1    Lipp, M.M.2    Waring, A.J.3
  • 44
    • 0028856079 scopus 로고
    • Alveolar lining layer is thin and continuous: Low-temperature scanning electron microscopy of rat lung
    • Bastacky, J., C. Y. C. Lee, J. A. Clements. 1995. Alveolar lining layer is thin and continuous: low-temperature scanning electron microscopy of rat lung. J. Appl. Physiol. 79:1615-1628.
    • (1995) J. Appl. Physiol. , vol.79 , pp. 1615-1628
    • Bastacky, J.1    Lee, C.Y.C.2    Clements, J.A.3
  • 45
    • 77951646756 scopus 로고    scopus 로고
    • Hydrophobic surfactant proteins induce a phosphatidylethanolamine to form cubic phases
    • Chavarha, M., H. Khoojinian, S. B. Hall. 2010. Hydrophobic surfactant proteins induce a phosphatidylethanolamine to form cubic phases. Biophys. J. 98:1549-1557.
    • (2010) Biophys. J. , vol.98 , pp. 1549-1557
    • Chavarha, M.1    Khoojinian, H.2    Hall, S.B.3
  • 46
    • 32044441404 scopus 로고    scopus 로고
    • Structures of pulmonary surfactant films adsorbed to an air-liquid interface in vitro
    • Bachofen, H., U. Gerber, S. Schürch. 2005. Structures of pulmonary surfactant films adsorbed to an air-liquid interface in vitro. Bio- chim. Biophys. Acta. 1720:59-72.
    • (2005) Bio- Chim. Biophys. Acta. , vol.1720 , pp. 59-72
    • Bachofen, H.1    Gerber, U.2    Schürch, S.3
  • 47
    • 0037077194 scopus 로고    scopus 로고
    • Multilayer formation upon compression of surfactant monolayers depends on protein concentration as well as lipid composition. An atomic force microscopy study
    • Diemel, R. V., M. M. E. Snel, J. J. Batenburg. 2002. Multilayer formation upon compression of surfactant monolayers depends on protein concentration as well as lipid composition. An atomic force microscopy study. J. Biol. Chem. 277:21179-21188.
    • (2002) J. Biol. Chem. , vol.277 , pp. 21179-21188
    • Diemel, R.V.1    Snel, M.M.E.2    Batenburg, J.J.3
  • 48
    • 33846371945 scopus 로고    scopus 로고
    • Multilayers at the surface of solutions of exogenous lung surfactant: Direct observation by neutron reflection
    • Follows, D., F. Tiberg, M. Larsson. 2007. Multilayers at the surface of solutions of exogenous lung surfactant: direct observation by neutron reflection. Biochim. Biophys. Acta. 1768:228-235.
    • (2007) Biochim. Biophys. Acta. , vol.1768 , pp. 228-235
    • Follows, D.1    Tiberg, F.2    Larsson, M.3
  • 49
    • 67650354619 scopus 로고    scopus 로고
    • The effect of a c-terminal peptide of surfactant protein B (SP-B) on oriented lipid bilayers, characterized by solid-state 2H- and 31P-NMR
    • Yang, T. C., M. McDonald, V. Booth. 2009. The effect of a C-terminal peptide of surfactant protein B (SP-B) on oriented lipid bilayers, characterized by solid-state 2H- and 31P-NMR. Biophys. J. 96:3762-3771.
    • (2009) Biophys. J. , vol.96 , pp. 3762-3771
    • Yang, T.C.1    McDonald, M.2    Booth, V.3
  • 50
    • 3142710053 scopus 로고    scopus 로고
    • Perturbation of dppc bilayers by high concentrations of pulmonary surfactant protein SP-B
    • Morrow, M. R., J. Stewart, K. M. Keough. 2004. Perturbation of DPPC bilayers by high concentrations of pulmonary surfactant protein SP-B. Eur. Biophys. J. 33:285-290.
    • (2004) Eur. Biophys. J. , vol.33 , pp. 285-290
    • Morrow, M.R.1    Stewart, J.2    Keough, K.M.3
  • 51
    • 0030894592 scopus 로고    scopus 로고
    • Pulmonary surfactant protein sp-b interacts similarly with dipalmitoylphosphatidylglycerol and dipalmitoylphosphatidylcholine in phosphatidylcholine/phosphati-dylglycerol mixtures
    • Dico, A. S., J. Hancock, K. M. Keough. 1997. Pulmonary surfactant protein SP-B interacts similarly with dipalmitoylphosphatidylglycerol and dipalmitoylphosphatidylcholine in phosphatidylcholine/phosphati- dylglycerol mixtures. Biochemistry. 36:4172-4177.
    • (1997) Biochemistry. , vol.36 , pp. 4172-4177
    • Dico, A.S.1    Hancock, J.2    Keough, K.M.3
  • 52
    • 77952526093 scopus 로고    scopus 로고
    • Critical structural and functional roles for the n-terminal insertion sequence in surfactant protein b analogs
    • Walther, F. J., A. J. Waring, .., R. H. Notter. 2010. Critical structural and functional roles for the N-terminal insertion sequence in surfactant protein B analogs. PLoS ONE. 5:e8672.
    • (2010) PLoS ONE. , vol.5
    • Walther, F.J.1    Waring, A.J.2    Notter, R.H.3
  • 54
    • 21244504685 scopus 로고    scopus 로고
    • Molecular dynamics study of the lung surfactant peptide SP-B1-25 with dppc monolayers: Insights into interactions and peptide position and orientation
    • Kandasamy, S. K., and R. G. Larson. 2005. Molecular dynamics study of the lung surfactant peptide SP-B1-25 with DPPC monolayers: insights into interactions and peptide position and orientation. Biophys. J. 88:1577-1592.
    • (2005) Biophys. J. , vol.88 , pp. 1577-1592
    • Kandasamy, S.K.1    Larson, R.G.2
  • 55
    • 0025340137 scopus 로고
    • Coupled changes between lipid order and polypeptide conformation at the membrane surface. A 2H NMR and Raman study of polylysine-phosphatidic acid systems
    • Laroche, G., E. J. Dufourc, J. Dufourcq. 1990. Coupled changes between lipid order and polypeptide conformation at the membrane surface. A 2H NMR and Raman study of polylysine-phosphatidic acid systems. Biochemistry. 29:6460-6465.
    • (1990) Biochemistry. , vol.29 , pp. 6460-6465
    • Laroche, G.1    Dufourc, E.J.2    Dufourcq, J.3
  • 56
    • 0035831154 scopus 로고    scopus 로고
    • Differential scanning calorimetry and (2)H nuclear magnetic resonance and fourier transform infrared spectroscopy studies of the effects of transmembrane a-helical peptides on the organization of phosphatidylcholine bilayers
    • Paré, C., M. Lafleur, R. N. McElhaney. 2001. Differential scanning calorimetry and (2)H nuclear magnetic resonance and Fourier transform infrared spectroscopy studies of the effects of transmembrane a-helical peptides on the organization of phosphatidylcholine bilayers. Biochim. Biophys. Acta. 1511:60-73.
    • (2001) Biochim. Biophys. Acta. , vol.1511 , pp. 60-73
    • Paré, C.1    Lafleur, M.2    McElhaney, R.N.3
  • 57
    • 0035853473 scopus 로고    scopus 로고
    • Pulmonary surfactant protein SP-B is significantly more immunoreactive in anionic than in zwitterionic bilayers
    • Oviedo, J. M., C. Casals, and J. Pérez-Gil. 2001. Pulmonary surfactant protein SP-B is significantly more immunoreactive in anionic than in zwitterionic bilayers. FEBS Lett. 494:236-240.
    • (2001) FEBS Lett. , vol.494 , pp. 236-240
    • Oviedo, J.M.1    Casals, C.2    Pérez-Gil, J.3


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