메뉴 건너뛰기




Volumn 93, Issue 1, 2007, Pages 164-175

Comparison of DPPC and DPPG environments in pulmonary surfactant models

Author keywords

[No Author keywords available]

Indexed keywords

DIPALMITOYLPHOSPHATIDYLCHOLINE; DIPALMITOYLPHOSPHATIDYLGLYCEROL; LUNG SURFACTANT; SURFACTANT PROTEIN A; SURFACTANT PROTEIN B;

EID: 34447291057     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.106.102681     Document Type: Article
Times cited : (20)

References (60)
  • 1
    • 0000455402 scopus 로고
    • New notions on a fundamental principle of respiratory mechanics: The retractile force of the lung, dependent on the surface tension in the alveoli
    • Von Neergaard, K. 1929. New notions on a fundamental principle of respiratory mechanics: the retractile force of the lung, dependent on the surface tension in the alveoli. Z. Gesamte Exp. Med. 66:373-394.
    • (1929) Z. Gesamte Exp. Med , vol.66 , pp. 373-394
    • Von Neergaard, K.1
  • 2
    • 0020960354 scopus 로고
    • Bovine pulmonary surfactant: Chemical composition and physical properties
    • Yu, S. H., N. Smith, P. G. R. Harding, and F. Possmayer. 1983. Bovine pulmonary surfactant: chemical composition and physical properties. Lipids. 18:522-529.
    • (1983) Lipids , vol.18 , pp. 522-529
    • Yu, S.H.1    Smith, N.2    Harding, P.G.R.3    Possmayer, F.4
  • 3
    • 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
  • 5
    • 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
  • 6
    • 0242353825 scopus 로고    scopus 로고
    • Metastability of a supercompressed fluid monolayer
    • Smith, E. C., J. M. Crane, T. G. Laderas, and S. B. Hall. 2003. Metastability of a supercompressed fluid monolayer. Biophys. J. 85:3048-3057.
    • (2003) Biophys. J , vol.85 , pp. 3048-3057
    • Smith, E.C.1    Crane, J.M.2    Laderas, T.G.3    Hall, S.B.4
  • 7
    • 34447289041 scopus 로고    scopus 로고
    • Lung surfactant: Cellular and molecular processing
    • Transformations. S. A. Rooney, editor. R.G. Landes, Georgetown, TX
    • Keough, K. M. W. 1998. Lung surfactant: cellular and molecular processing. In Chapter 1: Surfactant Composition and Extracellular Transformations. S. A. Rooney, editor. R.G. Landes, Georgetown, TX.
    • (1998) Surfactant Composition and Extracellular
    • Keough, K.M.W.1
  • 8
    • 0015401048 scopus 로고
    • Surface active material from dog lung. I. Method of isolation
    • King, R. J., and J. A. Clements. 1972. Surface active material from dog lung. I. Method of isolation. Am. J. Physiol. 223:707-714.
    • (1972) Am. J. Physiol , vol.223 , pp. 707-714
    • King, R.J.1    Clements, J.A.2
  • 9
    • 0015611306 scopus 로고
    • Isolation of apoproteins from canine surface active material
    • King, R. J., D. J. Klass, E. G. Gikas, and J. A. Clements. 1973. Isolation of apoproteins from canine surface active material. Am. J. Physiol. 224:788-795.
    • (1973) Am. J. Physiol , vol.224 , pp. 788-795
    • King, R.J.1    Klass, D.J.2    Gikas, E.G.3    Clements, J.A.4
  • 10
    • 0022376675 scopus 로고
    • Chemical characterization of lung surfactant apoproteins: Amino acid composition, N-terminal sequence and enzymatic digestion
    • Hawgood, S., H. Efrati, J. Schilling, and B. J. Benson. 1985. Chemical characterization of lung surfactant apoproteins: amino acid composition, N-terminal sequence and enzymatic digestion. Biochem. Soc. Trans. 13:1092-1096.
    • (1985) Biochem. Soc. Trans , vol.13 , pp. 1092-1096
    • Hawgood, S.1    Efrati, H.2    Schilling, J.3    Benson, B.J.4
  • 11
    • 0022844505 scopus 로고
    • Mannose-binding proteins isolated from rat liver contain carbohydrate-recognition domains linked to collagenous tails. Complete primary structures and homology with pulmonary surfactant apoprotein
    • Drickamer, K., M. S. Dordal, and L. Reynolds. 1986. Mannose-binding proteins isolated from rat liver contain carbohydrate-recognition domains linked to collagenous tails. Complete primary structures and homology with pulmonary surfactant apoprotein. J. Biol. Chem. 261:6878-6887.
    • (1986) J. Biol. Chem , vol.261 , pp. 6878-6887
    • Drickamer, K.1    Dordal, M.S.2    Reynolds, L.3
  • 12
    • 0030920246 scopus 로고    scopus 로고
    • The structure and function of surfactant protein A
    • McCormack, F. 1997. The structure and function of surfactant protein A. Chest. 111:114S-119S.
    • (1997) Chest , vol.111
    • McCormack, F.1
  • 13
    • 0031740744 scopus 로고    scopus 로고
    • Structure, processing and properties of surfactant protein A
    • McCormack, F. X. 1998. Structure, processing and properties of surfactant protein A. Biochim. Biophys. Acta. 1408:109-131.
    • (1998) Biochim. Biophys. Acta , vol.1408 , pp. 109-131
    • McCormack, F.X.1
  • 14
    • 0023890913 scopus 로고
    • Macromolecular organization of natural and recombinant lung surfactant protein SP 28-36. Structural homology with the complement factor C1q
    • Voss, T., H. Eistetter, K. P. Schäfer, and J. Engel. 1988. Macromolecular organization of natural and recombinant lung surfactant protein SP 28-36. Structural homology with the complement factor C1q. J. Mol. Biol. 201:219-227.
    • (1988) J. Mol. Biol , vol.201 , pp. 219-227
    • Voss, T.1    Eistetter, H.2    Schäfer, K.P.3    Engel, J.4
  • 15
    • 0024571345 scopus 로고
    • Aspects of secondary and quaternary structure of surfactant protein A from canine lung
    • King, R. J., D. Simon, and P. M. Horowitz. 1989. Aspects of secondary and quaternary structure of surfactant protein A from canine lung. Biochim. Biophys. Acta. 1001:294-301.
    • (1989) Biochim. Biophys. Acta , vol.1001 , pp. 294-301
    • King, R.J.1    Simon, D.2    Horowitz, P.M.3
  • 16
    • 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
  • 17
    • 0019811124 scopus 로고
    • Interaction of the lipid and protein components of pulmonary surfactant. Role of phosphatidylglycerol and calcium
    • King, R. J., and M. C. MacBeth. 1981. Interaction of the lipid and protein components of pulmonary surfactant. Role of phosphatidylglycerol and calcium. Biochim. Biophys. Acta. 647:159-168.
    • (1981) Biochim. Biophys. Acta , vol.647 , pp. 159-168
    • King, R.J.1    MacBeth, M.C.2
  • 18
    • 0027987812 scopus 로고
    • Chimeras of surfactant proteins A and D identify the carbohydrate recognition domains as essential for phospholipids interaction
    • Ogasawara, Y., F. X. McCormack, R. J. Mason, and D. R. Voelker. 1994. Chimeras of surfactant proteins A and D identify the carbohydrate recognition domains as essential for phospholipids interaction. J. Biol. Chem. 47:29785-29792.
    • (1994) J. Biol. Chem , vol.47 , pp. 29785-29792
    • Ogasawara, Y.1    McCormack, F.X.2    Mason, R.J.3    Voelker, D.R.4
  • 19
    • 0031663381 scopus 로고    scopus 로고
    • Structural changes of surfactant protein A induced by cations reorient the protein on lipid bilayers
    • Palaniyar, N., R. A. Ridsdale, C. F. Holterman, K. Inchley, F. Possmayer, and G. Harauz. 1998. Structural changes of surfactant protein A induced by cations reorient the protein on lipid bilayers. J. Struct. Biol. 122:297-310.
    • (1998) J. Struct. Biol , vol.122 , pp. 297-310
    • Palaniyar, N.1    Ridsdale, R.A.2    Holterman, C.F.3    Inchley, K.4    Possmayer, F.5    Harauz, G.6
  • 20
    • 0032924918 scopus 로고    scopus 로고
    • Palaniyar, N., R. A. Ridsdale, S. A. Hearn, F. Possmayer, and G. Harauz. 1999. Formation of membrane lattice structures and their specific interactions with surfactant protein A. Am. J. Physiol. 276 Lung Cell. Mol. Physiol. 20:L642-L649.
    • Palaniyar, N., R. A. Ridsdale, S. A. Hearn, F. Possmayer, and G. Harauz. 1999. Formation of membrane lattice structures and their specific interactions with surfactant protein A. Am. J. Physiol. 276 (Lung Cell. Mol. Physiol. 20:L642-L649.
  • 22
    • 0033983738 scopus 로고    scopus 로고
    • The roles of surfactant proteins A and D in innate immunity
    • Lawson, P. R., and K. B. M. Reid. 2000. The roles of surfactant proteins A and D in innate immunity. Immunol. Rev. 173:66-78.
    • (2000) Immunol. Rev , vol.173 , pp. 66-78
    • Lawson, P.R.1    Reid, K.B.M.2
  • 23
    • 11244287371 scopus 로고    scopus 로고
    • Immunoregulatory functions of surfactant proteins
    • Wright, J. R. 2005. Immunoregulatory functions of surfactant proteins. Nature Rev. Immunol. 5:58-68.
    • (2005) Nature Rev. Immunol , vol.5 , pp. 58-68
    • Wright, J.R.1
  • 24
    • 0031795751 scopus 로고    scopus 로고
    • Structure, biologic properties and expression of surfactant protein D (SP-D)
    • Crouch, E. C. 1998. Structure, biologic properties and expression of surfactant protein D (SP-D). Biochim. Biophys. Acta. 1408:278-289.
    • (1998) Biochim. Biophys. Acta , vol.1408 , pp. 278-289
    • Crouch, E.C.1
  • 25
    • 0034581319 scopus 로고    scopus 로고
    • Surfactant protein-D and pulmonary host defense
    • Crouch, E. C. 2000. Surfactant protein-D and pulmonary host defense. Respir. Res. 1:93-108.
    • (2000) Respir. Res , vol.1 , pp. 93-108
    • Crouch, E.C.1
  • 26
    • 0025239383 scopus 로고
    • Hydrophobic surfactant-associated polypeptides: SP-C is a lipopeptide with two palmitoylated cysteine residues, whereas SP-B lacks covalently linked fatty acyl groups
    • Curstedt, T., J. Johansson, P. Persson, A. Eklund, B. Robertson, B. Löwenadler, and H. Jörnvall. 1990. Hydrophobic surfactant-associated polypeptides: SP-C is a lipopeptide with two palmitoylated cysteine residues, whereas SP-B lacks covalently linked fatty acyl groups. Proc. Natl. Acad. Sci. USA. 87:2985-2989.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2985-2989
    • Curstedt, T.1    Johansson, J.2    Persson, P.3    Eklund, A.4    Robertson, B.5    Löwenadler, B.6    Jörnvall, H.7
  • 27
    • 0031796861 scopus 로고    scopus 로고
    • Structure and properties of surfactant protein B
    • Hawgood, S., M. Derrick, and F. Poulain. 1998. Structure and properties of surfactant protein B. Biochim. Biophys. Acta. 1408:150-160.
    • (1998) Biochim. Biophys. Acta , vol.1408 , pp. 150-160
    • Hawgood, S.1    Derrick, M.2    Poulain, F.3
  • 28
    • 0026634092 scopus 로고
    • Effects of surfactant apolipoproteins on liposome structure: Implications for tubular myelin formation
    • Poulain, F. R., L. Allen, M. C. Williams, R. L. Hamilton, and S. Hawgood. 1992. Effects of surfactant apolipoproteins on liposome structure: implications for tubular myelin formation. Am. J. Physiol. 262:L730-L739.
    • (1992) Am. J. Physiol , vol.262
    • Poulain, F.R.1    Allen, L.2    Williams, M.C.3    Hamilton, R.L.4    Hawgood, S.5
  • 30
    • 0032581011 scopus 로고    scopus 로고
    • Depth profiles of pulmonary surfactant B in phosphatidylcholine bilayers studied by fluorescence and electron spin resonance spectroscopy
    • Cruz, A., C. Casals, I. Plasencia, D. Marsh, and J. Pérez-Gil. 1998. Depth profiles of pulmonary surfactant B in phosphatidylcholine bilayers studied by fluorescence and electron spin resonance spectroscopy. Biochemistry. 37:9488-9496.
    • (1998) Biochemistry , vol.37 , pp. 9488-9496
    • Cruz, A.1    Casals, C.2    Plasencia, I.3    Marsh, D.4    Pérez-Gil, J.5
  • 31
    • 0031740469 scopus 로고    scopus 로고
    • Structure and properties of surfactant protein C
    • Johansson, J. 1998. Structure and properties of surfactant protein C. Biochim. Biophys. Acta. 1408:161-172.
    • (1998) Biochim. Biophys. Acta , vol.1408 , pp. 161-172
    • Johansson, J.1
  • 32
    • 0015894118 scopus 로고
    • Isolation and characterization of lamellar bodies and tubular myelin from rat lung homogenates
    • Gil, J., and O. K. Reiss. 1973. Isolation and characterization of lamellar bodies and tubular myelin from rat lung homogenates. J. Cell Biol. 58:152-171.
    • (1973) J. Cell Biol , vol.58 , pp. 152-171
    • Gil, J.1    Reiss, O.K.2
  • 33
    • 0019287284 scopus 로고
    • Isolation of lung lamellar bodies and their conversion to tubular myelin figures in vitro
    • Sanders, D. L., R. J. Hassett, and A. E. Vatter. 1980. Isolation of lung lamellar bodies and their conversion to tubular myelin figures in vitro. Anat. Rec. 198:485-501.
    • (1980) Anat. Rec , vol.198 , pp. 485-501
    • Sanders, D.L.1    Hassett, R.J.2    Vatter, A.E.3
  • 35
    • 0001616247 scopus 로고
    • Localization of lipid exchange sites between lung surfactants and surface monolayer: Freeze fracture study
    • Sen, A., S. W. Hui, M. Mosgrober-Anthony, B. A. Holm, and E. A. Egan. 1988. Localization of lipid exchange sites between lung surfactants and surface monolayer: freeze fracture study. J. Colloid Interface Sci. 126:355-360.
    • (1988) J. Colloid Interface Sci , vol.126 , pp. 355-360
    • Sen, A.1    Hui, S.W.2    Mosgrober-Anthony, M.3    Holm, B.A.4    Egan, E.A.5
  • 36
    • 0024333716 scopus 로고
    • Reconstitution of tubular myelin from synthetic lipids and proteins associated with pig pulmonary surfactant
    • Suzuki, Y., Y. Fujita, and K. Kogishi. 1989. Reconstitution of tubular myelin from synthetic lipids and proteins associated with pig pulmonary surfactant. Am. Rev. Respir. Dis. 140:75-81.
    • (1989) Am. Rev. Respir. Dis , vol.140 , pp. 75-81
    • Suzuki, Y.1    Fujita, Y.2    Kogishi, K.3
  • 37
    • 0026197257 scopus 로고
    • Changes in lipid structure produced by surfactant proteins SP-A, SP-B, and SP-C
    • Williams, M. C., S. Hawgood, and R. L. Hamilton. 1991. Changes in lipid structure produced by surfactant proteins SP-A, SP-B, and SP-C. Am. J. Respir. Cell Mol. Biol. 5:41-50.
    • (1991) Am. J. Respir. Cell Mol. Biol , vol.5 , pp. 41-50
    • Williams, M.C.1    Hawgood, S.2    Hamilton, R.L.3
  • 38
    • 0141642124 scopus 로고    scopus 로고
    • Interaction of pulmonary surfactant protein SP-A with DPPC/egg-PG bilayers
    • Morrow, M. R., N. Abu-Libdeh, J. Stewart, and K. M. W. Keough. 2003. Interaction of pulmonary surfactant protein SP-A with DPPC/egg-PG bilayers. Biophys. J. 85:2397-2405.
    • (2003) Biophys. J , vol.85 , pp. 2397-2405
    • Morrow, M.R.1    Abu-Libdeh, N.2    Stewart, J.3    Keough, K.M.W.4
  • 39
    • 3142710053 scopus 로고    scopus 로고
    • Perturbation of DPPC bilayers by high concentrations of pulmonary surfactant protein SP-B
    • Morrow, M. R., J. Stewart, S. Taneva, A. Dico, and K. M. W. 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    Taneva, S.3    Dico, A.4    Keough, K.M.W.5
  • 40
    • 0027175568 scopus 로고
    • Pulmonary surfactant-associated protein SP-B has little effect on acyl chains in dipalmitoylphosphatidylcholine dispersions
    • Morrow, M. R., J. Pèrez-Gil, G. Simatos, C. Boland, J. Stewart, D. Absolom, V. Sarin, and K. M. W. Keough. 1993. Pulmonary surfactant-associated protein SP-B has little effect on acyl chains in dipalmitoylphosphatidylcholine dispersions. Biochemistry. 32:4397-4402.
    • (1993) Biochemistry , vol.32 , pp. 4397-4402
    • Morrow, M.R.1    Pèrez-Gil, J.2    Simatos, G.3    Boland, C.4    Stewart, J.5    Absolom, D.6    Sarin, V.7    Keough, K.M.W.8
  • 41
    • 0030894592 scopus 로고    scopus 로고
    • Pulmonary surfactant protein SP-B interacts similarly with dipalmitoylphosphatidylglycerol and dipalmitoylphosphatidylcholine in phosphatidylcholine/phosphatidylglycerol mixtures
    • Dico, A. S., J. Hancock, M. R. Morrow, J. Stewart, S. Harris, and K. M. W. Keough. 1997. Pulmonary surfactant protein SP-B interacts similarly with dipalmitoylphosphatidylglycerol and dipalmitoylphosphatidylcholine in phosphatidylcholine/phosphatidylglycerol mixtures. Biochemistry. 36:4172-4177.
    • (1997) Biochemistry , vol.36 , pp. 4172-4177
    • Dico, A.S.1    Hancock, J.2    Morrow, M.R.3    Stewart, J.4    Harris, S.5    Keough, K.M.W.6
  • 42
    • 70449246528 scopus 로고
    • Phosphorus assay in column chromatography
    • Bartlett, G. R. 1959. Phosphorus assay in column chromatography. J. Biol. Chem. 234:466-468.
    • (1959) J. Biol. Chem , vol.234 , pp. 466-468
    • Bartlett, G.R.1
  • 43
    • 0023647323 scopus 로고
    • Differential scanning calorimetric studies of aqueous dispersions of phosphatidylcholines containing two polyenoic chains
    • Keough, K. M. W., and N. Kariel. 1987. Differential scanning calorimetric studies of aqueous dispersions of phosphatidylcholines containing two polyenoic chains. Biochim. Biophys. Acta. 902:11-18.
    • (1987) Biochim. Biophys. Acta , vol.902 , pp. 11-18
    • Keough, K.M.W.1    Kariel, N.2
  • 44
    • 0023837657 scopus 로고
    • Low-molecular-mass surfactant protein type 1. The primary structure of a hydrophobic 8-kDa polypeptide with eight half-cysteine residues
    • Curstedt, T., J. Johansson, J. Barros-Soderling, B. Robertson, G. Nilsson, M. Westberg, and H. Jornvall. 1988. Low-molecular-mass surfactant protein type 1. The primary structure of a hydrophobic 8-kDa polypeptide with eight half-cysteine residues. Eur. J. Biochem. 172:521-525.
    • (1988) Eur. J. Biochem , vol.172 , pp. 521-525
    • Curstedt, T.1    Johansson, J.2    Barros-Soderling, J.3    Robertson, B.4    Nilsson, G.5    Westberg, M.6    Jornvall, H.7
  • 45
    • 0028230032 scopus 로고
    • Pulmonary surfactant proteins SP-B and SP-C in spread monolayers at the air-water interface: I. Monolayers of pulmonary surfactant protein SP-B and phospholipids
    • Taneva, S., and K. M. W. Keough. 1994. Pulmonary surfactant proteins SP-B and SP-C in spread monolayers at the air-water interface: I. Monolayers of pulmonary surfactant protein SP-B and phospholipids. Biophys. J. 66:1137-1148.
    • (1994) Biophys. J , vol.66 , pp. 1137-1148
    • Taneva, S.1    Keough, K.M.W.2
  • 46
    • 0029031352 scopus 로고
    • Calcium ions and interactions of pulmonary surfactant proteins SP-B and SP-C with phospholipids in spread monolayers at the air/water interface
    • Taneva, S., and K. M. W. Keough. 1995. Calcium ions and interactions of pulmonary surfactant proteins SP-B and SP-C with phospholipids in spread monolayers at the air/water interface. Biochim. Biophys. Acta. 1236:185-195.
    • (1995) Biochim. Biophys. Acta , vol.1236 , pp. 185-195
    • Taneva, S.1    Keough, K.M.W.2
  • 47
    • 0023275396 scopus 로고
    • The major lung surfactant protein, SP 28-36, is a calcium dependent, carbohydrate-binding protein
    • Haagsman, H. P., S. Hawgood, T. Sargeant, D. Buckley, R. T. White, K. Drikamer, and B. J. Benson. 1987. The major lung surfactant protein, SP 28-36, is a calcium dependent, carbohydrate-binding protein. J. Biol. Chem. 262:13877-13880.
    • (1987) J. Biol. Chem , vol.262 , pp. 13877-13880
    • Haagsman, H.P.1    Hawgood, S.2    Sargeant, T.3    Buckley, D.4    White, R.T.5    Drikamer, K.6    Benson, B.J.7
  • 48
    • 0015522277 scopus 로고
    • Fluorescamine: A reagent for assay of amino acids, peptides and primary amines in the picomole range
    • Udenfriend, S., S. Stein, P. Bohlen, W. Dairman, W. Loimgrukes, and M. Weigele. 1972. Fluorescamine: a reagent for assay of amino acids, peptides and primary amines in the picomole range. Science. 178:871-872.
    • (1972) Science , vol.178 , pp. 871-872
    • Udenfriend, S.1    Stein, S.2    Bohlen, P.3    Dairman, W.4    Loimgrukes, W.5    Weigele, M.6
  • 51
    • 0000745176 scopus 로고
    • Quadrupole echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains
    • Davis, J. H., K. R. Jeffrey, M. Bloom, M. I. Valic, and T. P. Higgs. 1976. Quadrupole echo deuteron magnetic resonance spectroscopy in ordered hydrocarbon chains. Chem. Phys. Lett. 42:390-394.
    • (1976) Chem. Phys. Lett , vol.42 , pp. 390-394
    • Davis, J.H.1    Jeffrey, K.R.2    Bloom, M.3    Valic, M.I.4    Higgs, T.P.5
  • 55
    • 0032298428 scopus 로고    scopus 로고
    • Slow motions in bilayers containing anionic phospholipids
    • Kilfoil, M. L., and M. R. Morrow. 1998. Slow motions in bilayers containing anionic phospholipids. Physica A. 261:82-94.
    • (1998) Physica A , vol.261 , pp. 82-94
    • Kilfoil, M.L.1    Morrow, M.R.2
  • 56
    • 0033798421 scopus 로고    scopus 로고
    • Differential effects of surfactant protein A on regional organization of phospholipids monolayers containing surfactant protein B or C
    • Taneva, S. G., and K. M. W. Keough. 2000. Differential effects of surfactant protein A on regional organization of phospholipids monolayers containing surfactant protein B or C. Biophys. J. 79:2010-2023.
    • (2000) Biophys. J , vol.79 , pp. 2010-2023
    • Taneva, S.G.1    Keough, K.M.W.2
  • 57
    • 0021035007 scopus 로고
    • Reassembly of lipid-protein complexes of pulmonary surfactant. Proposed mechanism of interaction
    • King, R. J., M. C. Carmichael, and P. M. Horowitz. 1983. Reassembly of lipid-protein complexes of pulmonary surfactant. Proposed mechanism of interaction. J. Biol. Chem. 258:10672-10680.
    • (1983) J. Biol. Chem , vol.258 , pp. 10672-10680
    • King, R.J.1    Carmichael, M.C.2    Horowitz, P.M.3
  • 58
    • 0031951412 scopus 로고    scopus 로고
    • Differential partitioning of pulmonary surfactant protein SP-A into regions of monolayers of dipalmitoylphosphatidylcholine and dipalmitoylphosphatidylcholine/dipalmitoylphosphatidylglycerol
    • Ruano, M. L. F., K. Nag, L.-A. Worthman, C. Casals, J. Pérez-Gil, and K. M. W. Keough. 1998. Differential partitioning of pulmonary surfactant protein SP-A into regions of monolayers of dipalmitoylphosphatidylcholine and dipalmitoylphosphatidylcholine/dipalmitoylphosphatidylglycerol. Biophys. J. 74:1101-1109.
    • (1998) Biophys. J , vol.74 , pp. 1101-1109
    • Ruano, M.L.F.1    Nag, K.2    Worthman, L.-A.3    Casals, C.4    Pérez-Gil, J.5    Keough, K.M.W.6
  • 60
    • 0033729383 scopus 로고    scopus 로고
    • Pulmonary surfactant protein A interacts with gel-like regions in monolayers of pulmonary surfactant lipid extract
    • Worthman, L.-A., K. Nag, N. Rich, M. L. F. Ruano, C. Casals, J. Pérez-Gil, and K. M. W. Keough. 2000. Pulmonary surfactant protein A interacts with gel-like regions in monolayers of pulmonary surfactant lipid extract. Biophys. J. 79:2657-2666.
    • (2000) Biophys. J , vol.79 , pp. 2657-2666
    • Worthman, L.-A.1    Nag, K.2    Rich, N.3    Ruano, M.L.F.4    Casals, C.5    Pérez-Gil, J.6    Keough, K.M.W.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.