메뉴 건너뛰기




Volumn 85, Issue 4, 2003, Pages 2624-2632

Conformational changes in SP-B as a function of surface pressure

Author keywords

[No Author keywords available]

Indexed keywords

SURFACTANT PROTEIN B; WATER;

EID: 0141754049     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-3495(03)74685-2     Document Type: Article
Times cited : (14)

References (42)
  • 1
    • 0028908524 scopus 로고
    • An amphipathic helical motif common to tumourolytic polypeptide NK-lysin and pulmonary surfactant polypeptide SP-B
    • Andersson, M., T. Curstedt, H. Jornvall, and J. Johansson. 1995. An amphipathic helical motif common to tumourolytic polypeptide NK-lysin and pulmonary surfactant polypeptide SP-B. FEBS Lett. 362:328-332.
    • (1995) FEBS Lett. , vol.362 , pp. 328-332
    • Andersson, M.1    Curstedt, T.2    Jornvall, H.3    Johansson, J.4
  • 2
    • 0034602968 scopus 로고    scopus 로고
    • Ablation of a critical surfactant protein B intramolecular disulfide bond in transgenic mice
    • Beck, D. C., C.-L. Na, J. A. Whitsett, and T. E. Weaver. 2000. Ablation of a critical surfactant protein B intramolecular disulfide bond in transgenic mice. J. Biol. Chem. 275:3371-3376.
    • (2000) J. Biol. Chem. , vol.275 , pp. 3371-3376
    • Beck, D.C.1    Na, C.-L.2    Whitsett, J.A.3    Weaver, T.E.4
  • 4
    • 0000096033 scopus 로고
    • Capillary waves on the surface of simple liquids measured by x-ray reflectivity
    • Braslau, A., P. S. Pershan, G. Swislow, B. M. Ocko, and J. Als-Nielsen. 1988. Capillary waves on the surface of simple liquids measured by x-ray reflectivity. Phys. Rev. A. 38:2457-2470.
    • (1988) Phys. Rev. A , vol.38 , pp. 2457-2470
    • Braslau, A.1    Pershan, P.S.2    Swislow, G.3    Ocko, B.M.4    Als-Nielsen, J.5
  • 6
    • 0034757481 scopus 로고    scopus 로고
    • Two hydrophobic protein fractions of ovine pulmonary surfactant: Isolation, characterization, and biophysical activity
    • Bunger, H., R. P. Kruger, S. Pietschmann, N. Wustneck, L. Kaufner, R. Tschiersch, and U. Pison. 2001. Two hydrophobic protein fractions of ovine pulmonary surfactant: isolation, characterization, and biophysical activity. Protein Expr. Purif. 23:319-327.
    • (2001) Protein Expr. Purif. , vol.23 , pp. 319-327
    • Bunger, H.1    Kruger, R.P.2    Pietschmann, S.3    Wustneck, N.4    Kaufner, L.5    Tschiersch, R.6    Pison, U.7
  • 7
    • 0034971893 scopus 로고    scopus 로고
    • Role of surfactant protein A (SP-A)/lipid interactions for SP-A functions in the lung
    • Casals, C. 2001. Role of surfactant protein A (SP-A)/lipid interactions for SP-A functions in the lung. Pediatr. Pathol. Mol. Med. 20:249-268.
    • (2001) Pediatr. Pathol. Mol. Med. , vol.20 , pp. 249-268
    • Casals, C.1
  • 8
    • 0028912411 scopus 로고
    • Conformational flexibility of pulmonary surfactant proteins SP-B and SP-C, studied in aqueous organic solvents
    • Cruz, A., C. Casals, and J. Perez-Gil. 1995. Conformational flexibility of pulmonary surfactant proteins SP-B and SP-C, studied in aqueous organic solvents. Biochim. Biophys. Acta. 1255:68-76.
    • (1995) Biochim. Biophys. Acta , vol.1255 , pp. 68-76
    • Cruz, A.1    Casals, C.2    Perez-Gil, J.3
  • 9
    • 0023656392 scopus 로고
    • Two hydrophobic low-molecular-mass protein-fractions of pulmonary surfactant - Characterization and biophysical activity
    • Curstedt, T., H. Jornvall, B. Robertson, T. Bergman, and P. Berggren. 1987. Two hydrophobic low-molecular-mass protein-fractions of pulmonary surfactant - characterization and biophysical activity. Eur. J. Biochem. 168:255-262.
    • (1987) Eur. J. Biochem. , vol.168 , pp. 255-262
    • Curstedt, T.1    Jornvall, H.2    Robertson, B.3    Bergman, T.4    Berggren, P.5
  • 10
    • 0041020643 scopus 로고
    • X-ray reflectivity study of monolayers of amphiphilics at the air-water-interface
    • Daillant, J., J. J. Benattar, and L. Bosio. 1990. X-ray reflectivity study of monolayers of amphiphilics at the air-water-interface. J. Phys. Condens. Matter. 2:SA405-SA410.
    • (1990) J. Phys. Condens. Matter , vol.2
    • Daillant, J.1    Benattar, J.J.2    Bosio, L.3
  • 11
    • 0035831169 scopus 로고    scopus 로고
    • Secondary structure in lung surfactant SP-B peptides: IR and CD studies of bulk and monolayer phases
    • Dieudonne, D., R. Mendelsohn, R. S. Farid, and C. R. Flach. 2001. Secondary structure in lung surfactant SP-B peptides: IR and CD studies of bulk and monolayer phases. Biochim. Biophys. Acta. 1511:99-112.
    • (2001) Biochim. Biophys. Acta , vol.1511 , pp. 99-112
    • Dieudonne, D.1    Mendelsohn, R.2    Farid, R.S.3    Flach, C.R.4
  • 13
    • 0026320893 scopus 로고
    • Phases of phosphatidyl ethanolamine monolayers studied by synchrotron x-ray-scattering
    • Helm, C. A., P. Tippmannkrayer, H. Mohwald, J. Alsnielsen, and K. Kjaer. 1991. Phases of phosphatidyl ethanolamine monolayers studied by synchrotron x-ray-scattering. Biophys. J. 60:1457-1476.
    • (1991) Biophys. J. , vol.60 , pp. 1457-1476
    • Helm, C.A.1    Tippmannkrayer, P.2    Mohwald, H.3    Alsnielsen, J.4    Kjaer, K.5
  • 14
  • 15
    • 0025775999 scopus 로고
    • Surfactant protein B: Disulfide bridges, structural properties, and kringle similarities
    • Johansson, J., T. Curstedt, and H. Jornvall. 1991. Surfactant protein B: disulfide bridges, structural properties, and kringle similarities. Biochemistry. 30:6917-6921.
    • (1991) Biochemistry , vol.30 , pp. 6917-6921
    • Johansson, J.1    Curstedt, T.2    Jornvall, H.3
  • 16
    • 0033888949 scopus 로고    scopus 로고
    • Formation of three-dimensional protein-lipid aggregates in monolayer films induced by surfactant protein B
    • Krol, S., M. Ross, M. Sieber, S. Kunneke, H.-J. Galla, and A. Janshoff. 2000. Formation of three-dimensional protein-lipid aggregates in monolayer films induced by surfactant protein B. Biophys. J. 79:904-918.
    • (2000) Biophys. J. , vol.79 , pp. 904-918
    • Krol, S.1    Ross, M.2    Sieber, M.3    Kunneke, S.4    Galla, H.-J.5    Janshoff, A.6
  • 18
    • 0033562182 scopus 로고    scopus 로고
    • Structural conformation of bovine serum albumin layers at the air-water interface studied by neutron reflection
    • Lu, J. R., T. J. Su, and R. K. Thomas. 1999. Structural conformation of bovine serum albumin layers at the air-water interface studied by neutron reflection. J. Colloid Interface Sci. 213:426-437.
    • (1999) J. Colloid Interface Sci. , vol.213 , pp. 426-437
    • Lu, J.R.1    Su, T.J.2    Thomas, R.K.3
  • 20
    • 0023652867 scopus 로고
    • Protein sequence analysis studies on the low molecular weight hydrophobic proteins associated with bovine pulmonary surfactant
    • Olafson, R. W., U. Rink, S. Kielland, S. H. Yu, J. Chung, P. G. Harding, and F. Possmayer. 1987. Protein sequence analysis studies on the low molecular weight hydrophobic proteins associated with bovine pulmonary surfactant. Biochem. Biophys. Res. Commun. 148:1406-1411.
    • (1987) Biochem. Biophys. Res. Commun. , vol.148 , pp. 1406-1411
    • Olafson, R.W.1    Rink, U.2    Kielland, S.3    Yu, S.H.4    Chung, J.5    Harding, P.G.6    Possmayer, F.7
  • 21
    • 0026345305 scopus 로고
    • Characterization of lipid insertion into monomolecular layers mediated by lung surfactant proteins SP-B and SP-C
    • Oosterlaken-Dijksterhuis, M. A., H. P. Haagsman, L. M. G. Vangolde, and R. A. Demel. 1991. Characterization of lipid insertion into monomolecular layers mediated by lung surfactant proteins SP-B and SP-C. Biochemistry. 30:10965-10971.
    • (1991) Biochemistry , vol.30 , pp. 10965-10971
    • Oosterlaken-Dijksterhuis, M.A.1    Haagsman, H.P.2    Vangolde, L.M.G.3    Demel, R.A.4
  • 22
    • 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. Perez-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    Perez-Gil, J.3
  • 23
    • 0028791417 scopus 로고
    • External reflection absorption infrared spectroscopy study of lung surfactant proteins SP-B and SP-C in phospholipid monolayers at the air/water interface
    • Pastrana-Rios, B., S. Taneva, K. M. W. Keough, A. J. Mautone, and R. Mendelsohn. 1995. External reflection absorption infrared spectroscopy study of lung surfactant proteins SP-B and SP-C in phospholipid monolayers at the air/water interface. Biophys. J. 69:2531-2540.
    • (1995) Biophys. J. , vol.69 , pp. 2531-2540
    • Pastrana-Rios, B.1    Taneva, S.2    Keough, K.M.W.3    Mautone, A.J.4    Mendelsohn, R.5
  • 24
    • 11644271678 scopus 로고
    • The application of the specular reflection of neutrons to the study of surfaces and interfaces
    • Penfold, J., and R. K. Thomas. 1990. The application of the specular reflection of neutrons to the study of surfaces and interfaces. J. Phys. Condens. Matter. 2:1369-1412.
    • (1990) J. Phys. Condens. Matter , vol.2 , pp. 1369-1412
    • Penfold, J.1    Thomas, R.K.2
  • 25
    • 0023456101 scopus 로고
    • A time-of-flight neutron reflectometer for surface and interfacial studies
    • Penfold, J., R. C. Ward, and W. G. Williams. 1987. A time-of-flight neutron reflectometer for surface and interfacial studies. J. Phys. [E]. 20:1411-1417.
    • (1987) J. Phys. [E] , vol.20 , pp. 1411-1417
    • Penfold, J.1    Ward, R.C.2    Williams, W.G.3
  • 26
    • 0027207279 scopus 로고
    • Solubility of hydrophobic surfactant proteins in organic solvent/water mixtures. Structural studies on SP-B and SP-C in aqueous organic solvents and lipids
    • Pérez-Gil, J., A. Cruz, and C. Casals. 1993. Solubility of hydrophobic surfactant proteins in organic solvent/water mixtures. Structural studies on SP-B and SP-C in aqueous organic solvents and lipids. Biochim. Biophys. Acta. 1168:261-270.
    • (1993) Biochim. Biophys. Acta , vol.1168 , pp. 261-270
    • Pérez-Gil, J.1    Cruz, A.2    Casals, C.3
  • 27
    • 0034980458 scopus 로고    scopus 로고
    • String Fit: A new structurally oriented x-ray and neutron reflectivity evaluation technique
    • Politsch, E. 2001. String Fit: a new structurally oriented x-ray and neutron reflectivity evaluation technique. J. Appl. Crystallogr. 34:239-251.
    • (2001) J. Appl. Crystallogr. , vol.34 , pp. 239-251
    • Politsch, E.1
  • 28
    • 12444258568 scopus 로고    scopus 로고
    • Review issue of Biochimica et Biophysica Acta. 1998. Molecular basis of disease
    • Review Issue of Biochimica et Biophysica Acta. 1998. Molecular basis of disease. Biochim. Biophys. Acta. 1408:77-361.
    • (1998) Biochim. Biophys. Acta , vol.1408 , pp. 77-361
  • 29
    • 12444285621 scopus 로고    scopus 로고
    • Review issue of comparative biochemistry and physiology. 2001. Part A: Molecular & integrative physiology
    • Review Issue of Comparative Biochemistry and Physiology. 2001. Part A: molecular & integrative physiology. Comp. Biochem. Physiol. 129:1-303.
    • (2001) Comp. Biochem. Physiol. , vol.129 , pp. 1-303
  • 30
    • 12444261539 scopus 로고    scopus 로고
    • Review issue of pediatric pathology and molecular medicine
    • Review Issue of Pediatric Pathology and Molecular Medicine. 2001. Pediatr. Pathol. Mol. Med. 21:249-536.
    • (2001) Pediatr. Pathol. Mol. Med. , vol.21 , pp. 249-536
  • 31
    • 0343621506 scopus 로고    scopus 로고
    • Submolecular organization of DMPA in surface monolayers: Beyond the two-layer model
    • Schalke, M., P. Kruger, M. Weygand, and M. Losche. 2000. Submolecular organization of DMPA in surface monolayers: beyond the two-layer model. Biochim. Biophys. Acta. 1464:113-126.
    • (2000) Biochim. Biophys. Acta , vol.1464 , pp. 113-126
    • Schalke, M.1    Kruger, P.2    Weygand, M.3    Losche, M.4
  • 32
    • 0034353627 scopus 로고    scopus 로고
    • Structural models of lipid surface monolayers from x-ray and neutron reflectivity measurements
    • Schalke, M., and M. Losche. 2000. Structural models of lipid surface monolayers from x-ray and neutron reflectivity measurements. Adv. Colloid Interface Sci. 88:243-274.
    • (2000) Adv. Colloid Interface Sci. , vol.88 , pp. 243-274
    • Schalke, M.1    Losche, M.2
  • 34
    • 0001431603 scopus 로고    scopus 로고
    • Effect of pH on the adsorption of bovine serum albumin at the silica water interface studied by neutron reflection
    • Su, T. J., J. R. Lu, R. K. Thomas, and Z. F. Cui. 1999. Effect of pH on the adsorption of bovine serum albumin at the silica water interface studied by neutron reflection. J. Phys. Chem. B. 103:3727-3736.
    • (1999) J. Phys. Chem. B , vol.103 , pp. 3727-3736
    • Su, T.J.1    Lu, J.R.2    Thomas, R.K.3    Cui, Z.F.4
  • 35
    • 0001508128 scopus 로고    scopus 로고
    • The conformational structure of bovine serum albumin layers adsorbed at the silica-water interface
    • Su, T. J., J. R. Lu, R. K. Thomas, Z. F. Cui, and J. Penfold. 1998. The conformational structure of bovine serum albumin layers adsorbed at the silica-water interface. J. Phys. Chem. B. 102:8100-8108.
    • (1998) J. Phys. Chem. B , vol.102 , pp. 8100-8108
    • Su, T.J.1    Lu, J.R.2    Thomas, R.K.3    Cui, Z.F.4    Penfold, J.5
  • 37
    • 0028230032 scopus 로고
    • Pulmonary surfactant proteins SP-B and SP-C in spread monolayers at the air- water-interface. 1. 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. 1. 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
  • 38
    • 0032489671 scopus 로고    scopus 로고
    • Method of purification affects some interfacial properties of pulmonary surfactant proteins B and C and their mixtures with dipalmitoylphosphatidylcholine
    • Taneva, S. G., J. Stewart, L. Taylor, and K. M. W. Keough. 1998. Method of purification affects some interfacial properties of pulmonary surfactant proteins B and C and their mixtures with dipalmitoylphosphatidylcholine. Biochim. Biophys. Acta. 1370:138-150.
    • (1998) Biochim. Biophys. Acta , vol.1370 , pp. 138-150
    • Taneva, S.G.1    Stewart, J.2    Taylor, L.3    Keough, K.M.W.4
  • 39
    • 0034744529 scopus 로고    scopus 로고
    • Function of surfactant proteins B and C
    • Weaver, T. E., and J. J. Conkright. 2001. Function of surfactant proteins B and C. Annu. Rev. Physiol. 63:555-578.
    • (2001) Annu. Rev. Physiol. , vol.63 , pp. 555-578
    • Weaver, T.E.1    Conkright, J.J.2
  • 40
    • 0033796912 scopus 로고    scopus 로고
    • Dynamic interfacial properties of human apolipoproteins A-IV and B-17 at the air/water and oil/water interface
    • Weinberg, R. B., V. R. Cook, J. A. DeLozier, and G. S. Shelness. 2000. Dynamic interfacial properties of human apolipoproteins A-IV and B-17 at the air/water and oil/water interface. J. Lipid Res. 41:1419-1427.
    • (2000) J. Lipid Res. , vol.41 , pp. 1419-1427
    • Weinberg, R.B.1    Cook, V.R.2    DeLozier, J.A.3    Shelness, G.S.4
  • 41
    • 0023658582 scopus 로고
    • Characterization of the small hydrophobic proteins associated with pulmonary surfactant
    • Yu, S. H., W. Chung, R. W. Olafson, P. G. Harding, and F. Possmayer. 1987. Characterization of the small hydrophobic proteins associated with pulmonary surfactant. Biochim. Biophys. Acta. 921:437-448.
    • (1987) Biochim. Biophys. Acta , vol.921 , pp. 437-448
    • Yu, S.H.1    Chung, W.2    Olafson, R.W.3    Harding, P.G.4    Possmayer, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.