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Volumn 129, Issue 1, 2001, Pages 91-108

Surfactant-associated proteins: Functions and structural variation

Author keywords

C type lectins; Collectins; Dipalmitoyl phosphatidylcholine (DPPC); Lung; Pulmonary surfactant; Saposins; Surface properties; Surfactant proteins

Indexed keywords

COLLECTIN; DIPALMITOYLPHOSPHATIDYLCHOLINE; LECTIN; LUNG SURFACTANT; PROTEIN SUBUNIT; SPHINGOLIPID ACTIVATOR PROTEIN; SURFACTANT PROTEIN A; SURFACTANT PROTEIN B; SURFACTANT PROTEIN C; SURFACTANT PROTEIN D;

EID: 0035019559     PISSN: 10956433     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1095-6433(01)00308-7     Document Type: Conference Paper
Times cited : (170)

References (138)
  • 1
    • 0030762136 scopus 로고    scopus 로고
    • A scanning force- And fluorescence light microscopy study of the structure and function of a model pulmonary surfactant
    • Amrein M., von Nahmen A., Sieber M. A scanning force- and fluorescence light microscopy study of the structure and function of a model pulmonary surfactant. Eur. Biophys. J. 26:1997;349-357.
    • (1997) Eur. Biophys. J. , vol.26 , pp. 349-357
    • Amrein, M.1    Von Nahmen, A.2    Sieber, M.3
  • 2
    • 0028908524 scopus 로고
    • An amphipathic helical motif common to tumourolytic polypeptide NK-lysin and pulmonary surfactant polypeptide SP-B
    • Andersson M., Curstedt T., Jörnvall H., Johansson J. An amphipathic helical motif common to tumourolytic polypeptide NK-lysin and pulmonary surfactant polypeptide SP-B. FEBS Lett. 362:1995;328-332.
    • (1995) FEBS Lett. , vol.362 , pp. 328-332
    • Andersson, M.1    Curstedt, T.2    Jörnvall, H.3    Johansson, J.4
  • 3
    • 70449249103 scopus 로고
    • Surface properties in relation to atelectasis and hyaline membrane disease
    • Avery M.E., Mead J. Surface properties in relation to atelectasis and hyaline membrane disease. Am. J. Dis. Child. 97:1959;517-523.
    • (1959) Am. J. Dis. Child , vol.97 , pp. 517-523
    • Avery, M.E.1    Mead, J.2
  • 4
    • 0025300079 scopus 로고
    • Surfactant protein SP-B induces ordering at the surface of model membrane bilayers
    • Baatz J.E., Elledge B., Whitsett J.A. Surfactant protein SP-B induces ordering at the surface of model membrane bilayers. Biochemistry. 29:1990;6714-6720.
    • (1990) Biochemistry , vol.29 , pp. 6714-6720
    • Baatz, J.E.1    Elledge, B.2    Whitsett, J.A.3
  • 7
    • 0023834904 scopus 로고
    • The major apoprotein of rabbit pulmonary surfactant. Elucidation of primary sequence and cyclic AMP and developmental regulation
    • Boggaram V., Qing K., Mendelson C.R. The major apoprotein of rabbit pulmonary surfactant. Elucidation of primary sequence and cyclic AMP and developmental regulation. J. Biol. Chem. 263:1988;2939-2947.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2939-2947
    • Boggaram, V.1    Qing, K.2    Mendelson, C.R.3
  • 9
    • 13144282686 scopus 로고    scopus 로고
    • Altered surfactant homeostasis and alveolar type II cell morphology in mice lacking surfactant protein D
    • Botas C., Poulain F., Akiyama J., et al. Altered surfactant homeostasis and alveolar type II cell morphology in mice lacking surfactant protein D. Proc. Natl. Acad. Sci. USA. 95:1998;11869-11874.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11869-11874
    • Botas, C.1    Poulain, F.2    Akiyama, J.3
  • 10
    • 0017073905 scopus 로고
    • Circular-dichroism and electron-microscopy studies of human subcomponent C1q before and after limited proteolysis by pepsin
    • Brodsky D.B., Leonard K.R., Reid K.B. Circular-dichroism and electron-microscopy studies of human subcomponent C1q before and after limited proteolysis by pepsin. Biochem. J. 159:1976;279-286.
    • (1976) Biochem. J. , vol.159 , pp. 279-286
    • Brodsky, D.B.1    Leonard, K.R.2    Reid, K.B.3
  • 11
    • 0029096591 scopus 로고
    • Targeted disruption of the surfactant protein B gene disrupts surfactant homeostasis, causing respiratory failure in newborn mice
    • Clark J.C., Wert S.E., Bachurski C.J., et al. Targeted disruption of the surfactant protein B gene disrupts surfactant homeostasis, causing respiratory failure in newborn mice. Proc. Natl. Acad. Sci. USA. 92:1995;7794-7798.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7794-7798
    • Clark, J.C.1    Wert, S.E.2    Bachurski, C.J.3
  • 12
    • 84960963081 scopus 로고
    • Surface tension of lung extracts
    • Clements J.A. Surface tension of lung extracts. Proc. Soc. Exp. Biol. Med. 95:1957;170-172.
    • (1957) Proc. Soc. Exp. Biol. Med. , vol.95 , pp. 170-172
    • Clements, J.A.1
  • 13
    • 0009881244 scopus 로고
    • Pulmonary surface tension and the mucus lining of the lungs: Some theoretical considerations
    • Clements J.A., Brown E.S., Johnson R.P. Pulmonary surface tension and the mucus lining of the lungs: some theoretical considerations. J. Appl. Physiol. 12:1958;262-268.
    • (1958) J. Appl. Physiol. , vol.12 , pp. 262-268
    • Clements, J.A.1    Brown, E.S.2    Johnson, R.P.3
  • 14
    • 0026347862 scopus 로고
    • Pulmonary surfactant protein B (SP-B): Structure-function relationships
    • Cochrane C.G., Revak S.D. Pulmonary surfactant protein B (SP-B): structure-function relationships. Science. 254:1991;566-568.
    • (1991) Science , vol.254 , pp. 566-568
    • Cochrane, C.G.1    Revak, S.D.2
  • 16
    • 0029057298 scopus 로고
    • Neutralization of the positive charges of surfactant protein C. Effects on structure and function
    • Creuwels L.A.J.M., Boer E.H., Demel R.A., van Golde L.M.G., Haagsman H.P. Neutralization of the positive charges of surfactant protein C. Effects on structure and function. J. Biol. Chem. 270:1995;16225-16229.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16225-16229
    • Creuwels, L.A.J.M.1    Boer, E.H.2    Demel, R.A.3    Van Golde, L.M.G.4    Haagsman, H.P.5
  • 18
    • 0026046061 scopus 로고
    • Surfactant protein D. Increased accumulation in silica-induced pulmonary lipoproteinosis
    • Crouch E.C., Persson A., Chang D., Parghi D. Surfactant protein D. Increased accumulation in silica-induced pulmonary lipoproteinosis. Am. J. Pathol. 139:1991;765-776.
    • (1991) Am. J. Pathol. , vol.139 , pp. 765-776
    • Crouch, E.C.1    Persson, A.2    Chang, D.3    Parghi, D.4
  • 19
    • 0027466290 scopus 로고
    • Genomic organization of human surfactant protein D (SP-D). SP-D is encoded on chromosome 10q22.2-23.1
    • Crouch E.C., Rust K., Veile R., Donis K.H., Grosso L. Genomic organization of human surfactant protein D (SP-D). SP-D is encoded on chromosome 10q22.2-23.1. J. Biol. Chem. 268:1993;2976-2983.
    • (1993) J. Biol. Chem. , vol.268 , pp. 2976-2983
    • Crouch, E.C.1    Rust, K.2    Veile, R.3    Donis, K.H.4    Grosso, L.5
  • 20
    • 0032135111 scopus 로고    scopus 로고
    • Collectins and pulmonary host defense
    • Crouch E.C. Collectins and pulmonary host defense. Am. J. Respir. Cell. Mol. Biol. 19:1998;177-201.
    • (1998) Am. J. Respir. Cell. Mol. Biol. , vol.19 , pp. 177-201
    • Crouch, E.C.1
  • 21
    • 0028912411 scopus 로고
    • Conformational flexibility of pulmonary surfactant proteins SP-B and SP-C, studied in aqueous organic solvents
    • Cruz A., Casals C., Pérez-Gil J. Conformational flexibility of pulmonary surfactant proteins SP-B and SP-C, studied in aqueous organic solvents. Biochim. Biophys. Acta. 1255:1995;68-76.
    • (1995) Biochim. Biophys. Acta , vol.1255 , pp. 68-76
    • Cruz, A.1    Casals, C.2    Pérez-Gil, J.3
  • 22
    • 0023656392 scopus 로고
    • Two hydrophobic low-molecular-mass protein fractions of pulmonary surfactant. Characterization and biophysical activity
    • Curstedt T., Jörnvall H., Robertson B., Bergman T., Berggren P. Two hydrophobic low-molecular-mass protein fractions of pulmonary surfactant. Characterization and biophysical activity. Eur. J. Biochem. 168:1987;255-262.
    • (1987) Eur. J. Biochem. , vol.168 , pp. 255-262
    • Curstedt, T.1    Jörnvall, H.2    Robertson, B.3    Bergman, T.4    Berggren, P.5
  • 23
    • 0023837657 scopus 로고
    • Low-molecular-mass surfactant protein type 1. The primary structure of a hydrophobic 8-kDa polypeptide with eight half-cystine residues
    • Curstedt T., Johansson J., Barros S.J., Robertson B., Nilsson G., Westberg M., Jörnvall H. Low-molecular-mass surfactant protein type 1. The primary structure of a hydrophobic 8-kDa polypeptide with eight half-cystine residues. Eur. J. Biochem. 172:1988;521-525.
    • (1988) Eur. J. Biochem. , vol.172 , pp. 521-525
    • Curstedt, T.1    Johansson, J.2    Barros, S.J.3    Robertson, B.4    Nilsson, G.5    Westberg, M.6    Jörnvall, H.7
  • 24
    • 0000657639 scopus 로고
    • The evolution of the vertebrate pulmonary surfactant system
    • Daniels C.B., Orgeig S., Smits A.W. The evolution of the vertebrate pulmonary surfactant system. Physiol. Zool. 68:1995;539-566.
    • (1995) Physiol. Zool. , vol.68 , pp. 539-566
    • Daniels, C.B.1    Orgeig, S.2    Smits, A.W.3
  • 25
    • 0031690999 scopus 로고    scopus 로고
    • Evolution of surface activity related functions of vertebrate pulmonary surfactant
    • Daniels C.B., Lopatko O.V., Orgeig S. Evolution of surface activity related functions of vertebrate pulmonary surfactant. Clin. Exp. Pharmacol. Physiol. 25:1998;716-721.
    • (1998) Clin. Exp. Pharmacol. Physiol , vol.25 , pp. 716-721
    • Daniels, C.B.1    Lopatko, O.V.2    Orgeig, S.3
  • 26
    • 0024352183 scopus 로고
    • Expression of the 35kDa and low molecular weight surfactant-associated proteins in the lungs of infants dying with respiratory distress syndrome
    • deMello D.E., Phelps D.S., Patel G., Floros J., Lagunoff D. Expression of the 35kDa and low molecular weight surfactant-associated proteins in the lungs of infants dying with respiratory distress syndrome. Am. J. Pathol. 134:1989;1285-1293.
    • (1989) Am. J. Pathol. , vol.134 , pp. 1285-1293
    • Demello, D.E.1    Phelps, D.S.2    Patel, G.3    Floros, J.4    Lagunoff, D.5
  • 27
    • 0035862202 scopus 로고    scopus 로고
    • Functional tests for the characterization of surfactant protein B (SP-B) and a fluorescent SP-B analogue
    • Diemel R.V., Bader D., Walch M., et al. Functional tests for the characterization of surfactant protein B (SP-B) and a fluorescent SP-B analogue. Arch. Biochem. Biophys. 385:2001;338-347.
    • (2001) Arch. Biochem. Biophys , vol.385 , pp. 338-347
    • Diemel, R.V.1    Bader, D.2    Walch, M.3
  • 28
    • 0023115493 scopus 로고
    • Pulmonary surfactant and its components inhibit secretion of phosphatidylcholine from cultured rat alveolar type II cells
    • Dobbs L.G., Wright J.R., Hawgood S., Gonzalez R., Venstrom K., Nellenbogen J. Pulmonary surfactant and its components inhibit secretion of phosphatidylcholine from cultured rat alveolar type II cells. Proc. Natl. Acad. Sci. USA. 84:1987;1010-1014.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1010-1014
    • Dobbs, L.G.1    Wright, J.R.2    Hawgood, S.3    Gonzalez, R.4    Venstrom, K.5    Nellenbogen, J.6
  • 29
    • 0023710284 scopus 로고
    • Two distinct classes of carbohydrate-recognition domains in animal lectins
    • Drickamer K. Two distinct classes of carbohydrate-recognition domains in animal lectins. J. Biol. Chem. 263:1988;9557-9560.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9557-9560
    • Drickamer, K.1
  • 31
    • 0033428909 scopus 로고    scopus 로고
    • C-type lectin-like domains in Caenorhabditis elegans: Predictions from the complete genome sequence
    • Drickamer K., Dodd R.B. C-type lectin-like domains in Caenorhabditis elegans: predictions from the complete genome sequence. Glycobiology. 9:1999;1357-1369.
    • (1999) Glycobiology , vol.9 , pp. 1357-1369
    • Drickamer, K.1    Dodd, R.B.2
  • 32
    • 0023000540 scopus 로고
    • Isolation and characterization of cDNA clones for the 35-kDa pulmonary surfactant-associated protein
    • Floros J., Steinbrink R., Jacobs K., et al. Isolation and characterization of cDNA clones for the 35-kDa pulmonary surfactant-associated protein. J. Biol. Chem. 261:1986;9029-9033.
    • (1986) J. Biol. Chem. , vol.261 , pp. 9029-9033
    • Floros, J.1    Steinbrink, R.2    Jacobs, K.3
  • 33
    • 0031892937 scopus 로고    scopus 로고
    • Surfactant proteins: Molecular genetics of neonatal pulmonary diseases
    • Floros J., Kala P. Surfactant proteins: molecular genetics of neonatal pulmonary diseases. Annu. Rev. Physiol. 60:1998;365-384.
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 365-384
    • Floros, J.1    Kala, P.2
  • 35
    • 0023644774 scopus 로고
    • The complete amino acid sequence of echinoidin, a lectin from the coelomic fluid of the sea urchin Anthocidaris crassispina. Homologies with mammalian and insect lectins
    • Giga Y., Ikai A., Takahashi K. The complete amino acid sequence of echinoidin, a lectin from the coelomic fluid of the sea urchin Anthocidaris crassispina. Homologies with mammalian and insect lectins. J. Biol. Chem. 262:1987;6197-6203.
    • (1987) J. Biol. Chem. , vol.262 , pp. 6197-6203
    • Giga, Y.1    Ikai, A.2    Takahashi, K.3
  • 37
    • 0023902154 scopus 로고
    • CDNA, deduced polypeptide structure and chromosomal assignment of human pulmonary surfactant proteolipid, SPL(pVal)
    • Glasser S.W., Korfhagen T.R., Weaver T.E., et al. cDNA, deduced polypeptide structure and chromosomal assignment of human pulmonary surfactant proteolipid, SPL(pVal). J. Biol. Chem. 263:1988;9-12.
    • (1988) J. Biol. Chem. , vol.263 , pp. 9-12
    • Glasser, S.W.1    Korfhagen, T.R.2    Weaver, T.E.3
  • 40
    • 0014114144 scopus 로고
    • The biochemical development of surface activity in mammalian lung. I. The surface-active phospholipids; The separation and distribution of surface-active lecithin in the lung of the developing rabbit fetus
    • Gluck L., Motoyama E.K., Smits H.L., Kulovich M.V. The biochemical development of surface activity in mammalian lung. I. The surface-active phospholipids; the separation and distribution of surface-active lecithin in the lung of the developing rabbit fetus. Pediatr. Res. 1:1967;237-246.
    • (1967) Pediatr. Res. , vol.1 , pp. 237-246
    • Gluck, L.1    Motoyama, E.K.2    Smits, H.L.3    Kulovich, M.V.4
  • 41
    • 0031769679 scopus 로고    scopus 로고
    • Interactions of surfactant protein A with pathogens
    • Haagsman H.P. Interactions of surfactant protein A with pathogens. Biochim. Biophys. Acta. 1408:1998;264-277.
    • (1998) Biochim. Biophys. Acta , vol.1408 , pp. 264-277
    • Haagsman, H.P.1
  • 42
    • 0024833761 scopus 로고
    • Studies of the structure of lung surfactant protein SP-A
    • Haagsman H.P., White R.T., Schilling J., et al. Studies of the structure of lung surfactant protein SP-A. Am. J. Physiol. 257:1989;L421-L429.
    • (1989) Am. J. Physiol. , vol.257
    • Haagsman, H.P.1    White, R.T.2    Schilling, J.3
  • 43
    • 0025907154 scopus 로고
    • The lung lectin surfactant protein A aggregates phospholipid vesicles via a novel mechanism
    • Haagsman H.P., Elfring R.H., van Buel B.L., Voorhout W.F. The lung lectin surfactant protein A aggregates phospholipid vesicles via a novel mechanism. Biochem. J. 275:1991;273-276.
    • (1991) Biochem. J. , vol.275 , pp. 273-276
    • Haagsman, H.P.1    Elfring, R.H.2    Van Buel, B.L.3    Voorhout, W.F.4
  • 44
    • 0025734892 scopus 로고
    • Assembly and disulfide rearrangement of recombinant surfactant protein A in vitro
    • Haas C., Voss T., Engel J. Assembly and disulfide rearrangement of recombinant surfactant protein A in vitro. Eur. J. Biochem. 197:1991;799-803.
    • (1991) Eur. J. Biochem. , vol.197 , pp. 799-803
    • Haas, C.1    Voss, T.2    Engel, J.3
  • 45
    • 0026015327 scopus 로고
    • Expression and characterization of recombinant human acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial lipopolysaccharides
    • Hagen F.S., Grant F.J., Kuijper J.L., et al. Expression and characterization of recombinant human acyloxyacyl hydrolase, a leukocyte enzyme that deacylates bacterial lipopolysaccharides. Biochemistry. 30:1991;8415-8423.
    • (1991) Biochemistry , vol.30 , pp. 8415-8423
    • Hagen, F.S.1    Grant, F.J.2    Kuijper, J.L.3
  • 46
    • 0029903353 scopus 로고    scopus 로고
    • Interactions of recombinant human pulmonary surfactant protein D and SP-D multimers with influenza A
    • Hartshorn K., Chang D., Rust K., White M., Heuser J., Crouch E. Interactions of recombinant human pulmonary surfactant protein D and SP-D multimers with influenza A. Am. J. Physiol. 271:1996;L753-L762.
    • (1996) Am. J. Physiol. , vol.271
    • Hartshorn, K.1    Chang, D.2    Rust, K.3    White, M.4    Heuser, J.5    Crouch, E.6
  • 47
    • 0000625518 scopus 로고
    • Nucleotide and amino acid sequences of pulmonary surfactant protein SP 18 and evidence for cooperation between SP 18 and SP 28-36 in surfactant lipid adsorption
    • Hawgood S., Benson B.J., Schilling J., et al. Nucleotide and amino acid sequences of pulmonary surfactant protein SP 18 and evidence for cooperation between SP 18 and SP 28-36 in surfactant lipid adsorption. Proc. Natl. Acad. Sci. USA. 84:1987;66-70.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 66-70
    • Hawgood, S.1    Benson, B.J.2    Schilling, J.3
  • 48
  • 49
    • 0027976024 scopus 로고
    • Collectins: Collagenous C-type lectins of the innate immune defense system
    • Holmskov U., Malhotra R., Sim R.B., Jensenius J.C. Collectins: collagenous C-type lectins of the innate immune defense system. Immunol. Today. 15:1994;67-74.
    • (1994) Immunol. Today , vol.15 , pp. 67-74
    • Holmskov, U.1    Malhotra, R.2    Sim, R.B.3    Jensenius, J.C.4
  • 50
    • 0025743034 scopus 로고
    • Sulfatide activator protein. Alternative splicing that generates three mRNAs and a newly found mutation responsible for a clinical disease
    • Holtschmidt H., Sandhoff K., Kwon H.Y., Harzer K., Nakano T., Suzuki K. Sulfatide activator protein. Alternative splicing that generates three mRNAs and a newly found mutation responsible for a clinical disease. J. Biol. Chem. 266:1991;7556-7560.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7556-7560
    • Holtschmidt, H.1    Sandhoff, K.2    Kwon, H.Y.3    Harzer, K.4    Nakano, T.5    Suzuki, K.6
  • 51
    • 0023176747 scopus 로고
    • Isolation of a cDNA clone encoding a high molecular weight precursor to a 6-kDa pulmonary surfactant-associated protein
    • Jacobs K.A., Phelps D.S., Steinbrink R., et al. Isolation of a cDNA clone encoding a high molecular weight precursor to a 6-kDa pulmonary surfactant-associated protein. J. Biol. Chem. 262:1987;9808-9811.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9808-9811
    • Jacobs, K.A.1    Phelps, D.S.2    Steinbrink, R.3
  • 52
    • 0025775999 scopus 로고
    • Surfactant protein B: Disulfide bridges, structural properties, and kringle similarities
    • Johansson J., Curstedt T., Jörnvall H. Surfactant protein B: disulfide bridges, structural properties, and kringle similarities. Biochemistry. 30:1991;6917-6921.
    • (1991) Biochemistry , vol.30 , pp. 6917-6921
    • Johansson, J.1    Curstedt, T.2    Jörnvall, H.3
  • 53
    • 0028358907 scopus 로고
    • The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-helix
    • Johansson J., Szyperski T., Curstedt T., Wuthrich K. The NMR structure of the pulmonary surfactant-associated polypeptide SP-C in an apolar solvent contains a valyl-rich alpha-helix. Biochemistry. 33:1994;6015-6023.
    • (1994) Biochemistry , vol.33 , pp. 6015-6023
    • Johansson, J.1    Szyperski, T.2    Curstedt, T.3    Wuthrich, K.4
  • 55
    • 0002154771 scopus 로고    scopus 로고
    • Palmitoylation of proSP-C is not required for its intracellular targeting and proteolytic processing
    • Kabore A.F., Russo S.J., Wang W.-J., Beers M.F. Palmitoylation of proSP-C is not required for its intracellular targeting and proteolytic processing. Am. J. Respir. Crit. Care Med. 161:2000;A41.
    • (2000) Am. J. Respir. Crit. Care Med. , vol.161 , pp. 41
    • Kabore, A.F.1    Russo, S.J.2    Wang, W.-J.3    Beers, M.F.4
  • 56
    • 0030723438 scopus 로고    scopus 로고
    • Inhibition of bacterial growth by synthetic SP-B1-78 peptides
    • Kaser M.R., Skouteris G.G. Inhibition of bacterial growth by synthetic SP-B1-78 peptides. Peptides. 18:1997;1441-1444.
    • (1997) Peptides , vol.18 , pp. 1441-1444
    • Kaser, M.R.1    Skouteris, G.G.2
  • 57
    • 0026847422 scopus 로고
    • Characterization of a second human pulmonary surfactant-associated protein SP-A gene
    • Katyal S.L., Singh G., Locker J. Characterization of a second human pulmonary surfactant-associated protein SP-A gene. Am. J. Respir. Cell. Mol. Biol. 6:1992;446-452.
    • (1992) Am. J. Respir. Cell. Mol. Biol. , vol.6 , pp. 446-452
    • Katyal, S.L.1    Singh, G.2    Locker, J.3
  • 58
    • 0026876757 scopus 로고
    • The C-terminal domain of the pulmonary surfactant protein C precursor contains signals for intracellular targeting
    • Keller A., Steinhilber W., Schafer K.P., Voss T. The C-terminal domain of the pulmonary surfactant protein C precursor contains signals for intracellular targeting. Am. J. Respir. Cell. Mol. Biol. 6:1992;601-608.
    • (1992) Am. J. Respir. Cell. Mol. Biol. , vol.6 , pp. 601-608
    • Keller, A.1    Steinhilber, W.2    Schafer, K.P.3    Voss, T.4
  • 59
    • 0015611306 scopus 로고
    • Isolation of apoproteins from canine surface active material
    • King R.J., Klass D.J., Gikas E.G., Clements J.A. Isolation of apoproteins from canine surface active material. Am. J. Physiol. 224:1973;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
  • 60
    • 0026768211 scopus 로고
    • Saposins: Structure, function, distribution, and molecular genetics
    • Kishimoto Y., Hiraiwa M., O'Brien J.S. Saposins: structure, function, distribution, and molecular genetics. J. Lipid Res. 33:1992;1255-1267.
    • (1992) J. Lipid Res. , vol.33 , pp. 1255-1267
    • Kishimoto, Y.1    Hiraiwa, M.2    O'Brien, J.S.3
  • 61
    • 0001445596 scopus 로고
    • Composition of surface-active material isolated from beef lung
    • Klaus M.H., Clements J.A., Havel R.J. Composition of surface-active material isolated from beef lung. Proc. Natl. Acad. Sci. USA. 47:1961;1858-1859.
    • (1961) Proc. Natl. Acad. Sci. USA , vol.47 , pp. 1858-1859
    • Klaus, M.H.1    Clements, J.A.2    Havel, R.J.3
  • 62
    • 0026475221 scopus 로고
    • Murine pulmonary surfactant SP-A gene: Cloning, sequence, and transcriptional activity
    • Korfhagen T.R., Bruno M.D., Glasser S.W., et al. Murine pulmonary surfactant SP-A gene: cloning, sequence, and transcriptional activity. Am. J. Physiol. 263:1992;L546-L554.
    • (1992) Am. J. Physiol. , vol.263
    • Korfhagen, T.R.1    Bruno, M.D.2    Glasser, S.W.3
  • 63
    • 9544243825 scopus 로고    scopus 로고
    • Altered surfactant function and structure in SP-A gene targeted mice
    • Korfhagen T.R., Bruno M.D., Ross G.F., et al. Altered surfactant function and structure in SP-A gene targeted mice. Proc. Natl. Acad. Sci. USA. 93:1996;9594-9599.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 9594-9599
    • Korfhagen, T.R.1    Bruno, M.D.2    Ross, G.F.3
  • 64
    • 15144352324 scopus 로고    scopus 로고
    • Surfactant protein-D regulates surfactant phospholipid homeostasis in vivo
    • Korfhagen T.R., Sheftelyevich V., Burhans M.S., et al. Surfactant protein-D regulates surfactant phospholipid homeostasis in vivo. J. Biol. Chem. 273:1998;28438-28443.
    • (1998) J. Biol. Chem. , vol.273 , pp. 28438-28443
    • Korfhagen, T.R.1    Sheftelyevich, V.2    Burhans, M.S.3
  • 65
    • 0023759627 scopus 로고
    • Alveolar type II cells express a high-affinity receptor for pulmonary surfactant protein A
    • Kuroki Y., Mason R.J., Voelker D.R. Alveolar type II cells express a high-affinity receptor for pulmonary surfactant protein A. Proc. Natl. Acad. Sci. USA. 85:1988;5566-5570.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 5566-5570
    • Kuroki, Y.1    Mason, R.J.2    Voelker, D.R.3
  • 66
    • 0025936875 scopus 로고
    • Characterization of pulmonary surfactant protein D: Its copurification with lipids
    • Kuroki Y., Shiratori M., Ogasawara Y., Tsuzuki A., Akino T. Characterization of pulmonary surfactant protein D: its copurification with lipids. Biochim. Biophys. Acta. 1086:1991;185-190.
    • (1991) Biochim. Biophys. Acta , vol.1086 , pp. 185-190
    • Kuroki, Y.1    Shiratori, M.2    Ogasawara, Y.3    Tsuzuki, A.4    Akino, T.5
  • 69
    • 0026688586 scopus 로고
    • Primary and secondary structure of the pore-forming peptide of pathogenic Entamoeba histolytica
    • Leippe M., Tannich E., Nickel R., et al. Primary and secondary structure of the pore-forming peptide of pathogenic Entamoeba histolytica. EMBO J. 11:1992;3501-3506.
    • (1992) EMBO J. , vol.11 , pp. 3501-3506
    • Leippe, M.1    Tannich, E.2    Nickel, R.3
  • 70
    • 0027459854 scopus 로고
    • Structural similarity between bovine conglutinin and bovine lung surfactant protein D and demonstration of liver as a site of synthesis of conglutinin
    • Lim B.L., Lu J., Reid K.B. Structural similarity between bovine conglutinin and bovine lung surfactant protein D and demonstration of liver as a site of synthesis of conglutinin. Immunology. 78:1993;159-165.
    • (1993) Immunology , vol.78 , pp. 159-165
    • Lim, B.L.1    Lu, J.2    Reid, K.B.3
  • 71
    • 0030600233 scopus 로고    scopus 로고
    • Structural requirements for intracellular transport of pulmonary surfactant protein B (SP-B)
    • Lin S., Phillips K.S., Wilder M.R., Weaver T.E. Structural requirements for intracellular transport of pulmonary surfactant protein B (SP-B). Biochim. Biophys. Acta. 1312:1996;177-185.
    • (1996) Biochim. Biophys. Acta , vol.1312 , pp. 177-185
    • Lin, S.1    Phillips, K.S.2    Wilder, M.R.3    Weaver, T.E.4
  • 73
    • 0026740587 scopus 로고
    • Purification, characterization and cDNA cloning of human lung surfactant protein D
    • Lu J., Willis A.C., Reid K.B. Purification, characterization and cDNA cloning of human lung surfactant protein D. Biochem. J. 284:1992;795-802.
    • (1992) Biochem. J. , vol.284 , pp. 795-802
    • Lu, J.1    Willis, A.C.2    Reid, K.B.3
  • 74
    • 0027196291 scopus 로고
    • Pollen grains bind to lung alveolar type II cells (A549) via lung surfactant protein A (SP-A)
    • Malhotra R., Haurum J., Thiel S., Jensenius J.C., Sim R.B. Pollen grains bind to lung alveolar type II cells (A549) via lung surfactant protein A (SP-A). Biosci. Rep. 13:1993;79-90.
    • (1993) Biosci. Rep. , vol.13 , pp. 79-90
    • Malhotra, R.1    Haurum, J.2    Thiel, S.3    Jensenius, J.C.4    Sim, R.B.5
  • 75
    • 0031740744 scopus 로고    scopus 로고
    • Structure, processing and properties of surfactant protein A
    • McCormack F.X. Structure, processing and properties of surfactant protein A. Biochim. Biophys. Acta. 1408:1998;109-131.
    • (1998) Biochim. Biophys. Acta , vol.1408 , pp. 109-131
    • McCormack, F.X.1
  • 76
    • 0342516319 scopus 로고    scopus 로고
    • Conservation of surfactant proteins and epithelial cell diversity in amphibia and mammals
    • this volume
    • Miller, L.D., Wert, S.E., Whitsett, J.A., 2001. Conservation of surfactant proteins and epithelial cell diversity in amphibia and mammals, Comp. Biochem. Physiol. A, this volume.
    • (2001) Comp. Biochem. Physiol. a
    • Miller, L.D.1    Wert, S.E.2    Whitsett, J.A.3
  • 77
    • 0030346309 scopus 로고    scopus 로고
    • Palmitoylation: A post-translational modification that regulates signalling from G-protein coupled receptors
    • Morello J.P., Bouvier M. Palmitoylation: a post-translational modification that regulates signalling from G-protein coupled receptors. Biochem. Cell. Biol. 74:1996;449-457.
    • (1996) Biochem. Cell. Biol. , vol.74 , pp. 449-457
    • Morello, J.P.1    Bouvier, M.2
  • 79
    • 0025369310 scopus 로고
    • The positions of the disulfide bonds and the glycosylation site in a lectin of the acorn barnacle Megabalanus rosa
    • Muramoto K., Kamiya H. The positions of the disulfide bonds and the glycosylation site in a lectin of the acorn barnacle Megabalanus rosa. Biochim. Biophys. Acta. 1039:1990;52-60.
    • (1990) Biochim. Biophys. Acta , vol.1039 , pp. 52-60
    • Muramoto, K.1    Kamiya, H.2
  • 80
    • 0031771069 scopus 로고    scopus 로고
    • Genetics of the hydrophobic surfactant proteins
    • Nogee L.M. Genetics of the hydrophobic surfactant proteins. Biochim. Biophys. Acta. 1408:1998;323-333.
    • (1998) Biochim. Biophys. Acta , vol.1408 , pp. 323-333
    • Nogee, L.M.1
  • 81
    • 0026700098 scopus 로고
    • Pulmonary surfactant protein D specifically binds to phosphatidylinositol
    • Ogasawara Y., Kuroki Y., Akino T. Pulmonary surfactant protein D specifically binds to phosphatidylinositol. J. Biol. Chem. 267:1992;21244-21249.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21244-21249
    • Ogasawara, Y.1    Kuroki, Y.2    Akino, T.3
  • 82
    • 0023652867 scopus 로고
    • Protein sequence analysis studies on the low molecular weight hydrophobic proteins associated with bovine pulmonary surfactant
    • Olafson R.W., Rink U., Kielland S., Yu S.H., Chung J., Harding P.G., Possmayer F. Protein sequence analysis studies on the low molecular weight hydrophobic proteins associated with bovine pulmonary surfactant. Biochem. Biophys. Res. Commun. 148:1987;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
  • 84
    • 0025999791 scopus 로고
    • Fourier transform infrared studies of secondary structure and orientation of pulmonary surfactant SP-C and its effect on the dynamic surface properties of phospholipids
    • Pastrana B., Mautone A.J., Mendelsohn R. Fourier transform infrared studies of secondary structure and orientation of pulmonary surfactant SP-C and its effect on the dynamic surface properties of phospholipids. Biochemistry. 30:1991;10058-10064.
    • (1991) Biochemistry , vol.30 , pp. 10058-10064
    • Pastrana, B.1    Mautone, A.J.2    Mendelsohn, R.3
  • 85
    • 0025736562 scopus 로고
    • Homology of the precursor of pulmonary surfactant-associated protein SP-B with prosaposin and sulfated glycoprotein 1
    • Patthy L. Homology of the precursor of pulmonary surfactant-associated protein SP-B with prosaposin and sulfated glycoprotein 1. J. Biol. Chem. 266:1991;6035-6037.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6035-6037
    • Patthy, L.1
  • 86
    • 0000508925 scopus 로고
    • Properties, function and origin of the alveolar lining
    • Pattle R.E. Properties, function and origin of the alveolar lining. Nature. 175:1955;1125-1126.
    • (1955) Nature , vol.175 , pp. 1125-1126
    • Pattle, R.E.1
  • 87
    • 0031569218 scopus 로고    scopus 로고
    • Processing, subcellular localization, and function of 519 (granulysin), a human late T cell activation molecule with homology to small, lytic, granule proteins
    • Pena S.V., Hanson D.A., Carr B.A., Goralski T.J., Krensky A.M. Processing, subcellular localization, and function of 519 (granulysin), a human late T cell activation molecule with homology to small, lytic, granule proteins. J. Immunol. 158:1997;2680-2688.
    • (1997) J. Immunol. , vol.158 , pp. 2680-2688
    • Pena, S.V.1    Hanson, D.A.2    Carr, B.A.3    Goralski, T.J.4    Krensky, A.M.5
  • 88
    • 0023823173 scopus 로고
    • CP4: A pneumocyte-derived collagenous surfactant-associated protein. Evidence for heterogeneity of collagenous surfactant proteins
    • Persson A., Rust K., Chang D., Moxley M., Longmore W., Crouch E.C. CP4: a pneumocyte-derived collagenous surfactant-associated protein. Evidence for heterogeneity of collagenous surfactant proteins. Biochemistry. 27:1988;8576-8584.
    • (1988) Biochemistry , vol.27 , pp. 8576-8584
    • Persson, A.1    Rust, K.2    Chang, D.3    Moxley, M.4    Longmore, W.5    Crouch, E.C.6
  • 89
    • 0024403594 scopus 로고
    • Purification and biochemical characterization of CP4 (SP-D), a collagenous surfactant-associated protein
    • Persson A., Chang D., Rust K., Moxley M., Longmore W., Crouch E.C. Purification and biochemical characterization of CP4 (SP-D), a collagenous surfactant-associated protein. Biochemistry. 28:1989;6361-6367.
    • (1989) Biochemistry , vol.28 , pp. 6361-6367
    • Persson, A.1    Chang, D.2    Rust, K.3    Moxley, M.4    Longmore, W.5    Crouch, E.C.6
  • 91
    • 0026630978 scopus 로고
    • Pulmonary surfactant protein SP-C causes packing rearrangements of dipalmitoylphosphatidylcholine in spread monolayers
    • Pérez-Gil J., Nag K., Taneva S., Keough K.M. Pulmonary surfactant protein SP-C causes packing rearrangements of dipalmitoylphosphatidylcholine in spread monolayers. Biophys. J. 63:1992;197-204.
    • (1992) Biophys. J. , vol.63 , pp. 197-204
    • Pérez-Gil, J.1    Nag, K.2    Taneva, S.3    Keough, K.M.4
  • 92
    • 0022327720 scopus 로고
    • A comparison of the major surfactant-associated proteins in different species
    • Phelps D.S., Taeusch H.W.J. A comparison of the major surfactant-associated proteins in different species. Comp. Biochem. Physiol. B. 82:1985;441-446.
    • (1985) Comp. Biochem. Physiol. B , vol.82 , pp. 441-446
    • Phelps, D.S.1    Taeusch, H.W.J.2
  • 93
    • 0018608269 scopus 로고
    • Hydrophobic proteins of lamellated osmiophilic bodies isolated from pig lung
    • Phizackerley P.J., Town M.H., Newman G.E. Hydrophobic proteins of lamellated osmiophilic bodies isolated from pig lung. Biochem. J. 183:1979;731-736.
    • (1979) Biochem. J. , vol.183 , pp. 731-736
    • Phizackerley, P.J.1    Town, M.H.2    Newman, G.E.3
  • 94
    • 0024515871 scopus 로고
    • Structure and organization of the gene encoding human pulmonary surfactant proteolipid SP-B
    • Pilot-Matias T.J., Kister S.E., Fox J.L., Kropp K., Glasser S.W., Whitsett J.A. Structure and organization of the gene encoding human pulmonary surfactant proteolipid SP-B. DNA. 8:1989;75-86.
    • (1989) DNA , vol.8 , pp. 75-86
    • Pilot-Matias, T.J.1    Kister, S.E.2    Fox, J.L.3    Kropp, K.4    Glasser, S.W.5    Whitsett, J.A.6
  • 95
    • 0023765992 scopus 로고
    • A proposed nomenclature for pulmonary surfactant-associated proteins
    • Possmayer F. A proposed nomenclature for pulmonary surfactant-associated proteins. Am. Rev. Respir. Dis. 138:1988;990-998.
    • (1988) Am. Rev. Respir. Dis. , vol.138 , pp. 990-998
    • Possmayer, F.1
  • 96
    • 0029855554 scopus 로고    scopus 로고
    • Role of the palmitoylation of surfactant-associated protein C in surfactant film formation and stability
    • Qanbar R., Cheng S., Possmayer F., Schürch S. Role of the palmitoylation of surfactant-associated protein C in surfactant film formation and stability. Am. J. Physiol. 271:1996;L572-L580.
    • (1996) Am. J. Physiol. , vol.271
    • Qanbar, R.1    Cheng, S.2    Possmayer, F.3    Schürch, S.4
  • 97
    • 0031772692 scopus 로고    scopus 로고
    • Interactions of surfactant protein D with pathogens, allergens and phagocytes
    • Reid K.B. Interactions of surfactant protein D with pathogens, allergens and phagocytes. Biochim. Biophys. Acta. 1408:1998;290-295.
    • (1998) Biochim. Biophys. Acta , vol.1408 , pp. 290-295
    • Reid, K.B.1
  • 98
    • 0023639984 scopus 로고
    • Surfactant-associated protein inhibits phospholipid secretion from type II cells
    • Rice W.R., Ross G.F., Singleton F.M., Dingle S., Whitsett J.A. Surfactant-associated protein inhibits phospholipid secretion from type II cells. J. Appl. Physiol. 63:1987;692-698.
    • (1987) J. Appl. Physiol. , vol.63 , pp. 692-698
    • Rice, W.R.1    Ross, G.F.2    Singleton, F.M.3    Dingle, S.4    Whitsett, J.A.5
  • 99
    • 0025954412 scopus 로고
    • Human surfactant protein D: SP-D contains a C-type lectin carbohydrate recognition domain
    • Rust K., Grosso L., Zhang V., et al. Human surfactant protein D: SP-D contains a C-type lectin carbohydrate recognition domain. Arch. Biochem. Biophys. 290:1991;116-126.
    • (1991) Arch. Biochem. Biophys. , vol.290 , pp. 116-126
    • Rust, K.1    Grosso, L.2    Zhang, V.3
  • 100
    • 0023216264 scopus 로고
    • Isolation and sequence of a cDNA clone for the rat pulmonary surfactant-associated protein (PSP-A)
    • Sano K., Fisher J., Mason R.J., et al. Isolation and sequence of a cDNA clone for the rat pulmonary surfactant-associated protein (PSP-A). Biochem. Biophys. Res. Commun. 144:1987;367-374.
    • (1987) Biochem. Biophys. Res. Commun. , vol.144 , pp. 367-374
    • Sano, K.1    Fisher, J.2    Mason, R.J.3
  • 101
    • 0026675709 scopus 로고
    • Pulmonary SP-A enhances adsorption and appears to induce surface sorting of lipid extract surfactant
    • Schürch S., Possmayer F., Cheng S., Cockshutt A.M. Pulmonary SP-A enhances adsorption and appears to induce surface sorting of lipid extract surfactant. Am. J. Physiol. 263:1992;L210-L218.
    • (1992) Am. J. Physiol. , vol.263
    • Schürch, S.1    Possmayer, F.2    Cheng, S.3    Cockshutt, A.M.4
  • 102
    • 0029026845 scopus 로고
    • The surface-associated surfactant reservoir in the alveolar lining
    • Schürch S., Qanbar R., Bachofen H., Possmayer F. The surface-associated surfactant reservoir in the alveolar lining. Biol. Neonate. 67:(Suppl. 1):1995;61-76.
    • (1995) Biol. Neonate , vol.67 , Issue.SUPPL. 1 , pp. 61-76
    • Schürch, S.1    Qanbar, R.2    Bachofen, H.3    Possmayer, F.4
  • 103
    • 0026508881 scopus 로고
    • Primary structure of rat pulmonary surfactant protein D. cDNA and deduced amino acid sequence
    • Shimizu H., Fisher J.H., Papst P., et al. Primary structure of rat pulmonary surfactant protein D. cDNA and deduced amino acid sequence. J. Biol. Chem. 267:1992;1853-1857.
    • (1992) J. Biol. Chem. , vol.267 , pp. 1853-1857
    • Shimizu, H.1    Fisher, J.H.2    Papst, P.3
  • 104
    • 0027955997 scopus 로고
    • A saposin-like domain influences the intracellular localization, stability, and catalytic activity of human acyloxyacyl hydrolase
    • Staab J.F., Ginkel D.L., Rosenberg G.B., Munford R.S. A saposin-like domain influences the intracellular localization, stability, and catalytic activity of human acyloxyacyl hydrolase. J. Biol. Chem. 269:1994;23736-23742.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23736-23742
    • Staab, J.F.1    Ginkel, D.L.2    Rosenberg, G.B.3    Munford, R.S.4
  • 105
    • 0026580731 scopus 로고
    • Human surfactant protein-A contains blood group A antigenic determinants
    • Stahlman M.T., Gray M.E., Ross G.F., et al. Human surfactant protein-A contains blood group A antigenic determinants. Pediatr. Res. 31:1992;364-371.
    • (1992) Pediatr. Res. , vol.31 , pp. 364-371
    • Stahlman, M.T.1    Gray, M.E.2    Ross, G.F.3
  • 106
    • 0032956572 scopus 로고    scopus 로고
    • Surfactant protein A enhances the binding and deacylation of E. coli LPS by alveolar macrophages
    • Stamme C., Wright J.R. Surfactant protein A enhances the binding and deacylation of E. coli LPS by alveolar macrophages. Am. J. Physiol. 276:1999;L540-L547.
    • (1999) Am. J. Physiol. , vol.276
    • Stamme, C.1    Wright, J.R.2
  • 108
    • 0031913586 scopus 로고    scopus 로고
    • Conservation of surfactant protein A: Evidence for a single origin for vertebrate pulmonary surfactant
    • Sullivan L.C., Daniels C.B., Phillips I.D., Orgeig S., Whitsett J.A. Conservation of surfactant protein A: evidence for a single origin for vertebrate pulmonary surfactant. J. Mol. Evol. 46:1998;131-138.
    • (1998) J. Mol. Evol. , vol.46 , pp. 131-138
    • Sullivan, L.C.1    Daniels, C.B.2    Phillips, I.D.3    Orgeig, S.4    Whitsett, J.A.5
  • 109
    • 0024333716 scopus 로고
    • Reconstitution of tubular myelin from synthetic lipids and proteins associated with pig pulmonary surfactant
    • Suzuki Y., Fujita Y., Kogishi K. Reconstitution of tubular myelin from synthetic lipids and proteins associated with pig pulmonary surfactant. Am. Rev. Respir. Dis. 140:1989;75-81.
    • (1989) Am. Rev. Respir. Dis. , vol.140 , pp. 75-81
    • Suzuki, Y.1    Fujita, Y.2    Kogishi, K.3
  • 110
    • 0022360059 scopus 로고
    • Cloning and sequencing of cDNA of Sarcophaga peregrina humoral lectin induced on injury of the body wall
    • Takahashi H., Komano H., Kawaguchi N., Kitamura N., Nakanishi S., Natori S. Cloning and sequencing of cDNA of Sarcophaga peregrina humoral lectin induced on injury of the body wall. J. Biol. Chem. 260:1985;12228-12233.
    • (1985) J. Biol. Chem. , vol.260 , pp. 12228-12233
    • Takahashi, H.1    Komano, H.2    Kawaguchi, N.3    Kitamura, N.4    Nakanishi, S.5    Natori, S.6
  • 111
    • 0024324970 scopus 로고
    • Structures and functions associated with the group of mammalian lectins containing collagen-like sequences
    • Thiel S., Reid K.B. Structures and functions associated with the group of mammalian lectins containing collagen-like sequences. FEBS Lett. 250:1989;78-84.
    • (1989) FEBS Lett. , vol.250 , pp. 78-84
    • Thiel, S.1    Reid, K.B.2
  • 112
    • 0031772263 scopus 로고    scopus 로고
    • Interactions of surfactant protein A with epithelial cells and phagocytes
    • Tino M.J., Wright J.R. Interactions of surfactant protein A with epithelial cells and phagocytes. Biochim. Biophys. Acta. 1408:1998;241-263.
    • (1998) Biochim. Biophys. Acta , vol.1408 , pp. 241-263
    • Tino, M.J.1    Wright, J.R.2
  • 113
    • 0027163697 scopus 로고
    • Tracing the immune system's evolutionary history
    • Travis J. Tracing the immune system's evolutionary history. Science. 261:1993;164-165.
    • (1993) Science , vol.261 , pp. 164-165
    • Travis, J.1
  • 114
    • 0028948823 scopus 로고
    • Structural analysis of saposin C and B. Complete localization of disulfide bridges
    • Vaccaro A.M., Salvioli R., Barca A., et al. Structural analysis of saposin C and B. Complete localization of disulfide bridges. J. Biol. Chem. 270:1995;9953-9960.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9953-9960
    • Vaccaro, A.M.1    Salvioli, R.2    Barca, A.3
  • 116
    • 0034142378 scopus 로고    scopus 로고
    • Porcine lung surfactant protein D: Complementary DNA cloning, chromosomal localization, and tissue distribution
    • van Eijk M., Haagsman H.P., Skinner T., Archibold A., Reid K.B., Lawson P.R. Porcine lung surfactant protein D: complementary DNA cloning, chromosomal localization, and tissue distribution. J. Immunol. 164:2000;1442-1450.
    • (2000) J. Immunol. , vol.164 , pp. 1442-1450
    • Van Eijk, M.1    Haagsman, H.P.2    Skinner, T.3    Archibold, A.4    Reid, K.B.5    Lawson, P.R.6
  • 117
    • 0026469338 scopus 로고
    • Binding of surfactant protein A (SP-A) to herpes simplex virus type 1-infected cells is mediated by the carbohydrate moiety of SP-A
    • van Iwaarden J.F., van Strijp J.A., Visser H., Haagsman H.P., Verhoef J., van Golde L.M.G. Binding of surfactant protein A (SP-A) to herpes simplex virus type 1-infected cells is mediated by the carbohydrate moiety of SP-A. J. Biol. Chem. 267:1992;25039-25043.
    • (1992) J. Biol. Chem. , vol.267 , pp. 25039-25043
    • Van Iwaarden, J.F.1    Van Strijp, J.A.2    Visser, H.3    Haagsman, H.P.4    Verhoef, J.5    Van Golde, L.M.G.6
  • 121
    • 0033945468 scopus 로고    scopus 로고
    • Dimeric N-terminal segment of human surfactant protein B (dSP-B1-25) has enhanced surface properties compared to monomeric SP-B1-25
    • Veldhuizen E.J.A., Waring A.J., Walther F.J., Batenburg J.J., van Golde L.M.G., Haagsman H.P. Dimeric N-terminal segment of human surfactant protein B (dSP-B1-25) has enhanced surface properties compared to monomeric SP-B1-25. Biophys. J. 79:2000;377-384.
    • (2000) Biophys. J. , vol.79 , pp. 377-384
    • Veldhuizen, E.J.A.1    Waring, A.J.2    Walther, F.J.3    Batenburg, J.J.4    Van Golde, L.M.G.5    Haagsman, H.P.6
  • 122
    • 0030842893 scopus 로고    scopus 로고
    • The phase behavior of lipid monolayers containing pulmonary surfactant protein C studied by fluorescence light microscopy
    • von Nahmen A., Post A., Galla H.J., Sieber M. The phase behavior of lipid monolayers containing pulmonary surfactant protein C studied by fluorescence light microscopy. Eur. Biophys. J. 26:1997;359-369.
    • (1997) Eur. Biophys. J. , vol.26 , pp. 359-369
    • Von Nahmen, A.1    Post, A.2    Galla, H.J.3    Sieber, M.4
  • 123
    • 0031019895 scopus 로고    scopus 로고
    • The structure of a model pulmonary surfactant as revealed by scanning force microscopy
    • von Nahmen A., Schenk M., Sieber M., Amrein M. The structure of a model pulmonary surfactant as revealed by scanning force microscopy. Biophys. J. 72:1997;463-469.
    • (1997) Biophys. J. , vol.72 , pp. 463-469
    • Von Nahmen, A.1    Schenk, M.2    Sieber, M.3    Amrein, M.4
  • 125
    • 0000455402 scopus 로고
    • Neue Auffassungen über einen Grundbegriff der Atemmechanik
    • von Neergaard K. Neue Auffassungen über einen Grundbegriff der Atemmechanik. Z. Gesamte Exp. Med. 66:1929;373-394.
    • (1929) Z. Gesamte Exp. Med. , vol.66 , pp. 373-394
    • Von Neergaard, K.1
  • 126
    • 0023890913 scopus 로고
    • Macromolecular organization of natural and recombinant lung surfactant protein SP 28-36. Structural homology with the complement factor C1q
    • Voss T., Eistetter H., Schafer K.P., Engel J. Macromolecular organization of natural and recombinant lung surfactant protein SP 28-36. Structural homology with the complement factor C1q. J. Mol. Biol. 201:1988;219-227.
    • (1988) J. Mol. Biol. , vol.201 , pp. 219-227
    • Voss, T.1    Eistetter, H.2    Schafer, K.P.3    Engel, J.4
  • 127
    • 0026085036 scopus 로고
    • Structural comparison of recombinant pulmonary surfactant protein SP-A derived from two human coding sequences: Implications for the chain composition of natural human SP-A
    • Voss T., Melchers K., Scheirle G., Schafer K.P. Structural comparison of recombinant pulmonary surfactant protein SP-A derived from two human coding sequences: implications for the chain composition of natural human SP-A. Am. J. Respir. Cell. Mol. Biol. 4:1991;88-94.
    • (1991) Am. J. Respir. Cell. Mol. Biol. , vol.4 , pp. 88-94
    • Voss, T.1    Melchers, K.2    Scheirle, G.3    Schafer, K.P.4
  • 128
    • 0022456402 scopus 로고
    • Immunocytochemical localization of the major surfactant apoproteins in type II cells, Clara cells, and alveolar macrophages of rat lung
    • Walker S.R., Williams M.C., Benson B. Immunocytochemical localization of the major surfactant apoproteins in type II cells, Clara cells, and alveolar macrophages of rat lung. J. Histochem. Cytochem. 34:1986;1137-1148.
    • (1986) J. Histochem. Cytochem. , vol.34 , pp. 1137-1148
    • Walker, S.R.1    Williams, M.C.2    Benson, B.3
  • 129
    • 0029822715 scopus 로고    scopus 로고
    • Interaction of human lung surfactant proteins A and D with mite (Dermatophagoides pteronyssinus) allergens
    • Wang J.Y., Kishore U., Lim B.L., Strong P., Reid K.B. Interaction of human lung surfactant proteins A and D with mite (Dermatophagoides pteronyssinus) allergens. Clin. Exp. Immunol. 106:1996;367-373.
    • (1996) Clin. Exp. Immunol. , vol.106 , pp. 367-373
    • Wang, J.Y.1    Kishore, U.2    Lim, B.L.3    Strong, P.4    Reid, K.B.5
  • 130
    • 0345696724 scopus 로고
    • Low molecular weight human pulmonary surfactant protein (SP5): Isolation, characterization, and cDNA and amino acid sequences
    • Warr R.G., Hawgood S., Buckley D.I., et al. Low molecular weight human pulmonary surfactant protein (SP5): isolation, characterization, and cDNA and amino acid sequences. Proc. Natl. Acad. Sci. USA. 84:1987;7915-7919.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7915-7919
    • Warr, R.G.1    Hawgood, S.2    Buckley, D.I.3
  • 131
    • 0031820273 scopus 로고    scopus 로고
    • The C-type lectin superfamily in the immune system
    • Weis W.I., Taylor M.E., Drickamer K. The C-type lectin superfamily in the immune system. Immunol. Rev. 163:1998;19-34.
    • (1998) Immunol. Rev. , vol.163 , pp. 19-34
    • Weis, W.I.1    Taylor, M.E.2    Drickamer, K.3
  • 133
    • 0026197257 scopus 로고
    • Changes in lipid structure produced by surfactant proteins SP-A, SP-B, and SP-C
    • Williams M.C., Hawgood S., Hamilton R.L. Changes in lipid structure produced by surfactant proteins SP-A, SP-B, and SP-C. Am. J. Respir. Cell. Mol. Biol. 5:1991;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
  • 135
    • 0024358493 scopus 로고
    • Lung surfactant apoprotein SP-A (26-36 kDa) binds with high affinity to isolated alveolar type II cells
    • Wright J.R., Borchelt J.D., Hawgood S. Lung surfactant apoprotein SP-A (26-36 kDa) binds with high affinity to isolated alveolar type II cells. Proc. Natl. Acad. Sci. USA. 86:1989;5410-5414.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5410-5414
    • Wright, J.R.1    Borchelt, J.D.2    Hawgood, S.3
  • 136
    • 0023658582 scopus 로고
    • Characterization of the small hydrophobic proteins associated with pulmonary surfactant
    • Yu S.H., Chung W., Olafson R.W., Harding P.G., Possmayer F. Characterization of the small hydrophobic proteins associated with pulmonary surfactant. Biochim. Biophys. Acta. 921:1987;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
  • 137
    • 0026638739 scopus 로고
    • Effect of pulmonary surfactant protein B (SP-B) and calcium on phospholipid adsorption and squeeze-out of phosphatidylglycerol from binary phospholipid monolayers containing dipalmitoylphosphatidylcholine
    • Yu S.H., Possmayer F. Effect of pulmonary surfactant protein B (SP-B) and calcium on phospholipid adsorption and squeeze-out of phosphatidylglycerol from binary phospholipid monolayers containing dipalmitoylphosphatidylcholine. Biochim. Biophys. Acta. 1126:1992;26-34.
    • (1992) Biochim. Biophys. Acta , vol.1126 , pp. 26-34
    • Yu, S.H.1    Possmayer, F.2
  • 138
    • 0031759376 scopus 로고    scopus 로고
    • Thyroid transcription factor-1, hepatocyte nuclear factor-3beta and surfactant protein A and B in the developing chick lung
    • Zeng X., Yutzey K.E., Whitsett J.A. Thyroid transcription factor-1, hepatocyte nuclear factor-3beta and surfactant protein A and B in the developing chick lung. J. Anat. 193:1998;399-408.
    • (1998) J. Anat. , vol.193 , pp. 399-408
    • Zeng, X.1    Yutzey, K.E.2    Whitsett, J.A.3


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