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Volumn 7, Issue 10, 2012, Pages

"SP-G", a Putative New Surfactant Protein - Tissue Localization and 3D Structure

Author keywords

[No Author keywords available]

Indexed keywords

PEPTIDES AND PROTEINS; SURFACTANT PROTEIN B; SURFACTANT PROTEIN C; SURFACTANT PROTEIN G; UNCLASSIFIED DRUG;

EID: 84867627987     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0047789     Document Type: Article
Times cited : (26)

References (82)
  • 1
    • 0025118727 scopus 로고
    • Role of bovine pulmonary surfactant-associated proteins in the surface-active property of phospholipid mixtures
    • Yu SH, Possmayer F, (1990) Role of bovine pulmonary surfactant-associated proteins in the surface-active property of phospholipid mixtures. Biochim Biophys Acta 1046: 233-241.
    • (1990) Biochim Biophys Acta , vol.1046 , pp. 233-241
    • Yu, S.H.1    Possmayer, F.2
  • 2
    • 0035048532 scopus 로고    scopus 로고
    • Surfactant proteins a and d and pulmonary host defense
    • Crouch E, Wright JR, (2001) Surfactant proteins a and d and pulmonary host defense. Annu Rev Physiol 63: 521-554.
    • (2001) Annu Rev Physiol , vol.63 , pp. 521-554
    • Crouch, E.1    Wright, J.R.2
  • 4
    • 0033168175 scopus 로고    scopus 로고
    • Surfactant Protein D Binds to Mycobacterium tuberculosis Bacilli and Lipoarabinomannan via Carbohydrate-Lectin Interactions Resulting in Reduced Phagocytosis of the Bacteria by Macrophages1
    • Ferguson JS, Voelker DR, McCormack FX, Schlesinger LS, (1999) Surfactant Protein D Binds to Mycobacterium tuberculosis Bacilli and Lipoarabinomannan via Carbohydrate-Lectin Interactions Resulting in Reduced Phagocytosis of the Bacteria by Macrophages1. J Immunol 163: 312-321.
    • (1999) J Immunol , vol.163 , pp. 312-321
    • Ferguson, J.S.1    Voelker, D.R.2    McCormack, F.X.3    Schlesinger, L.S.4
  • 6
    • 11244287371 scopus 로고    scopus 로고
    • Immunoregulatory functions of surfactant proteins
    • Wright JR, (2005) Immunoregulatory functions of surfactant proteins. Nat Rev Immunol 5: 58-68.
    • (2005) Nat Rev Immunol , vol.5 , pp. 58-68
    • Wright, J.R.1
  • 7
    • 33644828798 scopus 로고    scopus 로고
    • Surfactant proteins SP-A and SP-D: structure, function and receptors
    • Kishore U, Greenhough TJ, Waters P, Shrive AK, Ghai R, et al. (2006) Surfactant proteins SP-A and SP-D: structure, function and receptors. Mol Immunol 43: 1293-1315.
    • (2006) Mol Immunol , vol.43 , pp. 1293-1315
    • Kishore, U.1    Greenhough, T.J.2    Waters, P.3    Shrive, A.K.4    Ghai, R.5
  • 8
    • 0035008879 scopus 로고    scopus 로고
    • Surfactant proteins in the digestive tract, mesentery, and other organs: evolutionary significance
    • Bourbon JR, Chailley-Heu B, (2001) Surfactant proteins in the digestive tract, mesentery, and other organs: evolutionary significance. Comp Biochem Physiol A Mol Integr Physiol 129: 151-161.
    • (2001) Comp Biochem Physiol A Mol Integr Physiol , vol.129 , pp. 151-161
    • Bourbon, J.R.1    Chailley-Heu, B.2
  • 9
    • 35148861531 scopus 로고    scopus 로고
    • Detection of Surfactant Proteins A and D in Human Tear Fluid and the Human Lacrimal System
    • Bräuer L, Kindler C, Jäger K, Sel S, Nölle B, et al. (2007) Detection of Surfactant Proteins A and D in Human Tear Fluid and the Human Lacrimal System. Invest Ophthalmol Vis Sci 48: 3945-3953.
    • (2007) Invest Ophthalmol Vis Sci , vol.48 , pp. 3945-3953
    • Bräuer, L.1    Kindler, C.2    Jäger, K.3    Sel, S.4    Nölle, B.5
  • 10
    • 69249216424 scopus 로고    scopus 로고
    • Human parotid and submandibular glands express and secrete surfactant proteins A, B, C and D
    • Bräuer L, Möschter S, Beileke S, Jäger K, Garreis F, et al. (2009) Human parotid and submandibular glands express and secrete surfactant proteins A, B, C and D. Histochem Cell Biol. 132: 331-338.
    • (2009) Histochem Cell Biol , vol.132 , pp. 331-338
    • Bräuer, L.1    Möschter, S.2    Beileke, S.3    Jäger, K.4    Garreis, F.5
  • 11
    • 84858665908 scopus 로고    scopus 로고
    • Detection of surfactant proteins A, B, C, and D in human gingiva and saliva
    • Bräuer L, Schicht M, Stengl C, Heinemann F, Götz W, et al. (2012) Detection of surfactant proteins A, B, C, and D in human gingiva and saliva. Biomed Tech (Berl) 57: 59-64.
    • (2012) Biomed Tech (Berl) , vol.57 , pp. 59-64
    • Bräuer, L.1    Schicht, M.2    Stengl, C.3    Heinemann, F.4    Götz, W.5
  • 13
    • 0023225188 scopus 로고
    • Biophysical activity of synthetic phospholipids combined with purified lung surfactant 6000 dalton apoprotein
    • Notter RH, Shapiro DL, Ohning B, Whitsett JA, (1987) Biophysical activity of synthetic phospholipids combined with purified lung surfactant 6000 dalton apoprotein. Chem Phys Lipids 44: 1-17.
    • (1987) Chem Phys Lipids , vol.44 , pp. 1-17
    • Notter, R.H.1    Shapiro, D.L.2    Ohning, B.3    Whitsett, J.A.4
  • 15
    • 15544369388 scopus 로고    scopus 로고
    • Surfactant Protein C Biosynthesis and Its Emerging Role in Conformational Lung Disease
    • Beers MF, Mulugeta S, (2005) Surfactant Protein C Biosynthesis and Its Emerging Role in Conformational Lung Disease. Annu Rev Physiol 67: 663-696.
    • (2005) Annu Rev Physiol , vol.67 , pp. 663-696
    • Beers, M.F.1    Mulugeta, S.2
  • 16
    • 36248985816 scopus 로고    scopus 로고
    • Detection and Localization of the Hydrophobic Surfactant Proteins B and C in Human Tear Fluid and the Human Lacrimal System
    • Bräuer L, Johl M, Börgermann J, Pleyer U, Tsokos M, et al. (2007) Detection and Localization of the Hydrophobic Surfactant Proteins B and C in Human Tear Fluid and the Human Lacrimal System. Curr Eye Res 32: 931-938.
    • (2007) Curr Eye Res , vol.32 , pp. 931-938
    • Bräuer, L.1    Johl, M.2    Börgermann, J.3    Pleyer, U.4    Tsokos, M.5
  • 17
    • 4644320152 scopus 로고    scopus 로고
    • Signal peptide prediction based on analysis of experimentally verified cleavage sites
    • Zhang Z, Henzel WJ, (2004) Signal peptide prediction based on analysis of experimentally verified cleavage sites. Protein Sci 13: 2819-2824.
    • (2004) Protein Sci , vol.13 , pp. 2819-2824
    • Zhang, Z.1    Henzel, W.J.2
  • 18
    • 0033909566 scopus 로고    scopus 로고
    • Protein sorting signals and prediction of subcellular localization
    • Nakai K, (2000) Protein sorting signals and prediction of subcellular localization. Adv Protein Chem 54: 277-344.
    • (2000) Adv Protein Chem , vol.54 , pp. 277-344
    • Nakai, K.1
  • 19
    • 78651324042 scopus 로고    scopus 로고
    • CREB in long-term potentiation in hippocampus: role of post-translational modifications-studies In silico
    • Kaleem A, Hoessli DC, Haq IU, Walker-Nasir E, Butt A, et al. (2011) CREB in long-term potentiation in hippocampus: role of post-translational modifications-studies In silico. J Cell Biochem 112: 138-146.
    • (2011) J Cell Biochem , vol.112 , pp. 138-146
    • Kaleem, A.1    Hoessli, D.C.2    Haq, I.U.3    Walker-Nasir, E.4    Butt, A.5
  • 20
    • 0031772193 scopus 로고    scopus 로고
    • Synthesis, processing and secretion of surfactant proteins B and C
    • Weaver TE, (1998) Synthesis, processing and secretion of surfactant proteins B and C. Biochim Biophys Acta. 1408: 173-179.
    • (1998) Biochim Biophys Acta , vol.1408 , pp. 173-179
    • Weaver, T.E.1
  • 21
    • 0037215592 scopus 로고    scopus 로고
    • Cysteine protease activity is required for surfactant protein B processing and lamellar body genesis
    • Guttentag S, Robinson L, Zhang P, Brasch F, Bühling F, et al. (2003) Cysteine protease activity is required for surfactant protein B processing and lamellar body genesis. Am J Respir Cell Mol Biol 28: 69-79.
    • (2003) Am J Respir Cell Mol Biol , vol.28 , pp. 69-79
    • Guttentag, S.1    Robinson, L.2    Zhang, P.3    Brasch, F.4    Bühling, F.5
  • 22
    • 0036384267 scopus 로고    scopus 로고
    • Specific mode of interaction between components of model pulmonary surfactants using computer simulations
    • Kaznessis YN, Kim S, Larson RG, (2002) Specific mode of interaction between components of model pulmonary surfactants using computer simulations. J Mol Biol 322: 569-582.
    • (2002) J Mol Biol , vol.322 , pp. 569-582
    • Kaznessis, Y.N.1    Kim, S.2    Larson, R.G.3
  • 23
    • 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 SK, Larson RG, (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
  • 24
    • 77954658153 scopus 로고    scopus 로고
    • Folding of lipid monolayers containing lung surfactant proteins SP-B(1-25) and SP-C studied via coarse-grained molecular dynamics simulations
    • Duncan SL, Larson RG, (2010) Folding of lipid monolayers containing lung surfactant proteins SP-B(1-25) and SP-C studied via coarse-grained molecular dynamics simulations. Biochim Biophys Acta 1798: 1632-1650.
    • (2010) Biochim Biophys Acta , vol.1798 , pp. 1632-1650
    • Duncan, S.L.1    Larson, R.G.2
  • 25
    • 79959670131 scopus 로고    scopus 로고
    • Lung surfactant protein SP-B promotes formation of bilayer reservoirs from monolayer and lipid transfer between the interface and subphase
    • Baoukina S, Tieleman DP, (2011) Lung surfactant protein SP-B promotes formation of bilayer reservoirs from monolayer and lipid transfer between the interface and subphase. Biophys J 100: 1678-1687.
    • (2011) Biophys J , vol.100 , pp. 1678-1687
    • Baoukina, S.1    Tieleman, D.P.2
  • 26
    • 0037093644 scopus 로고    scopus 로고
    • Increasing the precision of comparative models with YASARA NOVA-a self-parameterizing force field
    • Krieger E, Koraimann G, Vriend G, (2002) Increasing the precision of comparative models with YASARA NOVA-a self-parameterizing force field. Proteins 47: 393-402.
    • (2002) Proteins , vol.47 , pp. 393-402
    • Krieger, E.1    Koraimann, G.2    Vriend, G.3
  • 27
    • 74249090260 scopus 로고    scopus 로고
    • Improving physical realism, stereochemistry, and side-chain accuracy in homology modeling: Four approaches that performed well in CASP8
    • Krieger E, Joo K, Lee J, Lee J, Raman S, et al. (2009) Improving physical realism, stereochemistry, and side-chain accuracy in homology modeling: Four approaches that performed well in CASP8. Proteins 77Suppl 9: 114-122.
    • (2009) Proteins , vol.77 , pp. 114-122
    • Krieger, E.1    Joo, K.2    Lee, J.3    Lee, J.4    Raman, S.5
  • 28
    • 36749061828 scopus 로고    scopus 로고
    • Template-based modeling and free modeling by I-TASSER in CASP7
    • Zhang Y, (2007) Template-based modeling and free modeling by I-TASSER in CASP7. Proteins 69Suppl 8: 108-117.
    • (2007) Proteins , vol.69 , pp. 108-117
    • Zhang, Y.1
  • 29
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: a unified platform for automated protein structure and function prediction
    • Roy A, Kucukural A, Zhang Y, (2010) I-TASSER: a unified platform for automated protein structure and function prediction. Nat Protoc 5: 725-738.
    • (2010) Nat Protoc , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 30
    • 47349110113 scopus 로고    scopus 로고
    • A template-finding algorithm and a comprehensive benchmark for homology modeling of proteins
    • Vallat BK, Pillardy J, Elber R, (2008) A template-finding algorithm and a comprehensive benchmark for homology modeling of proteins. Proteins 72: 910-928.
    • (2008) Proteins , vol.72 , pp. 910-928
    • Vallat, B.K.1    Pillardy, J.2    Elber, R.3
  • 31
    • 68149132088 scopus 로고    scopus 로고
    • Building and assessing atomic models of proteins from structural templates: learning and benchmarks
    • Vallat BK, Pillardy J, Majek P, Meller J, Blom T, et al. (2009) Building and assessing atomic models of proteins from structural templates: learning and benchmarks. Proteins 76: 930-945.
    • (2009) Proteins , vol.76 , pp. 930-945
    • Vallat, B.K.1    Pillardy, J.2    Majek, P.3    Meller, J.4    Blom, T.5
  • 32
    • 3242887695 scopus 로고    scopus 로고
    • Protein structure prediction and analysis using the Robetta server
    • Kim DE, Chivian D, Baker D, (2004) Protein structure prediction and analysis using the Robetta server. Nucleic Acids Res 32: W526-W531.
    • (2004) Nucleic Acids Res , vol.32
    • Kim, D.E.1    Chivian, D.2    Baker, D.3
  • 33
    • 0000243829 scopus 로고
    • PROCHECK: a program to check the stereochemical quality of protein structures
    • Laskowski RA, MacArthur DS, Moss DS, Thornton JM, (1993) PROCHECK: a program to check the stereochemical quality of protein structures. J Appl Cryst 26: 283-291.
    • (1993) J Appl Cryst , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, D.S.2    Moss, D.S.3    Thornton, J.M.4
  • 34
    • 0027490731 scopus 로고
    • Recognition of errors in three-dimensional structures of proteins
    • Sippl MJ, (1993) Recognition of errors in three-dimensional structures of proteins. Proteins 17: 355-362.
    • (1993) Proteins , vol.17 , pp. 355-362
    • Sippl, M.J.1
  • 36
    • 10344223464 scopus 로고    scopus 로고
    • Making optimal use of empirical energy functions: force-field parameterization in crystal space
    • Krieger E, Darden T, Nabuurs SB, Finkelstein A, Vriend G, (2004) Making optimal use of empirical energy functions: force-field parameterization in crystal space. Proteins 57: 678-683.
    • (2004) Proteins , vol.57 , pp. 678-683
    • Krieger, E.1    Darden, T.2    Nabuurs, S.B.3    Finkelstein, A.4    Vriend, G.5
  • 39
    • 16344366696 scopus 로고    scopus 로고
    • NetAcet: prediction of N-terminal acetylation sites
    • Kiemer L, Bendtsen JD, Blom N, (2005) NetAcet: prediction of N-terminal acetylation sites. Bioinformatics 21: 1269-1270.
    • (2005) Bioinformatics , vol.21 , pp. 1269-1270
    • Kiemer, L.1    Bendtsen, J.D.2    Blom, N.3
  • 40
    • 2942564430 scopus 로고    scopus 로고
    • Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence
    • Blom N, Sicheritz-Ponten T, Gupta R, Gammeltoft S, Brunak S, (2004) Prediction of post-translational glycosylation and phosphorylation of proteins from the amino acid sequence. Proteomics 4: 1633-1649.
    • (2004) Proteomics , vol.4 , pp. 1633-1649
    • Blom, N.1    Sicheritz-Ponten, T.2    Gupta, R.3    Gammeltoft, S.4    Brunak, S.5
  • 41
    • 13644257223 scopus 로고    scopus 로고
    • Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites
    • Julenius K, Molgaard A, Gupta R, Brunak S, (2005) Prediction, conservation analysis, and structural characterization of mammalian mucin-type O-glycosylation sites. Glycobiology 15: 153-164.
    • (2005) Glycobiology , vol.15 , pp. 153-164
    • Julenius, K.1    Molgaard, A.2    Gupta, R.3    Brunak, S.4
  • 42
    • 0036370537 scopus 로고    scopus 로고
    • Prediction of glycosylation across the human proteome and the correlation to protein function
    • Gupta R, Brunak S (2002) Prediction of glycosylation across the human proteome and the correlation to protein function. Pac Symp Biocomput: 310-322.
    • (2002) Pac Symp Biocomput , pp. 310-322
    • Gupta, R.1    Brunak, S.2
  • 43
    • 0033579464 scopus 로고    scopus 로고
    • Sequence and structure-based prediction of eukaryotic protein phosphorylation sites
    • Blom N, Gammeltoft S, Brunak S, (1999) Sequence and structure-based prediction of eukaryotic protein phosphorylation sites. J Mol Biol 294: 1351-1362.
    • (1999) J Mol Biol , vol.294 , pp. 1351-1362
    • Blom, N.1    Gammeltoft, S.2    Brunak, S.3
  • 44
    • 54249148026 scopus 로고    scopus 로고
    • CSS-Palm 2.0: an updated software for palmitoylation sites prediction
    • Ren J, Wen L, Gao X, Jin C, Xue Y, et al. (2008) CSS-Palm 2.0: an updated software for palmitoylation sites prediction. Protein Eng Des Sel 21: 639-644.
    • (2008) Protein Eng Des Sel , vol.21 , pp. 639-644
    • Ren, J.1    Wen, L.2    Gao, X.3    Jin, C.4    Xue, Y.5
  • 45
    • 0037944247 scopus 로고    scopus 로고
    • Lipid compositional analysis of pulmonary surfactant monolayers and monolayer-associated reservoirs
    • Yu SH, Possmayer F, (2003) Lipid compositional analysis of pulmonary surfactant monolayers and monolayer-associated reservoirs. J Lipid Res 44: 621-629.
    • (2003) J Lipid Res , vol.44 , pp. 621-629
    • Yu, S.H.1    Possmayer, F.2
  • 46
    • 10044228172 scopus 로고    scopus 로고
    • More than a monolayer: relating lung surfactant structure and mechanics to composition
    • Alonso C, Alig T, Yoon J, Bringezu F, Warriner H, et al. (2004) More than a monolayer: relating lung surfactant structure and mechanics to composition. Biophys J 87: 4188-4202.
    • (2004) Biophys J , vol.87 , pp. 4188-4202
    • Alonso, C.1    Alig, T.2    Yoon, J.3    Bringezu, F.4    Warriner, H.5
  • 48
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
    • Hess B, Kutzner C, van der Spoel D, Lindahl E, (2008) GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation. J Chem Theory Comput 4: 435-447.
    • (2008) J Chem Theory Comput , vol.4 , pp. 435-447
    • Hess, B.1    Kutzner, C.2    van der Spoel, D.3    Lindahl, E.4
  • 49
    • 4444282928 scopus 로고    scopus 로고
    • A biomolecular force field based on the free enthalpy of hydration and solvation: the GROMOS force-field parameter sets 53A5 and 53A6
    • Oostenbrink C, Villa A, Mark AE, van Gunsteren WF, (2004) A biomolecular force field based on the free enthalpy of hydration and solvation: the GROMOS force-field parameter sets 53A5 and 53A6. J Comput Chem 25: 1656-1676.
    • (2004) J Comput Chem , vol.25 , pp. 1656-1676
    • Oostenbrink, C.1    Villa, A.2    Mark, A.E.3    van Gunsteren, W.F.4
  • 50
    • 65249151900 scopus 로고    scopus 로고
    • Lipid Models for United-Atom Molecular Dynamics Simulations of Proteins
    • Kukol A, (2009) Lipid Models for United-Atom Molecular Dynamics Simulations of Proteins. J Chem Theory Comput 5: 615-626.
    • (2009) J Chem Theory Comput , vol.5 , pp. 615-626
    • Kukol, A.1
  • 51
    • 84876084539 scopus 로고    scopus 로고
    • G43a1 force field modified to contain phosphorylated Ser, Thr and Tyr
    • Available
    • Smith GR (2002) G43a1 force field modified to contain phosphorylated Ser, Thr and Tyr. GROMACS User Contributions. Available: http://www.gromacs.org/Downloads/User_contributions/Force_fields.
    • (2002) GROMACS User Contributions
    • Smith, G.R.1
  • 52
    • 79960220458 scopus 로고    scopus 로고
    • CELLmicrocosmos 2.2 MembraneEditor: A Modular Interactive Shape-Based Software Approach to Solve Heterogeneous Membrane Packing Problems
    • Sommer B, Dingersen T, Gamroth C, Schneider SE, Rubert S, et al. (2011) CELLmicrocosmos 2.2 MembraneEditor: A Modular Interactive Shape-Based Software Approach to Solve Heterogeneous Membrane Packing Problems. J Chem Inf Model 51: 1165-1182.
    • (2011) J Chem Inf Model , vol.51 , pp. 1165-1182
    • Sommer, B.1    Dingersen, T.2    Gamroth, C.3    Schneider, S.E.4    Rubert, S.5
  • 53
    • 84943502952 scopus 로고
    • A molecular dynamics method for simulations in the canonical ensemble
    • Nosé' S, (1984) A molecular dynamics method for simulations in the canonical ensemble. Mol Phys 52: 255-268.
    • (1984) Mol Phys , vol.52 , pp. 255-268
    • Nosé', S.1
  • 54
    • 0001538909 scopus 로고
    • Canonical dynamics: Equilibrium phase-space distributions
    • Hoover WG, (1985) Canonical dynamics: Equilibrium phase-space distributions. Phys Rev A 31: 1695-1697.
    • (1985) Phys Rev A , vol.31 , pp. 1695-1697
    • Hoover, W.G.1
  • 55
    • 0019707626 scopus 로고
    • Polymorphic transitions in single crystals: A new molecular dynamics method
    • Parrinello M, Rahman A, (1981) Polymorphic transitions in single crystals: A new molecular dynamics method. J Appl Phys 52: 7182-7190.
    • (1981) J Appl Phys , vol.52 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 56
    • 84926811618 scopus 로고
    • Constant pressure molecular dynamics for molecular systems
    • Nosé' S, Klein ML, (1983) Constant pressure molecular dynamics for molecular systems. Mol Phys 50: 1055-1076.
    • (1983) Mol Phys , vol.50 , pp. 1055-1076
    • Nosé', S.1    Klein, M.L.2
  • 58
    • 38749123962 scopus 로고    scopus 로고
    • P-LINCS: A parallel linear constraint solver for molecular simulation
    • Hess B, (2008) P-LINCS: A parallel linear constraint solver for molecular simulation. J Chem Theory Comput 4: 116-122.
    • (2008) J Chem Theory Comput , vol.4 , pp. 116-122
    • Hess, B.1
  • 59
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N*log(N) method for Ewald sums in large systems
    • Darden T, York D, Pedersen L, (1993) Particle mesh Ewald: An N*log(N) method for Ewald sums in large systems. J Chem Phys 98: 10089-10092.
    • (1993) J Chem Phys , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 62
    • 0022472744 scopus 로고
    • Immunologic identification of a pulmonary surfactant-associated protein of molecular weight = 6000 daltons
    • Whitsett JA, Hull WM, Ohning B, Ross G, Weaver TE, (1986) Immunologic identification of a pulmonary surfactant-associated protein of molecular weight = 6000 daltons. Pediatr Res 20: 744-749.
    • (1986) Pediatr Res , vol.20 , pp. 744-749
    • Whitsett, J.A.1    Hull, W.M.2    Ohning, B.3    Ross, G.4    Weaver, T.E.5
  • 63
    • 0023658582 scopus 로고
    • Characterization of the small hydrophobic proteins associated with pulmonary surfactant
    • Yu SH, Chung W, Olafson RW, Harding PG, Possmayer F, (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
  • 64
    • 0015611306 scopus 로고
    • Isolation of apoproteins from canine surface active material
    • King RJ, Klass DJ, Gikas EG, Clements JA, (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
  • 66
    • 84863092259 scopus 로고    scopus 로고
    • SFTA2-A Novel Secretory Peptide Highly Expressed in the Lung-Is Modulated by Lipopolysaccharide but Not Hyperoxia
    • Mittal RA, Hammel M, Schwarz J, Heschl KM, Bretschneider N, et al. (2012) SFTA2-A Novel Secretory Peptide Highly Expressed in the Lung-Is Modulated by Lipopolysaccharide but Not Hyperoxia. PLoS ONE 7: e40011.
    • (2012) PLoS ONE , vol.7
    • Mittal, R.A.1    Hammel, M.2    Schwarz, J.3    Heschl, K.M.4    Bretschneider, N.5
  • 67
    • 0034212227 scopus 로고    scopus 로고
    • Palmitoylation of a pulmonary surfactant protein C analogue affects the surface associated lipid reservoir and film stability
    • Gustafsson M, Palmblad M, Curstedt T, Johansson J, Schürch S, (2000) Palmitoylation of a pulmonary surfactant protein C analogue affects the surface associated lipid reservoir and film stability. Biochim Biophys Acta 1466: 169-178.
    • (2000) Biochim Biophys Acta , vol.1466 , pp. 169-178
    • Gustafsson, M.1    Palmblad, M.2    Curstedt, T.3    Johansson, J.4    Schürch, S.5
  • 68
    • 0023902154 scopus 로고
    • cDNA, deduced polypeptide structure and chromosomal assignment of human pulmonary surfactant proteolipid, SPL(pVal)
    • Glasser SW, Korfhagen TR, Weaver TE, Clark JC, Pilot-Matias T, et al. (1988) cDNA, deduced polypeptide structure and chromosomal assignment of human pulmonary surfactant proteolipid, SPL(pVal). J Biol Chem 263: 9-12.
    • (1988) J Biol Chem , vol.263 , pp. 9-12
    • Glasser, S.W.1    Korfhagen, T.R.2    Weaver, T.E.3    Clark, J.C.4    Pilot-Matias, T.5
  • 69
    • 0026803165 scopus 로고
    • Intracellular processing of pulmonary surfactant protein B in an endosomal/lysosomal compartment
    • Voorhout WF, Veenendaal T, Haagsman HP, Weaver TE, Whitsett JA, et al. (1992) Intracellular processing of pulmonary surfactant protein B in an endosomal/lysosomal compartment. Am J Physiol 263: L479-486.
    • (1992) Am J Physiol , vol.263
    • Voorhout, W.F.1    Veenendaal, T.2    Haagsman, H.P.3    Weaver, T.E.4    Whitsett, J.A.5
  • 70
    • 0034603170 scopus 로고    scopus 로고
    • The Role of Homodimers in Surfactant Protein B Function in Vivo
    • Beck DC, Ikegami M, Na C-L, Zaltash S, Johansson J, et al. (2000) The Role of Homodimers in Surfactant Protein B Function in Vivo. J Biol Chem 275: 3365-3370.
    • (2000) J Biol Chem , vol.275 , pp. 3365-3370
    • Beck, D.C.1    Ikegami, M.2    Na, C.-L.3    Zaltash, S.4    Johansson, J.5
  • 73
    • 0028067189 scopus 로고
    • Temporal-spatial distribution of SP-B and SP-C proteins and mRNAs in developing respiratory epithelium of human lung
    • Khoor A, Stahlman MT, Gray ME, Whitsett JA, (1994) Temporal-spatial distribution of SP-B and SP-C proteins and mRNAs in developing respiratory epithelium of human lung. J Histochem Cytochem 42: 1187-1199.
    • (1994) J Histochem Cytochem , vol.42 , pp. 1187-1199
    • Khoor, A.1    Stahlman, M.T.2    Gray, M.E.3    Whitsett, J.A.4
  • 74
    • 0031180866 scopus 로고    scopus 로고
    • Conductive airway surfactant: surface-tension function, biochemical composition, and possible alveolar origin
    • Bernhard W, Haagsman HP, Tschernig T, Poets CF, Postle AD, et al. (1997) Conductive airway surfactant: surface-tension function, biochemical composition, and possible alveolar origin. Am J Respir Cell Mol Biol 17: 41-50.
    • (1997) Am J Respir Cell Mol Biol , vol.17 , pp. 41-50
    • Bernhard, W.1    Haagsman, H.P.2    Tschernig, T.3    Poets, C.F.4    Postle, A.D.5
  • 75
    • 0033531949 scopus 로고    scopus 로고
    • Differential display identification of plunc, a novel gene expressed in embryonic palate, nasal epithelium, and adult lung
    • Weston WM, LeClair EE, Trzyna W, McHugh KM, Nugent P, et al. (1999) Differential display identification of plunc, a novel gene expressed in embryonic palate, nasal epithelium, and adult lung. J Biol Chem 274: 13698-13703.
    • (1999) J Biol Chem , vol.274 , pp. 13698-13703
    • Weston, W.M.1    LeClair, E.E.2    Trzyna, W.3    McHugh, K.M.4    Nugent, P.5
  • 76
    • 0034805942 scopus 로고    scopus 로고
    • Genomic organization of the mouse plunc gene and expression in the developing airways and thymus
    • LeClair EE, Nguyen L, Bingle L, MacGowan A, Singleton V, et al. (2001) Genomic organization of the mouse plunc gene and expression in the developing airways and thymus. Biochem Biophys Res Commun 284: 792-797.
    • (2001) Biochem Biophys Res Commun , vol.284 , pp. 792-797
    • LeClair, E.E.1    Nguyen, L.2    Bingle, L.3    MacGowan, A.4    Singleton, V.5
  • 78
    • 78349262746 scopus 로고    scopus 로고
    • The ocular surfactant system and its relevance in the dry eye
    • Schicht M, Posa A, Paulsen F, Bräuer L, (2010) The ocular surfactant system and its relevance in the dry eye. Klin Monbl Augenheilkd 227: 864-70.
    • (2010) Klin Monbl Augenheilkd , vol.227 , pp. 864-870
    • Schicht, M.1    Posa, A.2    Paulsen, F.3    Bräuer, L.4
  • 81
    • 2342619404 scopus 로고    scopus 로고
    • Immunodetection of surfactant proteins in human organ of Corti, Eustachian tube and kidney
    • Kankavi O, (2003) Immunodetection of surfactant proteins in human organ of Corti, Eustachian tube and kidney. Acta Biochim Pol 50: 1057-1064.
    • (2003) Acta Biochim Pol , vol.50 , pp. 1057-1064
    • Kankavi, O.1
  • 82
    • 81855194433 scopus 로고    scopus 로고
    • Cryopreservation and in vitro culture of primary cell types from lung tissue of a stranded pygmy sperm whale (Kogia breviceps)
    • Annalaura Mancia, Spyropoulos DD, McFee WE, Newton DA, Baatz JE, (2012) Cryopreservation and in vitro culture of primary cell types from lung tissue of a stranded pygmy sperm whale (Kogia breviceps). Comp Biochem Physiol C Toxicol Pharmacol 155: 136-142.
    • (2012) Comp Biochem Physiol C Toxicol Pharmacol , vol.155 , pp. 136-142
    • Annalaura, M.1    Spyropoulos, D.D.2    McFee, W.E.3    Newton, D.A.4    Baatz, J.E.5


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