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Volumn 152, Issue 1-3, 2010, Pages 80-88

Cell-free synthesis and folding of transmembrane OmpA reveals higher order structures and premature truncations

Author keywords

Cell free translation; Dimerization; Lipid vesicles; OmpA folding; Premature termination

Indexed keywords

LIPID; MONOMER; OUTER MEMBRANE PROTEIN A; PHOSPHORYLCHOLINE; POLYPEPTIDE;

EID: 78149283352     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bpc.2010.08.003     Document Type: Article
Times cited : (7)

References (54)
  • 1
    • 33947171595 scopus 로고    scopus 로고
    • Preparative scale cell-free expression systems: new tools for the large scale preparation of integral membrane proteins for functional and structural studies
    • Schwarz D., Klammt C., Koglin A., Lohr F., Schneider B., Dotsch V., Bernhard F. Preparative scale cell-free expression systems: new tools for the large scale preparation of integral membrane proteins for functional and structural studies. Methods 2007, 41:355-369.
    • (2007) Methods , vol.41 , pp. 355-369
    • Schwarz, D.1    Klammt, C.2    Koglin, A.3    Lohr, F.4    Schneider, B.5    Dotsch, V.6    Bernhard, F.7
  • 3
    • 0242317916 scopus 로고    scopus 로고
    • Reconstitution of membrane proteins into liposomes
    • Rigaud J.L., Levy D. Reconstitution of membrane proteins into liposomes. Meth. Enzymol. 2003, 372:65-86.
    • (2003) Meth. Enzymol. , vol.372 , pp. 65-86
    • Rigaud, J.L.1    Levy, D.2
  • 4
    • 7044272757 scopus 로고    scopus 로고
    • Membrane proteins, lipids and detergents: not just a soap opera
    • Seddon A.M., Curnow P., Booth P.J. Membrane proteins, lipids and detergents: not just a soap opera. Biochim. Biophys. Acta 2004, 1666:105-117.
    • (2004) Biochim. Biophys. Acta , vol.1666 , pp. 105-117
    • Seddon, A.M.1    Curnow, P.2    Booth, P.J.3
  • 8
    • 33947171595 scopus 로고    scopus 로고
    • Preparative scale cell-free expression systems: new tools for the large scale preparation of integral membrane proteins for functional and structural studies
    • Schwartz D., Klammt C., Koglin A., Löhr F., Schneider B., Dötsch V., Bernhard F. Preparative scale cell-free expression systems: new tools for the large scale preparation of integral membrane proteins for functional and structural studies. Methods 2007, 41:355-369.
    • (2007) Methods , vol.41 , pp. 355-369
    • Schwartz, D.1    Klammt, C.2    Koglin, A.3    Löhr, F.4    Schneider, B.5    Dötsch, V.6    Bernhard, F.7
  • 9
    • 67749124075 scopus 로고    scopus 로고
    • NMR-based characterization of a refolding intermediate of b2-microglobulin labeled using a wheat germ cell-free system
    • Kameda A., Morita E.H., Sakurai K., Naiki H., Goto Y. NMR-based characterization of a refolding intermediate of b2-microglobulin labeled using a wheat germ cell-free system. Prot. Sci. 2009, 18:1592-1601.
    • (2009) Prot. Sci. , vol.18 , pp. 1592-1601
    • Kameda, A.1    Morita, E.H.2    Sakurai, K.3    Naiki, H.4    Goto, Y.5
  • 12
    • 34447630299 scopus 로고    scopus 로고
    • Functional cell-free synthesis of a seven helix membrane protein: in situ insertion of bacteriorhodopsin into liposomes
    • Kalmbach R., Chizhov I., Schumacher M.C., Friedrich T., Bamberg E., Engelhard M. Functional cell-free synthesis of a seven helix membrane protein: in situ insertion of bacteriorhodopsin into liposomes. J. Mol. Biol. 2007, 371:639-648.
    • (2007) J. Mol. Biol. , vol.371 , pp. 639-648
    • Kalmbach, R.1    Chizhov, I.2    Schumacher, M.C.3    Friedrich, T.4    Bamberg, E.5    Engelhard, M.6
  • 13
  • 14
    • 54049126868 scopus 로고    scopus 로고
    • Wheat germ cell-free translation, purification, and assembly of a functional human stearoyl-CoA desaturase complex
    • Goren M.A., Fox B.G. Wheat germ cell-free translation, purification, and assembly of a functional human stearoyl-CoA desaturase complex. Prot. Exp. Purif. 2008, 62:171-178.
    • (2008) Prot. Exp. Purif. , vol.62 , pp. 171-178
    • Goren, M.A.1    Fox, B.G.2
  • 15
    • 0035066331 scopus 로고    scopus 로고
    • Structure of outer membrane protein A transmembrane domain by NMR structure determination
    • Arora A., Abildgaard F., Bushweller J.H., Tamm L.K. Structure of outer membrane protein A transmembrane domain by NMR structure determination. Nat. Struct. Biol. 2001, 8:334-338.
    • (2001) Nat. Struct. Biol. , vol.8 , pp. 334-338
    • Arora, A.1    Abildgaard, F.2    Bushweller, J.H.3    Tamm, L.K.4
  • 16
    • 0031733336 scopus 로고    scopus 로고
    • Structure of the outer membrane protein A transmembrane domain
    • Pautsch A., Schulz G.E. Structure of the outer membrane protein A transmembrane domain. Nat. Struct. Biol. 1998, 5:1013-1017.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1013-1017
    • Pautsch, A.1    Schulz, G.E.2
  • 17
    • 0029822373 scopus 로고    scopus 로고
    • Folding intermediates of a beta-barrel membrane protein. Kinetic evidence for a multi-step membrane insertion mechanism
    • Kleinschmidt J.H., Tamm L.K. Folding intermediates of a beta-barrel membrane protein. Kinetic evidence for a multi-step membrane insertion mechanism. Biochemistry 1996, 35:12993-13000.
    • (1996) Biochemistry , vol.35 , pp. 12993-13000
    • Kleinschmidt, J.H.1    Tamm, L.K.2
  • 18
    • 0033586795 scopus 로고    scopus 로고
    • Outer membrane protein A of Escherichia coli inserts and folds into lipid bilayers by a concerted mechanism
    • Kleinschmidt J.H., den Blaauwen T., Driessen A.J.M., Tamm L.K. Outer membrane protein A of Escherichia coli inserts and folds into lipid bilayers by a concerted mechanism. Biochemistry 1999, 38:5006-5016.
    • (1999) Biochemistry , vol.38 , pp. 5006-5016
    • Kleinschmidt, J.H.1    den Blaauwen, T.2    Driessen, A.J.M.3    Tamm, L.K.4
  • 19
    • 0033586718 scopus 로고    scopus 로고
    • Time-resolved distance determination by tryptophan fluorescence quenching: probing intermediates in membrane protein folding
    • Kleinschmidt J.H., Tamm L.K. Time-resolved distance determination by tryptophan fluorescence quenching: probing intermediates in membrane protein folding. Biochemistry 1999, 38:4996-5005.
    • (1999) Biochemistry , vol.38 , pp. 4996-5005
    • Kleinschmidt, J.H.1    Tamm, L.K.2
  • 20
    • 0242657339 scopus 로고    scopus 로고
    • Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR
    • Tamm L.K., Abildgaard F., Arora A., Blad H., Bushweller J.H. Structure, dynamics and function of the outer membrane protein A (OmpA) and influenza hemagglutinin fusion domain in detergent micelles by solution NMR. FEBS Lett. 2003, 555:139-143.
    • (2003) FEBS Lett. , vol.555 , pp. 139-143
    • Tamm, L.K.1    Abildgaard, F.2    Arora, A.3    Blad, H.4    Bushweller, J.H.5
  • 21
    • 7044247850 scopus 로고    scopus 로고
    • Folding and assembly of beta-barrel membrane proteins
    • Tamm L.K., Hong H., Liang B. Folding and assembly of beta-barrel membrane proteins. Biochim. Biophys. Acta 2004, 1666(1-2):250-263.
    • (2004) Biochim. Biophys. Acta , vol.1666 , Issue.1-2 , pp. 250-263
    • Tamm, L.K.1    Hong, H.2    Liang, B.3
  • 22
    • 0037984384 scopus 로고    scopus 로고
    • Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide
    • Bulieris P.V., Behrens S., Holst O., Kleinschmidt J.H. Folding and insertion of the outer membrane protein OmpA is assisted by the chaperone Skp and by lipopolysaccharide. J. Biol. Chem. 2003, 278:9092-9099.
    • (2003) J. Biol. Chem. , vol.278 , pp. 9092-9099
    • Bulieris, P.V.1    Behrens, S.2    Holst, O.3    Kleinschmidt, J.H.4
  • 23
    • 0017671931 scopus 로고
    • Purification of protein A, an outer membrane component missing in Escherichia coli K-12 ompA mutants
    • Chai T.J., Foulds J. Purification of protein A, an outer membrane component missing in Escherichia coli K-12 ompA mutants. Biochim. Biophys. Acta 1977, 493:210-215.
    • (1977) Biochim. Biophys. Acta , vol.493 , pp. 210-215
    • Chai, T.J.1    Foulds, J.2
  • 24
    • 34347406730 scopus 로고    scopus 로고
    • A molecular Swiss army knife: OmpA structure, function and expression
    • Smith S.G., Mahon V., Lambert M.A., Fagan R.P. A molecular Swiss army knife: OmpA structure, function and expression. FEMS Microbiol. Lett. 2007, 273:1-11.
    • (2007) FEMS Microbiol. Lett. , vol.273 , pp. 1-11
    • Smith, S.G.1    Mahon, V.2    Lambert, M.A.3    Fagan, R.P.4
  • 25
    • 0030068232 scopus 로고    scopus 로고
    • Outer membrane protein A of Escherichia coli contributes to invasion of brain microvascular endothelial cells
    • Prasadarao N.V., Wass C.A., Weiser J.N., Stins M.F., Huang S.H., Kim K.S. Outer membrane protein A of Escherichia coli contributes to invasion of brain microvascular endothelial cells. Infect. Immun. 1996, 64:146-153.
    • (1996) Infect. Immun. , vol.64 , pp. 146-153
    • Prasadarao, N.V.1    Wass, C.A.2    Weiser, J.N.3    Stins, M.F.4    Huang, S.H.5    Kim, K.S.6
  • 26
    • 33748109925 scopus 로고    scopus 로고
    • Proteomic analysis of Escherichia coli biofilms reveals the overexpression of the outer membrane protein OmpA
    • Orme R., Douglas C.W., Rimmer S., Webb M. Proteomic analysis of Escherichia coli biofilms reveals the overexpression of the outer membrane protein OmpA. Proteomics 2006, 6:4269-4277.
    • (2006) Proteomics , vol.6 , pp. 4269-4277
    • Orme, R.1    Douglas, C.W.2    Rimmer, S.3    Webb, M.4
  • 27
    • 33750255413 scopus 로고    scopus 로고
    • Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening
    • Hong H., Szabo G., Tamm L.K. Electrostatic couplings in OmpA ion-channel gating suggest a mechanism for pore opening. Nat. Chem. Biol. 2006, 2:627-635.
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 627-635
    • Hong, H.1    Szabo, G.2    Tamm, L.K.3
  • 28
    • 0026770209 scopus 로고
    • Refolding and oriented insertion of a membrane protein into a lipid bilayer
    • Surrey T., Jähnig F. Refolding and oriented insertion of a membrane protein into a lipid bilayer. Proc. Natl Acad. Sci. USA 1992, 89:7457-7461.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 7457-7461
    • Surrey, T.1    Jähnig, F.2
  • 29
    • 0038831330 scopus 로고    scopus 로고
    • The periplasmic Escherichia coli peptidylprolyl cis-trans-isomerase FkpA
    • Ramm K., Plückthun A. The periplasmic Escherichia coli peptidylprolyl cis-trans-isomerase FkpA. J. Biol. Chem. 2000, 275:17106-17113.
    • (2000) J. Biol. Chem. , vol.275 , pp. 17106-17113
    • Ramm, K.1    Plückthun, A.2
  • 30
    • 0036849659 scopus 로고    scopus 로고
    • Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins
    • Bitto E., McKay D.B. Crystallographic structure of SurA, a molecular chaperone that facilitates folding of outer membrane porins. Structure 2002, 10:1489-1498.
    • (2002) Structure , vol.10 , pp. 1489-1498
    • Bitto, E.1    McKay, D.B.2
  • 31
    • 0000374766 scopus 로고    scopus 로고
    • Cell-free coupled transcription-traslation systems from Eschrichia coli
    • Oxfrod University Press, Oxford, UK, S.J. Higgins, B.D. Hames (Eds.)
    • Kramer G., Kudlicky W., Hardesty B. Cell-free coupled transcription-traslation systems from Eschrichia coli. Protein Expression: a Practical Aproach 1999, 201-223. Oxfrod University Press, Oxford, UK. S.J. Higgins, B.D. Hames (Eds.).
    • (1999) Protein Expression: a Practical Aproach , pp. 201-223
    • Kramer, G.1    Kudlicky, W.2    Hardesty, B.3
  • 32
    • 33646122246 scopus 로고    scopus 로고
    • Characterization of protein expression and folding in cell-free systems by maldi-tof mass spectrometry
    • Jungbauer L.M., Cavagnero S. Characterization of protein expression and folding in cell-free systems by maldi-tof mass spectrometry. Anal. Chem. 2006, 78:2841-2852.
    • (2006) Anal. Chem. , vol.78 , pp. 2841-2852
    • Jungbauer, L.M.1    Cavagnero, S.2
  • 33
    • 0017926606 scopus 로고
    • Major proteins of the Escherichia coli outer cell envelope membrane. Interaction of protein II with lipopolysaccharide
    • Schweizer M., Hindennach I., Garten W., Henning U. Major proteins of the Escherichia coli outer cell envelope membrane. Interaction of protein II with lipopolysaccharide. Eur. J. Biochem. 1978, 82:211-217.
    • (1978) Eur. J. Biochem. , vol.82 , pp. 211-217
    • Schweizer, M.1    Hindennach, I.2    Garten, W.3    Henning, U.4
  • 34
    • 33646727775 scopus 로고    scopus 로고
    • Folding kinetics of the outer membrane proteins OmpA and FomA into phospholipid bilayers
    • Kleinschmidt J.H. Folding kinetics of the outer membrane proteins OmpA and FomA into phospholipid bilayers. Chem. Phys. Lipids 2006, 141:30-47.
    • (2006) Chem. Phys. Lipids , vol.141 , pp. 30-47
    • Kleinschmidt, J.H.1
  • 35
    • 0344234283 scopus 로고    scopus 로고
    • A new era in membrane channel biology
    • Walian P., Jap B.K. A new era in membrane channel biology. Structure 2003, 11:1467-1468.
    • (2003) Structure , vol.11 , pp. 1467-1468
    • Walian, P.1    Jap, B.K.2
  • 36
    • 34447630299 scopus 로고    scopus 로고
    • Functional cell-free synthesis of a seven helix membrane protein: in situ insertion of bacteriorhodopsin into liposomes
    • Kalmbach R., Chizhov I., Schumacher M.C., Friedrich T., Bamberg E., Engelhard M. Functional cell-free synthesis of a seven helix membrane protein: in situ insertion of bacteriorhodopsin into liposomes. J. Mol. Biol. 2007, 371:639-648.
    • (2007) J. Mol. Biol. , vol.371 , pp. 639-648
    • Kalmbach, R.1    Chizhov, I.2    Schumacher, M.C.3    Friedrich, T.4    Bamberg, E.5    Engelhard, M.6
  • 37
    • 70350520053 scopus 로고    scopus 로고
    • The periplasmic chaperone skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potential
    • Patel G.J., Behrens-Kneip S., Holst O., Kleinschmidt J.H. The periplasmic chaperone skp facilitates targeting, insertion, and folding of OmpA into lipid membranes with a negative membrane surface potential. Biochemistry 2009, 48:10235-10245.
    • (2009) Biochemistry , vol.48 , pp. 10235-10245
    • Patel, G.J.1    Behrens-Kneip, S.2    Holst, O.3    Kleinschmidt, J.H.4
  • 38
    • 0036441481 scopus 로고    scopus 로고
    • Secondary and tertiary structure formation of the b-barrel membrane protein OmpA is synchronized and depends on membrane thickness
    • Kleinschmidt J.H., Tamm L.K. Secondary and tertiary structure formation of the b-barrel membrane protein OmpA is synchronized and depends on membrane thickness. J. Mol. Biol. 2002, 324:319-330.
    • (2002) J. Mol. Biol. , vol.324 , pp. 319-330
    • Kleinschmidt, J.H.1    Tamm, L.K.2
  • 40
    • 0036306814 scopus 로고    scopus 로고
    • The activation energy for insertion of transmembrane alpha-helices is dependent on membrane composition
    • Meijberg M., Booth P.J. The activation energy for insertion of transmembrane alpha-helices is dependent on membrane composition. J. Mol. Biol. 2002, 319:839-853.
    • (2002) J. Mol. Biol. , vol.319 , pp. 839-853
    • Meijberg, M.1    Booth, P.J.2
  • 41
    • 67651111837 scopus 로고    scopus 로고
    • Negatively charged liposome as a potent inhibitor of post-translation during in vitro synthesis of green fluorescent protein
    • Bui H.T., Umakoshi H., Suga K., Nishida M., Shimanouchi T., Kuboi R. Negatively charged liposome as a potent inhibitor of post-translation during in vitro synthesis of green fluorescent protein. Biochem. Eng. J. 2009, 46:154-160.
    • (2009) Biochem. Eng. J. , vol.46 , pp. 154-160
    • Bui, H.T.1    Umakoshi, H.2    Suga, K.3    Nishida, M.4    Shimanouchi, T.5    Kuboi, R.6
  • 42
    • 0033587549 scopus 로고    scopus 로고
    • Modulation of folding and assembly of the membrane protein bacteriorhodopsin by intermolecular forces within the lipid bilayer
    • Curran A.R., Templer R.H., Booth P.J. Modulation of folding and assembly of the membrane protein bacteriorhodopsin by intermolecular forces within the lipid bilayer. Biochemistry 1999, 38:9328-9336.
    • (1999) Biochemistry , vol.38 , pp. 9328-9336
    • Curran, A.R.1    Templer, R.H.2    Booth, P.J.3
  • 43
    • 0032530656 scopus 로고    scopus 로고
    • Phospholipid-assisted protein folding: phosphatidylethanolamine is required at a late step of the conformational maturation of the polytopic membrane protein lactose permease
    • Bogdanov M., Dowhan W. Phospholipid-assisted protein folding: phosphatidylethanolamine is required at a late step of the conformational maturation of the polytopic membrane protein lactose permease. EMBO J. 1998, 17:5255-5264.
    • (1998) EMBO J. , vol.17 , pp. 5255-5264
    • Bogdanov, M.1    Dowhan, W.2
  • 44
    • 0037077723 scopus 로고    scopus 로고
    • Influence of lipids on membrane assembly and stability of the potassium channel KcsA
    • van Dalen A., Hegger S., Killian J.A., de Kruijff B. Influence of lipids on membrane assembly and stability of the potassium channel KcsA. FEBS Lett. 2002, 525:33-38.
    • (2002) FEBS Lett. , vol.525 , pp. 33-38
    • van Dalen, A.1    Hegger, S.2    Killian, J.A.3    de Kruijff, B.4
  • 45
    • 1642447757 scopus 로고    scopus 로고
    • Elastic coupling of integral membrane protein stability to lipid bilayer forces
    • Hong H., Tamm L.K. Elastic coupling of integral membrane protein stability to lipid bilayer forces. Proc. Natl Acad. Sci. USA 2004, 101:4065-4070.
    • (2004) Proc. Natl Acad. Sci. USA , vol.101 , pp. 4065-4070
    • Hong, H.1    Tamm, L.K.2
  • 46
    • 0032421354 scopus 로고    scopus 로고
    • Functions of lipid rafts in biological membranes
    • Brown D.A., London E. Functions of lipid rafts in biological membranes. Ann. Rev. Cell. Dev. Biol. 1998, 14:111-136.
    • (1998) Ann. Rev. Cell. Dev. Biol. , vol.14 , pp. 111-136
    • Brown, D.A.1    London, E.2
  • 47
    • 1842536499 scopus 로고    scopus 로고
    • Rafts: scale-dependent, active lipid organization at the cell surface
    • Mayor S., Rao M. Rafts: scale-dependent, active lipid organization at the cell surface. Traffic 2004, 5:231-240.
    • (2004) Traffic , vol.5 , pp. 231-240
    • Mayor, S.1    Rao, M.2
  • 48
    • 0035374452 scopus 로고    scopus 로고
    • The early interaction of the outer membrane protein PhoE with the periplasmic chaperone Skp occurs at the cytoplasmic membrane
    • Harms N., Koningstein G., Dontje W., Muller M., Oudega B., Luirink J., de Cock H. The early interaction of the outer membrane protein PhoE with the periplasmic chaperone Skp occurs at the cytoplasmic membrane. J. Biol. Chem. 2001, 276:18804-18811.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18804-18811
    • Harms, N.1    Koningstein, G.2    Dontje, W.3    Muller, M.4    Oudega, B.5    Luirink, J.6    de Cock, H.7
  • 49
    • 0038105593 scopus 로고    scopus 로고
    • Skp, a molecular chaperone of Gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins
    • Schäfer U., Beck K., Müller M. Skp, a molecular chaperone of Gram-negative bacteria, is required for the formation of soluble periplasmic intermediates of outer membrane proteins. J. Biol. Chem. 1999, 274:24567-24574.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24567-24574
    • Schäfer, U.1    Beck, K.2    Müller, M.3
  • 50
    • 22144495426 scopus 로고    scopus 로고
    • Interactions between periplasmic chaperones and bacterial outer membrane proteins
    • Mogensen J.E., Otzen D.E. Interactions between periplasmic chaperones and bacterial outer membrane proteins. Mol. Microbiol. 2005, 57:326-346.
    • (2005) Mol. Microbiol. , vol.57 , pp. 326-346
    • Mogensen, J.E.1    Otzen, D.E.2
  • 51
    • 77951975923 scopus 로고    scopus 로고
    • In vitro association of fragments of a b-sheet membrane protein
    • Debnath D., Nielsen K.L., Otzen D.E. In vitro association of fragments of a b-sheet membrane protein. Biophys. Chem. 2010, 148:112-120.
    • (2010) Biophys. Chem. , vol.148 , pp. 112-120
    • Debnath, D.1    Nielsen, K.L.2    Otzen, D.E.3
  • 52
    • 0029918686 scopus 로고    scopus 로고
    • SurA assists the folding of Escherichia coli outer membrane proteins
    • Lazar S.W., Kolter R. SurA assists the folding of Escherichia coli outer membrane proteins. J. Bacteriol. 1996, 178:1770-1773.
    • (1996) J. Bacteriol. , vol.178 , pp. 1770-1773
    • Lazar, S.W.1    Kolter, R.2
  • 53
    • 0035863210 scopus 로고    scopus 로고
    • The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity
    • Behrens S., Maier R., De Cock H., Schmid F.X., Gross C.A. The SurA periplasmic PPIase lacking its parvulin domains functions in vivo and has chaperone activity. EMBO J. 2001, 20:285-294.
    • (2001) EMBO J. , vol.20 , pp. 285-294
    • Behrens, S.1    Maier, R.2    De Cock, H.3    Schmid, F.X.4    Gross, C.A.5
  • 54
    • 67749124075 scopus 로고    scopus 로고
    • NMR-based characterization of a refolding intermediate of beta2-microglobulin labeled using a wheat germ cell-free system
    • Kameda A., Morita E.H., Sakurai K., Naiki H., Goto Y. NMR-based characterization of a refolding intermediate of beta2-microglobulin labeled using a wheat germ cell-free system. Prot. Sci. 2009, 18:1592-1601.
    • (2009) Prot. Sci. , vol.18 , pp. 1592-1601
    • Kameda, A.1    Morita, E.H.2    Sakurai, K.3    Naiki, H.4    Goto, Y.5


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