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Volumn 10, Issue 10, 2011, Pages

Cross-linking measurements of in vivo protein complex topologies

Author keywords

[No Author keywords available]

Indexed keywords

ARTICLE; BACTERIAL CELL; COMPLEX FORMATION; CROSS LINKING; CRYSTAL STRUCTURE; ESCHERICHIA COLI; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN INTERACTION; PROTEIN LOCALIZATION; PROTEIN STRUCTURE; BINDING SITE; CHEMISTRY; CONFORMATION; HUMAN; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; METABOLISM; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION;

EID: 80054023027     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M110.006841     Document Type: Article
Times cited : (83)

References (52)
  • 1
    • 0024406857 scopus 로고
    • A novel genetic system to detect protein-protein interactions
    • DOI 10.1038/340245a0
    • Fields, S., and Song, O. (1989) A novel genetic system to detect proteinprotein interactions. Nature 340, 245-246 (Pubitemid 19171591)
    • (1989) Nature , vol.340 , Issue.6230 , pp. 245-246
    • Fields, S.1    Song, O.-K.2
  • 2
    • 0031631358 scopus 로고    scopus 로고
    • Co-immunoprecipitation. Identification of interacting proteins
    • Anderson, N. G. (1998) Co-immunoprecipitation. Identification of interacting proteins. Methods Mol. Biol. 88, 3412-3421
    • (1998) Methods Mol. Biol. , vol.88 , pp. 3412-3421
    • Anderson, N.G.1
  • 3
    • 0032828715 scopus 로고    scopus 로고
    • A generic protein purification method for protein complex characterization and proteome exploration
    • DOI 10.1038/13732
    • Rigaut, G., Shevchenko, A., Rutz, B., Wilm, M., Mann, M., and Séraphin, B. (1999) A generic protein purification method for protein complex characterization and proteome exploration. Nat. Biotechnol. 17, 1030-1032 (Pubitemid 29474865)
    • (1999) Nature Biotechnology , vol.17 , Issue.10 , pp. 1030-1032
    • Rigaut, G.1    Shevchenko, A.2    Rutz, B.3    Wilm, M.4    Mann, M.5    Seraphin, B.6
  • 4
    • 0034854563 scopus 로고    scopus 로고
    • High-throughput yeast two-hybrid assays for large-scale protein interaction mapping
    • DOI 10.1006/meth.2001.1190
    • Walhout, A. J., and Vidal, M. (2001) High-throughput yeast two-hybrid assays for large-scale protein interaction mapping. Methods 24, 297-306 (Pubitemid 32846435)
    • (2001) Methods , vol.24 , Issue.3 , pp. 297-306
    • Walhout, A.J.M.1    Vidal, M.2
  • 6
    • 2442503251 scopus 로고    scopus 로고
    • Tandem affinity purification and identification of protein complex components
    • DOI 10.1016/j.ymeth.2003.11.019, PII S1046202303003189
    • Gould, K. L., Ren, L., Feoktistova, A. S., Jennings, J. L., and Link, A. J. (2004) Tandem affinity purification and identification of protein complex components. Methods 33, 239-244 (Pubitemid 38648845)
    • (2004) Methods , vol.33 , Issue.3 , pp. 239-244
    • Gould, K.L.1    Ren, L.2    Feoktistova, A.S.3    Jennings, J.L.4    Link, A.J.5
  • 8
    • 13844267071 scopus 로고    scopus 로고
    • Chemical cross-linking and FTICR mass spectrometry for protein structure characterization
    • Sinz, A. (2005) Chemical cross-linking and FTICR mass spectrometry for protein structure characterization. Anal. Bioanal. Chem. 381, 44-47
    • (2005) Anal. Bioanal. Chem. , vol.381 , pp. 44-47
    • Sinz, A.1
  • 9
    • 63049119068 scopus 로고    scopus 로고
    • Identification of protein-protein interactions and topologies in living cells with chemical cross-linking and mass spectrometry
    • Zhang, H., Tang, X., Munske, G. R., Tolic, N., Anderson, G. A., and Bruce, J. E. (2009) Identification of protein-protein interactions and topologies in living cells with chemical cross-linking and mass spectrometry. Mol. Cell. Proteomics 8, 409-420
    • (2009) Mol. Cell. Proteomics , vol.8 , pp. 409-420
    • Zhang, H.1    Tang, X.2    Munske, G.R.3    Tolic, N.4    Anderson, G.A.5    Bruce, J.E.6
  • 11
    • 11844289583 scopus 로고    scopus 로고
    • Mass spectrometry identifiable cross-linking strategy for studying protein-protein interactions
    • DOI 10.1021/ac0488762
    • Tang, X., Munske, G. R., Siems, W. F., and Bruce, J. E. (2005) Mass spectrometry identifiable cross-linking strategy for studying proteinprotein interactions. Anal. Chem. 77, 311-318 (Pubitemid 40096700)
    • (2005) Analytical Chemistry , vol.77 , Issue.1 , pp. 311-318
    • Tang, X.1    Munske, G.R.2    Siems, W.F.3    Bruce, J.E.4
  • 14
    • 34948860098 scopus 로고    scopus 로고
    • Informatics strategies for large-scale novel cross-linking analysis
    • DOI 10.1021/pr070035z
    • Anderson, G. A., Tolic, N., Tang, X., Zheng, C., and Bruce, J. E. (2007) Informatics strategies for large-scale novel cross-linking analysis. J. Proteome Res. 6, 3412-3421 (Pubitemid 47522731)
    • (2007) Journal of Proteome Research , vol.6 , Issue.9 , pp. 3412-3421
    • Anderson, G.A.1    Tolic, N.2    Tang, X.3    Zheng, C.4    Bruce, J.E.5
  • 15
    • 78649887149 scopus 로고    scopus 로고
    • Improved Strategies for Rapid Identification of Chemically Cross-linked Peptides
    • Hoopmann, M. R., Weisbrod, C. R., and Bruce, J. E. (2010) Improved Strategies for Rapid Identification of Chemically Cross-linked Peptides. J. Proteome Res. 9, 6323-6333
    • (2010) J. Proteome Res. , vol.9 , pp. 6323-6333
    • Hoopmann, M.R.1    Weisbrod, C.R.2    Bruce, J.E.3
  • 16
    • 34547727671 scopus 로고    scopus 로고
    • High-speed data reduction, feature detection, and MS/MS spectrum quality assessment of shotgun proteomics data sets using high-resolution mass spectrometry
    • DOI 10.1021/ac0700833
    • Hoopmann, M. R., Finney, G. L., and MacCoss, M. J. (2007) High-speed data reduction, feature detection, and MS/MS spectrum quality assessment of shotgun proteomics data sets using high-resolution mass spectrometry. Anal. Chem. 79, 5620-5632 (Pubitemid 47229808)
    • (2007) Analytical Chemistry , vol.79 , Issue.15 , pp. 5620-5632
    • Hoopmann, M.R.1    Finney, G.L.2    MacCoss, M.J.3
  • 17
    • 21644476468 scopus 로고    scopus 로고
    • PatchDock and SymmDock: Servers for rigid and symmetric docking
    • DOI 10.1093/nar/gki481
    • Schneidman-Duhovny, D., Inbar, Y., Nussinov, R., and Wolfson, H. J. (2005) PatchDock and SymmDock: servers for rigid and symmetric docking. Nucleic Acids Res. 33, W363-367 (Pubitemid 44529944)
    • (2005) Nucleic Acids Research , vol.33 , Issue.WEB. SERV. ISS.
    • Schneidman-Duhovny, D.1    Inbar, Y.2    Nussinov, R.3    Wolfson, H.J.4
  • 18
    • 50549092426 scopus 로고    scopus 로고
    • Accelerating and focusing protein-protein docking correlations using multi-dimensional rotational FFT generating functions
    • Ritchie, D. W., Kozakov, D., and Vajda, S. (2008) Accelerating and focusing protein-protein docking correlations using multi-dimensional rotational FFT generating functions. Bioinformatics 24, 1865-1873
    • (2008) Bioinformatics , vol.24 , pp. 1865-1873
    • Ritchie, D.W.1    Kozakov, D.2    Vajda, S.3
  • 19
    • 77952536672 scopus 로고    scopus 로고
    • A new cross-linking strategy: Protein interaction reporter (PIR) technology for protein-protein interaction studies
    • Tang, X., and Bruce, J. E. (2010) A new cross-linking strategy: protein interaction reporter (PIR) technology for protein-protein interaction studies. Mol. BioSyst. 6, 939-947
    • (2010) Mol. BioSyst. , vol.6 , pp. 939-947
    • Tang, X.1    Bruce, J.E.2
  • 20
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • Perkins, D. N., Pappin, D. J., Creasy, D. M., and Cottrell, J. S. (1999) Probability-based protein identification by searching sequence databases using mass spectrometry data. Electrophoresis 20, 3551-3567 (Pubitemid 30007252)
    • (1999) Electrophoresis , vol.20 , Issue.18 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 23
    • 33847345976 scopus 로고    scopus 로고
    • Profiling the membrane proteome of Shewanella oneidensis MR-1 with new affinity labeling probes
    • DOI 10.1021/pr060480e
    • Tang, X., Yi, W., Munske, G. R., Adhikari, D. P., Zakharova, N. L., and Bruce, J. E. (2007) Profiling the membrane proteome of Shewanella oneidensis MR-1 with new affinity labeling probes. J. Proteome Res. 6, 724-734 (Pubitemid 46340175)
    • (2007) Journal of Proteome Research , vol.6 , Issue.2 , pp. 724-734
    • Tang, X.1    Yi, W.2    Munske, G.R.3    Adhikari, D.P.4    Zakharova, N.L.5    Bruce, J.E.6
  • 25
    • 37249067732 scopus 로고    scopus 로고
    • The origin of protein interactions and allostery in colocalization
    • DOI 10.1038/nature06524, PII NATURE06524
    • Kuriyan, J., and Eisenberg, D. (2007) The origin of protein interactions and allostery in colocalization. Nature 450, 983-990 (Pubitemid 350273628)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 983-990
    • Kuriyan, J.1    Eisenberg, D.2
  • 26
    • 4744373535 scopus 로고    scopus 로고
    • Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture
    • DOI 10.1038/nsmb828
    • Korndörfer, I. P., Dommel, M. K., and Skerra, A. (2004) Structure of the periplasmic chaperone Skp suggests functional similarity with cytosolic chaperones despite differing architecture. Nat. Struct. Mol. Biol. 11, 1015-1020 (Pubitemid 39315307)
    • (2004) Nature Structural and Molecular Biology , vol.11 , Issue.10 , pp. 1015-1020
    • Korndorfer, I.P.1    Dommel, M.K.2    Skerra, A.3
  • 27
    • 60549101514 scopus 로고    scopus 로고
    • The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains
    • Walton, T. A., Sandoval, C. M., Fowler, C. A., Pardi, A., and Sousa, M. C. (2009) The cavity-chaperone Skp protects its substrate from aggregation but allows independent folding of substrate domains. Proc. Natl. Acad. Sci. U. S. A. 106, 1772-1777
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 1772-1777
    • Walton, T.A.1    Sandoval, C.M.2    Fowler, C.A.3    Pardi, A.4    Sousa, M.C.5
  • 28
    • 0033556141 scopus 로고    scopus 로고
    • Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein
    • DOI 10.1046/j.1432-1327.1999.00010.x
    • De Cock, H., Schäfer, U., Potgeter, M., Demel, R., Müller, M., and Tommassen, J. (1999) Affinity of the periplasmic chaperone Skp of Escherichia coli for phospholipids, lipopolysaccharides and non-native outer membrane proteins. Role of Skp in the biogenesis of outer membrane protein. Eur. J. Biochem. 259, 96-103 (Pubitemid 29030823)
    • (1999) European Journal of Biochemistry , vol.259 , Issue.1-2 , pp. 96-103
    • De Cock, H.1    Schafer, U.2    Potgeter, M.3    Demel, R.4    Muller, M.5    Tommassen, J.6
  • 29
    • 0042878499 scopus 로고    scopus 로고
    • Membrane protein folding on the example of outer membrane protein A of Escherichia coli
    • Kleinschmidt, J. H. (2003) Membrane protein folding on the example of outer membrane protein A of Escherichia coli. Cell. Mol. Life Sci. 60, 1547-1558
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1547-1558
    • Kleinschmidt, J.H.1
  • 30
    • 4143114616 scopus 로고    scopus 로고
    • Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation
    • DOI 10.1016/j.molcel.2004.07.023, PII S1097276504004435
    • Walton, T. A., and Sousa, M. C. (2004) Crystal structure of Skp, a prefoldin-like chaperone that protects soluble and membrane proteins from aggregation. Mol. Cell 15, 367-374 (Pubitemid 39092753)
    • (2004) Molecular Cell , vol.15 , Issue.3 , pp. 367-374
    • Walton, T.A.1    Sousa, M.C.2
  • 31
    • 0032127966 scopus 로고    scopus 로고
    • Crystallization of 5-keto-4-deoxyuronate isomerase from Escherichia coli
    • DOI 10.1107/S090744499701785X
    • Dunten, P., Jaffe, H., and Aksamit, R. R. (1998) Crystallization of 5-keto-4-deoxyuronate isomerase from Escherichia coli. Acta Crystallogr. D Biol. Crystallogr. 54, 678-680 (Pubitemid 28343820)
    • (1998) Acta Crystallographica Section D: Biological Crystallography , vol.54 , Issue.4 , pp. 678-680
    • Dunten, P.1
  • 33
    • 34347406730 scopus 로고    scopus 로고
    • A molecular Swiss army knife: OmpA structure, function and expression
    • DOI 10.1111/j.1574-6968.2007.00778.x
    • Smith, S. G., Mahon, V., Lambert, M. A., and Fagan, R. P. (2007) A molecular Swiss army knife: OmpA structure, function and expression. FEMS Microbiol. Lett. 273, 1-11 (Pubitemid 47024891)
    • (2007) FEMS Microbiology Letters , vol.273 , Issue.1 , pp. 1-11
    • Smith, S.G.J.1    Mahon, V.2    Lambert, M.A.3    Fagan, R.P.4
  • 35
    • 0035188469 scopus 로고    scopus 로고
    • Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli
    • DOI 10.1046/j.1365-2958.2001.02250.x
    • Arié, J. P., Sassoon, N., and Betton, J. M. (2001) Chaperone function of FkpA, a heat shock prolyl isomerase, in the periplasm of Escherichia coli. Mol. Microbiol. 39, 199-210 (Pubitemid 32063107)
    • (2001) Molecular Microbiology , vol.39 , Issue.1 , pp. 199-210
    • Arie, J.-P.1    Sassoon, N.2    Betton, J.-M.3
  • 36
    • 0346366809 scopus 로고    scopus 로고
    • Structural and Functional Studies of FkpA from Escherichia coli, a cis/trans Peptidyl-prolyl Isomerase with Chaperone Activity
    • DOI 10.1016/j.jmb.2003.10.056
    • Saul, F. A., Arié, J. P., Vulliez-le Normand, B., Kahn, R., Betton, J. M., and Bentley, G. A. (2004) Structural and functional studies of FkpA from Escherichia coli, a cis/trans peptidyl-prolyl isomerase with chaperone activity. J. Mol. Biol. 335, 595-608 (Pubitemid 37532659)
    • (2004) Journal of Molecular Biology , vol.335 , Issue.2 , pp. 595-608
    • Saul, F.A.1    Arie, J.-P.2    Vulliez-le, N.B.3    Kahn, R.4    Betton, J.-M.5    Bentley, G.A.6
  • 37
    • 0028864461 scopus 로고
    • A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor
    • Stoller, G., Rücknagel, K. P., Nierhaus, K. H., Schmid, F. X., Fischer, G., and Rahfeld, J. U. (1995) A ribosome-associated peptidyl-prolyl cis/trans isomerase identified as the trigger factor. EMBO J. 14, 4939-4948
    • (1995) EMBO J. , vol.14 , pp. 4939-4948
    • Stoller, G.1    Rücknagel, K.P.2    Nierhaus, K.H.3    Schmid, F.X.4    Fischer, G.5    Rahfeld, J.U.6
  • 38
    • 70349684496 scopus 로고    scopus 로고
    • OmpA influences Escherichia coli biofilm formation by repressing cellulose production through the CpxRA two-component system
    • Ma, Q., and Wood, T. K. (2009) OmpA influences Escherichia coli biofilm formation by repressing cellulose production through the CpxRA two-component system. Environ. Microbiol. 11, 2735-2746
    • (2009) Environ. Microbiol. , vol.11 , pp. 2735-2746
    • Ma, Q.1    Wood, T.K.2
  • 39
    • 0022358531 scopus 로고
    • Bacteriophage receptor area of outer membrane protein OmpA of Escherichia coli K-12
    • Morona, R., Krämer, C., and Henning, U. (1985) Bacteriophage receptor area of outer membrane protein OmpA of Escherichia coli K-12. J. Bacteriol. 164, 539-543 (Pubitemid 16195160)
    • (1985) Journal of Bacteriology , vol.164 , Issue.2 , pp. 539-543
    • Morona, R.1    Kramer, C.2    Henning, U.3
  • 40
    • 0036291172 scopus 로고    scopus 로고
    • The function of OmpA in Escherichia coli
    • Wang, Y. (2002) The function of OmpA in Escherichia coli. Biochem. Biophys. Res. Commun. 292, 396-401
    • (2002) Biochem. Biophys. Res. Commun. , vol.292 , pp. 396-401
    • Wang, Y.1
  • 41
    • 0031733336 scopus 로고    scopus 로고
    • Structure of the outer membrane protein A transmembrane domain
    • DOI 10.1038/2983
    • Pautsch, A., and Schulz, G. E. (1998) Structure of the outer membrane protein A transmembrane domain. Nat. Struct. Biol. 5, 1013-1017 (Pubitemid 28506635)
    • (1998) Nature Structural Biology , vol.5 , Issue.11 , pp. 1013-1017
    • Pautsch, A.1    Schulz, G.E.2
  • 42
    • 1442325407 scopus 로고    scopus 로고
    • Structure of the OmpA-like domain of RmpM from Neisseria meningitidis
    • DOI 10.1111/j.1365-2958.2003.03903.x
    • Grizot, S., and Buchanan, S. K. (2004) Structure of the OmpA-like domain of RmpM from Neisseria meningitidis. Mol. Microbiol. 51, 1027-1037 (Pubitemid 38270797)
    • (2004) Molecular Microbiology , vol.51 , Issue.4 , pp. 1027-1037
    • Grizot, S.1    Buchanan, S.K.2
  • 43
    • 78149283352 scopus 로고    scopus 로고
    • Cell-free synthesis and folding of transmembrane OmpA reveals higher order structures and premature truncations
    • Debnath, D. K., and Otzen, D. E. (2010) Cell-free synthesis and folding of transmembrane OmpA reveals higher order structures and premature truncations. Biophys. Chem. 152, 80-88
    • (2010) Biophys. Chem. , vol.152 , pp. 80-88
    • Debnath, D.K.1    Otzen, D.E.2
  • 44
    • 0030071704 scopus 로고    scopus 로고
    • An alternative topological model for Escherichia coli OmpA
    • Stathopoulos, C. (1996) An alternative topological model for Escherichia coli OmpA. Protein Sci. 5, 170-173
    • (1996) Protein Sci. , vol.5 , pp. 170-173
    • Stathopoulos, C.1
  • 45
    • 0029823940 scopus 로고    scopus 로고
    • Secondary structure of the outer membrane proteins OmpA of Escherichia coli and OprF of Pseudomonas aeruginosa
    • Sugawara, E., Steiert, M., Rouhani, S., and Nikaido, H. (1996) Secondary structure of the outer membrane proteins OmpA of Escherichia coli and OprF of Pseudomonas aeruginosa. J. Bacteriol. 178, 6067-6069 (Pubitemid 26337797)
    • (1996) Journal of Bacteriology , vol.178 , Issue.20 , pp. 6067-6069
    • Sugawara, E.1    Steiert, M.2    Rouhani, S.3    Nikaido, H.4
  • 46
    • 49849103395 scopus 로고    scopus 로고
    • Protein disorder is positively correlated with gene expression in Escherichia coli
    • Paliy, O., Gargac, S. M., Cheng, Y., Uversky, V. N., and Dunker, A. K. (2008) Protein disorder is positively correlated with gene expression in Escherichia coli. J. Proteome Res. 7, 2234-2245
    • (2008) J. Proteome Res. , vol.7 , pp. 2234-2245
    • Paliy, O.1    Gargac, S.M.2    Cheng, Y.3    Uversky, V.N.4    Dunker, A.K.5
  • 47
    • 0001913048 scopus 로고    scopus 로고
    • Predicting Protein Disorder for N-, C-, and Internal Regions. Genome informatics
    • Li, X., Romero, P., Rani, M., Dunker, A. K., and Obradovic, Z. (1999) Predicting Protein Disorder for N-, C-, and Internal Regions. Genome informatics. Workshop on Genome Informatics 10, 30-40
    • (1999) Workshop on Genome Informatics , vol.10 , pp. 30-40
    • Li, X.1    Romero, P.2    Rani, M.3    Dunker, A.K.4    Obradovic, Z.5
  • 49
    • 67049119327 scopus 로고    scopus 로고
    • Prediction of protein binding regions in disordered proteins
    • Mészáros, B., Simon, I., and Dosztányi, Z. (2009) Prediction of protein binding regions in disordered proteins. PLoS Comput. Biol. 5, e1000376
    • (2009) PLoS Comput. Biol. , vol.5
    • Mészáros, B.1    Simon, I.2    Dosztányi, Z.3
  • 50
    • 0034695440 scopus 로고    scopus 로고
    • Refolded outer membrane protein A of Escherichia coli forms ion channels with two conductance states in planar lipid bilayers
    • DOI 10.1074/jbc.275.3.1594
    • Arora, A., Rinehart, D., Szabo, G., and Tamm, L. K. (2000) Refolded outer membrane protein A of Escherichia coli forms ion channels with two conductance states in planar lipid bilayers. J. Biol. Chem. 275, 1594-1600 (Pubitemid 30060774)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.3 , pp. 1594-1600
    • Arora, A.1    Rinehart, D.2    Szabo, G.3    Tamm, L.K.4
  • 51
    • 17844405030 scopus 로고    scopus 로고
    • Kinetics of folding of Escherichia coli OmpA from narrow to large pore conformation in a planar bilayer
    • DOI 10.1021/bi047278e
    • Zakharian, E., and Reusch, R. N. (2005) Kinetics of folding of Escherichia coli OmpA from narrow to large pore conformation in a planar bilayer. Biochemistry 44, 6701-6707 (Pubitemid 40593821)
    • (2005) Biochemistry , vol.44 , Issue.17 , pp. 6701-6707
    • Zakharian, E.1    Reusch, R.N.2
  • 52
    • 0033081475 scopus 로고    scopus 로고
    • Strategy for membrane protein crystallization exemplified with OmpA and OmpX
    • DOI 10.1002/(SICI)1097-0134(19990201)34:2<167::AID-PROT2>3.0.CO;2-H
    • Pautsch, A., Vogt, J., Model, K., Siebold, C., and Schulz, G. E. (1999) Strategy for membrane protein crystallization exemplified with OmpA and OmpX. Proteins 34, 167-172 (Pubitemid 29028802)
    • (1999) Proteins: Structure, Function and Genetics , vol.34 , Issue.2 , pp. 167-172
    • Pautsch, A.1    Vogt, J.2    Model, K.3    Siebold, C.4    Schulz, G.E.5


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