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Volumn , Issue , 2006, Pages 1-23

Direct Characterization of Protein Complexes by Electrospray Ionization Mass Spectrometry and Ion Mobility Analysis

Author keywords

ESI MS analysis of noncovalent protein complexes; Protein complex determination in biochemical pathway understanding; Solution phase equilibria and gas phase dissociation

Indexed keywords


EID: 84889465822     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1002/9780470146330.ch1     Document Type: Chapter
Times cited : (2)

References (54)
  • 1
    • 33646013923 scopus 로고    scopus 로고
    • Mass spectrometry of macromolecular assemblies: preservation and dissociation
    • Benesch, J. L. P., and Robinson, C. V. (2006). Mass spectrometry of macromolecular assemblies: preservation and dissociation. Curr. Opin. Struct. Biol. 16: 245-251.
    • (2006) Curr. Opin. Struct. Biol. , vol.16 , pp. 245-251
    • Benesch, J.L.P.1    Robinson, C.V.2
  • 2
    • 4444243006 scopus 로고    scopus 로고
    • Investigation of intact protein complexes by mass spectrometry
    • Heck, A. J. R., and van den Heuvel, R. H. H. (2004). Investigation of intact protein complexes by mass spectrometry. Mass Spectrom. Rev. 23: 368-389.
    • (2004) Mass Spectrom. Rev. , vol.23 , pp. 368-389
    • Heck, A.J.R.1    Van Den Heuvel, R.H.H.2
  • 3
    • 33748368713 scopus 로고    scopus 로고
    • Mass measurements of increased accuracy resolve heterogeneous populations of intact ribosomes
    • McKay, A. R., Ruotolo, B. T., Ilag, L. L., and Robinson, C. V. (2006). Mass measurements of increased accuracy resolve heterogeneous populations of intact ribosomes. J. Am. Chem. Soc. 128: 11433-11442.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 11433-11442
    • McKay, A.R.1    Ruotolo, B.T.2    Ilag, L.L.3    Robinson, C.V.4
  • 4
    • 0041317054 scopus 로고    scopus 로고
    • Electrospray wings for molecular elephants (Nobel Lecture)
    • Fenn, J. B. (2003). Electrospray wings for molecular elephants (Nobel Lecture). Angew. Chem. Int. Ed. 42: 3871-3894.
    • (2003) Angew. Chem. Int. Ed. , vol.42 , pp. 3871-3894
    • Fenn, J.B.1
  • 5
    • 0030621966 scopus 로고    scopus 로고
    • Studying noncovalent protein complexes by electrospray ionization mass spectrometry
    • Loo, J. A. (1997). Studying noncovalent protein complexes by electrospray ionization mass spectrometry. Mass Spectrom. Rev. 16: 1-23.
    • (1997) Mass Spectrom. Rev. , vol.16 , pp. 1-23
    • Loo, J.A.1
  • 6
    • 0001413545 scopus 로고
    • Detection of noncovalent receptor- ligand complexes by mass spectrometry
    • Ganem, B., Li, Y. T., and Henion, J. D. (1991). Detection of noncovalent receptor- ligand complexes by mass spectrometry. J. Am. Chem. Soc. 113: 6294-6296.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 6294-6296
    • Ganem, B.1    Li, Y.T.2    Henion, J.D.3
  • 7
    • 0343071628 scopus 로고
    • Observation of noncovalent enzyme-substrate and enzyme-product complexes by ion-spray mass spectrometry
    • Ganem, B., Li, Y. T., and Henion, J. D. (1991). Observation of noncovalent enzyme-substrate and enzyme-product complexes by ion-spray mass spectrometry. J. Am. Chem. Soc. 113: 7818-7819.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 7818-7819
    • Ganem, B.1    Li, Y.T.2    Henion, J.D.3
  • 8
    • 0011275132 scopus 로고
    • Direct observation of a ternary complex between the dimeric enzyme HIV-1 protease and a substrate-based inhibitor
    • Baca, M., and Kent, S. B. H. (1992). Direct observation of a ternary complex between the dimeric enzyme HIV-1 protease and a substrate-based inhibitor. J. Am. Chem. Soc. 114: 3992-3993.
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 3992-3993
    • Baca, M.1    Kent, S.B.H.2
  • 9
    • 0001401150 scopus 로고
    • Observation of the heme-globin complex in native myoglobin by electrospray-ionization mass spectrometry
    • Katta, V., and Chait, B. T. (1991). Observation of the heme-globin complex in native myoglobin by electrospray-ionization mass spectrometry. J. Am. Chem. Soc. 113: 8534-8535.
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 8534-8535
    • Katta, V.1    Chait, B.T.2
  • 10
    • 0000391707 scopus 로고
    • Observation of a noncovalent ribonuclease S-protein/S-peptide complex by electrospray ionization mass spectrometry
    • Ogorzalek Loo, R. R., Goodlett, D. R., Smith, R. D., and Loo, J. A. (1993). Observation of a noncovalent ribonuclease S-protein/S-peptide complex by electrospray ionization mass spectrometry. J. Am. Chem. Soc. 115: 4391-4392.
    • (1993) J. Am. Chem. Soc. , vol.115 , pp. 4391-4392
    • Ogorzalek Loo, R.R.1    Goodlett, D.R.2    Smith, R.D.3    Loo, J.A.4
  • 12
    • 23744516059 scopus 로고    scopus 로고
    • Estimates of protein surface areas in solution by electrospray ionization mass spectrometry
    • Kaltashov, I. A., and Mohimen, A. (2005). Estimates of protein surface areas in solution by electrospray ionization mass spectrometry. Anal. Chem. 77: 5370-5379.
    • (2005) Anal. Chem. , vol.77 , pp. 5370-5379
    • Kaltashov, I.A.1    Mohimen, A.2
  • 13
    • 84989056711 scopus 로고
    • Primary to quaternary protein structure determination with electrospray ionization and magnetic sector mass spectrometry
    • Loo, J. A., Ogorzalek Loo, R. R., and Andrews, P. C. (1993). Primary to quaternary protein structure determination with electrospray ionization and magnetic sector mass spectrometry. Org. Mass Spectrom. 28: 1640-1649.
    • (1993) Org. Mass Spectrom. , vol.28 , pp. 1640-1649
    • Loo, J.A.1    Ogorzalek Loo, R.R.2    Andrews, P.C.3
  • 14
    • 0028798172 scopus 로고
    • Observation of large subunit protein complexes by electrospray ionization mass spectrometry
    • Loo, J. A. (1995). Observation of large subunit protein complexes by electrospray ionization mass spectrometry. J. Mass Spectrom. 30: 180-183.
    • (1995) J. Mass Spectrom. , vol.30 , pp. 180-183
    • Loo, J.A.1
  • 15
    • 0028500350 scopus 로고
    • Investigation of protein-protein noncovalent interactions in soybean agglutinin by electrospray ionization time-of-flight mass spectrometry
    • Tang, X.-J., Brewer, C. F., Saha, S., Chernushevich, I., Ens, W., and Standing, K. G. (1994). Investigation of protein-protein noncovalent interactions in soybean agglutinin by electrospray ionization time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom. 8: 750-754.
    • (1994) Rapid Commun. Mass Spectrom. , vol.8 , pp. 750-754
    • Tang, X.-J.1    Brewer, C.F.2    Saha, S.3    Chernushevich, I.4    Ens, W.5    Standing, K.G.6
  • 16
    • 0000753479 scopus 로고    scopus 로고
    • In New Methods for the Study of Biomolecular Complexes
    • (NATO ASI Series, Ser. C) (W. Ens, K. G. Standing, and I. V. Chernushevich, Eds.), Kluwer, Dordrecht, The Netherlands
    • Chernushevich, I. V., Ens, W., and Standing, K. G. (1998). In New Methods for the Study of Biomolecular Complexes (NATO ASI Series, Ser. C) (W. Ens, K. G. Standing, and I. V. Chernushevich, Eds.), Vol. 510, pp. 101-116, Kluwer, Dordrecht, The Netherlands.
    • (1998) , vol.510 , pp. 101-116
    • Chernushevich, I.V.1    Ens, W.2    Standing, K.G.3
  • 17
    • 0035029535 scopus 로고    scopus 로고
    • The effect of the source pressure on the abundance of ions of noncovalent protein assemblies in an electrospray ionization orthogonal time-of-flight instrument
    • Tahallah, N., Pinkse, M., Maier, C. S., and Heck, A. J. (2001). The effect of the source pressure on the abundance of ions of noncovalent protein assemblies in an electrospray ionization orthogonal time-of-flight instrument. Rapid Commun. Mass Spectrom. 15: 596-601.
    • (2001) Rapid Commun. Mass Spectrom. , vol.15 , pp. 596-601
    • Tahallah, N.1    Pinkse, M.2    Maier, C.S.3    Heck, A.J.4
  • 18
    • 0034103427 scopus 로고    scopus 로고
    • Detection of intact megadalton protein assemblies of vanillyl-alcohol oxidase by mass spectrometry
    • Van Berkel, W. J. H., Van Den Heuvel, R. H. H., Versluis, C., and Heck, A. J. R. (2000). Detection of intact megadalton protein assemblies of vanillyl-alcohol oxidase by mass spectrometry. Protein Sci. 9: 435-439.
    • (2000) Protein Sci. , vol.9 , pp. 435-439
    • Van Berkel, W.J.H.1    Van Den Heuvel, R.H.H.2    Versluis, C.3    Heck, A.J.R.4
  • 19
    • 0005211231 scopus 로고    scopus 로고
    • In New Methods for the Study of Biomolecular Complexes
    • (W. Ens, K. G. Standing, and I. V. Chernushevich, Eds.), Kluwer, Dordrecht, The Netherlands
    • Loo, J. A., Sannes-Lowery, K. A., Hu, P., Mack, D. P., and Mei, H.-Y. (1998). In New Methods for the Study of Biomolecular Complexes (W. Ens, K. G. Standing, and I. V. Chernushevich, Eds.), pp. 83-99, Kluwer, Dordrecht, The Netherlands.
    • (1998) , pp. 83-99
    • Loo, J.A.1    Sannes-Lowery, K.A.2    Hu, P.3    Mack, D.P.4    Mei, H.-Y.5
  • 21
    • 0031573676 scopus 로고    scopus 로고
    • HIV-1 Tat peptide binding to TAR RNA by electrospray ionization mass spectrometry
    • Sannes-Lowery, K. A., Hu, P., Mack, D. P., Mei, H.-Y., and Loo, J. A. (1997). HIV-1 Tat peptide binding to TAR RNA by electrospray ionization mass spectrometry. Anal. Chem. 69: 5130-5135.
    • (1997) Anal. Chem. , vol.69 , pp. 5130-5135
    • Sannes-Lowery, K.A.1    Hu, P.2    Mack, D.P.3    Mei, H.-Y.4    Loo, J.A.5
  • 22
    • 0029794153 scopus 로고    scopus 로고
    • Probing the nature of noncovalent interactions by mass spectrometry. A study of protein-CoA ligand binding and assembly
    • Robinson, C. V., Chung, E. W., Kragelund, B. B., Knudsen, J., Aplin, R. T., Poulsen, F. M., and Dobson, C. M. (1996). Probing the nature of noncovalent interactions by mass spectrometry. A study of protein-CoA ligand binding and assembly. J. Am. Chem. Soc. 118: 8646-8653.
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 8646-8653
    • Robinson, C.V.1    Chung, E.W.2    Kragelund, B.B.3    Knudsen, J.4    Aplin, R.T.5    Poulsen, F.M.6    Dobson, C.M.7
  • 23
    • 0033590014 scopus 로고    scopus 로고
    • Studying aminoglycoside antibiotic binding to HIV-1 TAR RNA by electrospray ionization mass spectrometry
    • Sannes-Lowery, K. A., Mei, H.-Y., and Loo, J. A. (1999). Studying aminoglycoside antibiotic binding to HIV-1 TAR RNA by electrospray ionization mass spectrometry. Int. J. Mass Spectrom. 193: 115-122.
    • (1999) Int. J. Mass Spectrom. , vol.193 , pp. 115-122
    • Sannes-Lowery, K.A.1    Mei, H.-Y.2    Loo, J.A.3
  • 25
    • 33750971747 scopus 로고    scopus 로고
    • Top-down ESI-ECD-FT-ICR mass spectrometry localizes noncovalent protein-ligand binding sites
    • Xie, Y., Zhang, J., Yin, S., and Loo, J. A. (2006). Top-down ESI-ECD-FT-ICR mass spectrometry localizes noncovalent protein-ligand binding sites. J. Am. Chem. Soc. 128: 14432-14433.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 14432-14433
    • Xie, Y.1    Zhang, J.2    Yin, S.3    Loo, J.A.4
  • 26
    • 0000178042 scopus 로고
    • Micro-electrospray mass spectrometry: ultra-high-sensitivity analysis of peptides and proteins
    • Emmett, M. R., and Caprioli, R. M. (1994). Micro-electrospray mass spectrometry: ultra-high-sensitivity analysis of peptides and proteins. J. Am. Soc. Mass Spectrom. 5: 605-613.
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 605-613
    • Emmett, M.R.1    Caprioli, R.M.2
  • 27
    • 0029685702 scopus 로고    scopus 로고
    • Analytical properties of the nanoelectrospray ion source
    • Wilm, M., and Mann, M. (1996). Analytical properties of the nanoelectrospray ion source. Anal. Chem. 68: 1-8.
    • (1996) Anal. Chem. , vol.68 , pp. 1-8
    • Wilm, M.1    Mann, M.2
  • 28
    • 0037954045 scopus 로고    scopus 로고
    • Thermal dissociation of multimeric protein complexes by using nanoelectrospray mass spectrometry
    • Benesch, J. L. P., Sobott, F., and Robinson, C. V. (2003). Thermal dissociation of multimeric protein complexes by using nanoelectrospray mass spectrometry. Anal. Chem. 75: 2208-2214.
    • (2003) Anal. Chem. , vol.75 , pp. 2208-2214
    • Benesch, J.L.P.1    Sobott, F.2    Robinson, C.V.3
  • 29
    • 0027657256 scopus 로고
    • The observation of non-covalent interactions in solution by electrospray ionization mass spectrometry: promise, pitfalls and prognosis
    • Smith, R. D., and Light-Wahl, K. J. (1993). The observation of non-covalent interactions in solution by electrospray ionization mass spectrometry: promise, pitfalls and prognosis. Biol. Mass Spectrom. 22: 493-501.
    • (1993) Biol. Mass Spectrom. , vol.22 , pp. 493-501
    • Smith, R.D.1    Light-Wahl, K.J.2
  • 31
    • 0037086063 scopus 로고    scopus 로고
    • A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies
    • Sobott, F., Hernandez, H., McCammon, M. G., Tito, M. A., and Robinson, C. V. (2002). A tandem mass spectrometer for improved transmission and analysis of large macromolecular assemblies. Anal. Chem. 74: 1402-1407.
    • (2002) Anal. Chem. , vol.74 , pp. 1402-1407
    • Sobott, F.1    Hernandez, H.2    McCammon, M.G.3    Tito, M.A.4    Robinson, C.V.5
  • 32
    • 1542723081 scopus 로고    scopus 로고
    • Collisional cooling of large ions in electrospray mass spectrometry
    • Chernushevich, I. V., and Thomson, B. A. (2004). Collisional cooling of large ions in electrospray mass spectrometry. Anal. Chem. 76: 1754-1760.
    • (2004) Anal. Chem. , vol.76 , pp. 1754-1760
    • Chernushevich, I.V.1    Thomson, B.A.2
  • 33
    • 0034852208 scopus 로고    scopus 로고
    • An introduction to quadrupole-time-of-flight mass spectrometry
    • Chernushevich, I. V., Loboda, A. V., and Thomson, B. A. (2001). An introduction to quadrupole-time-of-flight mass spectrometry. J. Mass Spectrom. 36: 849-865.
    • (2001) J. Mass Spectrom. , vol.36 , pp. 849-865
    • Chernushevich, I.V.1    Loboda, A.V.2    Thomson, B.A.3
  • 34
    • 0033971534 scopus 로고    scopus 로고
    • Analysis of non-covalent protein complexes up to 290 kDa using electrospray ionization and ion trap mass spectrometry
    • Wang, Y., Schubert, M., Ingendoh, A., and Franzen, J. (2000). Analysis of non-covalent protein complexes up to 290 kDa using electrospray ionization and ion trap mass spectrometry. Rapid Commun. Mass Spectrom. 14: 12-17.
    • (2000) Rapid Commun. Mass Spectrom. , vol.14 , pp. 12-17
    • Wang, Y.1    Schubert, M.2    Ingendoh, A.3    Franzen, J.4
  • 37
    • 0034716184 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry: a technology for studying noncovalent macromolecular complexes
    • Loo, J. A. (2000). Electrospray ionization mass spectrometry: a technology for studying noncovalent macromolecular complexes. Int. J. Mass Spectrom. 200: 175-186.
    • (2000) Int. J. Mass Spectrom. , vol.200 , pp. 175-186
    • Loo, J.A.1
  • 39
    • 33645531493 scopus 로고    scopus 로고
    • Coupling desorption electrospray ionization with ion mobility/mass spectrometry for analysis of protein structure: evidence for desorption of folded and denatured states
    • Myung, S., Wiseman, J. M., Valentine, S. J., Takats, Z., Cooks, R. G., and Clemmer, D. E. (2006). Coupling desorption electrospray ionization with ion mobility/mass spectrometry for analysis of protein structure: evidence for desorption of folded and denatured states. J. Phys. Chem. B 110: 5045-5051.
    • (2006) J. Phys. Chem. B , vol.110 , pp. 5045-5051
    • Myung, S.1    Wiseman, J.M.2    Valentine, S.J.3    Takats, Z.4    Cooks, R.G.5    Clemmer, D.E.6
  • 41
    • 0141643426 scopus 로고    scopus 로고
    • Nanoelectrospray ion mobility spectrometry and ion trap mass spectrometry
    • Colgrave, M. L., Bramwell, C. J., and Creaser, C. S. (2003). Nanoelectrospray ion mobility spectrometry and ion trap mass spectrometry. Int. J. Mass Spectrom. 229: 209-216.
    • (2003) Int. J. Mass Spectrom. , vol.229 , pp. 209-216
    • Colgrave, M.L.1    Bramwell, C.J.2    Creaser, C.S.3
  • 42
    • 0034784941 scopus 로고    scopus 로고
    • Charge-reduced nano electrospray ionization combined with differential mobility analysis of peptides, proteins, glycoproteins, noncovalent protein complexes and viruses
    • Bacher, G., Szymanski, W. W., Kaufman, S. L., Zollner, P., Blaas, D., and Allmaier, G. (2001). Charge-reduced nano electrospray ionization combined with differential mobility analysis of peptides, proteins, glycoproteins, noncovalent protein complexes and viruses. J. Mass Spectrom. 36: 1038-1052.
    • (2001) J. Mass Spectrom. , vol.36 , pp. 1038-1052
    • Bacher, G.1    Szymanski, W.W.2    Kaufman, S.L.3    Zollner, P.4    Blaas, D.5    Allmaier, G.6
  • 43
    • 33646910002 scopus 로고    scopus 로고
    • 20S Proteasomes have the potential to keep substrates in store for continual degradation
    • Sharon, M., Witt, S., Felderer, K., Rockel, B., Baumeister, W., and Robinson, C. V. (2006). 20S Proteasomes have the potential to keep substrates in store for continual degradation. J. Biol. Chem. 281: 9569-9575.
    • (2006) J. Biol. Chem. , vol.281 , pp. 9569-9575
    • Sharon, M.1    Witt, S.2    Felderer, K.3    Rockel, B.4    Baumeister, W.5    Robinson, C.V.6
  • 44
    • 0031106762 scopus 로고    scopus 로고
    • A study of Src SH2 domain protein-phosphopeptide binding interactions by electrospray ionization mass spectrometry
    • Loo, J. A., Hu, P., McConnell, P., and Mueller, W. T. (1997). A study of Src SH2 domain protein-phosphopeptide binding interactions by electrospray ionization mass spectrometry. J. Am. Soc. Mass Spectrom. 8: 234-243.
    • (1997) J. Am. Soc. Mass Spectrom. , vol.8 , pp. 234-243
    • Loo, J.A.1    Hu, P.2    McConnell, P.3    Mueller, W.T.4
  • 45
    • 0029035380 scopus 로고
    • Recognition of cellwall peptide ligands by vancomycin group antibiotics: studies using ion spray mass spectrometry
    • Lim, H.-K., Hsieh, Y. L., Ganem, B., and Henion, J. (1995). Recognition of cellwall peptide ligands by vancomycin group antibiotics: studies using ion spray mass spectrometry. J. Mass Spectrom. 30: 708-714.
    • (1995) J. Mass Spectrom. , vol.30 , pp. 708-714
    • Lim, H.-K.1    Hsieh, Y.L.2    Ganem, B.3    Henion, J.4
  • 46
    • 0031956947 scopus 로고    scopus 로고
    • Quantitative evaluation of protein-protein and ligand-protein equilibria of a large allosteric enzyme by electrospray ionization time-of-flight mass spectrometry
    • Ayed, A., Krutchinsky, A. N., Ens, W., Standing, K. G., and Duckworth, H. W. (1998). Quantitative evaluation of protein-protein and ligand-protein equilibria of a large allosteric enzyme by electrospray ionization time-of-flight mass spectrometry. Rapid Commun. Mass Spectrom. 12: 339-344.
    • (1998) Rapid Commun. Mass Spectrom. , vol.12 , pp. 339-344
    • Ayed, A.1    Krutchinsky, A.N.2    Ens, W.3    Standing, K.G.4    Duckworth, H.W.5
  • 47
    • 0000876636 scopus 로고
    • Measurement of macromolecular binding using electrospray mass spectrometry. Determination of dissociation constants for oligonucleotide-serum albumin complexes
    • Greig, M. J., Gaus, H., Cummins, L. L., Sasmor, H., and Griffey, R. H. (1995). Measurement of macromolecular binding using electrospray mass spectrometry. Determination of dissociation constants for oligonucleotide-serum albumin complexes. J. Am. Chem. Soc. 117: 10765-10766.
    • (1995) J. Am. Chem. Soc. , vol.117 , pp. 10765-10766
    • Greig, M.J.1    Gaus, H.2    Cummins, L.L.3    Sasmor, H.4    Griffey, R.H.5
  • 48
    • 0034193686 scopus 로고    scopus 로고
    • Measuring dissociation constants of RNA and aminoglycoside antibiotics by electrospray ionization mass spectrometry
    • Sannes-Lowery, K. A., Griffey, R. H., and Hofstadler, S. A. (2000). Measuring dissociation constants of RNA and aminoglycoside antibiotics by electrospray ionization mass spectrometry. Anal. Biochem. 280: 264-271.
    • (2000) Anal. Biochem. , vol.280 , pp. 264-271
    • Sannes-Lowery, K.A.1    Griffey, R.H.2    Hofstadler, S.A.3
  • 49
    • 0038338887 scopus 로고    scopus 로고
    • Quantitative determination of noncovalent binding interactions using automated nanoelectrospray mass spectrometry
    • Zhang, S., Pelt, C. K. V., and Wilson, D. B. (2003). Quantitative determination of noncovalent binding interactions using automated nanoelectrospray mass spectrometry. Anal. Chem. 75: 3010-3018.
    • (2003) Anal. Chem. , vol.75 , pp. 3010-3018
    • Zhang, S.1    Pelt, C.K.V.2    Wilson, D.B.3
  • 51
    • 0036780842 scopus 로고    scopus 로고
    • Fourier transform-ion cyclotron resonance mass spectrometric resolution, identification, and screening of non-covalent complexes of Hck Src homology 2 domain receptor and ligands from a 324-member peptide combinatorial library
    • Wigger, M., Eyler, J. R., Benner, S. A., Li, W., and Marshall, A. G. (2002). Fourier transform-ion cyclotron resonance mass spectrometric resolution, identification, and screening of non-covalent complexes of Hck Src homology 2 domain receptor and ligands from a 324-member peptide combinatorial library. J. Am. Soc. Mass Spectrom. 13: 1162-1169.
    • (2002) J. Am. Soc. Mass Spectrom. , vol.13 , pp. 1162-1169
    • Wigger, M.1    Eyler, J.R.2    Benner, S.A.3    Li, W.4    Marshall, A.G.5
  • 52
    • 0037420384 scopus 로고    scopus 로고
    • Origin of asymmetric charge partitioning in the dissociation of gas-phase protein homodimers
    • Jurchen, J. C., and Williams, E. R. (2003). Origin of asymmetric charge partitioning in the dissociation of gas-phase protein homodimers. J. Am. Chem. Soc. 125: 2817-2826.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 2817-2826
    • Jurchen, J.C.1    Williams, E.R.2
  • 53
    • 0037464588 scopus 로고    scopus 로고
    • A vision for the future of genomics research
    • Collins, F. S., Green, E. D., Guttmacher, A. E., and Guyer, M. S. (2003). A vision for the future of genomics research. Nature 422: 835-847.
    • (2003) Nature , vol.422 , pp. 835-847
    • Collins, F.S.1    Green, E.D.2    Guttmacher, A.E.3    Guyer, M.S.4
  • 54
    • 0242416659 scopus 로고    scopus 로고
    • Realizing the potential of the genome revolution: The Genomes to Life program
    • Frazier, M. E., Johnson, G. M., Thomassen, D. G., Oliver, C. E., and Patrinos, A. (2003). Realizing the potential of the genome revolution: The Genomes to Life program. Science 300: 290-294.
    • (2003) Science , vol.300 , pp. 290-294
    • Frazier, M.E.1    Johnson, G.M.2    Thomassen, D.G.3    Oliver, C.E.4    Patrinos, A.5


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