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Volumn 16, Issue 5, 2007, Pages 938-946

Estrogen receptor-ligand complexes measured by chip-based nanoelectrospray mass spectrometry: An approach for the screening of endocrine disruptors

Author keywords

Electrospray ionization mass spectrometry; Endocrine disruptors; Estrogen receptor; Noncovalent; Nuclear receptor; Solution affinity

Indexed keywords

4 HYDROXYTAMOXIFEN; 4,4' ISOPROPYLIDENEDIPHENOL; DIETHYLSTILBESTROL; ENDOCRINE DISRUPTOR; ESTRADIOL; ESTROGEN RECEPTOR ALPHA; GENISTEIN;

EID: 34247572309     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1110/ps.062664107     Document Type: Article
Times cited : (43)

References (56)
  • 1
    • 4544221115 scopus 로고    scopus 로고
    • Influence of droplet size, capillary-cone distance and selected instrumental parameters for the analysis of noncovalent protein-ligand complexes by nano-electrospray ionization mass spectrometry
    • Benkestock, K., Sundqvist, G., Edlund, P.O., and Roeraade, J. 2004. Influence of droplet size, capillary-cone distance and selected instrumental parameters for the analysis of noncovalent protein-ligand complexes by nano-electrospray ionization mass spectrometry. J. Mass Spectrom. 39: 1059-1067.
    • (2004) J. Mass Spectrom , vol.39 , pp. 1059-1067
    • Benkestock, K.1    Sundqvist, G.2    Edlund, P.O.3    Roeraade, J.4
  • 2
    • 0033972376 scopus 로고    scopus 로고
    • Issues arising when interpreting results from an in vitro assay for estrogenic activity
    • Beresford, N., Routledge, E.J., Harris, C.A., and Sumpter, J.P. 2000. Issues arising when interpreting results from an in vitro assay for estrogenic activity. Toxicol. Appl. Pharmacol. 162: 22-33.
    • (2000) Toxicol. Appl. Pharmacol , vol.162 , pp. 22-33
    • Beresford, N.1    Routledge, E.J.2    Harris, C.A.3    Sumpter, J.P.4
  • 3
    • 0242438098 scopus 로고    scopus 로고
    • Identification of natural ligands of retinoic acid receptor-related orphan receptor α ligand-binding domain expressed in Sf9 cells - A mass spectrometry approach
    • Bitsch, F., Aichholz, R., Kallen, J., Geisse, S., Fournier, B., and Schlaeppi, J.M. 2003. Identification of natural ligands of retinoic acid receptor-related orphan receptor α ligand-binding domain expressed in Sf9 cells - A mass spectrometry approach. Anal. Biochem. 323: 139-149.
    • (2003) Anal. Biochem , vol.323 , pp. 139-149
    • Bitsch, F.1    Aichholz, R.2    Kallen, J.3    Geisse, S.4    Fournier, B.5    Schlaeppi, J.M.6
  • 5
    • 0031762676 scopus 로고    scopus 로고
    • Rapid screening of environmental chemicals for estrogen receptor binding capacity
    • Bolger, R., Wiese, T.E., Ervin, K., Nestich, S., and Checovich, W. 1998. Rapid screening of environmental chemicals for estrogen receptor binding capacity. Environ. Health Perspect. 106: 551-557.
    • (1998) Environ. Health Perspect , vol.106 , pp. 551-557
    • Bolger, R.1    Wiese, T.E.2    Ervin, K.3    Nestich, S.4    Checovich, W.5
  • 7
    • 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
  • 8
    • 0027428381 scopus 로고
    • Developmental effects of endocrine-disrupting chemicals in wildlife and humans
    • Colborn, T., Saal, F.S.V., and Soto, A.M. 1993. Developmental effects of endocrine-disrupting chemicals in wildlife and humans. Environ. Health Perspect. 101: 378-384.
    • (1993) Environ. Health Perspect , vol.101 , pp. 378-384
    • Colborn, T.1    Saal, F.S.V.2    Soto, A.M.3
  • 9
    • 0037824630 scopus 로고    scopus 로고
    • Mass spectrometric determination of association constants of adenylate kinase with two noncovalent inhibitors
    • Daniel, J.M., McCombie, G., Wendt, S., and Zenobi, R. 2003. Mass spectrometric determination of association constants of adenylate kinase with two noncovalent inhibitors. J. Am. Soc. Mass Spectrom. 14: 442-448.
    • (2003) J. Am. Soc. Mass Spectrom , vol.14 , pp. 442-448
    • Daniel, J.M.1    McCombie, G.2    Wendt, S.3    Zenobi, R.4
  • 11
    • 0034967293 scopus 로고    scopus 로고
    • Mass spectrometric study of the Escherichia coli repressor proteins, Iclr and GclR, and their complexes with DNA
    • Donald, L.J., Hosfield, D.J., Cuvelier, S.L., Ens, W., Standing, K.G., and Duckworth, H.W. 2001. Mass spectrometric study of the Escherichia coli repressor proteins, Iclr and GclR, and their complexes with DNA. Protein Sci. 10: 1370-1380.
    • (2001) Protein Sci , vol.10 , pp. 1370-1380
    • Donald, L.J.1    Hosfield, D.J.2    Cuvelier, S.L.3    Ens, W.4    Standing, K.G.5    Duckworth, H.W.6
  • 12
    • 0036377428 scopus 로고    scopus 로고
    • Advantages and drawbacks of nanospray for studying noncovalent protein-DNA complexes by mass spectrometry
    • Gabelica, V., Vreuls, C., Filee, P., Duval, V., Joris, B., and De Pauw, E. 2002. Advantages and drawbacks of nanospray for studying noncovalent protein-DNA complexes by mass spectrometry. Rapid Commun. Mass Spectrom. 16: 1723-1728. .
    • (2002) Rapid Commun. Mass Spectrom , vol.16 , pp. 1723-1728
    • Gabelica, V.1    Vreuls, C.2    Filee, P.3    Duval, V.4    Joris, B.5    De Pauw, E.6
  • 13
    • 0037941316 scopus 로고    scopus 로고
    • Influence of response factors on determining equilibrium association constants of noncovalent complexes by electrospray ionization mass spectrometry
    • Gabelica, V., Galic, N., Rosu, F., Houssier, C., and De Pauw, E. 2003. Influence of response factors on determining equilibrium association constants of noncovalent complexes by electrospray ionization mass spectrometry. J. Mass Spectrom. 38: 491-501.
    • (2003) J. Mass Spectrom , vol.38 , pp. 491-501
    • Gabelica, V.1    Galic, N.2    Rosu, F.3    Houssier, C.4    De Pauw, E.5
  • 14
    • 0035805514 scopus 로고    scopus 로고
    • Crystal structure of a mutant hER α ligand-binding domain reveals key structural features for the mechanism of partial agonism
    • Gangloff, M., Ruff, M., Eiler, S., Duclaud, S., Wurtz, J.M., and Moras, D. 2001. Crystal structure of a mutant hER α ligand-binding domain reveals key structural features for the mechanism of partial agonism. J. Biol. Chem. 276: 15059-15065.
    • (2001) J. Biol. Chem , vol.276 , pp. 15059-15065
    • Gangloff, M.1    Ruff, M.2    Eiler, S.3    Duclaud, S.4    Wurtz, J.M.5    Moras, D.6
  • 15
    • 0033080755 scopus 로고    scopus 로고
    • Geoghegan, K.F., Dixon, H.B., Rosner, P.J., Hoth, L.R., Lanzetti, A.J., Borzilleri, K.A., Marr, E.S., Pezzullo, L.H., Martin, L.B., LeMotte, P.K., et al. 1999. Spontaneous α-N-6-phosphogluconoylation of a His tag in Escherichia coli: The cause of extra mass of 258 or 178 Da in fusion proteins. Anal. Biochem. 267: 169-184.
    • Geoghegan, K.F., Dixon, H.B., Rosner, P.J., Hoth, L.R., Lanzetti, A.J., Borzilleri, K.A., Marr, E.S., Pezzullo, L.H., Martin, L.B., LeMotte, P.K., et al. 1999. Spontaneous α-N-6-phosphogluconoylation of a "His tag" in Escherichia coli: The cause of extra mass of 258 or 178 Da in fusion proteins. Anal. Biochem. 267: 169-184.
  • 16
    • 0036187372 scopus 로고    scopus 로고
    • Structural and functional evidence for ligand-independent transcriptional activation by the estrogen-related receptor 3
    • Greschik, H., Wurtz, J.M., Sanglier, S., Bourguet, W., van Dorsselaer, A., Moras, D., and Renaud, J.P. 2002. Structural and functional evidence for ligand-independent transcriptional activation by the estrogen-related receptor 3. Mol. Cell 9: 303-313.
    • (2002) Mol. Cell , vol.9 , pp. 303-313
    • Greschik, H.1    Wurtz, J.M.2    Sanglier, S.3    Bourguet, W.4    van Dorsselaer, A.5    Moras, D.6    Renaud, J.P.7
  • 17
    • 0030833331 scopus 로고    scopus 로고
    • Reproductive health in humans and wildlife: Are adverse trends associated with environmental chemical exposure?
    • Harrison, P.T.C., Holmes, P., and Humfrey, C.D.N. 1997. Reproductive health in humans and wildlife: Are adverse trends associated with environmental chemical exposure? Sci. Total Environ. 205: 97-106.
    • (1997) Sci. Total Environ , vol.205 , pp. 97-106
    • Harrison, P.T.C.1    Holmes, P.2    Humfrey, C.D.N.3
  • 18
    • 0032532125 scopus 로고    scopus 로고
    • Direct determination of solution binding constants for noncovalent complexes between bacterial cell wall peptide analogues and vancomycin group antibiotics by electrospray ionization mass spectrometry
    • Jorgensen, T.J.D., Roepstorff, P., and Heck, A.J.R. 1998. Direct determination of solution binding constants for noncovalent complexes between bacterial cell wall peptide analogues and vancomycin group antibiotics by electrospray ionization mass spectrometry. Anal. Chem. 70: 4427-4432.
    • (1998) Anal. Chem , vol.70 , pp. 4427-4432
    • Jorgensen, T.J.D.1    Roepstorff, P.2    Heck, A.J.R.3
  • 19
    • 0036135966 scopus 로고    scopus 로고
    • Use of electrospray ionization mass spectrometry to study binding interactions between a replication terminator protein and DNA
    • Kapur, A., Beck, J.L., Brown, S.E., Dixon, N.E., and Sheil, M.M. 2002. Use of electrospray ionization mass spectrometry to study binding interactions between a replication terminator protein and DNA. Protein Sci. 11: 147-157.
    • (2002) Protein Sci , vol.11 , pp. 147-157
    • Kapur, A.1    Beck, J.L.2    Brown, S.E.3    Dixon, N.E.4    Sheil, M.M.5
  • 20
    • 0141482197 scopus 로고    scopus 로고
    • Use of a microchip device coupled with mass spectrometry for ligand screening of a multi-protein target
    • Keetch, C.A., Hernandez, H., Sterling, A., Baumert, M., Allen, M.H., and Robinson, C.V. 2003. Use of a microchip device coupled with mass spectrometry for ligand screening of a multi-protein target. Anal. Chem. 75: 4937-4941.
    • (2003) Anal. Chem , vol.75 , pp. 4937-4941
    • Keetch, C.A.1    Hernandez, H.2    Sterling, A.3    Baumert, M.4    Allen, M.H.5    Robinson, C.V.6
  • 22
    • 0023808861 scopus 로고
    • The estrogen-receptor binds tightly to its responsive element as a ligand-induced homodimer
    • Kumar, V. and Chambon, P. 1988. The estrogen-receptor binds tightly to its responsive element as a ligand-induced homodimer. Cell 55: 145-156.
    • (1988) Cell , vol.55 , pp. 145-156
    • Kumar, V.1    Chambon, P.2
  • 23
    • 0036388229 scopus 로고    scopus 로고
    • Detection of a receptor-ligand noncovalent complex using a triple quadrupole mass spectrometer
    • Lengqvist, J., Griffiths, W.J., Perlmann, T., and Sjovall, J. 2002. Detection of a receptor-ligand noncovalent complex using a triple quadrupole mass spectrometer. Rapid Commun. Mass Spectrom. 16: 2003-2006.
    • (2002) Rapid Commun. Mass Spectrom , vol.16 , pp. 2003-2006
    • Lengqvist, J.1    Griffiths, W.J.2    Perlmann, T.3    Sjovall, J.4
  • 24
    • 4043140077 scopus 로고    scopus 로고
    • Polyunsaturated fatty acids including docosahexaenoic and arachidonic acid bind to the retinoid X receptor α ligand-binding domain
    • Lengqvist, J., de Urquiza, A.M., Bergman, A.C., Willson, T.M., Sjovall, J., Perlmann, T., and Griffiths, W.J. 2004. Polyunsaturated fatty acids including docosahexaenoic and arachidonic acid bind to the retinoid X receptor α ligand-binding domain. Mol. Cell. Proteomics 3: 692-703.
    • (2004) Mol. Cell. Proteomics , vol.3 , pp. 692-703
    • Lengqvist, J.1    de Urquiza, A.M.2    Bergman, A.C.3    Willson, T.M.4    Sjovall, J.5    Perlmann, T.6    Griffiths, W.J.7
  • 25
    • 25144441148 scopus 로고    scopus 로고
    • Electrospray mass spectrometry for the direct accurate mass measurement of ligands in complex with the retinoid X receptor α ligand binding domain
    • Lengqvist, J., Alvelius, G., Jornvall, H., Sjovall, J., Perlmann, T., and Griffiths, W.J. 2005. Electrospray mass spectrometry for the direct accurate mass measurement of ligands in complex with the retinoid X receptor α ligand binding domain. J. Am. Soc. Mass Spectrom. 16: 1631-1640.
    • (2005) J. Am. Soc. Mass Spectrom , vol.16 , pp. 1631-1640
    • Lengqvist, J.1    Alvelius, G.2    Jornvall, H.3    Sjovall, J.4    Perlmann, T.5    Griffiths, W.J.6
  • 26
    • 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
  • 27
    • 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.F., McConnell, P., Mueller, W.T., Sawyer, T.K., and Thanabal, V. 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.F.2    McConnell, P.3    Mueller, W.T.4    Sawyer, T.K.5    Thanabal, V.6
  • 28
    • 10044245924 scopus 로고    scopus 로고
    • Understanding the selectivity of genistein for human estrogen receptor-β using X-ray crystallography and computational methods
    • Manas, E.S., Xu, Z.B., Unwalla, R.J., and Somers, W.S. 2004. Understanding the selectivity of genistein for human estrogen receptor-β using X-ray crystallography and computational methods. Structure 12: 2197-2207.
    • (2004) Structure , vol.12 , pp. 2197-2207
    • Manas, E.S.1    Xu, Z.B.2    Unwalla, R.J.3    Somers, W.S.4
  • 29
    • 0034839464 scopus 로고    scopus 로고
    • Gas-phase binding of noncovalent protein complexes between bovine pancreatic trypsin inhibitor and its target enzymes studied by electrospray ionization tandem mass spectrometry
    • Nesatyy, V.J. 2001. Gas-phase binding of noncovalent protein complexes between bovine pancreatic trypsin inhibitor and its target enzymes studied by electrospray ionization tandem mass spectrometry. J. Mass Spectrom. 36: 950-959.
    • (2001) J. Mass Spectrom , vol.36 , pp. 950-959
    • Nesatyy, V.J.1
  • 30
    • 0033762869 scopus 로고    scopus 로고
    • Interactions of dietary estrogens with human estrogen receptors and the effect on estrogen receptor-estrogen response element complex formation
    • Nikov, G.N., Hopkins, N.E., Boue, S., and Alworth, W.L. 2000. Interactions of dietary estrogens with human estrogen receptors and the effect on estrogen receptor-estrogen response element complex formation. Environ. Health Perspect. 108: 867-872.
    • (2000) Environ. Health Perspect , vol.108 , pp. 867-872
    • Nikov, G.N.1    Hopkins, N.E.2    Boue, S.3    Alworth, W.L.4
  • 31
    • 0036711669 scopus 로고    scopus 로고
    • Estrogen receptor binding assay method for endocrine disruptors using fluorescence polarization
    • Ohno, K., Fukushima, T., Santa, T., Waizumi, N., Tokuyama, H., Maeda, M., and Imai, K. 2002. Estrogen receptor binding assay method for endocrine disruptors using fluorescence polarization. Anal. Chem. 74: 4391-4396.
    • (2002) Anal. Chem , vol.74 , pp. 4391-4396
    • Ohno, K.1    Fukushima, T.2    Santa, T.3    Waizumi, N.4    Tokuyama, H.5    Maeda, M.6    Imai, K.7
  • 32
    • 0041418170 scopus 로고    scopus 로고
    • Study on interactions of endocrine disruptors with estrogen receptor using fluorescence polarization
    • Ohno, K., Suzuki, S., Fukushima, T., Maeda, M., Santa, T., and Imai, K. 2003. Study on interactions of endocrine disruptors with estrogen receptor using fluorescence polarization. Analyst 128: 1091-1096.
    • (2003) Analyst , vol.128 , pp. 1091-1096
    • Ohno, K.1    Suzuki, S.2    Fukushima, T.3    Maeda, M.4    Santa, T.5    Imai, K.6
  • 33
    • 33745238662 scopus 로고    scopus 로고
    • Stability of complementary and mismatched DNA duplexes: Comparison and contrast in gas versus solution phases
    • Pan, S., Sun, X.J., and Lee, J.K. 2006. Stability of complementary and mismatched DNA duplexes: Comparison and contrast in gas versus solution phases. Int. J. Mass Spectrom. 253: 238-248.
    • (2006) Int. J. Mass Spectrom , vol.253 , pp. 238-248
    • Pan, S.1    Sun, X.J.2    Lee, J.K.3
  • 34
    • 4744344760 scopus 로고    scopus 로고
    • Features of the ESI mechanism that affect the observation of multiply charged noncovalent protein complexes and the determination of the association constant by the titration method
    • Peschke, M., Verkerk, U.H., and Kebarle, P. 2004. Features of the ESI mechanism that affect the observation of multiply charged noncovalent protein complexes and the determination of the association constant by the titration method. J. Am. Soc. Mass Spectrom. 15: 1424-1434.
    • (2004) J. Am. Soc. Mass Spectrom , vol.15 , pp. 1424-1434
    • Peschke, M.1    Verkerk, U.H.2    Kebarle, P.3
  • 36
    • 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
  • 37
    • 0036756804 scopus 로고    scopus 로고
    • Electrospray ionization mass spectrometry analysis revealed a similar to 310 kDa noncovalent hexamer of HPr kinase/phosphatase from Bacillus subtilis
    • Sanglier, S., Ramstrom, H., Haiech, J., Leize, E., and Van Dorsselaer, A. 2002. Electrospray ionization mass spectrometry analysis revealed a similar to 310 kDa noncovalent hexamer of HPr kinase/phosphatase from Bacillus subtilis. Int. J. Mass Spectrom. 219: 681-696.
    • (2002) Int. J. Mass Spectrom , vol.219 , pp. 681-696
    • Sanglier, S.1    Ramstrom, H.2    Haiech, J.3    Leize, E.4    Van Dorsselaer, A.5
  • 39
    • 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
  • 40
    • 0035894046 scopus 로고    scopus 로고
    • Influence of pressure in the first pumping stage on analyte desolvation and fragmentation in nano-ESI MS
    • Schmidt, A., Bahr, U., and Karas, M. 2001. Influence of pressure in the first pumping stage on analyte desolvation and fragmentation in nano-ESI MS. Anal. Chem. 73: 6040-6046.
    • (2001) Anal. Chem , vol.73 , pp. 6040-6046
    • Schmidt, A.1    Bahr, U.2    Karas, M.3
  • 41
    • 0032446607 scopus 로고    scopus 로고
    • The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen
    • Shiau, A.K., Barstad, D., Loria, P.M., Cheng, L., Kushner, P.J., Agard, D.A., and Greene, G.L. 1998. The structural basis of estrogen receptor/coactivator recognition and the antagonism of this interaction by tamoxifen. Cell 95: 927-937.
    • (1998) Cell , vol.95 , pp. 927-937
    • Shiau, A.K.1    Barstad, D.2    Loria, P.M.3    Cheng, L.4    Kushner, P.J.5    Agard, D.A.6    Greene, G.L.7
  • 42
    • 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
  • 44
    • 0032052810 scopus 로고    scopus 로고
    • An updated review of environmental estrogen and androgen mimics and antagonists
    • Sonnenschein, C. and Soto, A.M. 1998. An updated review of environmental estrogen and androgen mimics and antagonists. J. Steroid Biochem. Mol. Biol. 65: 143-150.
    • (1998) J. Steroid Biochem. Mol. Biol , vol.65 , pp. 143-150
    • Sonnenschein, C.1    Soto, A.M.2
  • 46
  • 47
    • 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.R. 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.R.4
  • 48
    • 0035193327 scopus 로고    scopus 로고
    • Probing molecular interactions in intact antibody: Antigen complexes, an electrospray time-of-flight mass spectrometry approach
    • Tito, M.A., Miller, J., Walker, N., Griffin, K.F., Williamson, E.D., Despeyroux-Hill, D., Titball, R.W., and Robinson, C.V. 2001. Probing molecular interactions in intact antibody: Antigen complexes, an electrospray time-of-flight mass spectrometry approach. Biophys. J. 81: 3503-3509.
    • (2001) Biophys. J , vol.81 , pp. 3503-3509
    • Tito, M.A.1    Miller, J.2    Walker, N.3    Griffin, K.F.4    Williamson, E.D.5    Despeyroux-Hill, D.6    Titball, R.W.7    Robinson, C.V.8
  • 49
    • 3543008337 scopus 로고    scopus 로고
    • Determination of dissociation constants for protein-ligand complexes by electrospray ionization mass spectrometry
    • Tjernberg, A., Carno, S., Oliv, F., Benkestock, K., Edlund, P.O., Griffiths, W.J., and Hallen, D. 2004. Determination of dissociation constants for protein-ligand complexes by electrospray ionization mass spectrometry. Anal. Chem. 76: 4325-4331.
    • (2004) Anal. Chem , vol.76 , pp. 4325-4331
    • Tjernberg, A.1    Carno, S.2    Oliv, F.3    Benkestock, K.4    Edlund, P.O.5    Griffiths, W.J.6    Hallen, D.7
  • 50
    • 0032784099 scopus 로고    scopus 로고
    • Covalent and noncovalent dissociations of gas-phase complexes of avoparcin and bacterial receptor mimicking precursor peptides studied by collisionally activated decomposition mass spectrometry
    • van der Kerk-van Hoof, A. and Heck, A.J.R. 1999. Covalent and noncovalent dissociations of gas-phase complexes of avoparcin and bacterial receptor mimicking precursor peptides studied by collisionally activated decomposition mass spectrometry. J. Mass Spectrom. 34: 813-819.
    • (1999) J. Mass Spectrom , vol.34 , pp. 813-819
    • van der Kerk-van Hoof, A.1    Heck, A.J.R.2
  • 51
    • 0141958921 scopus 로고    scopus 로고
    • Influence of solution and gas phase processes on protein-carbohydrate binding affinities determined by nanoelectrospray Fourier transform ion cyclotron resonance mass spectrometry
    • Wang, W.J., Kitova, E.N., and Klassen, J.S. 2003. Influence of solution and gas phase processes on protein-carbohydrate binding affinities determined by nanoelectrospray Fourier transform ion cyclotron resonance mass spectrometry. Anal. Chem. 75: 4945-4955.
    • (2003) Anal. Chem , vol.75 , pp. 4945-4955
    • Wang, W.J.1    Kitova, E.N.2    Klassen, J.S.3
  • 53
    • 0030200078 scopus 로고    scopus 로고
    • Intact noncovalent dimer of estrogen receptor ligand-binding domain can be detected by electrospray ionization mass spectrometry
    • Witkowska, H.E., Green, B.N., Carlquist, M., and Shackleton, C.H.L. 1996. Intact noncovalent dimer of estrogen receptor ligand-binding domain can be detected by electrospray ionization mass spectrometry. Steroids 61: 433-438.
    • (1996) Steroids , vol.61 , pp. 433-438
    • Witkowska, H.E.1    Green, B.N.2    Carlquist, M.3    Shackleton, C.H.L.4
  • 54
    • 21344447983 scopus 로고    scopus 로고
    • Determination of zinc to β-peptide binding constants with electrospray ionization mass spectrometry
    • Wortmann, A., Rossi, F., Lelais, G., and Zenobi, R. 2005. Determination of zinc to β-peptide binding constants with electrospray ionization mass spectrometry. J. Mass Spectrom. 40: 777-784.
    • (2005) J. Mass Spectrom , vol.40 , pp. 777-784
    • Wortmann, A.1    Rossi, F.2    Lelais, G.3    Zenobi, R.4
  • 56
    • 0038338887 scopus 로고    scopus 로고
    • Quantitative determination of noncovalent binding interactions using automated nanoelectrospray mass spectrometry
    • Zhang, S., Van Pelt, C.K., 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    Van Pelt, C.K.2    Wilson, D.B.3


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