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Volumn 366, Issue 4, 2007, Pages 1282-1293

Functional Characterization and Conformational Analysis of the Herpesvirus saimiri Tip-C484 Protein

Author keywords

hydrogen exchange; kinase activation; Lck; mass spectrometry; unstructured protein

Indexed keywords

AMIDE; DEUTERIUM; HYDROGEN; PHOSPHOTRANSFERASE; PROTEIN DERIVATIVE; PROTEIN KINASE LCK; RECOMBINANT PROTEIN; TYROSINE KINASE INTERACTING PROTEIN; UNCLASSIFIED DRUG;

EID: 33846642597     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.12.026     Document Type: Article
Times cited : (18)

References (48)
  • 2
    • 33646161719 scopus 로고    scopus 로고
    • Regulation of intracellular signalling by the terminal membrane proteins of members of the Gammaherpesvirinae
    • Brinkmann M.M., and Schulz T.F. Regulation of intracellular signalling by the terminal membrane proteins of members of the Gammaherpesvirinae. J. Gen. Virol. 87 (2006) 1047-1074
    • (2006) J. Gen. Virol. , vol.87 , pp. 1047-1074
    • Brinkmann, M.M.1    Schulz, T.F.2
  • 3
    • 0025277298 scopus 로고
    • The divergence between two oncogenic Herpesvirus saimiri strains in a genomic region related to the transforming phenotype
    • Biesinger B., Trimble J.J., Desrosiers R.C., and Fleckenstein B. The divergence between two oncogenic Herpesvirus saimiri strains in a genomic region related to the transforming phenotype. Virology 176 (1990) 505-514
    • (1990) Virology , vol.176 , pp. 505-514
    • Biesinger, B.1    Trimble, J.J.2    Desrosiers, R.C.3    Fleckenstein, B.4
  • 5
    • 0023275402 scopus 로고
    • In vitro immortalization of marmoset cells with three subgroups of herpesvirus saimiri
    • Szomolanyi E., Medveczky P., and Mulder C. In vitro immortalization of marmoset cells with three subgroups of herpesvirus saimiri. J. Virol. 61 (1987) 3485-3490
    • (1987) J. Virol. , vol.61 , pp. 3485-3490
    • Szomolanyi, E.1    Medveczky, P.2    Mulder, C.3
  • 6
    • 0022654506 scopus 로고
    • Nononcogenic deletion mutants of herpesvirus saimiri are defective for in vitro immortalization
    • Desrosiers R.C., Silva D.P., Waldron L.M., and Letvin N.L. Nononcogenic deletion mutants of herpesvirus saimiri are defective for in vitro immortalization. J. Virol. 57 (1986) 701-705
    • (1986) J. Virol. , vol.57 , pp. 701-705
    • Desrosiers, R.C.1    Silva, D.P.2    Waldron, L.M.3    Letvin, N.L.4
  • 7
    • 0028940769 scopus 로고
    • The product of the Herpesvirus saimiri open reading frame 1 (tip) interacts with T cell-specific kinase p56lck in transformed cells
    • Biesinger B., Tsygankov A.Y., Fickenscher H., Emmrich F., Fleckenstein B., Bolen J.B., and Broker B.M. The product of the Herpesvirus saimiri open reading frame 1 (tip) interacts with T cell-specific kinase p56lck in transformed cells. J. Biol. Chem. 270 (1995) 4729-4734
    • (1995) J. Biol. Chem. , vol.270 , pp. 4729-4734
    • Biesinger, B.1    Tsygankov, A.Y.2    Fickenscher, H.3    Emmrich, F.4    Fleckenstein, B.5    Bolen, J.B.6    Broker, B.M.7
  • 8
    • 0029088419 scopus 로고
    • Transcriptional and post-transcriptional regulation of the receptor for urokinase-type plasminogen activator by cytokines and tumor promoters in the human lung carcinoma cell line A549
    • Lund L.R., Ellis V., Roenne E., Pyke C., and Danoe K. Transcriptional and post-transcriptional regulation of the receptor for urokinase-type plasminogen activator by cytokines and tumor promoters in the human lung carcinoma cell line A549. Biochem. J. 310 (1995) 345-352
    • (1995) Biochem. J. , vol.310 , pp. 345-352
    • Lund, L.R.1    Ellis, V.2    Roenne, E.3    Pyke, C.4    Danoe, K.5
  • 9
    • 0029655457 scopus 로고    scopus 로고
    • A herpesvirus saimiri membrane protein required for interleukin-2 independence forms a stable complex with p56lck
    • Lund T., Medveczky M.M., Neame P.J., and Medveczky P.G. A herpesvirus saimiri membrane protein required for interleukin-2 independence forms a stable complex with p56lck. J. Virol. 70 (1996) 600-606
    • (1996) J. Virol. , vol.70 , pp. 600-606
    • Lund, T.1    Medveczky, M.M.2    Neame, P.J.3    Medveczky, P.G.4
  • 10
    • 0025876228 scopus 로고
    • Identification and characterization of the herpesvirus saimiri oncoprotein STP-C488
    • Jung J.U., and Desrosiers R.C. Identification and characterization of the herpesvirus saimiri oncoprotein STP-C488. J. Virol. 65 (1991) 6953-6960
    • (1991) J. Virol. , vol.65 , pp. 6953-6960
    • Jung, J.U.1    Desrosiers, R.C.2
  • 11
    • 0027771757 scopus 로고
    • Expression of the collagen-like putative oncoprotein of Herpesvirus saimiri in transformed T cells
    • Medveczky M.M., Geck P., Vassallo R., and Medveczky P.G. Expression of the collagen-like putative oncoprotein of Herpesvirus saimiri in transformed T cells. Virus Genes 7 (1993) 349-365
    • (1993) Virus Genes , vol.7 , pp. 349-365
    • Medveczky, M.M.1    Geck, P.2    Vassallo, R.3    Medveczky, P.G.4
  • 12
    • 0027437210 scopus 로고
    • IL-2 independent growth and cytotoxicity of herpesvirus saimiri-infected human CD8 cells and involvement of two open reading frame sequences of the virus
    • Medveczky M.M., Geck P., Sullivan J.L., Serbousek D., Djeu J.Y., and Medveczky P.G. IL-2 independent growth and cytotoxicity of herpesvirus saimiri-infected human CD8 cells and involvement of two open reading frame sequences of the virus. Virology 196 (1993) 402-412
    • (1993) Virology , vol.196 , pp. 402-412
    • Medveczky, M.M.1    Geck, P.2    Sullivan, J.L.3    Serbousek, D.4    Djeu, J.Y.5    Medveczky, P.G.6
  • 13
    • 1842294583 scopus 로고    scopus 로고
    • Functional phenotype of transformed human alphabeta and gammadelta T cells determined by different subgroup C strains of herpesvirus Saimiri
    • Fickenscher H., Bokel C., Knappe A., Biesinger B., Meinl E., Fleischer B., et al. Functional phenotype of transformed human alphabeta and gammadelta T cells determined by different subgroup C strains of herpesvirus Saimiri. J. Virol. 71 (1997) 2252-2263
    • (1997) J. Virol. , vol.71 , pp. 2252-2263
    • Fickenscher, H.1    Bokel, C.2    Knappe, A.3    Biesinger, B.4    Meinl, E.5    Fleischer, B.6
  • 14
    • 0031906144 scopus 로고    scopus 로고
    • STP and Tip are essential for herpesvirus saimiri oncogenicity
    • Duboise S.M., Guo J., Czajak S., Desrosiers R.C., and Jung J.U. STP and Tip are essential for herpesvirus saimiri oncogenicity. J. Virol. 72 (1998) 1308-1313
    • (1998) J. Virol. , vol.72 , pp. 1308-1313
    • Duboise, S.M.1    Guo, J.2    Czajak, S.3    Desrosiers, R.C.4    Jung, J.U.5
  • 15
    • 0033948011 scopus 로고    scopus 로고
    • Lck protein tyrosine kinase is a key regulator of T-cell activation and a target for signal intervention by Herpesvirus saimiri and other viral gene products
    • Isakov N., and Biesinger B. Lck protein tyrosine kinase is a key regulator of T-cell activation and a target for signal intervention by Herpesvirus saimiri and other viral gene products. Eur. J. Biochem. 267 (2000) 3413-3421
    • (2000) Eur. J. Biochem. , vol.267 , pp. 3413-3421
    • Isakov, N.1    Biesinger, B.2
  • 16
    • 0032927057 scopus 로고    scopus 로고
    • The Lck binding domain of herpesvirus saimiri tip-484 constitutively activates Lck and STAT3 in T cells
    • Lund T.C., Prator P.C., Medveczky M.M., and Medveczky P.G. The Lck binding domain of herpesvirus saimiri tip-484 constitutively activates Lck and STAT3 in T cells. J. Virol. 73 (1999) 1689-1694
    • (1999) J. Virol. , vol.73 , pp. 1689-1694
    • Lund, T.C.1    Prator, P.C.2    Medveczky, M.M.3    Medveczky, P.G.4
  • 18
    • 0034715580 scopus 로고    scopus 로고
    • Activation of the Lck tyrosine protein kinase by the Herpesvirus saimiri tip protein involves two binding interactions
    • Hartley D.A., Amdjadi K., Hurley T.R., Lund T.C., Medveczky P.G., and Sefton B.M. Activation of the Lck tyrosine protein kinase by the Herpesvirus saimiri tip protein involves two binding interactions. Virology 276 (2000) 339-348
    • (2000) Virology , vol.276 , pp. 339-348
    • Hartley, D.A.1    Amdjadi, K.2    Hurley, T.R.3    Lund, T.C.4    Medveczky, P.G.5    Sefton, B.M.6
  • 19
    • 9744266665 scopus 로고    scopus 로고
    • Characterization of Lck-binding elements in the herpesviral regulatory Tip protein
    • Bauer F., Hofinger E., Hoffmann S., Rosch P., Schweimer K., and Sticht H. Characterization of Lck-binding elements in the herpesviral regulatory Tip protein. Biochemistry 43 (2004) 14932-14939
    • (2004) Biochemistry , vol.43 , pp. 14932-14939
    • Bauer, F.1    Hofinger, E.2    Hoffmann, S.3    Rosch, P.4    Schweimer, K.5    Sticht, H.6
  • 20
    • 33749467078 scopus 로고    scopus 로고
    • Growth transformation of human T cells by herpesvirus saimiri requires multiple tip-lck interaction motifs
    • Heck E., Friedrich U., Gack M.U., Lengenfelder D., Schmidt M., Muller-Fleckenstein I., et al. Growth transformation of human T cells by herpesvirus saimiri requires multiple tip-lck interaction motifs. J. Virol. 80 (2006) 9934-9942
    • (2006) J. Virol. , vol.80 , pp. 9934-9942
    • Heck, E.1    Friedrich, U.2    Gack, M.U.3    Lengenfelder, D.4    Schmidt, M.5    Muller-Fleckenstein, I.6
  • 21
    • 0037161298 scopus 로고    scopus 로고
    • Structural investigation of the binding of a herpesviral protein to the SH3 domain of tyrosine kinase Lck
    • Schweimer K., Hoffmann S., Bauer F., Friedrich U., Kardinal C., Feller S.M., et al. Structural investigation of the binding of a herpesviral protein to the SH3 domain of tyrosine kinase Lck. Biochemistry 41 (2002) 5120-5130
    • (2002) Biochemistry , vol.41 , pp. 5120-5130
    • Schweimer, K.1    Hoffmann, S.2    Bauer, F.3    Friedrich, U.4    Kardinal, C.5    Feller, S.M.6
  • 23
    • 10044296373 scopus 로고    scopus 로고
    • SAXS study of the PIR domain from the Grb14 molecular adaptor: a natively unfolded protein with a transient structure primer?
    • Moncoq K., Broutin I., Craescu C.T., Vachette P., Ducruix A., and Durand D. SAXS study of the PIR domain from the Grb14 molecular adaptor: a natively unfolded protein with a transient structure primer?. Biophys. J. 87 (2004) 4056-4064
    • (2004) Biophys. J. , vol.87 , pp. 4056-4064
    • Moncoq, K.1    Broutin, I.2    Craescu, C.T.3    Vachette, P.4    Ducruix, A.5    Durand, D.6
  • 24
    • 0033575209 scopus 로고    scopus 로고
    • Activation of the lck tyrosine-protein kinase by the binding of the tip protein of herpesvirus saimiri in the absence of regulatory tyrosine phosphorylation
    • Hartley D.A., Hurley T.R., Hardwick J.S., Lund T.C., Medveczky P.G., and Sefton B.M. Activation of the lck tyrosine-protein kinase by the binding of the tip protein of herpesvirus saimiri in the absence of regulatory tyrosine phosphorylation. J. Biol. Chem. 274 (1999) 20056-20059
    • (1999) J. Biol. Chem. , vol.274 , pp. 20056-20059
    • Hartley, D.A.1    Hurley, T.R.2    Hardwick, J.S.3    Lund, T.C.4    Medveczky, P.G.5    Sefton, B.M.6
  • 25
    • 0033063429 scopus 로고    scopus 로고
    • Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor
    • Schindler T., Sicheri F., Pico A., Gazit A., Levitzki A., and Kuriyan J. Crystal structure of Hck in complex with a Src family-selective tyrosine kinase inhibitor. Mol. Cell 3 (1999) 639-648
    • (1999) Mol. Cell , vol.3 , pp. 639-648
    • Schindler, T.1    Sicheri, F.2    Pico, A.3    Gazit, A.4    Levitzki, A.5    Kuriyan, J.6
  • 26
    • 33748751555 scopus 로고    scopus 로고
    • HIV-1 Nef selectively activates Src family kinases Hck, Lyn, and c-Src through direct SH3 domain interaction
    • Trible R.P., Emert-Sedlak L., and Smithgall T.E. HIV-1 Nef selectively activates Src family kinases Hck, Lyn, and c-Src through direct SH3 domain interaction. J. Biol. Chem. 281 (2006) 27029-27038
    • (2006) J. Biol. Chem. , vol.281 , pp. 27029-27038
    • Trible, R.P.1    Emert-Sedlak, L.2    Smithgall, T.E.3
  • 27
    • 0031060289 scopus 로고    scopus 로고
    • Herpesvirus saimiri Tip-484 membrane protein markedly increases p56lck activity in T cells
    • Lund T., Medveczky M.M., and Medveczky P.G. Herpesvirus saimiri Tip-484 membrane protein markedly increases p56lck activity in T cells. J. Virol. 71 (1997) 378-382
    • (1997) J. Virol. , vol.71 , pp. 378-382
    • Lund, T.1    Medveczky, M.M.2    Medveczky, P.G.3
  • 28
    • 0029917331 scopus 로고    scopus 로고
    • A functional screen in yeast for regulators and antagonizers of heterologous protein tyrosine kinases
    • Superti-Furga G., Jonsson K., and Courtneidge S.A. A functional screen in yeast for regulators and antagonizers of heterologous protein tyrosine kinases. Nature Biotechnol. 14 (1996) 600-605
    • (1996) Nature Biotechnol. , vol.14 , pp. 600-605
    • Superti-Furga, G.1    Jonsson, K.2    Courtneidge, S.A.3
  • 29
    • 0037378105 scopus 로고    scopus 로고
    • Regulation of c-Fes tyrosine kinase activity by coiled-coil and SH2 domains: analysis with Saccharomyces cerevisiae
    • Takashima Y., Delfino F.J., Engen J.R., Superti-Furga G., and Smithgall T.E. Regulation of c-Fes tyrosine kinase activity by coiled-coil and SH2 domains: analysis with Saccharomyces cerevisiae. Biochemistr 42 (2003) 3567-3574
    • (2003) Biochemistr , vol.42 , pp. 3567-3574
    • Takashima, Y.1    Delfino, F.J.2    Engen, J.R.3    Superti-Furga, G.4    Smithgall, T.E.5
  • 30
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • Wales T.E., and Engen J.R. Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrom. Rev. 25 (2006) 158-170
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 31
    • 0031018084 scopus 로고    scopus 로고
    • Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry
    • Smith D.L., Deng Y., and Zhang Z. Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry. J. Mass Spectrom. 32 (1997) 135-146
    • (1997) J. Mass Spectrom. , vol.32 , pp. 135-146
    • Smith, D.L.1    Deng, Y.2    Zhang, Z.3
  • 33
    • 33749326831 scopus 로고    scopus 로고
    • Identification and characterization of EX1 kinetics in H/D exchange mass spectrometry by peak width analysis
    • Weis D.D., Hotchko M.T., Wales E., Ten Eyck L.F., and Engen J.R. Identification and characterization of EX1 kinetics in H/D exchange mass spectrometry by peak width analysis. J. Am. Soc. Mass Spectrom. 17 (2006) 1498-1509
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1498-1509
    • Weis, D.D.1    Hotchko, M.T.2    Wales, E.3    Ten Eyck, L.F.4    Engen, J.R.5
  • 35
    • 0030199899 scopus 로고    scopus 로고
    • Mass spectrometric determination of isotopic exchange rates of amide hydrogens located on the surfaces of proteins
    • Dharmasiri K., and Smith D.L. Mass spectrometric determination of isotopic exchange rates of amide hydrogens located on the surfaces of proteins. Anal. Chem. 68 (1996) 2340-2344
    • (1996) Anal. Chem. , vol.68 , pp. 2340-2344
    • Dharmasiri, K.1    Smith, D.L.2
  • 36
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson H.J., and Wright P.E. Intrinsically unstructured proteins and their functions. Nature Rev. Mol. Cell Biol. 6 (2005) 197-208
    • (2005) Nature Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 37
    • 0344936739 scopus 로고    scopus 로고
    • Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions
    • Radhakrishnan I., Perez-Alvarado G.C., Parker D., Dyson H.J., Montminy M.R., and Wright P.E. Solution structure of the KIX domain of CBP bound to the transactivation domain of CREB: a model for activator:coactivator interactions. Cell 91 (1997) 741-752
    • (1997) Cell , vol.91 , pp. 741-752
    • Radhakrishnan, I.1    Perez-Alvarado, G.C.2    Parker, D.3    Dyson, H.J.4    Montminy, M.R.5    Wright, P.E.6
  • 38
    • 0029993105 scopus 로고    scopus 로고
    • Analysis of the structural properties of cAMP-responsive element-binding protein (CREB) and phosphorylated CREB
    • Richards J.P., Bachinger H.P., Goodman R.H., and Brennan R.G. Analysis of the structural properties of cAMP-responsive element-binding protein (CREB) and phosphorylated CREB. J. Biol. Chem. 271 (1996) 13716-13723
    • (1996) J. Biol. Chem. , vol.271 , pp. 13716-13723
    • Richards, J.P.1    Bachinger, H.P.2    Goodman, R.H.3    Brennan, R.G.4
  • 39
    • 0032479055 scopus 로고    scopus 로고
    • Conformational preferences in the Ser133-phosphorylated and non-phosphorylated forms of the kinase inducible transactivation domain of CREB
    • Radhakrishnan I., Perez-Alvarado G.C., Dyson H.J., and Wright P.E. Conformational preferences in the Ser133-phosphorylated and non-phosphorylated forms of the kinase inducible transactivation domain of CREB. FEBS Letters 430 (1998) 317-322
    • (1998) FEBS Letters , vol.430 , pp. 317-322
    • Radhakrishnan, I.1    Perez-Alvarado, G.C.2    Dyson, H.J.3    Wright, P.E.4
  • 40
    • 0035932969 scopus 로고    scopus 로고
    • Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45
    • Zhou P., Lugovskoy A.A., McCarty J.S., Li P., and Wagner G. Solution structure of DFF40 and DFF45 N-terminal domain complex and mutual chaperone activity of DFF40 and DFF45. Proc. Natl Acad. Sci. USA 98 (2001) 6051-6055
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , pp. 6051-6055
    • Zhou, P.1    Lugovskoy, A.A.2    McCarty, J.S.3    Li, P.4    Wagner, G.5
  • 41
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.1
  • 42
    • 0000448017 scopus 로고    scopus 로고
    • Single-step purification/solubilization of recombinant proteins: application to surfactant protein B
    • (808)
    • Holzinger A., Phillips K.S., and Weaver T.E. Single-step purification/solubilization of recombinant proteins: application to surfactant protein B. Biotechniques 20 (1996) 804-806 (808)
    • (1996) Biotechniques , vol.20 , pp. 804-806
    • Holzinger, A.1    Phillips, K.S.2    Weaver, T.E.3
  • 43
    • 33749358013 scopus 로고    scopus 로고
    • Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip
    • Weis D.D., Kjellen P., Sefton B.M., and Engen J.R. Altered dynamics in Lck SH3 upon binding to the LBD1 domain of Herpesvirus saimiri Tip. Protein Sci 15 (2006) 2402-2410
    • (2006) Protein Sci , vol.15 , pp. 2402-2410
    • Weis, D.D.1    Kjellen, P.2    Sefton, B.M.3    Engen, J.R.4
  • 44
    • 23444449590 scopus 로고    scopus 로고
    • Conformational differences between arrestin2 and pre-activated mutants as revealed by hydrogen exchange mass spectrometry
    • Carter J.M., Gurevich V.V., Prossnitz E.R., and Engen J.R. Conformational differences between arrestin2 and pre-activated mutants as revealed by hydrogen exchange mass spectrometry. J. Mol. Biol. 351 (2005) 865-878
    • (2005) J. Mol. Biol. , vol.351 , pp. 865-878
    • Carter, J.M.1    Gurevich, V.V.2    Prossnitz, E.R.3    Engen, J.R.4
  • 45
    • 29344471038 scopus 로고    scopus 로고
    • An examination of dynamics crosstalk between SH2 and SH3 domains by hydrogen/deuterium exchange and mass spectrometry
    • Hochrein J.M., Lerner E.C., Schiavone A.P., Smithgall T.E., and Engen J.R. An examination of dynamics crosstalk between SH2 and SH3 domains by hydrogen/deuterium exchange and mass spectrometry. Protein Sci. 15 (2006) 65-73
    • (2006) Protein Sci. , vol.15 , pp. 65-73
    • Hochrein, J.M.1    Lerner, E.C.2    Schiavone, A.P.3    Smithgall, T.E.4    Engen, J.R.5
  • 46
    • 6444222991 scopus 로고
    • Use of glass electrodes to measure acidities in deuterium oxide
    • Glasoe P., and Long F. Use of glass electrodes to measure acidities in deuterium oxide. J. Phys. Chem. 64 (1960) 188-193
    • (1960) J. Phys. Chem. , vol.64 , pp. 188-193
    • Glasoe, P.1    Long, F.2
  • 47
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation
    • Zhang Z., and Smith D.L. Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation. Protein Sci. 2 (1993) 522-531
    • (1993) Protein Sci. , vol.2 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2
  • 48
    • 0036463721 scopus 로고    scopus 로고
    • Hydrogen exchange-mass spectrometry: optimization of digestion conditions
    • Wang L., Pan H., and Smith D.L. Hydrogen exchange-mass spectrometry: optimization of digestion conditions. Mol. Cell Proteomics 1 (2002) 132-138
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 132-138
    • Wang, L.1    Pan, H.2    Smith, D.L.3


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