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Volumn 402, Issue 5, 2010, Pages 892-904

Molecular Insight into the Conformational Dynamics of the Elongin BC Complex and Its Interaction with HIV-1 Vif

Author keywords

APOBEC3; E3 ubiquitin ligase; Hydrogen exchange mass spectrometry; Protein conformation; Viral SOCS box

Indexed keywords

BINDING PROTEIN; CYTIDINE DEAMINASE; DEUTERIUM; ELONGATION BC COMPLEX; HETERODIMER; PROTEASOME; PROTEIN APOBEC3; RECOMBINANT PROTEIN; SUPPRESSOR OF CYTOKINE SIGNALING; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG; VIF PROTEIN; ELONGIN; HYDROGEN; PROTEIN BINDING; TRANSCRIPTION FACTOR; VIF PROTEIN, HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 77957235518     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2010.08.026     Document Type: Article
Times cited : (23)

References (47)
  • 1
    • 0029126892 scopus 로고
    • Inhibition of transcription elongation by the VHL tumor suppressor protein
    • Duan D.R., Pause A., Burgess W.H., Aso T., Chen D.Y., Garrett K.P., et al. Inhibition of transcription elongation by the VHL tumor suppressor protein. Science 1995, 269:1402-1406.
    • (1995) Science , vol.269 , pp. 1402-1406
    • Duan, D.R.1    Pause, A.2    Burgess, W.H.3    Aso, T.4    Chen, D.Y.5    Garrett, K.P.6
  • 2
    • 0032540499 scopus 로고    scopus 로고
    • The Elongin BC complex and the von Hippel-Lindau tumor suppressor protein
    • Conaway J.W., Kamura T., Conaway R.C. The Elongin BC complex and the von Hippel-Lindau tumor suppressor protein. Biochim. Biophys. Acta 1998, 1377:M49-54.
    • (1998) Biochim. Biophys. Acta , vol.1377
    • Conaway, J.W.1    Kamura, T.2    Conaway, R.C.3
  • 3
    • 33646733227 scopus 로고    scopus 로고
    • Crystal structure of the SOCS2-elongin C-elongin B complex defines a prototypical SOCS box ubiquitin ligase
    • Bullock A.N., Debreczeni J.E., Edwards A.M., Sundstrom M., Knapp S. Crystal structure of the SOCS2-elongin C-elongin B complex defines a prototypical SOCS box ubiquitin ligase. Proc. Natl Acad. Sci. USA 2006, 103:7637-7642.
    • (2006) Proc. Natl Acad. Sci. USA , vol.103 , pp. 7637-7642
    • Bullock, A.N.1    Debreczeni, J.E.2    Edwards, A.M.3    Sundstrom, M.4    Knapp, S.5
  • 4
    • 48449086930 scopus 로고    scopus 로고
    • The SOCS box domain of SOCS3: structure and interaction with the elonginBC-cullin5 ubiquitin ligase
    • Babon J.J., Sabo J.K., Soetopo A., Yao S., Bailey M.F., Zhang J.G., et al. The SOCS box domain of SOCS3: structure and interaction with the elonginBC-cullin5 ubiquitin ligase. J. Mol. Biol. 2008, 381:928-940.
    • (2008) J. Mol. Biol. , vol.381 , pp. 928-940
    • Babon, J.J.1    Sabo, J.K.2    Soetopo, A.3    Yao, S.4    Bailey, M.F.5    Zhang, J.G.6
  • 5
    • 35748984946 scopus 로고    scopus 로고
    • Structure of the SOCS4-ElonginB/C complex reveals a distinct SOCS box interface and the molecular basis for SOCS-dependent EGFR degradation
    • Bullock A.N., Rodriguez M.C., Debreczeni J.E., Songyang Z., Knapp S. Structure of the SOCS4-ElonginB/C complex reveals a distinct SOCS box interface and the molecular basis for SOCS-dependent EGFR degradation. Structure 2007, 15:1493-1504.
    • (2007) Structure , vol.15 , pp. 1493-1504
    • Bullock, A.N.1    Rodriguez, M.C.2    Debreczeni, J.E.3    Songyang, Z.4    Knapp, S.5
  • 6
    • 10044230343 scopus 로고    scopus 로고
    • Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation
    • Mehle A., Goncalves J., Santa-Marta M., McPike M., Gabuzda D. Phosphorylation of a novel SOCS-box regulates assembly of the HIV-1 Vif-Cul5 complex that promotes APOBEC3G degradation. Genes Dev. 2004, 18:2861-2866.
    • (2004) Genes Dev. , vol.18 , pp. 2861-2866
    • Mehle, A.1    Goncalves, J.2    Santa-Marta, M.3    McPike, M.4    Gabuzda, D.5
  • 7
    • 33846804177 scopus 로고    scopus 로고
    • Analysis of Vif-induced APOBEC3G degradation using an alpha-complementation assay
    • Fang L., Landau N.R. Analysis of Vif-induced APOBEC3G degradation using an alpha-complementation assay. Virology 2007, 359:162-169.
    • (2007) Virology , vol.359 , pp. 162-169
    • Fang, L.1    Landau, N.R.2
  • 8
    • 10044228286 scopus 로고    scopus 로고
    • Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines
    • Yu Y., Xiao Z., Ehrlich E.S., Yu X., Yu X.F. Selective assembly of HIV-1 Vif-Cul5-ElonginB-ElonginC E3 ubiquitin ligase complex through a novel SOCS box and upstream cysteines. Genes Dev. 2004, 18:2867-2872.
    • (2004) Genes Dev. , vol.18 , pp. 2867-2872
    • Yu, Y.1    Xiao, Z.2    Ehrlich, E.S.3    Yu, X.4    Yu, X.F.5
  • 9
    • 0037043699 scopus 로고    scopus 로고
    • Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein
    • Sheehy A.M., Gaddis N.C., Choi J.D., Malim M.H. Isolation of a human gene that inhibits HIV-1 infection and is suppressed by the viral Vif protein. Nature 2002, 418:646-650.
    • (2002) Nature , vol.418 , pp. 646-650
    • Sheehy, A.M.1    Gaddis, N.C.2    Choi, J.D.3    Malim, M.H.4
  • 10
    • 21444439295 scopus 로고    scopus 로고
    • Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function
    • Kobayashi M., Takaori-Kondo A., Miyauchi Y., Iwai K., Uchiyama T. Ubiquitination of APOBEC3G by an HIV-1 Vif-Cullin5-Elongin B-Elongin C complex is essential for Vif function. J. Biol. Chem. 2005, 280:18573-18578.
    • (2005) J. Biol. Chem. , vol.280 , pp. 18573-18578
    • Kobayashi, M.1    Takaori-Kondo, A.2    Miyauchi, Y.3    Iwai, K.4    Uchiyama, T.5
  • 11
    • 1542379821 scopus 로고    scopus 로고
    • Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway
    • Mehle A., Strack B., Ancuta P., Zhang C., McPike M., Gabuzda D. Vif overcomes the innate antiviral activity of APOBEC3G by promoting its degradation in the ubiquitin-proteasome pathway. J. Biol. Chem. 2004, 279:7792-7798.
    • (2004) J. Biol. Chem. , vol.279 , pp. 7792-7798
    • Mehle, A.1    Strack, B.2    Ancuta, P.3    Zhang, C.4    McPike, M.5    Gabuzda, D.6
  • 12
    • 50149097544 scopus 로고    scopus 로고
    • Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly
    • Stanley B.J., Ehrlich E.S., Short L., Yu Y., Xiao Z., Yu X.F., Xiong Y. Structural insight into the human immunodeficiency virus Vif SOCS box and its role in human E3 ubiquitin ligase assembly. J. Virol. 2008, 82:8656-8663.
    • (2008) J. Virol. , vol.82 , pp. 8656-8663
    • Stanley, B.J.1    Ehrlich, E.S.2    Short, L.3    Yu, Y.4    Xiao, Z.5    Yu, X.F.6    Xiong, Y.7
  • 13
    • 77950845533 scopus 로고    scopus 로고
    • Polyubiquitination of APOBEC3G is essential for its degradation by HIV-1 Vif
    • Shao Q., Wang Y., Hildreth J.E., Liu B. Polyubiquitination of APOBEC3G is essential for its degradation by HIV-1 Vif. J. Virol. 2010, 84:4840-4844.
    • (2010) J. Virol. , vol.84 , pp. 4840-4844
    • Shao, Q.1    Wang, Y.2    Hildreth, J.E.3    Liu, B.4
  • 14
    • 0033053198 scopus 로고    scopus 로고
    • Mutational analysis of the human immunodeficiency virus type 1 Vif protein
    • Simon J.H., Sheehy A.M., Carpenter E.A., Fouchier R.A., Malim M.H. Mutational analysis of the human immunodeficiency virus type 1 Vif protein. J. Virol. 1999, 73:2675-2681.
    • (1999) J. Virol. , vol.73 , pp. 2675-2681
    • Simon, J.H.1    Sheehy, A.M.2    Carpenter, E.A.3    Fouchier, R.A.4    Malim, M.H.5
  • 15
    • 61349119266 scopus 로고    scopus 로고
    • The SOCS box encodes a hierarchy of affinities for Cullin5: implications for ubiquitin ligase formation and cytokine signalling suppression
    • Babon J.J., Sabo J.K., Zhang J.G., Nicola N.A., Norton R.S. The SOCS box encodes a hierarchy of affinities for Cullin5: implications for ubiquitin ligase formation and cytokine signalling suppression. J. Mol. Biol. 2009, 387:162-174.
    • (2009) J. Mol. Biol. , vol.387 , pp. 162-174
    • Babon, J.J.1    Sabo, J.K.2    Zhang, J.G.3    Nicola, N.A.4    Norton, R.S.5
  • 17
    • 77957244332 scopus 로고    scopus 로고
    • Structural Disorder in the HIV-1 Vif protein and interaction-dependent gain of structure
    • Reingewertz T.H., Shalev D.E., Friedler A. Structural Disorder in the HIV-1 Vif protein and interaction-dependent gain of structure. Protein Pept. Lett. 2010, 17:988-998.
    • (2010) Protein Pept. Lett. , vol.17 , pp. 988-998
    • Reingewertz, T.H.1    Shalev, D.E.2    Friedler, A.3
  • 19
    • 77953480345 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry: what is it and what can it tell us?
    • Marcsisin S.R., Engen J.R. Hydrogen exchange mass spectrometry: what is it and what can it tell us?. Anal. Bioanal. Chem. 2010, 397:967-972.
    • (2010) Anal. Bioanal. Chem. , vol.397 , pp. 967-972
    • Marcsisin, S.R.1    Engen, J.R.2
  • 20
    • 33644761306 scopus 로고    scopus 로고
    • Hydrogen exchange mass spectrometry for the analysis of protein dynamics
    • Wales T.E., Engen J.R. Hydrogen exchange mass spectrometry for the analysis of protein dynamics. Mass Spectrom. Rev. 2006, 25:158-170.
    • (2006) Mass Spectrom. Rev. , vol.25 , pp. 158-170
    • Wales, T.E.1    Engen, J.R.2
  • 21
    • 70349613463 scopus 로고    scopus 로고
    • Analysis of protein conformation and dynamics by hydrogen/deuterium exchange MS
    • Engen J.R. Analysis of protein conformation and dynamics by hydrogen/deuterium exchange MS. Anal. Chem. 2009, 81:7870-7875.
    • (2009) Anal. Chem. , vol.81 , pp. 7870-7875
    • Engen, J.R.1
  • 22
    • 77953757638 scopus 로고    scopus 로고
    • Dissection of HIV Vif interaction with the human E3 ubiquitin ligase
    • Wolfe L.S., Stanley B.J., Liu C., Eliason W.K., Xiong Y. Dissection of HIV Vif interaction with the human E3 ubiquitin ligase. J. Virol. 2010, 84:7135-7139.
    • (2010) J. Virol. , vol.84 , pp. 7135-7139
    • Wolfe, L.S.1    Stanley, B.J.2    Liu, C.3    Eliason, W.K.4    Xiong, Y.5
  • 23
    • 77954684927 scopus 로고    scopus 로고
    • The SOCS-box of HIV-1 Vif interacts with ElonginBC by induced-folding to recruit its Cul5-containing ubiquitin ligase complex
    • Bergeron J.R., Huthoff H., Veselkov D.A., Beavil R.L., Simpson P.J., Matthews S.J., et al. The SOCS-box of HIV-1 Vif interacts with ElonginBC by induced-folding to recruit its Cul5-containing ubiquitin ligase complex. PLoS Pathog. 2010, 6:e1000925.
    • (2010) PLoS Pathog. , vol.6
    • Bergeron, J.R.1    Huthoff, H.2    Veselkov, D.A.3    Beavil, R.L.4    Simpson, P.J.5    Matthews, S.J.6
  • 24
    • 0038121525 scopus 로고    scopus 로고
    • Analysis of protein complexes with hydrogen exchange and mass spectrometry
    • Engen J.R. Analysis of protein complexes with hydrogen exchange and mass spectrometry. Analyst 2003, 128:623-628.
    • (2003) Analyst , vol.128 , pp. 623-628
    • Engen, J.R.1
  • 25
    • 0027529263 scopus 로고
    • Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation
    • Zhang Z., Smith D.L. Determination of amide hydrogen exchange by mass spectrometry: a new tool for protein structure elucidation. Protein Sci. 1993, 2:522-531.
    • (1993) Protein Sci. , vol.2 , pp. 522-531
    • Zhang, Z.1    Smith, D.L.2
  • 26
    • 0026455196 scopus 로고
    • Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR
    • Mayne L., Paterson Y., Cerasoli D., Englander S.W. Effect of antibody binding on protein motions studied by hydrogen-exchange labeling and two-dimensional NMR. Biochemistry 1992, 31:10678-10685.
    • (1992) Biochemistry , vol.31 , pp. 10678-10685
    • Mayne, L.1    Paterson, Y.2    Cerasoli, D.3    Englander, S.W.4
  • 27
    • 75749146563 scopus 로고    scopus 로고
    • Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors
    • Zhang J., Adrian F.J., Jahnke W., Cowan-Jacob S.W., Li A.G., Iacob R.E., et al. Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors. Nature 2010, 463:501-506.
    • (2010) Nature , vol.463 , pp. 501-506
    • Zhang, J.1    Adrian, F.J.2    Jahnke, W.3    Cowan-Jacob, S.W.4    Li, A.G.5    Iacob, R.E.6
  • 28
    • 0035823058 scopus 로고    scopus 로고
    • Solution structure and dynamics of yeast elongin C in complex with a von Hippel-Lindau peptide
    • Botuyan M.V., Mer G., Yi G.S., Koth C.M., Case D.A., Edwards A.M., et al. Solution structure and dynamics of yeast elongin C in complex with a von Hippel-Lindau peptide. J. Mol. Biol. 2001, 312:177-186.
    • (2001) J. Mol. Biol. , vol.312 , pp. 177-186
    • Botuyan, M.V.1    Mer, G.2    Yi, G.S.3    Koth, C.M.4    Case, D.A.5    Edwards, A.M.6
  • 30
    • 18444368709 scopus 로고    scopus 로고
    • Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL
    • Hon W.C., Wilson M.I., Harlos K., Claridge T.D., Schofield C.J., Pugh C.W., et al. Structural basis for the recognition of hydroxyproline in HIF-1 alpha by pVHL. Nature 2002, 417:975-978.
    • (2002) Nature , vol.417 , pp. 975-978
    • Hon, W.C.1    Wilson, M.I.2    Harlos, K.3    Claridge, T.D.4    Schofield, C.J.5    Pugh, C.W.6
  • 31
    • 0033532061 scopus 로고    scopus 로고
    • The elongin B ubiquitin homology domain. Identification of elongin B sequences important for interaction with elongin C
    • Brower C.S., Shilatifard A., Mather T., Kamura T., Takagi Y., Haque D., et al. The elongin B ubiquitin homology domain. Identification of elongin B sequences important for interaction with elongin C. J. Biol. Chem. 1999, 274:13629-13636.
    • (1999) J. Biol. Chem. , vol.274 , pp. 13629-13636
    • Brower, C.S.1    Shilatifard, A.2    Mather, T.3    Kamura, T.4    Takagi, Y.5    Haque, D.6
  • 32
    • 34548713478 scopus 로고    scopus 로고
    • Mass spectrometry analysis of HIV-1 Vif reveals an increase in ordered structure upon oligomerization in regions necessary for viral infectivity
    • Auclair J.R., Green K.M., Shandilya S., Evans J.E., Somasundaran M., Schiffer C.A. Mass spectrometry analysis of HIV-1 Vif reveals an increase in ordered structure upon oligomerization in regions necessary for viral infectivity. Proteins 2007, 69:270-284.
    • (2007) Proteins , vol.69 , pp. 270-284
    • Auclair, J.R.1    Green, K.M.2    Shandilya, S.3    Evans, J.E.4    Somasundaran, M.5    Schiffer, C.A.6
  • 33
    • 0037458718 scopus 로고    scopus 로고
    • Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins
    • Yang B., Gao L., Li L., Lu Z., Fan X., Patel C.A., et al. Potent suppression of viral infectivity by the peptides that inhibit multimerization of human immunodeficiency virus type 1 (HIV-1) Vif proteins. J. Biol. Chem. 2003, 278:6596-6602.
    • (2003) J. Biol. Chem. , vol.278 , pp. 6596-6602
    • Yang, B.1    Gao, L.2    Li, L.3    Lu, Z.4    Fan, X.5    Patel, C.A.6
  • 34
    • 0035895896 scopus 로고    scopus 로고
    • The multimerization of human immunodeficiency virus type I Vif protein: a requirement for Vif function in the viral life cycle
    • Yang S., Sun Y., Zhang H. The multimerization of human immunodeficiency virus type I Vif protein: a requirement for Vif function in the viral life cycle. J. Biol. Chem. 2001, 276:4889-4893.
    • (2001) J. Biol. Chem. , vol.276 , pp. 4889-4893
    • Yang, S.1    Sun, Y.2    Zhang, H.3
  • 35
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai Y., Milne J.S., Mayne L., Englander S.W. Primary structure effects on peptide group hydrogen exchange. Proteins 1993, 17:75-86.
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 36
    • 56949093065 scopus 로고    scopus 로고
    • Hydrogen atom scrambling in selectively labeled anionic peptides upon collisional activation by MALDI tandem time-of-flight mass spectrometry
    • Bache N., Rand K.D., Roepstorff P., Ploug M., Jorgensen T.J. Hydrogen atom scrambling in selectively labeled anionic peptides upon collisional activation by MALDI tandem time-of-flight mass spectrometry. J. Am. Soc. Mass Spectrom. 2008, 19:1719-1725.
    • (2008) J. Am. Soc. Mass Spectrom. , vol.19 , pp. 1719-1725
    • Bache, N.1    Rand, K.D.2    Roepstorff, P.3    Ploug, M.4    Jorgensen, T.J.5
  • 37
    • 75749148378 scopus 로고    scopus 로고
    • Investigating solution-phase protein structure and dynamics by hydrogen exchange mass spectrometry
    • Chapter 17, Unit 17.6
    • Morgan C.R., Engen J.R. Investigating solution-phase protein structure and dynamics by hydrogen exchange mass spectrometry. Curr. Protoc. Protein Sci. 2009, 1-17. Chapter 17, Unit 17.6.
    • (2009) Curr. Protoc. Protein Sci. , pp. 1-17
    • Morgan, C.R.1    Engen, J.R.2
  • 38
    • 0033400674 scopus 로고    scopus 로고
    • Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC
    • Feldman D.E., Thulasiraman V., Ferreyra R.G., Frydman J. Formation of the VHL-elongin BC tumor suppressor complex is mediated by the chaperonin TRiC. Mol. Cell 1999, 4:1051-1061.
    • (1999) Mol. Cell , vol.4 , pp. 1051-1061
    • Feldman, D.E.1    Thulasiraman, V.2    Ferreyra, R.G.3    Frydman, J.4
  • 41
    • 0029874943 scopus 로고    scopus 로고
    • Phosphorylation of Vif and its role in HIV-1 replication
    • Yang X., Goncalves J., Gabuzda D. Phosphorylation of Vif and its role in HIV-1 replication. J. Biol. Chem. 1996, 271:10121-10129.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10121-10129
    • Yang, X.1    Goncalves, J.2    Gabuzda, D.3
  • 42
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 1976, 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 43
    • 0032010153 scopus 로고    scopus 로고
    • A universal algorithm for fast and automated charge state deconvolution of electrospray mass-to-charge ratio spectra
    • Zhang Z., Marshall A.G. A universal algorithm for fast and automated charge state deconvolution of electrospray mass-to-charge ratio spectra. J. Am. Soc. Mass Spectrom. 1998, 9:225-233.
    • (1998) J. Am. Soc. Mass Spectrom. , vol.9 , pp. 225-233
    • Zhang, Z.1    Marshall, A.G.2
  • 44
    • 51549121010 scopus 로고    scopus 로고
    • High-speed and high-resolution UPLC separation at zero degrees celsius
    • Wales T.E., Fadgen K.E., Gerhardt G.C., Engen J.R. High-speed and high-resolution UPLC separation at zero degrees celsius. Anal. Chem. 2008, 80:6815-6820.
    • (2008) Anal. Chem. , vol.80 , pp. 6815-6820
    • Wales, T.E.1    Fadgen, K.E.2    Gerhardt, G.C.3    Engen, J.R.4
  • 45
    • 0036463721 scopus 로고    scopus 로고
    • Hydrogen exchange-mass spectrometry: optimization of digestion conditions
    • Wang L., Pan H., Smith D.L. Hydrogen exchange-mass spectrometry: optimization of digestion conditions. Mol. Cell. Proteomics 2002, 1:132-138.
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 132-138
    • Wang, L.1    Pan, H.2    Smith, D.L.3
  • 46
    • 33645725976 scopus 로고    scopus 로고
    • Simultaneous qualitative and quantitative analysis of the Escherichia coli proteome: a sweet tale
    • Silva J.C., Denny R., Dorschel C., Gorenstein M.V., Li G.Z., Richardson K., et al. Simultaneous qualitative and quantitative analysis of the Escherichia coli proteome: a sweet tale. Mol. Cell. Proteomics 2006, 5:589-607.
    • (2006) Mol. Cell. Proteomics , vol.5 , pp. 589-607
    • Silva, J.C.1    Denny, R.2    Dorschel, C.3    Gorenstein, M.V.4    Li, G.Z.5    Richardson, K.6
  • 47
    • 33751337111 scopus 로고    scopus 로고
    • Semi-automated data processing of hydrogen exchange mass spectra using HX-Express
    • Weis D.D., Engen J.R., Kass I.J. Semi-automated data processing of hydrogen exchange mass spectra using HX-Express. J. Am. Soc. Mass Spectrom. 2006, 17:1700-1703.
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1700-1703
    • Weis, D.D.1    Engen, J.R.2    Kass, I.J.3


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