메뉴 건너뛰기




Volumn 179, Issue 1, 2012, Pages 10-17

The combination of hydrogen/deuterium exchange or chemical cross-linking techniques with mass spectrometry: Mapping of human 14-3-3ζ homodimer interface

Author keywords

14 3 3 Homodimer; Chemical cross linking; H D exchange; Mass spectrometry; Protein protein interaction

Indexed keywords

DEUTERIUM; HOMODIMER;

EID: 84862265339     PISSN: 10478477     EISSN: 10958657     Source Type: Journal    
DOI: 10.1016/j.jsb.2012.04.016     Document Type: Article
Times cited : (21)

References (27)
  • 1
    • 0036672615 scopus 로고    scopus 로고
    • Specificity of 14-3-3 isoform dimer interactions and phosphorylation
    • Aitken A., Baxter H., Dubois T., Clokie S., Mackie S., et al. Specificity of 14-3-3 isoform dimer interactions and phosphorylation. Biochem. Soc. Trans. 2002, 30:351-360.
    • (2002) Biochem. Soc. Trans. , vol.30 , pp. 351-360
    • Aitken, A.1    Baxter, H.2    Dubois, T.3    Clokie, S.4    Mackie, S.5
  • 2
    • 21044450171 scopus 로고    scopus 로고
    • The crystal structure of the non-liganded 14-3-3sigma protein: insights into determinants of isoform specific ligand binding and dimerization
    • Benzinger A., Popowicz G.M., Holak T.A., Hermeking H. The crystal structure of the non-liganded 14-3-3sigma protein: insights into determinants of isoform specific ligand binding and dimerization. Cell Res. 2005, 15:219-227.
    • (2005) Cell Res. , vol.15 , pp. 219-227
    • Benzinger, A.1    Popowicz, G.M.2    Holak, T.A.3    Hermeking, H.4
  • 3
    • 0037433504 scopus 로고    scopus 로고
    • Docking of protein-protein complexes on the basis of highly ambiguous intermolecular distance restraints derived from 1H/15N chemical shift mapping and backbone 15N-1H residual dipolar couplings using conjoined rigid body/torsion angle dynamics
    • Clore G.M., Schwieters C.D. Docking of protein-protein complexes on the basis of highly ambiguous intermolecular distance restraints derived from 1H/15N chemical shift mapping and backbone 15N-1H residual dipolar couplings using conjoined rigid body/torsion angle dynamics. J. Am. Chem. Soc. 2003, 125:2902-2912.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 2902-2912
    • Clore, G.M.1    Schwieters, C.D.2
  • 4
    • 33744482032 scopus 로고    scopus 로고
    • Proteomic analysis of the 14-3-3 family in Arabidopsis
    • Fuller B., Stevens S.M., Sehnke P.C., Ferl R.J. Proteomic analysis of the 14-3-3 family in Arabidopsis. Proteomics 2006, 6:3050-3059.
    • (2006) Proteomics , vol.6 , pp. 3050-3059
    • Fuller, B.1    Stevens, S.M.2    Sehnke, P.C.3    Ferl, R.J.4
  • 5
    • 33646898172 scopus 로고    scopus 로고
    • Structural determinants of 14-3-3 binding specificities and regulation of subcellular localization of 14-3-3-ligand complexes: a comparison of the X-ray crystal structures of all human 14-3-3 isoforms
    • Gardino A.K., Smerdon S.J., Yaffe M.B. Structural determinants of 14-3-3 binding specificities and regulation of subcellular localization of 14-3-3-ligand complexes: a comparison of the X-ray crystal structures of all human 14-3-3 isoforms. Semin. Cancer Biol. 2006, 16:173-182.
    • (2006) Semin. Cancer Biol. , vol.16 , pp. 173-182
    • Gardino, A.K.1    Smerdon, S.J.2    Yaffe, M.B.3
  • 6
    • 29344452931 scopus 로고    scopus 로고
    • Protein kinase a phosphorylates and regulates dimerization of 14-3-3 epsilon
    • Gu Y.M., Jin Y.H., Choi J.K., Baek K.H., Yeo C.Y., et al. Protein kinase a phosphorylates and regulates dimerization of 14-3-3 epsilon. FEBS Lett. 2006, 580:305-310.
    • (2006) FEBS Lett. , vol.580 , pp. 305-310
    • Gu, Y.M.1    Jin, Y.H.2    Choi, J.K.3    Baek, K.H.4    Yeo, C.Y.5
  • 7
    • 0038825874 scopus 로고    scopus 로고
    • Detection and characterization of methionine oxidation in peptides by collision-induced dissociation and electron capture dissociation
    • Guan Z., Yates N.A., Bakhtiar R. Detection and characterization of methionine oxidation in peptides by collision-induced dissociation and electron capture dissociation. J. Am. Soc. Mass Spectrom. 2003, 14:605-613.
    • (2003) J. Am. Soc. Mass Spectrom. , vol.14 , pp. 605-613
    • Guan, Z.1    Yates, N.A.2    Bakhtiar, R.3
  • 8
    • 0029067231 scopus 로고
    • Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: implications for function as adapter proteins
    • Jones D.H., Ley S., Aitken A. Isoforms of 14-3-3 protein can form homo- and heterodimers in vivo and in vitro: implications for function as adapter proteins. FEBS Lett. 1995, 368:55-58.
    • (1995) FEBS Lett. , vol.368 , pp. 55-58
    • Jones, D.H.1    Ley, S.2    Aitken, A.3
  • 9
    • 12244285932 scopus 로고    scopus 로고
    • Chemical cross-linking and high-performance Fourier transform ion cyclotron resonance mass spectrometry for protein interaction analysis: application to a calmodulin/target peptide complex
    • Kalkhof S., Ihling C., Mechtler K., Sinz A. Chemical cross-linking and high-performance Fourier transform ion cyclotron resonance mass spectrometry for protein interaction analysis: application to a calmodulin/target peptide complex. Anal. Chem. 2005, 77:495-503.
    • (2005) Anal. Chem. , vol.77 , pp. 495-503
    • Kalkhof, S.1    Ihling, C.2    Mechtler, K.3    Sinz, A.4
  • 10
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: a program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graph. 1996, 14:51-55.
    • (1996) J. Mol. Graph. , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 11
    • 0034654011 scopus 로고    scopus 로고
    • Acetylation: a regulatory modification to rival phosphorylation?
    • Kouzarides T. Acetylation: a regulatory modification to rival phosphorylation?. EMBO J. 2000, 19:1176-1179.
    • (2000) EMBO J. , vol.19 , pp. 1176-1179
    • Kouzarides, T.1
  • 12
    • 0029046812 scopus 로고
    • Crystal structure of the zeta isoform of the 14-3-3 protein
    • Liu D., Bienkowska J., Petosa C., Collier R.J., Fu H., et al. Crystal structure of the zeta isoform of the 14-3-3 protein. Nature 1995, 376:191-194.
    • (1995) Nature , vol.376 , pp. 191-194
    • Liu, D.1    Bienkowska, J.2    Petosa, C.3    Collier, R.J.4    Fu, H.5
  • 13
    • 22544461952 scopus 로고    scopus 로고
    • Sphingosine activates protein kinase A type II by a novel cAMP-independent mechanism
    • Ma Y., Pitson S., Hercus T., Murphy J., Lopez A., et al. Sphingosine activates protein kinase A type II by a novel cAMP-independent mechanism. J. Biol. Chem. 2005, 280:26011-26017.
    • (2005) J. Biol. Chem. , vol.280 , pp. 26011-26017
    • Ma, Y.1    Pitson, S.2    Hercus, T.3    Murphy, J.4    Lopez, A.5
  • 14
    • 33947599164 scopus 로고    scopus 로고
    • Defining the interacting regions between apomyoglobin and lipid membrane by hydrogen/deuterium exchange coupled to mass spectrometry
    • Man P., Montagner C., Vernier G., Dublet B., Chenal A., et al. Defining the interacting regions between apomyoglobin and lipid membrane by hydrogen/deuterium exchange coupled to mass spectrometry. J. Mol. Biol. 2007, 368:464-472.
    • (2007) J. Mol. Biol. , vol.368 , pp. 464-472
    • Man, P.1    Montagner, C.2    Vernier, G.3    Dublet, B.4    Chenal, A.5
  • 15
    • 0027371622 scopus 로고
    • Antibodies against the major brain isoforms of 14-3-3 protein. An antibody specific for the N-acetylated amino-terminus of a protein
    • Martin H., Patel Y., Jones D., Howell S., Robinson K., et al. Antibodies against the major brain isoforms of 14-3-3 protein. An antibody specific for the N-acetylated amino-terminus of a protein. FEBS Lett. 1993, 331:296-303.
    • (1993) FEBS Lett. , vol.331 , pp. 296-303
    • Martin, H.1    Patel, Y.2    Jones, D.3    Howell, S.4    Robinson, K.5
  • 16
    • 1042266643 scopus 로고    scopus 로고
    • 14-3-3zeta C-terminal stretch changes its conformation upon ligand binding and phosphorylation at Thr232
    • Obsilova V., Herman P., Vecer J., Sulc M., Teisinger J., et al. 14-3-3zeta C-terminal stretch changes its conformation upon ligand binding and phosphorylation at Thr232. J. Biol. Chem. 2004, 279:4531-4540.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4531-4540
    • Obsilova, V.1    Herman, P.2    Vecer, J.3    Sulc, M.4    Teisinger, J.5
  • 17
    • 0043092653 scopus 로고    scopus 로고
    • Proteomic identification of 14-3-3zeta as a mitogen-activated protein kinase-activated protein kinase 2 substrate: role in dimer formation and ligand binding
    • Powell D.W., Rane M.J., Joughin B.A., Kalmukova R., Hong J.H., et al. Proteomic identification of 14-3-3zeta as a mitogen-activated protein kinase-activated protein kinase 2 substrate: role in dimer formation and ligand binding. Mol. Cell Biol. 2003, 23:5376-5387.
    • (2003) Mol. Cell Biol. , vol.23 , pp. 5376-5387
    • Powell, D.W.1    Rane, M.J.2    Joughin, B.A.3    Kalmukova, R.4    Hong, J.H.5
  • 20
    • 33745742438 scopus 로고    scopus 로고
    • Chemical cross-linking and mass spectrometry to map three-dimensional protein structures and protein-protein interactions
    • Sinz A. Chemical cross-linking and mass spectrometry to map three-dimensional protein structures and protein-protein interactions. Mass. Spectrom. Rev. 2006, 25:663-682.
    • (2006) Mass. Spectrom. Rev. , vol.25 , pp. 663-682
    • Sinz, A.1
  • 21
    • 0003174184 scopus 로고
    • Analysis of proteins
    • John Wiley & Sons, Inc., Hoboken US, F.M. Ausubel (Ed.)
    • Smith J.A. Analysis of proteins. Short Protocols in Molecular Biology 1995, 10.5-10.11. John Wiley & Sons, Inc., Hoboken US. F.M. Ausubel (Ed.).
    • (1995) Short Protocols in Molecular Biology
    • Smith, J.A.1
  • 22
    • 77954123833 scopus 로고    scopus 로고
    • The binding affinity of carcinogenic N-nitrosodimethylamine and N-nitrosomethylaniline to cytochromes P450 2B4, 2E1 and 3A6 does not dictate the rate of their enzymatic N-demethylation
    • Sulc M., Hodek P., Stiborova M. The binding affinity of carcinogenic N-nitrosodimethylamine and N-nitrosomethylaniline to cytochromes P450 2B4, 2E1 and 3A6 does not dictate the rate of their enzymatic N-demethylation. Gen. Physiol. Biophys. 2010, 29:175-185.
    • (2010) Gen. Physiol. Biophys. , vol.29 , pp. 175-185
    • Sulc, M.1    Hodek, P.2    Stiborova, M.3
  • 23
    • 0024289285 scopus 로고
    • Investigation of the bicinchoninic acid protein assay identification of the groups responsible for color formation
    • Wiechelman K.J., Braun R.D., Fitzpatric J.D. Investigation of the bicinchoninic acid protein assay identification of the groups responsible for color formation. Anal. Biochem. 1988, 17:231-237.
    • (1988) Anal. Biochem. , vol.17 , pp. 231-237
    • Wiechelman, K.J.1    Braun, R.D.2    Fitzpatric, J.D.3
  • 24
    • 4444358273 scopus 로고    scopus 로고
    • 14-3-3 Proteins-a focus on cancer and human disease
    • Wilker E., Yaffe M.B. 14-3-3 Proteins-a focus on cancer and human disease. J. Mol. Cell Cardiol. 2004, 37:633-642.
    • (2004) J. Mol. Cell Cardiol. , vol.37 , pp. 633-642
    • Wilker, E.1    Yaffe, M.B.2
  • 25
    • 0141815677 scopus 로고    scopus 로고
    • The dimeric versus monomeric status of 14-3-3zeta is controlled by phosphorylation of Ser58 at the dimer interface
    • Woodcock J.M., Murphy J., Stomski F.C., Berndt M.C., Lopez A.F. The dimeric versus monomeric status of 14-3-3zeta is controlled by phosphorylation of Ser58 at the dimer interface. J. Biol. Chem. 2003, 178:36323-36327.
    • (2003) J. Biol. Chem. , vol.178 , pp. 36323-36327
    • Woodcock, J.M.1    Murphy, J.2    Stomski, F.C.3    Berndt, M.C.4    Lopez, A.F.5
  • 26
    • 33751248527 scopus 로고    scopus 로고
    • Structural basis for protein-protein interactions in the 14-3-3 protein family
    • Yang X., Lee W.H., Sobott F., Papagrigoriou E., Robinson C.V., et al. Structural basis for protein-protein interactions in the 14-3-3 protein family. Proc. Natl. Acad. Sci. USA 2006, 103(46):17237-17242.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , Issue.46 , pp. 17237-17242
    • Yang, X.1    Lee, W.H.2    Sobott, F.3    Papagrigoriou, E.4    Robinson, C.V.5
  • 27
    • 80053645046 scopus 로고    scopus 로고
    • Discovery and structural characterization of a small molecule 14-3-3 protein-protein interaction inhibitor
    • Zhao J., Du Y., Horton J.R., Upadhyay A.K., Lou B., et al. Discovery and structural characterization of a small molecule 14-3-3 protein-protein interaction inhibitor. Proc. Natl. Acad. Sci. USA 2011, 108(39):16212-16216.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , Issue.39 , pp. 16212-16216
    • Zhao, J.1    Du, Y.2    Horton, J.R.3    Upadhyay, A.K.4    Lou, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.