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Volumn 48, Issue 9, 2009, Pages 1954-1963

Formation of monomeric S100B and S100A11 proteins at low ionic strength

Author keywords

[No Author keywords available]

Indexed keywords

BINDING AFFINITIES; BIOLOGICAL RESPONSE; CALCIUM BINDINGS; CALCIUM SIGNALING; CIRCULAR DICHROISMS; CONCENTRATION DEPENDENTS; CONFORMATIONAL CHANGES; DIMER INTERFACES; DISSOCIATION CONSTANTS; EF HANDS; ELECTROSPRAY MASS SPECTROMETRIES; HETERODIMERS; HOMODIMERS; HSQC NMR; IN LINES; INTERFACE SURFACES; LOW IONIC STRENGTHS; MONOMER-DIMER EQUILIBRIUMS; MONOMERIC PROTEINS; SURFACE AREAS; TERTIARY STRUCTURES; UNIQUE FEATURES;

EID: 64549085938     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi802086a     Document Type: Article
Times cited : (12)

References (70)
  • 1
    • 33744782044 scopus 로고    scopus 로고
    • Calcium-dependent and -independent interactions of the S100 protein family
    • Santamaria-Kisiel, L., Rintala-Dempsey, A. C., and Shaw, G. S. (2006) Calcium-dependent and -independent interactions of the S100 protein family. Biochem. J. 396, 201-214.
    • (2006) Biochem. J , vol.396 , pp. 201-214
    • Santamaria-Kisiel, L.1    Rintala-Dempsey, A.C.2    Shaw, G.S.3
  • 2
    • 4444371768 scopus 로고    scopus 로고
    • S100 proteins in mouse and man: From evolution to function and pathology (including an update of the nomenclature)
    • Marenholz, I., Heizmann, C. W., and Fritz, G. (2004) S100 proteins in mouse and man: From evolution to function and pathology (including an update of the nomenclature). Biochem. Biophys. Res. Commun. 322, 1111-1122.
    • (2004) Biochem. Biophys. Res. Commun. 322 , pp. 1111-1122
    • Marenholz, I.1    Heizmann, C.W.2    Fritz, G.3
  • 3
    • 2442584614 scopus 로고    scopus 로고
    • Human S100B protein interacts with the Escherichia coli division protein FtsZ in a calcium-sensitive manner
    • Ferguson, P. L., and Shaw, G. S. (2004) Human S100B protein interacts with the Escherichia coli division protein FtsZ in a calcium-sensitive manner. J. Biol. Chem. 279, 18806-18813.
    • (2004) J. Biol. Chem , vol.279 , pp. 18806-18813
    • Ferguson, P.L.1    Shaw, G.S.2
  • 5
    • 0033534740 scopus 로고    scopus 로고
    • Role of the C-terminal extension in the interaction of S100A1 with GFAP, tubulin, the S100A1- and S100B-inhibitory peptide, TRTK-12, and a peptide derived from p53, and the S100A1 inhibitory effect on GFAP polymerization
    • Garbuglia, M., Verzini, M., Rustandi, R. R., Osterloh, D., Weber, D. J., Gerke, V., and Donato, R. (1999) Role of the C-terminal extension in the interaction of S100A1 with GFAP, tubulin, the S100A1- and S100B-inhibitory peptide, TRTK-12, and a peptide derived from p53, and the S100A1 inhibitory effect on GFAP polymerization. Biochem. Biophys. Res. Commun. 254, 36-41.
    • (1999) Biochem. Biophys. Res. Commun , vol.254 , pp. 36-41
    • Garbuglia, M.1    Verzini, M.2    Rustandi, R.R.3    Osterloh, D.4    Weber, D.J.5    Gerke, V.6    Donato, R.7
  • 6
    • 33744931917 scopus 로고    scopus 로고
    • The S100A4 metastasis factor regulates cellular motility via a direct interaction with myosin-IIA
    • Li, Z. H., and Bresnick, A. R. (2006) The S100A4 metastasis factor regulates cellular motility via a direct interaction with myosin-IIA. Cancer Res. 66, 5173-5180.
    • (2006) Cancer Res , vol.66 , pp. 5173-5180
    • Li, Z.H.1    Bresnick, A.R.2
  • 7
    • 0020716234 scopus 로고
    • A rapid separation of S100 subunits by high performance liquid chromatography: The subunit compositions of S100 proteins
    • Isobe, T., Ishioka, N., Masuda, T., Takahashi, Y., Ganno, S., and Okuyama, T. (1983) A rapid separation of S100 subunits by high performance liquid chromatography: The subunit compositions of S100 proteins. Biochem. Int. 6, 419-426.
    • (1983) Biochem. Int , vol.6 , pp. 419-426
    • Isobe, T.1    Ishioka, N.2    Masuda, T.3    Takahashi, Y.4    Ganno, S.5    Okuyama, T.6
  • 8
    • 0023917095 scopus 로고
    • Two calcium-binding proteins associated with specific stages of myeloid cell differentiation are expressed by subsets of macrophages in inflammatory tissues
    • Zwadlo, G., Bruggen, J., Gerhards, G., Schlegel, R., and Sorg, C. (1988) Two calcium-binding proteins associated with specific stages of myeloid cell differentiation are expressed by subsets of macrophages in inflammatory tissues. Clin. Exp. Immunol. 72, 510-515.
    • (1988) Clin. Exp. Immunol , vol.72 , pp. 510-515
    • Zwadlo, G.1    Bruggen, J.2    Gerhards, G.3    Schlegel, R.4    Sorg, C.5
  • 9
    • 0032478114 scopus 로고    scopus 로고
    • Solution structure of calcium-bound rat S100B(ββ) as determined by nuclear magnetic resonance spectroscopy
    • Drohat, A. C., Baldisseri, D. M., Rustandi, R. R., and Weber, D. J. (1998) Solution structure of calcium-bound rat S100B(ββ) as determined by nuclear magnetic resonance spectroscopy. Biochemistry 37, 2729-2740.
    • (1998) Biochemistry , vol.37 , pp. 2729-2740
    • Drohat, A.C.1    Baldisseri, D.M.2    Rustandi, R.R.3    Weber, D.J.4
  • 10
    • 0032939805 scopus 로고    scopus 로고
    • The use of dipolar couplings for determining the solution structure of rat apo-S100B(ββ)
    • Drohat, A. C., Tjandra, N., Baldisseri, D. M., and Weber, D. J. (1999) The use of dipolar couplings for determining the solution structure of rat apo-S100B(ββ). Protein Sci. 8, 800-809.
    • (1999) Protein Sci , vol.8 , pp. 800-809
    • Drohat, A.C.1    Tjandra, N.2    Baldisseri, D.M.3    Weber, D.J.4
  • 11
    • 0030587521 scopus 로고    scopus 로고
    • The solution structure of the bovine S100B protein dimer in the calcium-free state
    • Kilby, P. M., Van Eldik, L. J., and Roberts, G. C. (1996) The solution structure of the bovine S100B protein dimer in the calcium-free state. Structure 4, 1041-1052.
    • (1996) Structure , vol.4 , pp. 1041-1052
    • Kilby, P.M.1    Van Eldik, L.J.2    Roberts, G.C.3
  • 12
    • 0032520214 scopus 로고    scopus 로고
    • A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form
    • Smith, S. P., and Shaw, G. S. (1998) A novel calcium-sensitive switch revealed by the structure of human S100B in the calcium-bound form. Structure 6, 211-222.
    • (1998) Structure , vol.6 , pp. 211-222
    • Smith, S.P.1    Shaw, G.S.2
  • 13
  • 17
    • 0242691764 scopus 로고    scopus 로고
    • High resolution solution structure of apo calcyclin and structural variations in the S100 family of calcium-binding proteins
    • Maler, L., Potts, B. C., and Chazin, W. J. (1999) High resolution solution structure of apo calcyclin and structural variations in the S100 family of calcium-binding proteins. J. Biomol. NMR 13, 233-247.
    • (1999) J. Biomol. NMR , vol.13 , pp. 233-247
    • Maler, L.1    Potts, B.C.2    Chazin, W.J.3
  • 19
    • 0032520233 scopus 로고    scopus 로고
    • A novel mode of target recognition suggested by the 2.0 Å structure of holo S100B from bovine brain
    • Matsumura, H., Shiba, T., Inoue, T., Harada, S., and Kai, Y. (1998) A novel mode of target recognition suggested by the 2.0 Å structure of holo S100B from bovine brain. Structure 6, 233-241.
    • (1998) Structure , vol.6 , pp. 233-241
    • Matsumura, H.1    Shiba, T.2    Inoue, T.3    Harada, S.4    Kai, Y.5
  • 22
    • 33947679761 scopus 로고    scopus 로고
    • Crystal structure study on human S100A13 at 2.0 Å resolution
    • Li, M., Zhang, P. F., Pan, X. W., and Chang, W. R. (2007) Crystal structure study on human S100A13 at 2.0 Å resolution. Biochem. Biophys. Res. Commun. 356, 616-621.
    • (2007) Biochem. Biophys. Res. Commun , vol.356 , pp. 616-621
    • Li, M.1    Zhang, P.F.2    Pan, X.W.3    Chang, W.R.4
  • 23
    • 40449132497 scopus 로고    scopus 로고
    • Structure of calcium-bound human S100A13 at pH 7.5 at 1.8 Å resolution
    • Imai, F. L., Nagata, K., Yonezawa, N., Nakano, M., and Tanokura, M. (2008) Structure of calcium-bound human S100A13 at pH 7.5 at 1.8 Å resolution. Acta Crystallogr. F64, 70-76.
    • (2008) Acta Crystallogr , vol.F64 , pp. 70-76
    • Imai, F.L.1    Nagata, K.2    Yonezawa, N.3    Nakano, M.4    Tanokura, M.5
  • 24
    • 0037133530 scopus 로고    scopus 로고
    • Role of the N-terminal Helix I for dimerization and stability of the calcium-binding protein S100B
    • Ferguson, P. L., and Shaw, G. S. (2002) Role of the N-terminal Helix I for dimerization and stability of the calcium-binding protein S100B. Biochemistry 41, 3637-3646.
    • (2002) Biochemistry , vol.41 , pp. 3637-3646
    • Ferguson, P.L.1    Shaw, G.S.2
  • 25
    • 50849102039 scopus 로고    scopus 로고
    • Analysis of the structure of human apo-S100B at low temperature indicates a unimodal conformational distribution is adopted by calcium-free S100 proteins
    • Malik, S., Revington, M., Smith, S. P., and Shaw, G. S. (2008) Analysis of the structure of human apo-S100B at low temperature indicates a unimodal conformational distribution is adopted by calcium-free S100 proteins. Proteins 73, 28-42.
    • (2008) Proteins , vol.73 , pp. 28-42
    • Malik, S.1    Revington, M.2    Smith, S.P.3    Shaw, G.S.4
  • 26
    • 0242304102 scopus 로고    scopus 로고
    • Monitoring of S100 homodimerization and heterodimeric interactions by the yeast two-hybrid system
    • Deloulme, J. C., Gentil, B. J., and Baudier, J. (2003) Monitoring of S100 homodimerization and heterodimeric interactions by the yeast two-hybrid system. Microsc. Res. Tech. 60, 560-568.
    • (2003) Microsc. Res. Tech , vol.60 , pp. 560-568
    • Deloulme, J.C.1    Gentil, B.J.2    Baudier, J.3
  • 27
    • 0034634613 scopus 로고    scopus 로고
    • S100A6 and S100A11 are specific targets of the calcium- and zinc-binding S100B protein in vivo
    • Deloulme, J. C., Assard, N., Mbele, G. O., Mangin, C., Kuwano, R., and Baudier, J. (2000) S100A6 and S100A11 are specific targets of the calcium- and zinc-binding S100B protein in vivo. J. Biol. Chem. 275, 35302-35310.
    • (2000) J. Biol. Chem , vol.275 , pp. 35302-35310
    • Deloulme, J.C.1    Assard, N.2    Mbele, G.O.3    Mangin, C.4    Kuwano, R.5    Baudier, J.6
  • 31
    • 4544343310 scopus 로고    scopus 로고
    • Identification of intracellular target proteins of the calcium-signaling protein S100A12
    • Hatakeyama, T., Okada, M., Shimamoto, S., Kubota, Y., and Kobayashi, R. (2004) Identification of intracellular target proteins of the calcium-signaling protein S100A12. Eur. J. Biochem. 271, 3765-3775.
    • (2004) Eur. J. Biochem , vol.271 , pp. 3765-3775
    • Hatakeyama, T.1    Okada, M.2    Shimamoto, S.3    Kubota, Y.4    Kobayashi, R.5
  • 32
    • 0030811660 scopus 로고    scopus 로고
    • Oligomerization state of S100B at nanomolar concentration determined by large-zone analytical gel filtration chromatography
    • Drohat, A. C., Nenortas, E., Beckett, D., and Weber, D. J. (1997) Oligomerization state of S100B at nanomolar concentration determined by large-zone analytical gel filtration chromatography. Protein Sci. 6, 1577-1582.
    • (1997) Protein Sci , vol.6 , pp. 1577-1582
    • Drohat, A.C.1    Nenortas, E.2    Beckett, D.3    Weber, D.J.4
  • 33
    • 0034769732 scopus 로고    scopus 로고
    • Salt-dependent monomer-dimer equilibrium of bovine β-lactoglobulin at pH 3
    • Sakurai, K., Oobatake, M., and Goto, Y. (2001) Salt-dependent monomer-dimer equilibrium of bovine β-lactoglobulin at pH 3. Protein Sci. 10, 2325-2335.
    • (2001) Protein Sci , vol.10 , pp. 2325-2335
    • Sakurai, K.1    Oobatake, M.2    Goto, Y.3
  • 34
    • 0032533366 scopus 로고    scopus 로고
    • Lyotropic-salt-induced changes in monomer/dimer/tetramer association equilibrium of formyltransferase from the hyperthermophilic Methanopyrus kan-dleri in relation to the activity and thermostability of the enzyme
    • Shima, S., Tziatzios, C., Schubert, D., Fukada, H., Takahashi, K., Ermler, U., and Thauer, R. K. (1998) Lyotropic-salt-induced changes in monomer/dimer/tetramer association equilibrium of formyltransferase from the hyperthermophilic Methanopyrus kan-dleri in relation to the activity and thermostability of the enzyme. Eur. J. Biochem. 258, 85-92.
    • (1998) Eur. J. Biochem , vol.258 , pp. 85-92
    • Shima, S.1    Tziatzios, C.2    Schubert, D.3    Fukada, H.4    Takahashi, K.5    Ermler, U.6    Thauer, R.K.7
  • 36
    • 15244345079 scopus 로고    scopus 로고
    • The monomer-dimer equilibrium of stromal cell-derived factor-1 (CXCL 12) is altered by pH, phosphate, sulfate, and heparin
    • Veldkamp, C. T., Peterson, F. C., Pelzek, A. J., and Volkman, B. F. (2005) The monomer-dimer equilibrium of stromal cell-derived factor-1 (CXCL 12) is altered by pH, phosphate, sulfate, and heparin. Protein Sci. 14, 1071-1081.
    • (2005) Protein Sci. 14 , pp. 1071-1081
    • Veldkamp, C.T.1    Peterson, F.C.2    Pelzek, A.J.3    Volkman, B.F.4
  • 37
    • 0032125821 scopus 로고    scopus 로고
    • Detection of a Monomeric Intermediate Associated with Dimerization of Protein Hu by Mass Spectrometry
    • Vis, H., Heinemann, U., Dobson, C. M., and Robinson, C. V. (1998) Detection of a Monomeric Intermediate Associated with Dimerization of Protein Hu by Mass Spectrometry. J. Am. Chem. Soc. 120, 6427-6428.
    • (1998) J. Am. Chem. Soc , vol.120 , pp. 6427-6428
    • Vis, H.1    Heinemann, U.2    Dobson, C.M.3    Robinson, C.V.4
  • 38
    • 0030016315 scopus 로고    scopus 로고
    • Structural influence of cation binding to recombinant human brain S100b: Evidence for calcium-induced exposure of a hydrophobic surface
    • Smith, S. P., Barber, K. R., Dunn, S. D., and Shaw, G. S. (1996) Structural influence of cation binding to recombinant human brain S100b: Evidence for calcium-induced exposure of a hydrophobic surface. Biochemistry 35, 8805-8814.
    • (1996) Biochemistry , vol.35 , pp. 8805-8814
    • Smith, S.P.1    Barber, K.R.2    Dunn, S.D.3    Shaw, G.S.4
  • 40
    • 33644663381 scopus 로고    scopus 로고
    • Folding kinetics of the S100A11 protein dimer studied by time-resolved electrospray mass spectrometry and pulsed hydrogen-deuterium exchange
    • Pan, J., Rintala-Dempsey, A. C., Li, Y., Shaw, G. S., and Konermann, L. (2006) Folding kinetics of the S100A11 protein dimer studied by time-resolved electrospray mass spectrometry and pulsed hydrogen-deuterium exchange. Biochemistry 45, 3005-3013.
    • (2006) Biochemistry , vol.45 , pp. 3005-3013
    • Pan, J.1    Rintala-Dempsey, A.C.2    Li, Y.3    Shaw, G.S.4    Konermann, L.5
  • 41
    • 33845406931 scopus 로고    scopus 로고
    • Insights into S100 target specificity examined by a new interaction between S100A11 and annexin A2
    • Rintala-Dempsey, A. C., Santamaria-Kisiel, L., Liao, Y., Lajoie, G., and Shaw, G. S. (2006) Insights into S100 target specificity examined by a new interaction between S100A11 and annexin A2. Biochemistry 45, 14695-14705.
    • (2006) Biochemistry , vol.45 , pp. 14695-14705
    • Rintala-Dempsey, A.C.1    Santamaria-Kisiel, L.2    Liao, Y.3    Lajoie, G.4    Shaw, G.S.5
  • 42
    • 0030895690 scopus 로고    scopus 로고
    • Identification and structural influence of a differentially modified N-terminal methionine in human S100b
    • Smith, S. P., Barber, K. R., and Shaw, G. S. (1997) Identification and structural influence of a differentially modified N-terminal methionine in human S100b. Protein Sci. 6, 1110-1113.
    • (1997) Protein Sci , vol.6 , pp. 1110-1113
    • Smith, S.P.1    Barber, K.R.2    Shaw, G.S.3
  • 43
    • 0006925492 scopus 로고
    • Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity
    • Kay, L. E., Keifer, P., and Saarinen, T. (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J. Am. Chem. Soc. 114, 10663-10665.
    • (1992) J. Am. Chem. Soc , vol.114 , pp. 10663-10665
    • Kay, L.E.1    Keifer, P.2    Saarinen, T.3
  • 44
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes. J. Biomol. NMR 6, 277-293.
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 45
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • Johnson, B. A., and Belvins, R. A. (1994) NMRView: A computer program for the visualization and analysis of NMR data. J. Biomol. NMR 4, 603-614.
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Belvins, R.A.2
  • 46
    • 0029836953 scopus 로고    scopus 로고
    • Discovering high-affinity ligands for proteins: SAR by NMR
    • Shuker, S. B., Hajduk, P. J., Meadows, R. P., and Fesik, S. W. (1996) Discovering high-affinity ligands for proteins: SAR by NMR. Science 274, 1531-1534.
    • (1996) Science , vol.274 , pp. 1531-1534
    • Shuker, S.B.1    Hajduk, P.J.2    Meadows, R.P.3    Fesik, S.W.4
  • 47
    • 0028857598 scopus 로고
    • Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements
    • Altieri, A. S., Hinton, D. P., and Byrd, R. A. (1995) Association of biomolecular systems via pulsed field gradient NMR self-diffusion measurements. J. Am. Chem. Soc. 117, 7566-7567.
    • (1995) J. Am. Chem. Soc , vol.117 , pp. 7566-7567
    • Altieri, A.S.1    Hinton, D.P.2    Byrd, R.A.3
  • 48
    • 0000857723 scopus 로고    scopus 로고
    • Characterisation of protein unfolding by NMR diffusion measurements
    • Jones, J. A., Wilkins, D. K., Smith, L. J., and Dobson, C. M. (1997) Characterisation of protein unfolding by NMR diffusion measurements. J. Biomol. NMR 10, 199-203.
    • (1997) J. Biomol. NMR , vol.10 , pp. 199-203
    • Jones, J.A.1    Wilkins, D.K.2    Smith, L.J.3    Dobson, C.M.4
  • 49
    • 0033554852 scopus 로고    scopus 로고
    • Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques
    • Wilkins, D. K., Grimshaw, S. B., Receveur, V., Dobson, C. M., Jones, J. A., and Smith, L. J. (1999) Hydrodynamic radii of native and denatured proteins measured by pulse field gradient NMR techniques. Biochemistry 38, 16424-16431.
    • (1999) Biochemistry , vol.38 , pp. 16424-16431
    • Wilkins, D.K.1    Grimshaw, S.B.2    Receveur, V.3    Dobson, C.M.4    Jones, J.A.5    Smith, L.J.6
  • 50
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • Garcia De La Torre, J., Huertas, M. L., and Carrasco, B. (2000) Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78, 719-730.
    • (2000) Biophys. J , vol.78 , pp. 719-730
    • Garcia De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 51
    • 14844314784 scopus 로고    scopus 로고
    • Mutually antagonistic actions of S100A4 and S100A1 on normal and metastatic pheno-types
    • Wang, G., Zhang, S., Fernig, D. G., Martin-Fernandez, M., Rudland, P. S., and Barraclough, R. (2005) Mutually antagonistic actions of S100A4 and S100A1 on normal and metastatic pheno-types. Oncogene 24, 1445-1454.
    • (2005) Oncogene , vol.24 , pp. 1445-1454
    • Wang, G.1    Zhang, S.2    Fernig, D.G.3    Martin-Fernandez, M.4    Rudland, P.S.5    Barraclough, R.6
  • 52
    • 0034622580 scopus 로고    scopus 로고
    • Identification of hydrophobic amino acid residues involved in the formation of S100P ho-modimers in vivo
    • Koltzscher, M., and Gerke, V. (2000) Identification of hydrophobic amino acid residues involved in the formation of S100P ho-modimers in vivo. Biochemistry 39, 9533-9539.
    • (2000) Biochemistry , vol.39 , pp. 9533-9539
    • Koltzscher, M.1    Gerke, V.2
  • 53
    • 0031174297 scopus 로고    scopus 로고
    • Assignment and secondary structure of calcium-bound human S100B
    • Smith, S. P., and Shaw, G. S. (1997) Assignment and secondary structure of calcium-bound human S100B. J. Biomol. NMR 10, 77-88.
    • (1997) J. Biomol. NMR , vol.10 , pp. 77-88
    • Smith, S.P.1    Shaw, G.S.2
  • 56
    • 0032843242 scopus 로고    scopus 로고
    • 2+-bound rat S100B(ββ) upon binding to a peptide derived from the C-terminal regulatory domain of p53
    • 2+-bound rat S100B(ββ) upon binding to a peptide derived from the C-terminal regulatory domain of p53. Protein Sci. 8, 1743-1751.
    • (1999) Protein Sci , vol.8 , pp. 1743-1751
    • Rustandi, R.R.1    Baldisseri, D.M.2    Drohat, A.C.3    Weber, D.J.4
  • 57
    • 0020490704 scopus 로고
    • Physiochemical and optical studies on calcium-and potassium-induced conformational changes in bovine brain S-100b protein
    • Mani, R. J. (1982) Physiochemical and optical studies on calcium-and potassium-induced conformational changes in bovine brain S-100b protein. Biochemistry 21, 2607-2612.
    • (1982) Biochemistry , vol.21 , pp. 2607-2612
    • Mani, R.J.1
  • 58
    • 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
  • 59
    • 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
  • 60
    • 34548768193 scopus 로고    scopus 로고
    • Symmetric Behaviour of Hemoglobin α- and β-Subunits during Acid-Induced Denaturation Observed by Electrospray Mass Spectrometry
    • Boys, B. L., Kuprowski, M. C., and Konermann, L. (2007) Symmetric Behaviour of Hemoglobin α- and β-Subunits during Acid-Induced Denaturation Observed by Electrospray Mass Spectrometry. Biochemistry 46, 10675-10684.
    • (2007) Biochemistry , vol.46 , pp. 10675-10684
    • Boys, B.L.1    Kuprowski, M.C.2    Konermann, L.3
  • 61
    • 0142215597 scopus 로고    scopus 로고
    • Protein-ligand and protein-protein interactions studied by electrospray ionization and mass spectrometry
    • Burkitt, W. I., Derrick, P. J., Lafitte, D., and Bronstein, I. (2003) Protein-ligand and protein-protein interactions studied by electrospray ionization and mass spectrometry. Biochem. Soc. Trans. 31, 985-989.
    • (2003) Biochem. Soc. Trans , vol.31 , pp. 985-989
    • Burkitt, W.I.1    Derrick, P.J.2    Lafitte, D.3    Bronstein, I.4
  • 62
    • 34250748490 scopus 로고    scopus 로고
    • Analysis of Protein Mixtures by Electrospray Mass Spectrometry: Effects of Conformation and Desolvation Behavior on the Signal Intensities of Hemoglobin Subunits
    • Kuprowski, M. C., Boys, B. L., and Konermann, L. (2007) Analysis of Protein Mixtures by Electrospray Mass Spectrometry: Effects of Conformation and Desolvation Behavior on the Signal Intensities of Hemoglobin Subunits. J. Am. Soc. Mass Spectrom. 18, 1279-1285.
    • (2007) J. Am. Soc. Mass Spectrom , vol.18 , pp. 1279-1285
    • Kuprowski, M.C.1    Boys, B.L.2    Konermann, L.3
  • 63
    • 0033520512 scopus 로고    scopus 로고
    • Accessing the global minimum conformation of stefin A dimer by annealing under partially denaturing conditions
    • Jerala, R., and Zerovnik, E. (1999) Accessing the global minimum conformation of stefin A dimer by annealing under partially denaturing conditions. J. Mol. Biol. 291, 1079-1089.
    • (1999) J. Mol. Biol , vol.291 , pp. 1079-1089
    • Jerala, R.1    Zerovnik, E.2
  • 64
    • 57749116016 scopus 로고    scopus 로고
    • Catalytically Active Monomer of Glutathione S-Transferase π and Key Residues Involved in the Electrostatic Interaction between Subunits
    • Huang, Y. C., Misquitta, S., Blond, S. Y., Adams, E., and Colman, R. F. (2008) Catalytically Active Monomer of Glutathione S-Transferase π and Key Residues Involved in the Electrostatic Interaction between Subunits. J. Biol. Chem. 283, 32880-32888.
    • (2008) J. Biol. Chem , vol.283 , pp. 32880-32888
    • Huang, Y.C.1    Misquitta, S.2    Blond, S.Y.3    Adams, E.4    Colman, R.F.5
  • 65
    • 0021773239 scopus 로고
    • Hydrodynamic properties of bovine brain S-100 proteins
    • Mani, R. S., and Kay, C. M. (1984) Hydrodynamic properties of bovine brain S-100 proteins. FEBS Lett. 166, 258-262.
    • (1984) FEBS Lett , vol.166 , pp. 258-262
    • Mani, R.S.1    Kay, C.M.2
  • 66
    • 0035984339 scopus 로고    scopus 로고
    • Studies of Biomolecular Conformations and Conformational Dynamics by Mass Spectrometry
    • Kaltashov, I. A., and Eyles, S. J. (2002) Studies of Biomolecular Conformations and Conformational Dynamics by Mass Spectrometry. Mass Spectrom. Rev. 21, 37-71.
    • (2002) Mass Spectrom. Rev , vol.21 , pp. 37-71
    • Kaltashov, I.A.1    Eyles, S.J.2
  • 67
    • 0036967268 scopus 로고    scopus 로고
    • Intramolecular dynamics of low molecular weight protein tyrosine phosphatase in monomer-dimer equilibrium studied by NMR: A model for changes in dynamics upon target binding
    • Akerud, T., Thulin, E., Van Etten, R. L., and Akke, M. (2002) Intramolecular dynamics of low molecular weight protein tyrosine phosphatase in monomer-dimer equilibrium studied by NMR: A model for changes in dynamics upon target binding. J. Mol. Biol. 322, 137-152.
    • (2002) J. Mol. Biol , vol.322 , pp. 137-152
    • Akerud, T.1    Thulin, E.2    Van Etten, R.L.3    Akke, M.4
  • 69
    • 0037093642 scopus 로고    scopus 로고
    • Coupling of ligand binding and dimerization of helix-loop-helix peptides: Spectroscopic and sedimentation analyses of calbindin D9k EF-hands
    • Julenius, K., Robblee, J., Thulin, E., Finn, B. E., Fairman, R., and Linse, S. (2002) Coupling of ligand binding and dimerization of helix-loop-helix peptides: Spectroscopic and sedimentation analyses of calbindin D9k EF-hands. Proteins 47, 323-333.
    • (2002) Proteins , vol.47 , pp. 323-333
    • Julenius, K.1    Robblee, J.2    Thulin, E.3    Finn, B.E.4    Fairman, R.5    Linse, S.6
  • 70
    • 0027971545 scopus 로고
    • Effects of anions on the positive ion electrospray ionization mass spectra of peptides and proteins
    • Mirza, U. A., and Chait, B. T. (1994) Effects of anions on the positive ion electrospray ionization mass spectra of peptides and proteins. Anal. Chem. 66, 2898-2904.
    • (1994) Anal. Chem , vol.66 , pp. 2898-2904
    • Mirza, U.A.1    Chait, B.T.2


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