메뉴 건너뛰기




Volumn 33, Issue 3, 2006, Pages 179-190

Combinations of SPR and MS for characterization of native and recombinant proteins in cell lysates

Author keywords

14 3 3 proteins; Affinity purification; Recombinant; Surface plasmon resonance mass spectrometry (SPR MS)

Indexed keywords

BIOASSAY; CELLS; MASS SPECTROMETRY; MOLECULAR STRUCTURE; MOLECULAR WEIGHT; SURFACE PLASMON RESONANCE;

EID: 33748340239     PISSN: 10736085     EISSN: None     Source Type: Journal    
DOI: 10.1385/MB:33:3:179     Document Type: Article
Times cited : (14)

References (17)
  • 1
    • 0023388644 scopus 로고
    • Analytical biotechnology of recombinant products
    • Borman, S., (1987) Analytical biotechnology of recombinant products. Anal. Chem. 59, 969A-973A.
    • (1987) Anal. Chem. , vol.59
    • Borman, S.1
  • 2
    • 0002747447 scopus 로고
    • A non-label technology for real-time biospecific interaction analysis
    • Fägerstam, L.G., (1991) A non-label technology for real-time biospecific interaction analysis. Tech. Prot. Chem. II, 65-71.
    • (1991) Tech. Prot. Chem. , vol.2 , pp. 65-71
    • Fägerstam, L.G.1
  • 3
    • 0346731181 scopus 로고    scopus 로고
    • Biomolecular interaction analysis and MS
    • Mattei, B., Borch, J., and Roepstorff, P. (2004) Biomolecular interaction analysis and MS. Anal. Chem. 76, 18A-25A.
    • (2004) Anal. Chem. , vol.76
    • Mattei, B.1    Borch, J.2    Roepstorff, P.3
  • 5
    • 4043100606 scopus 로고    scopus 로고
    • Integration of surface plasmon resonance with mass spectrometry: Automated ligand fishing and sample preparation for MALDI MS using a Biacore 3000 biosensor
    • Zhukov, A., Schurenberg, M., Jansson, O., Areskoug, D., and Buijs, J. (2004) Integration of surface plasmon resonance with mass spectrometry: automated ligand fishing and sample preparation for MALDI MS using a Biacore 3000 biosensor. J. Biomol. Tech. 15, 112-119.
    • (2004) J. Biomol. Tech. , vol.15 , pp. 112-119
    • Zhukov, A.1    Schurenberg, M.2    Jansson, O.3    Areskoug, D.4    Buijs, J.5
  • 6
    • 0037271476 scopus 로고    scopus 로고
    • Design and use of multi-affinity surfaces in biomolecular interaction analysis-mass spectrometry (BIA/MS): A step toward the design of SPR/MS arrays
    • Nedelkov, D. and Nelson, R.W. (2003) Design and use of multi-affinity surfaces in biomolecular interaction analysis-mass spectrometry (BIA/MS): a step toward the design of SPR/MS arrays. J. Mol. Recognit. 16, 15-19.
    • (2003) J. Mol. Recognit. , vol.16 , pp. 15-19
    • Nedelkov, D.1    Nelson, R.W.2
  • 7
    • 1642450651 scopus 로고    scopus 로고
    • 14-3-3 proteins: Regulation of signal-induced events
    • Ferl, R.J., (2004) 14-3-3 proteins: regulation of signal-induced events. Physiol Plantarum. 120, 173-178.
    • (2004) Physiol Plantarum. , vol.120 , pp. 173-178
    • Ferl, R.J.1
  • 8
    • 0034528346 scopus 로고    scopus 로고
    • 14-3-3 proteins: Regulation of subcellular localization by molecular interference
    • Muslin, A.J. and H.M. Xing. (2000) 14-3-3 proteins: regulation of subcellular localization by molecular interference. Cell. Signal. 12, 703-709.
    • (2000) Cell. Signal. , vol.12 , pp. 703-709
    • Muslin, A.J.1    Xing, H.M.2
  • 9
    • 0033719624 scopus 로고    scopus 로고
    • Evolution of the 14-3-3 protein family: Does the large number of isoforms in multicellular organisms reflect functional specificity?
    • Rosenquist, M., Sehnke, P., Ferl, R. J., Sommarin, M., and Larsson, C. (2000) Evolution of the 14-3-3 protein family: Does the large number of isoforms in multicellular organisms reflect functional specificity? J. Mol. Evol. 51, 446-458.
    • (2000) J. Mol. Evol. , vol.51 , pp. 446-458
    • Rosenquist, M.1    Sehnke, P.2    Ferl, R.J.3    Sommarin, M.4    Larsson, C.5
  • 10
    • 0033579441 scopus 로고    scopus 로고
    • Binding of 14-3-3 protein to the plasma membrane H+-ATPase AHA2 involves the three C-terminal residues Tyr(946)-Thr-Val and requires phosphorylation of Thr(947)
    • Fuglsang, A.T., Visconti, S., Drumm, K., et al., (1999) Binding of 14-3-3 protein to the plasma membrane H+-ATPase AHA2 involves the three C-terminal residues Tyr(946)-Thr-Val and requires phosphorylation of Thr(947). J. Biol. Chem. 274, 36,774-36,780.
    • (1999) J. Biol. Chem. , vol.274
    • Fuglsang, A.T.1    Visconti, S.2    Drumm, K.3
  • 11
    • 0033373242 scopus 로고    scopus 로고
    • Phosphorylation of Thr-948 at the C terminus of the plasma membrane H+-ATPase creates a binding site for the regulatory 14-3-3 protein
    • Svennelid, F., Olsson, A., Piotrowski, M., et al., (1999) Phosphorylation of Thr-948 at the C terminus of the plasma membrane H+-ATPase creates a binding site for the regulatory 14-3-3 protein. Plant Cell. 11, 2379-2391.
    • (1999) Plant Cell. , vol.11 , pp. 2379-2391
    • Svennelid, F.1    Olsson, A.2    Piotrowski, M.3
  • 12
    • 0142211242 scopus 로고    scopus 로고
    • The binding site for regulatory 14-3-3 protein in plant plasma membrane H+-ATPase - Involvement of a region promoting phosphorylation-independent interaction in addition to the phosphorylation-dependent C-terminal end
    • Fuglsang, A. T., Borch, J., Bych, K., Jahn, T. P., Roepstorff, P., Palmgren, M. G. (2003) The binding site for regulatory 14-3-3 protein in plant plasma membrane H+-ATPase - Involvement of a region promoting phosphorylation-independent interaction in addition to the phosphorylation- dependent C-terminal end. J. Biol. Chem. 278, 42,266-42,272.
    • (2003) J. Biol. Chem. , vol.278
    • Fuglsang, A.T.1    Borch, J.2    Bych, K.3    Jahn, T.P.4    Roepstorff, P.5    Palmgren, M.G.6
  • 13
    • 0032033440 scopus 로고    scopus 로고
    • The 14-3-3 proteins associate with the plant plasma membrane H+-ATPase to generate a fusicoccin binding complex and a fusicoccin responsive system
    • Baunsgaard, L., Fuglsang, A. T., Jahn, T., Korthout, H. A., de Boer, A. H., Palmgren, M. G. (1998) The 14-3-3 proteins associate with the plant plasma membrane H+-ATPase to generate a fusicoccin binding complex and a fusicoccin responsive system. Plant J. 13, 661-671.
    • (1998) Plant J. , vol.13 , pp. 661-671
    • Baunsgaard, L.1    Fuglsang, A.T.2    Jahn, T.3    Korthout, H.A.4    De Boer, A.H.5    Palmgren, M.G.6
  • 14
    • 0033119238 scopus 로고    scopus 로고
    • Phosphorylation-dependent interactions between enzymes of plant metabolism and 14-3-3 proteins
    • Moorhead, G., Douglas, P., Cotelle, V., et al., (1999) Phosphorylation-dependent interactions between enzymes of plant metabolism and 14-3-3 proteins. Plant J. 18, 1-12.
    • (1999) Plant J. , vol.18 , pp. 1-12
    • Moorhead, G.1    Douglas, P.2    Cotelle, V.3
  • 15
    • 0029927505 scopus 로고    scopus 로고
    • Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels
    • Shevchenko, A., M. Wilm, O. Vorm, and M. Mann. (1996) Mass spectrometric sequencing of proteins from silver-stained polyacrylamide gels. Anal. Chem. 68, 850-858.
    • (1996) Anal. Chem. , vol.68 , pp. 850-858
    • Shevchenko, A.1    Wilm, M.2    Vorm, O.3    Mann, M.4
  • 16
    • 15144343751 scopus 로고    scopus 로고
    • Matrix-assisted laser desorption/ionization mass spectrometry sample preparation techniques designed for various peptide and protein analytes
    • Kussmann, M., Lassing, U., Sturmer, C. A., Przybylski, M., and Roepstorff, P. (1997) Matrix-assisted laser desorption/ionization mass spectrometry sample preparation techniques designed for various peptide and protein analytes. J.Mass. Spectrom. 32, 593-601.
    • (1997) J.Mass. Spectrom. , vol.32 , pp. 593-601
    • Kussmann, M.1    Lassing, U.2    Sturmer, C.A.3    Przybylski, M.4    Roepstorff, P.5
  • 17
    • 0037096075 scopus 로고    scopus 로고
    • A rapid screening method to monitor expression of recombinant proteins from various prokaryotic and eukaryotic expression systems using matrix-assisted laser desorption ionization-time-of-flight mass spectrometry
    • Jebanathirajah, J.A., Andersen, S., Blagoev, B., and Roepstorff, P. (2002) A rapid screening method to monitor expression of recombinant proteins from various prokaryotic and eukaryotic expression systems using matrix-assisted laser desorption ionization-time-of-flight mass spectrometry. Anal. Biochem. 305, 242-250.
    • (2002) Anal. Biochem. , vol.305 , pp. 242-250
    • Jebanathirajah, J.A.1    Andersen, S.2    Blagoev, B.3    Roepstorff, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.