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Volumn 14, Issue 2, 2010, Pages 247-254

Lanthanide-tagged proteins - an illuminating partnership

Author keywords

[No Author keywords available]

Indexed keywords

EUROPIUM; LANTHANIDE; PROTEIN; TERBIUM;

EID: 77949910887     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cbpa.2010.01.004     Document Type: Review
Times cited : (103)

References (39)
  • 1
    • 33344469835 scopus 로고    scopus 로고
    • Benefitting from the unique properties of lanthanide ions
    • Bunzli J.-C.G. Benefitting from the unique properties of lanthanide ions. Acc Chem Res 39 (2006) 53-61
    • (2006) Acc Chem Res , vol.39 , pp. 53-61
    • Bunzli, J.-C.G.1
  • 4
    • 35548988910 scopus 로고    scopus 로고
    • Paramagnetism-based NMR restraints provide maximum allowed probabilities for the different conformations of partially independent protein domains
    • Bertini I., Gupta Y.K., Luchinat C., Parigi G., Peana M., Sgheri L., and Yuan J. Paramagnetism-based NMR restraints provide maximum allowed probabilities for the different conformations of partially independent protein domains. J Am Chem Soc 129 (2007) 12786-12794
    • (2007) J Am Chem Soc , vol.129 , pp. 12786-12794
    • Bertini, I.1    Gupta, Y.K.2    Luchinat, C.3    Parigi, G.4    Peana, M.5    Sgheri, L.6    Yuan, J.7
  • 5
    • 0033105255 scopus 로고    scopus 로고
    • Thiol-reactive luminescent chelates of terbium and europium
    • Chen J., and Selvin P.R. Thiol-reactive luminescent chelates of terbium and europium. Bioconjug Chem 10 (1999) 311-315
    • (1999) Bioconjug Chem , vol.10 , pp. 311-315
    • Chen, J.1    Selvin, P.R.2
  • 6
    • 38949175718 scopus 로고    scopus 로고
    • Lanthanide-binding peptides for NMR measurements of residual dipolar couplings and paramagnetic effects from multiple angles
    • Enhancements in NMR structure determination are obtained by the attachment of lanthanide-binding peptides through different positions on the peptide to the same site on the protein target together with coordination to a series of lanthanide ions.
    • Su X.C., McAndrew K., Huber T., and Otting G. Lanthanide-binding peptides for NMR measurements of residual dipolar couplings and paramagnetic effects from multiple angles. J Am Chem Soc 130 (2008) 1681-1687. Enhancements in NMR structure determination are obtained by the attachment of lanthanide-binding peptides through different positions on the peptide to the same site on the protein target together with coordination to a series of lanthanide ions.
    • (2008) J Am Chem Soc , vol.130 , pp. 1681-1687
    • Su, X.C.1    McAndrew, K.2    Huber, T.3    Otting, G.4
  • 7
    • 0036085517 scopus 로고    scopus 로고
    • Principles and biophysical applications of lanthanide-based probes
    • Selvin P.R. Principles and biophysical applications of lanthanide-based probes. Annu Rev Biophys Biomol Struct 31 (2002) 275-302
    • (2002) Annu Rev Biophys Biomol Struct , vol.31 , pp. 275-302
    • Selvin, P.R.1
  • 8
    • 0037419375 scopus 로고    scopus 로고
    • Lanthanide-binding tags as versatile protein coexpression probes
    • Franz K.J., Nitz M., and Imperiali B. Lanthanide-binding tags as versatile protein coexpression probes. Chembiochem 4 (2003) 265-271
    • (2003) Chembiochem , vol.4 , pp. 265-271
    • Franz, K.J.1    Nitz, M.2    Imperiali, B.3
  • 9
  • 10
    • 0037419262 scopus 로고    scopus 로고
    • A powerful combinatorial screen to identify high-affinity terbium(III)-binding peptides
    • Nitz M., Franz K.J., Maglathlin R.L., and Imperiali B. A powerful combinatorial screen to identify high-affinity terbium(III)-binding peptides. Chembiochem 4 (2003) 272-276
    • (2003) Chembiochem , vol.4 , pp. 272-276
    • Nitz, M.1    Franz, K.J.2    Maglathlin, R.L.3    Imperiali, B.4
  • 11
    • 30144437411 scopus 로고    scopus 로고
    • Rapid combinatorial screening of peptide libraries for the selection of lanthanide-binding tags (LBTs)
    • Martin L.J., Sculimbrene B.R., Nitz M., and Imperiali B. Rapid combinatorial screening of peptide libraries for the selection of lanthanide-binding tags (LBTs). QSAR Comb. Sci. 24 (2005) 1149-1157
    • (2005) QSAR Comb. Sci. , vol.24 , pp. 1149-1157
    • Martin, L.J.1    Sculimbrene, B.R.2    Nitz, M.3    Imperiali, B.4
  • 13
    • 33749680579 scopus 로고    scopus 로고
    • Site-specific labelling of proteins with a rigid lanthanide-binding tag
    • Su X.C., Huber T., Dixon N.E., and Otting G. Site-specific labelling of proteins with a rigid lanthanide-binding tag. Chembiochem 7 (2006) 1599-1604
    • (2006) Chembiochem , vol.7 , pp. 1599-1604
    • Su, X.C.1    Huber, T.2    Dixon, N.E.3    Otting, G.4
  • 14
    • 34250217022 scopus 로고    scopus 로고
    • Double-lanthanide-binding tags for macromolecular crystallographic structure determination
    • A double lanthanide-ion binding peptide is developed and utilized in X-ray crystallographic structure determination as a fusion to the N-terminus of ubiquitin. Notably, phases were determined solely from the bound lanthanide and were robust, allowing automated model building.
    • Silvaggi N.R., Martin L.J., Schwalbe H., Imperiali B., and Allen K.N. Double-lanthanide-binding tags for macromolecular crystallographic structure determination. J Am Chem Soc 129 (2007) 7114-7120. A double lanthanide-ion binding peptide is developed and utilized in X-ray crystallographic structure determination as a fusion to the N-terminus of ubiquitin. Notably, phases were determined solely from the bound lanthanide and were robust, allowing automated model building.
    • (2007) J Am Chem Soc , vol.129 , pp. 7114-7120
    • Silvaggi, N.R.1    Martin, L.J.2    Schwalbe, H.3    Imperiali, B.4    Allen, K.N.5
  • 15
    • 0242299265 scopus 로고    scopus 로고
    • Protein alignment by a coexpressed lanthanide-binding tag for the measurement of residual dipolar couplings
    • Wohnert J., Franz K.J., Nitz M., Imperiali B., and Schwalbe H. Protein alignment by a coexpressed lanthanide-binding tag for the measurement of residual dipolar couplings. J Am Chem Soc 125 (2003) 13338-13339
    • (2003) J Am Chem Soc , vol.125 , pp. 13338-13339
    • Wohnert, J.1    Franz, K.J.2    Nitz, M.3    Imperiali, B.4    Schwalbe, H.5
  • 16
    • 46449126204 scopus 로고    scopus 로고
    • Structure determination of a Galectin-3-carbohydrate complex using paramagnetism-based NMR constraints
    • The problem of decrease or disappearance of NOEs in extensively hydrogen-bonded structures is circumvented in this study by the use of RDCs and PCSs incorporated through use of a lanthanide-ion binding peptide fused to Galectin at the C-terminus.
    • Zhuang T., Lee H.S., Imperiali B., and Prestegard J.H. Structure determination of a Galectin-3-carbohydrate complex using paramagnetism-based NMR constraints. Protein Sci 17 (2008) 1220-1231. The problem of decrease or disappearance of NOEs in extensively hydrogen-bonded structures is circumvented in this study by the use of RDCs and PCSs incorporated through use of a lanthanide-ion binding peptide fused to Galectin at the C-terminus.
    • (2008) Protein Sci , vol.17 , pp. 1220-1231
    • Zhuang, T.1    Lee, H.S.2    Imperiali, B.3    Prestegard, J.H.4
  • 20
    • 67649408735 scopus 로고    scopus 로고
    • Two-point anchoring of a lanthanide-binding peptide to a target protein enhances the paramagnetic anisotropic effect
    • Saio T., Ogura K., Yokochi M., Kobashigawa Y., and Inagaki F. Two-point anchoring of a lanthanide-binding peptide to a target protein enhances the paramagnetic anisotropic effect. J Biomol NMR 44 (2009) 157-166
    • (2009) J Biomol NMR , vol.44 , pp. 157-166
    • Saio, T.1    Ogura, K.2    Yokochi, M.3    Kobashigawa, Y.4    Inagaki, F.5
  • 22
    • 43049119634 scopus 로고    scopus 로고
    • Chemoenzymatic synthesis of polyprenyl phosphates
    • Hartley M.D., Larkin A., and Imperiali B. Chemoenzymatic synthesis of polyprenyl phosphates. Bioorg Med Chem 16 (2008) 5149-5156
    • (2008) Bioorg Med Chem , vol.16 , pp. 5149-5156
    • Hartley, M.D.1    Larkin, A.2    Imperiali, B.3
  • 23
    • 33846376481 scopus 로고    scopus 로고
    • LBT/PTD dual tagged vector for purification, cellular protein delivery and visualization in living cells
    • This paper reports the first demonstration of the uptake and subsequent visualization of an LBT-protein conjugate in living cells.
    • Goda N., Tenno T., Inomata K., Iwaya N., Sasaki Y., Shirakawa M., and Hiroaki H. LBT/PTD dual tagged vector for purification, cellular protein delivery and visualization in living cells. Biochim Biophys Acta 1773 (2007) 141-146. This paper reports the first demonstration of the uptake and subsequent visualization of an LBT-protein conjugate in living cells.
    • (2007) Biochim Biophys Acta , vol.1773 , pp. 141-146
    • Goda, N.1    Tenno, T.2    Inomata, K.3    Iwaya, N.4    Sasaki, Y.5    Shirakawa, M.6    Hiroaki, H.7
  • 24
    • 47349116310 scopus 로고    scopus 로고
    • Intracellular protein delivery activity of peptides derived from insulin-like growth factor binding proteins 3 and 5
    • Goda N., Tenno T., Inomata K., Shirakawa M., Tanaka T., and Hiroaki H. Intracellular protein delivery activity of peptides derived from insulin-like growth factor binding proteins 3 and 5. Exp Cell Res 314 (2008) 2352-2361
    • (2008) Exp Cell Res , vol.314 , pp. 2352-2361
    • Goda, N.1    Tenno, T.2    Inomata, K.3    Shirakawa, M.4    Tanaka, T.5    Hiroaki, H.6
  • 27
    • 46149091062 scopus 로고    scopus 로고
    • + channels
    • + channel in the open and closed (CTX-bond) states. The studies provide the foundation for a new model of channel activation.
    • + channel in the open and closed (CTX-bond) states. The studies provide the foundation for a new model of channel activation.
    • (2008) Neuron , vol.59 , pp. 98-109
    • Posson, D.J.1    Selvin, P.R.2
  • 28
    • 0037133590 scopus 로고    scopus 로고
    • Engineering a terbium-binding site into an integral membrane protein for luminescence energy transfer
    • Vazquez-Ibar J.L., Weinglass A.B., and Kaback H.R. Engineering a terbium-binding site into an integral membrane protein for luminescence energy transfer. Proc Natl Acad Sci U S A 99 (2002) 3487-3492
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 3487-3492
    • Vazquez-Ibar, J.L.1    Weinglass, A.B.2    Kaback, H.R.3
  • 29
    • 0034807765 scopus 로고    scopus 로고
    • Luminescence resonance energy transfer analysis of RNA polymerase complexes
    • Heyduk T. Luminescence resonance energy transfer analysis of RNA polymerase complexes. Methods 25 (2001) 44-53
    • (2001) Methods , vol.25 , pp. 44-53
    • Heyduk, T.1
  • 32
    • 0028077111 scopus 로고
    • Luminescence energy transfer using a terbium chelate: improvements on fluorescence energy transfer
    • Selvin P.R., and Hearst J.E. Luminescence energy transfer using a terbium chelate: improvements on fluorescence energy transfer. Proc Natl Acad Sci U S A 91 (1994) 10024-10028
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 10024-10028
    • Selvin, P.R.1    Hearst, J.E.2
  • 33
    • 36048946776 scopus 로고    scopus 로고
    • In vivo measurement of intramolecular distances using genetically encoded reporters
    • This study provides the first proof-of-concept for a new strategy for the application of LRET to complex membrane-bound proteins that involves the use of genetically encoded LBT and 6-His sequences as donor and acceptor components.
    • Sandtner W., Bezanilla F., and Correa A.M. In vivo measurement of intramolecular distances using genetically encoded reporters. Biophys J 93 (2007) L45-47. This study provides the first proof-of-concept for a new strategy for the application of LRET to complex membrane-bound proteins that involves the use of genetically encoded LBT and 6-His sequences as donor and acceptor components.
    • (2007) Biophys J , vol.93
    • Sandtner, W.1    Bezanilla, F.2    Correa, A.M.3
  • 35
    • 33744941073 scopus 로고    scopus 로고
    • Lanthanide-binding tags as luminescent probes for studying protein interactions
    • Sculimbrene B.R., and Imperiali B. Lanthanide-binding tags as luminescent probes for studying protein interactions. J Am Chem Soc 128 (2006) 7346-7352
    • (2006) J Am Chem Soc , vol.128 , pp. 7346-7352
    • Sculimbrene, B.R.1    Imperiali, B.2
  • 36
    • 33646344655 scopus 로고    scopus 로고
    • Design of a protein kinase-inducible domain
    • Balakrishnan S., and Zondlo N.J. Design of a protein kinase-inducible domain. J Am Chem Soc 128 (2006) 5590-5591
    • (2006) J Am Chem Soc , vol.128 , pp. 5590-5591
    • Balakrishnan, S.1    Zondlo, N.J.2
  • 37
    • 67651121511 scopus 로고    scopus 로고
    • Direct measurement of the kinetics of CBM9 fusion-tag bioprocessing using luminescence resonance energy transfer
    • Kavoosi M., Creagh A.L., Turner R.F., Kilburn D.G., and Haynes C.A. Direct measurement of the kinetics of CBM9 fusion-tag bioprocessing using luminescence resonance energy transfer. Biotechnol Prog 25 (2009) 874-881
    • (2009) Biotechnol Prog , vol.25 , pp. 874-881
    • Kavoosi, M.1    Creagh, A.L.2    Turner, R.F.3    Kilburn, D.G.4    Haynes, C.A.5
  • 38
    • 64549094197 scopus 로고    scopus 로고
    • Development of lanthanide-labeled human INSL3 as a alternative probe to radioactively labeled INSL3 for use in bioassays
    • Shabananpoor F., Hughes R.A., Bathgate R.A., Separovic F., and Wade J.D. Development of lanthanide-labeled human INSL3 as a alternative probe to radioactively labeled INSL3 for use in bioassays. Ann N Y Acad Sci 1160 (2009) 87-90
    • (2009) Ann N Y Acad Sci , vol.1160 , pp. 87-90
    • Shabananpoor, F.1    Hughes, R.A.2    Bathgate, R.A.3    Separovic, F.4    Wade, J.D.5
  • 39
    • 0034600246 scopus 로고    scopus 로고
    • Lanthanide induced pseudocontact shifts for solution structure refinements of macromolecules in shells up to 40 Å from the metal ion
    • Allegrozzi M., Bertini I., Janik M.B.L., Lee Y.-M., Liu G., and Luchinat C. Lanthanide induced pseudocontact shifts for solution structure refinements of macromolecules in shells up to 40 Å from the metal ion. J Am Chem Soc 122 (2000) 4154-4161
    • (2000) J Am Chem Soc , vol.122 , pp. 4154-4161
    • Allegrozzi, M.1    Bertini, I.2    Janik, M.B.L.3    Lee, Y.-M.4    Liu, G.5    Luchinat, C.6


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