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Volumn 100, Issue 10, 2011, Pages 2513-2521

Labeling of specific cysteines in proteins using reversible metal protection

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EID: 79959630494     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2011.03.063     Document Type: Article
Times cited : (29)

References (21)
  • 2
    • 77952339435 scopus 로고    scopus 로고
    • Fluorescence applications in molecular neurobiology
    • Taraska, J. W., and W. N. Zagotta. 2010. Fluorescence applications in molecular neurobiology. Neuron. 66:170-189.
    • (2010) Neuron , vol.66 , pp. 170-189
    • Taraska, J.W.1    Zagotta, W.N.2
  • 3
    • 70349510724 scopus 로고    scopus 로고
    • Short-distance probes for protein backbone structure based on energy transfer between bimane and transition metal ions
    • Taraska, J. W., M. C. Puljung, and W. N. Zagotta. 2009. Short-distance probes for protein backbone structure based on energy transfer between bimane and transition metal ions. Proc. Natl. Acad. Sci. USA. 106:16227-16232.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 16227-16232
    • Taraska, J.W.1    Puljung, M.C.2    Zagotta, W.N.3
  • 4
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • DOI 10.1146/annurev.biochem.67.1.509
    • Tsien, R. Y. 1998. The green fluorescent protein. Annu. Rev. Biochem. 67:509-544. (Pubitemid 28411137)
    • (1998) Annual Review of Biochemistry , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 5
    • 67649604544 scopus 로고    scopus 로고
    • Mapping the structure and conformational movements of proteins with transition metal ion FRET
    • Taraska, J. W., M. C. Puljung, ..., W. N. Zagotta. 2009. Mapping the structure and conformational movements of proteins with transition metal ion FRET. Nat. Methods. 6:532-537.
    • (2009) Nat. Methods , vol.6 , pp. 532-537
    • Taraska, J.W.1    Puljung, M.C.2    Zagotta, W.N.3
  • 6
    • 36048946776 scopus 로고    scopus 로고
    • In vivo measurement of intramolecular distances using genetically encoded reporters
    • DOI 10.1529/biophysj.107.119073
    • Sandtner, W., F. Bezanilla, and A. M. Correa. 2007. In vivo measurement of intramolecular distances using genetically encoded reporters. Biophys. J. 93:L45-L47. (Pubitemid 350097088)
    • (2007) Biophysical Journal , vol.93 , Issue.9
    • Sandtner, W.1    Bezanilla, F.2    Correa, A.M.3
  • 8
    • 0036737063 scopus 로고    scopus 로고
    • A general strategy for sitespecific double labeling of globular proteins for kinetic FRET studies
    • Ratner, V., E. Kahana, ..., E. Haas. 2002. A general strategy for sitespecific double labeling of globular proteins for kinetic FRET studies. Bioconjug. Chem. 13:1163-1170.
    • (2002) Bioconjug. Chem. , vol.13 , pp. 1163-1170
    • Ratner, V.1    Kahana, E.2    Haas, E.3
  • 9
    • 33748109969 scopus 로고    scopus 로고
    • Short-range molecular rearrangements in ion channels detected by tryptophan quenching of bimane fluorescence
    • DOI 10.1085/jgp.200609556
    • Islas, L. D., and W. N. Zagotta. 2006. Short-range molecular rearrangements in ion channels detected by tryptophan quenching of bimane fluorescence. J. Gen. Physiol. 128:337-346. (Pubitemid 44306712)
    • (2006) Journal of General Physiology , vol.128 , Issue.3 , pp. 337-346
    • Islas, L.D.1    Zagotta, W.N.2
  • 10
    • 0033635163 scopus 로고    scopus 로고
    • Gating rearrangements in cyclic nucleotide-gated channels revealed by patch-clamp fluorometry
    • Zheng, J., and W. N. Zagotta. 2000. Gating rearrangements in cyclic nucleotide-gated channels revealed by patch-clamp fluorometry. Neuron. 28:369-374.
    • (2000) Neuron , vol.28 , pp. 369-374
    • Zheng, J.1    Zagotta, W.N.2
  • 11
    • 11144240635 scopus 로고    scopus 로고
    • Orthogonal site-specific protein modification by engineering reversible thiol protection mechanisms
    • DOI 10.1110/ps.04965405
    • Smith, J. J., D. W. Conrad, ..., H. W. Hellinga. 2005. Orthogonal sitespecific protein modification by engineering reversible thiol protection mechanisms. Protein Sci. 14:64-73. (Pubitemid 40054117)
    • (2005) Protein Science , vol.14 , Issue.1 , pp. 64-73
    • Smith, J.J.1    Conrad, D.W.2    Cuneo, M.J.3    Hellinga, H.W.4
  • 12
    • 68849128052 scopus 로고    scopus 로고
    • A method for sitespecific labeling of multiple protein thiols
    • Kuiper, J. M., R. Pluta, ..., B. Poolman. 2009. A method for sitespecific labeling of multiple protein thiols. Protein Sci. 18:1033-1041.
    • (2009) Protein Sci. , vol.18 , pp. 1033-1041
    • Kuiper, J.M.1    Pluta, R.2    Poolman, B.3
  • 13
    • 0141831003 scopus 로고    scopus 로고
    • Structural basis for modulation and agonist specificity of HCN pacemaker channels
    • DOI 10.1038/nature01922
    • Zagotta, W. N., N. B. Olivier, ..., E. Gouaux. 2003. Structural basis for modulation and agonist specificity of HCN pacemaker channels. Nature. 425:200-205. (Pubitemid 37150901)
    • (2003) Nature , vol.425 , Issue.6954 , pp. 200-205
    • Zagotta, W.N.1    Olivier, N.B.2    Black, K.D.3    Young, E.C.4    Olson, R.5    Gouaux, E.6
  • 14
    • 0024707204 scopus 로고
    • Unusually stable helix formation in short alanine-based peptides
    • Marqusee, S., V. H. Robbins, and R. L. Baldwin. 1989. Unusually stable helix formation in short alanine-based peptides. Proc. Natl. Acad. Sci. USA. 86:5286-5290.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5286-5290
    • Marqusee, S.1    Robbins, V.H.2    Baldwin, R.L.3
  • 15
    • 0014592230 scopus 로고
    • Computed circular dichroism spectra for the evaluation of protein conformation
    • Greenfield, N., and G. D. Fasman. 1969. Computed circular dichroism spectra for the evaluation of protein conformation. Biochemistry. 8:4108-4116.
    • (1969) Biochemistry , vol.8 , pp. 4108-4116
    • Greenfield, N.1    Fasman, G.D.2
  • 16
    • 0028951220 scopus 로고
    • Localization of regions affecting an allosteric transition in cyclic nucleotide-activated channels
    • Gordon, S. E., and W. N. Zagotta. 1995. Localization of regions affecting an allosteric transition in cyclic nucleotide-activated channels. Neuron. 14:857-864.
    • (1995) Neuron , vol.14 , pp. 857-864
    • Gordon, S.E.1    Zagotta, W.N.2
  • 18
    • 35648985153 scopus 로고    scopus 로고
    • Metal binding to ligands: Cadmium complexes with glutathione revisited
    • DOI 10.1016/j.ab.2007.07.015, PII S0003269707004599
    • Leverrier, P., C. Montigny, ..., P. Champeil. 2007. Metal binding to ligands: cadmium complexes with glutathione revisited. Anal. Biochem. 371:215-228. (Pubitemid 350019445)
    • (2007) Analytical Biochemistry , vol.371 , Issue.2 , pp. 215-228
    • Leverrier, P.1    Montigny, C.2    Garrigos, M.3    Champeil, P.4
  • 19
    • 42949165600 scopus 로고    scopus 로고
    • 2+ binding site in the voltage sensor of BK and shaker potassium channels
    • DOI 10.1085/jgp.200809980
    • 2+ binding site in the voltage sensor of BK and Shaker potassium channels. J. Gen. Physiol. 131:483-502. (Pubitemid 351620105)
    • (2008) Journal of General Physiology , vol.131 , Issue.5 , pp. 483-502
    • Ma, Z.1    Kin, Y.W.2    Horrigan, F.T.3
  • 20
    • 0025754301 scopus 로고
    • The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis
    • Spurlino, J. C., G. Y. Lu, and F. A. Quiocho. 1991. The 2.3-A resolution structure of the maltose-or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis. J. Biol. Chem. 266:5202-5219. (Pubitemid 21909478)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.8 , pp. 5202-5219
    • Spurlino, J.C.1    Lu, G.-Y.2    Quiocho, F.A.3


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