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Volumn 18, Issue 4, 2007, Pages 1259-1265

Identification of an orthogonal peptide binding motif for biarsenical multiuse affinity probes

Author keywords

[No Author keywords available]

Indexed keywords

BINDING ENERGY; ESCHERICHIA COLI; PROBES; RNA;

EID: 34547218393     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc0603900     Document Type: Article
Times cited : (30)

References (28)
  • 1
    • 12344296442 scopus 로고    scopus 로고
    • Dynamic motion of helix A in the amino-terminal domain of calmodulin is stabilized upon calcium activation
    • Chen, B., Mayer, M. U., Markillie, L. M., Stenoien, D. L., and Squier, T. C. (2005) Dynamic motion of helix A in the amino-terminal domain of calmodulin is stabilized upon calcium activation. Biochemistry 44, 905-914.
    • (2005) Biochemistry , vol.44 , pp. 905-914
    • Chen, B.1    Mayer, M.U.2    Markillie, L.M.3    Stenoien, D.L.4    Squier, T.C.5
  • 2
    • 15444381327 scopus 로고    scopus 로고
    • Structural uncoupling between opposing domains of oxidized calmodulin underlies the enhanced binding affinity and inhibition of the plasma membrane Ca-ATPase
    • Chen, B., Mayer, M. U., and Squier, T. C. (2005) Structural uncoupling between opposing domains of oxidized calmodulin underlies the enhanced binding affinity and inhibition of the plasma membrane Ca-ATPase. Biochemistry 44, 4737-4747.
    • (2005) Biochemistry , vol.44 , pp. 4737-4747
    • Chen, B.1    Mayer, M.U.2    Squier, T.C.3
  • 3
    • 0034581376 scopus 로고    scopus 로고
    • Fluorescent labeling of recombinant proteins in living cells with FlAsH
    • Griffin, B. A., Adams, S. R., Jones, J., and Tsien, R. Y. (2000) Fluorescent labeling of recombinant proteins in living cells with FlAsH. Methods Enzymol. 327, 565-578.
    • (2000) Methods Enzymol , vol.327 , pp. 565-578
    • Griffin, B.A.1    Adams, S.R.2    Jones, J.3    Tsien, R.Y.4
  • 4
    • 0032503999 scopus 로고    scopus 로고
    • Specific covalent labeling of recombinant protein molecules inside live cells
    • Griffin, B. A., Adams, S. R., and Tsien, R. Y. (1998) Specific covalent labeling of recombinant protein molecules inside live cells. Science 281, 269-272.
    • (1998) Science , vol.281 , pp. 269-272
    • Griffin, B.A.1    Adams, S.R.2    Tsien, R.Y.3
  • 5
    • 33644811688 scopus 로고    scopus 로고
    • One-step, non-denaturing isolation of an RNA polymerase enzyme complex using an improved multi-use affinity probe resin
    • Mayer, M. U., Shi, L., and Squier, T. C. (2005) One-step, non-denaturing isolation of an RNA polymerase enzyme complex using an improved multi-use affinity probe resin. Mol. Biosys. 1, 53-56.
    • (2005) Mol. Biosys , vol.1 , pp. 53-56
    • Mayer, M.U.1    Shi, L.2    Squier, T.C.3
  • 6
    • 0033996150 scopus 로고    scopus 로고
    • A novel method of affinity-purifying proteins using a bisarsenical fluorescein
    • Thorn, K. S., Naber, N., Matuska, M., Vale, R. D., and Cooke, R. (2000) A novel method of affinity-purifying proteins using a bisarsenical fluorescein. Protein Sci. 9, 213-217.
    • (2000) Protein Sci , vol.9 , pp. 213-217
    • Thorn, K.S.1    Naber, N.2    Matuska, M.3    Vale, R.D.4    Cooke, R.5
  • 9
    • 33646872862 scopus 로고    scopus 로고
    • Accumulation of FlAsH/Lumio Green in active mitochondria can be reversed by beta-mercaptoethanol for specific staining of tetracysteine-tagged proteins
    • Langhorst, M. F., Genisyuerek, S., and Stuermer, C. A. (2006) Accumulation of FlAsH/Lumio Green in active mitochondria can be reversed by beta-mercaptoethanol for specific staining of tetracysteine-tagged proteins. Histochem. Cell Biol. 125, 743-747.
    • (2006) Histochem. Cell Biol , vol.125 , pp. 743-747
    • Langhorst, M.F.1    Genisyuerek, S.2    Stuermer, C.A.3
  • 11
    • 0037140742 scopus 로고    scopus 로고
    • New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: Synthesis and biological applications
    • Adams, S. R., Campbell, R. E., Gross, L. A., Martin, B. R., Walkup, G. K., Yao, Y., Llopis, J., and Tsien, R. Y. (2002) New biarsenical ligands and tetracysteine motifs for protein labeling in vitro and in vivo: synthesis and biological applications. J. Am. Chem. Soc. 124, 6063-6076.
    • (2002) J. Am. Chem. Soc , vol.124 , pp. 6063-6076
    • Adams, S.R.1    Campbell, R.E.2    Gross, L.A.3    Martin, B.R.4    Walkup, G.K.5    Yao, Y.6    Llopis, J.7    Tsien, R.Y.8
  • 12
    • 27144448780 scopus 로고    scopus 로고
    • Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity
    • Martin, B. R., Giepmans, B. N., Adams, S. R., and Tsien, R. Y. (2005) Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity. Nat. Biotechnol. 23, 1308-1314.
    • (2005) Nat. Biotechnol , vol.23 , pp. 1308-1314
    • Martin, B.R.1    Giepmans, B.N.2    Adams, S.R.3    Tsien, R.Y.4
  • 14
    • 0034802605 scopus 로고    scopus 로고
    • The protein-labeling reagent FLASH-EDT2 binds not only to CCXXCC motifs but also non-specifically to endogenous cysteine- rich proteins
    • Stroffekova, K., Proenza, C., and Beam, K. G. (2001) The protein-labeling reagent FLASH-EDT2 binds not only to CCXXCC motifs but also non-specifically to endogenous cysteine- rich proteins. Pflugers Archiv. 442, 859-866.
    • (2001) Pflugers Archiv , vol.442 , pp. 859-866
    • Stroffekova, K.1    Proenza, C.2    Beam, K.G.3
  • 15
    • 0024448151 scopus 로고
    • Calculation of protein extinction coefficients from amino-acid sequence data
    • Gill, S. C., and von Hippel, P. H. (1989) Calculation of protein extinction coefficients from amino-acid sequence data. Anal. Biochem. 182, 319-326.
    • (1989) Anal. Biochem , vol.182 , pp. 319-326
    • Gill, S.C.1    von Hippel, P.H.2
  • 16
    • 33947400202 scopus 로고    scopus 로고
    • Remodeling of bacterial RNA polymerase supramolecular complex in response to environmental conditions
    • Verma, S., Xiong, Y., Mayer, M. U., and Squier, T. C. (2007) Remodeling of bacterial RNA polymerase supramolecular complex in response to environmental conditions. Biochemistry 46, 3023-3035.
    • (2007) Biochemistry , vol.46 , pp. 3023-3035
    • Verma, S.1    Xiong, Y.2    Mayer, M.U.3    Squier, T.C.4
  • 17
    • 30144446085 scopus 로고    scopus 로고
    • SlyD proteins from different species exhibit high prolyl isomerase and chaperone activities
    • Scholz, C., Eckert, B., Hagn, F., Schaarschmidt, P., Balbach, J., and Schmid, F. X. (2006) SlyD proteins from different species exhibit high prolyl isomerase and chaperone activities. Biochemistry 45, 20-33.
    • (2006) Biochemistry , vol.45 , pp. 20-33
    • Scholz, C.1    Eckert, B.2    Hagn, F.3    Schaarschmidt, P.4    Balbach, J.5    Schmid, F.X.6
  • 18
    • 0031663369 scopus 로고    scopus 로고
    • The green fluorescent protein
    • Tsien, R. Y. (1998) The green fluorescent protein. Annu. Rev. Biochem. 67, 509-544.
    • (1998) Annu. Rev. Biochem , vol.67 , pp. 509-544
    • Tsien, R.Y.1
  • 19
    • 33644623648 scopus 로고    scopus 로고
    • Molecular biology and mutation of green fluorescent protein
    • Zacharias, D. A., and Tsien, R. Y. (2006) Molecular biology and mutation of green fluorescent protein. Methods Biochem. Anal. 47, 83-120.
    • (2006) Methods Biochem. Anal , vol.47 , pp. 83-120
    • Zacharias, D.A.1    Tsien, R.Y.2
  • 20
    • 33645798851 scopus 로고    scopus 로고
    • The fluorescent toolbox for assessing protein location and function
    • Giepmans, B. N., Adams, S. R., Ellisman, M. H., and Tsien, R. Y. (2006) The fluorescent toolbox for assessing protein location and function. Science 312, 217-224.
    • (2006) Science , vol.312 , pp. 217-224
    • Giepmans, B.N.1    Adams, S.R.2    Ellisman, M.H.3    Tsien, R.Y.4
  • 21
    • 9444247617 scopus 로고    scopus 로고
    • Short tetracysteine tags to beta-tubulin demonstrate the significance of small labels for live cell imaging
    • Andresen, M., Schmitz-Salue, R., and Jakobs, S. (2004) Short tetracysteine tags to beta-tubulin demonstrate the significance of small labels for live cell imaging. Mol. Biol. Cell 15, 5616-5622.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5616-5622
    • Andresen, M.1    Schmitz-Salue, R.2    Jakobs, S.3
  • 24
    • 33745213371 scopus 로고    scopus 로고
    • CrAsH: A biarsenical multi-use affinity probe with low non-specific fluorescence
    • Cao, H., Chen, B., Squier, T. C., and Mayer, M. U. (2006) CrAsH: a biarsenical multi-use affinity probe with low non-specific fluorescence. Chem. Commun. (Cambridge, U.K.) 2601-2603.
    • (2006) Chem. Commun. (Cambridge, U.K.) , pp. 2601-2603
    • Cao, H.1    Chen, B.2    Squier, T.C.3    Mayer, M.U.4
  • 25
    • 33748805519 scopus 로고    scopus 로고
    • Improved photostable FRET-competent biarsenical-tetracysteine probes based on fluorinated fluoresceins
    • Spagnuolo, C. C., Vermeij, R. J., and Jares-Erijman, E. A. (2006) Improved photostable FRET-competent biarsenical-tetracysteine probes based on fluorinated fluoresceins. J. Am. Chem. Soc. 128, 12040-12041.
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 12040-12041
    • Spagnuolo, C.C.1    Vermeij, R.J.2    Jares-Erijman, E.A.3
  • 26
    • 33645921635 scopus 로고    scopus 로고
    • Fluorophore-assisted light inactivation of calmodulin involves singlet-oxygen mediated cross-linking and methionine oxidation
    • Yan, P., Xiong, Y., Chen, B., Negash, S., Squier, T. C., and Mayer, M. U. (2006) Fluorophore-assisted light inactivation of calmodulin involves singlet-oxygen mediated cross-linking and methionine oxidation. Biochemistry 45, 4736-4748.
    • (2006) Biochemistry , vol.45 , pp. 4736-4748
    • Yan, P.1    Xiong, Y.2    Chen, B.3    Negash, S.4    Squier, T.C.5    Mayer, M.U.6


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