메뉴 건너뛰기




Volumn 17, Issue 4, 2006, Pages 967-974

Site-specific, covalent attachment of proteins to a solid surface

Author keywords

[No Author keywords available]

Indexed keywords

COPPER COMPOUNDS; CYCLOADDITION; MOLECULAR BIOLOGY;

EID: 33746760427     PISSN: 10431802     EISSN: None     Source Type: Journal    
DOI: 10.1021/bc060125e     Document Type: Article
Times cited : (122)

References (48)
  • 1
    • 15944408802 scopus 로고    scopus 로고
    • A proteomic microarray approach for exploring ligand-initiated nuclear hormone receptor pharmacology, receptor selectivity, and heterodimer functionality
    • Kim, S. H., Tamrazi, A., Carlson, K. E., and Katzenellenbogen, J. A. (2005) A proteomic microarray approach for exploring ligand-initiated nuclear hormone receptor pharmacology, receptor selectivity, and heterodimer functionality. Mol. Cell Prot. 4, 267-277.
    • (2005) Mol. Cell Prot. , vol.4 , pp. 267-277
    • Kim, S.H.1    Tamrazi, A.2    Carlson, K.E.3    Katzenellenbogen, J.A.4
  • 2
    • 5644229499 scopus 로고    scopus 로고
    • Screening yeast proteins for DNA binding identified a biosynthetic enzyme for the amino acid arginine that also unexpectedly binds to DNA and regulates genes directly
    • Hall, D. A., Zhu, H., Zhu, X., Royce, T., Gerstein, M., and Snyder, M. (2004) Screening yeast proteins for DNA binding identified a biosynthetic enzyme for the amino acid arginine that also unexpectedly binds to DNA and regulates genes directly. Science 306, 482-484.
    • (2004) Science , vol.306 , pp. 482-484
    • Hall, D.A.1    Zhu, H.2    Zhu, X.3    Royce, T.4    Gerstein, M.5    Snyder, M.6
  • 3
    • 9344247454 scopus 로고    scopus 로고
    • Finding new components of the target of rapamycin (TOR) signaling network through chemical genetics and proteome chips
    • Huang, J., Zhu, H., Haggarty, S. J., Spring, D. R., Hwang, H., Jin, F., Snyder, M., and Schreiber, S. L. (2004) Finding new components of the target of rapamycin (TOR) signaling network through chemical genetics and proteome chips. Proc. Natl. Acad. Sci. U.S.A. 101, 16594-16599.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 16594-16599
    • Huang, J.1    Zhu, H.2    Haggarty, S.J.3    Spring, D.R.4    Hwang, H.5    Jin, F.6    Snyder, M.7    Schreiber, S.L.8
  • 5
    • 0034622925 scopus 로고    scopus 로고
    • Printing proteins as microarrays for high-throughput function determination
    • MacBeath, G. and Schreiber, S. L. (2000) Printing proteins as microarrays for high-throughput function determination. Science 289, 1760-1763.
    • (2000) Science , vol.289 , pp. 1760-1763
    • MacBeath, G.1    Schreiber, S.L.2
  • 7
    • 0024999014 scopus 로고
    • Purification and site-specific immobilization of genetically engineered glucose de-hydrogenase on thiopropyl-sepharose
    • Persson, M., Bulow, L., and Mosbach, K. (1990) Purification and site-specific immobilization of genetically engineered glucose de-hydrogenase on thiopropyl-sepharose. FEBS Lett. 270, 41-44.
    • (1990) FEBS Lett. , vol.270 , pp. 41-44
    • Persson, M.1    Bulow, L.2    Mosbach, K.3
  • 8
    • 3042852630 scopus 로고    scopus 로고
    • Immobilization of oriented protein molecules on poly(ethylene glycol)-coated Si(IIl)
    • Cha, T., Guo, A., Jun, Y., Pei, D., and Zhu, X.-Y. (2004) Immobilization of oriented protein molecules on poly(ethylene glycol)-coated Si(IIl). Proteomics 4, 1965-1976.
    • (2004) Proteomics , vol.4 , pp. 1965-1976
    • Cha, T.1    Guo, A.2    Jun, Y.3    Pei, D.4    Zhu, X.-Y.5
  • 10
    • 0037117516 scopus 로고    scopus 로고
    • Supramolecular chemistry and self-assembly special feature: Selective immobilization of proteins to self-assembled monolayers presenting active site-directed capture ligands
    • Hodneland, C. D., Lee, S.-L., Min, D.-H., and Mrksich, M. (2002) Supramolecular chemistry and self-assembly special feature: selective immobilization of proteins to self-assembled monolayers presenting active site-directed capture ligands. Proc. Natl. Acad. Sci. U.S.A. 99, 5048-5052.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 5048-5052
    • Hodneland, C.D.1    Lee, S.-L.2    Min, D.-H.3    Mrksich, M.4
  • 11
  • 13
    • 8844258757 scopus 로고    scopus 로고
    • Chemoselective attachment of biologically active proteins to surfaces by expressed protein ligation and its application for "protein chip" fabrication
    • Camarero, J. A., Kwon, Y., and Coleman, M. A. (2004) Chemoselective attachment of biologically active proteins to surfaces by expressed protein ligation and its application for "protein chip" fabrication. J. Am. Chem. Soc. 126, 14730-14731.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 14730-14731
    • Camarero, J.A.1    Kwon, Y.2    Coleman, M.A.3
  • 14
  • 15
    • 0942287129 scopus 로고    scopus 로고
    • Versatile protein biotinylation strategies for potential high-throughput proteomics
    • Lue, R. Y. P., Chen, G. Y. J., Hu, Y., Zhu, Q., Yao, S. Q. (2004) Versatile protein biotinylation strategies for potential high-throughput proteomics. J. Am. Chem. Soc. 126, 1055-1062.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 1055-1062
    • Lue, R.Y.P.1    Chen, G.Y.J.2    Hu, Y.3    Zhu, Q.4    Yao, S.Q.5
  • 16
    • 3042546498 scopus 로고    scopus 로고
    • Labeling proteins with small molecules by site-specific posttranslational modification
    • Yin, J., Liu, F., Li, X., and Walsh, C. T. (2004) Labeling proteins with small molecules by site-specific posttranslational modification. J. Am. Chem. Soc. 126, 7754-7755.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 7754-7755
    • Yin, J.1    Liu, F.2    Li, X.3    Walsh, C.T.4
  • 17
    • 33746311225 scopus 로고    scopus 로고
    • Selective immobilization of proteins onto solid supports through split-inteinmediated protein trans-splicing
    • Kwon, Y., Coleman, M. A., and Camarero, J. A. (2006) Selective immobilization of proteins onto solid supports through split-inteinmediated protein trans-splicing. Angew. Chem., Int. Ed. 45, 1726-1729.
    • (2006) Angew. Chem., Int. Ed. , vol.45 , pp. 1726-1729
    • Kwon, Y.1    Coleman, M.A.2    Camarero, J.A.3
  • 19
    • 0034677879 scopus 로고    scopus 로고
    • Cell surface engineering by a modified Staudinger reaction
    • Saxon, E. and Bertozzi, C. R. (2000) Cell surface engineering by a modified Staudinger reaction. Science 287, 2007-2010.
    • (2000) Science , vol.287 , pp. 2007-2010
    • Saxon, E.1    Bertozzi, C.R.2
  • 20
    • 19644391139 scopus 로고    scopus 로고
    • Targeting quantum dots to surface proteins in living cells with biotin ligase
    • Howarth, M., Takao, K., Hayashi, Y., and Ting, A. Y. (2005) Targeting quantum dots to surface proteins in living cells with biotin ligase. Proc. Natl. Acad. Sci. U.S.A. 102, 7583-7588.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 7583-7588
    • Howarth, M.1    Takao, K.2    Hayashi, Y.3    Ting, A.Y.4
  • 22
    • 0000096835 scopus 로고    scopus 로고
    • Click chemistry: Diverse chemical function from a few good reactions
    • Kolb, H. C., Finn, M. G., and Sharpless, K. B. (2001) Click chemistry: diverse chemical function from a few good reactions. Angew. Chem., Int. Ed. 40, 2004-2021.
    • (2001) Angew. Chem., Int. Ed. , vol.40 , pp. 2004-2021
    • Kolb, H.C.1    Finn, M.G.2    Sharpless, K.B.3
  • 24
    • 0037462106 scopus 로고    scopus 로고
    • Activity-based protein profiling in vivo using a copper(I)-catalyzed azide-alkyne [3 + 2] cycloaddition
    • Speers, A. E., Adam, G. C., and Cravatt, B. F. (2003) Activity-based protein profiling in vivo using a copper(I)-catalyzed azide-alkyne [3 + 2] cycloaddition. J. Am. Chem. Soc. 125, 4686-4687.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 4686-4687
    • Speers, A.E.1    Adam, G.C.2    Cravatt, B.F.3
  • 25
    • 0037039298 scopus 로고    scopus 로고
    • Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation
    • Kiick, K. L., Saxon, E., Tirrell, D. A., and Bertozzi, C. R. (2002) Incorporation of azides into recombinant proteins for chemoselective modification by the Staudinger ligation. Proc. Natl. Acad. Sci. U.S.A. 99, 19-24.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 19-24
    • Kiick, K.L.1    Saxon, E.2    Tirrell, D.A.3    Bertozzi, C.R.4
  • 26
    • 0141843623 scopus 로고    scopus 로고
    • Site-specific protein immobilization by Staudinger ligation
    • Soellner, M. B., Dickson, K. A., Nilsson, B. L., and Raines, R. T. (2003) Site-specific protein immobilization by Staudinger ligation. J. Am. Chem. Soc. 125, 11790-11791.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 11790-11791
    • Soellner, M.B.1    Dickson, K.A.2    Nilsson, B.L.3    Raines, R.T.4
  • 27
    • 20144371207 scopus 로고    scopus 로고
    • Evaluation of geranylazide and farnesylazide diphosphate for incorporation of prenylazides into a C/AAX box-containing peptide using protein farnesyltransferase
    • Rose, M. W., Rose, N. D., Boggs, J., Lenevich, S., Xu, J., Barany, G., and Distefano, M. D. (2005) Evaluation of geranylazide and farnesylazide diphosphate for incorporation of prenylazides into a C/AAX box-containing peptide using protein farnesyltransferase. J. Pept. Res. 65, 529-537.
    • (2005) J. Pept. Res. , vol.65 , pp. 529-537
    • Rose, M.W.1    Rose, N.D.2    Boggs, J.3    Lenevich, S.4    Xu, J.5    Barany, G.6    Distefano, M.D.7
  • 28
    • 0033607724 scopus 로고    scopus 로고
    • Enantioselective synthesis of (-)-Bifurcadiol: A natural antitumor marine product
    • Di Guardia, S., Valls, R., Mesguiche, V., Brunei, J.-M., and Culioli, G. (1999) Enantioselective synthesis of (-)-Bifurcadiol: a natural antitumor marine product. Tetrahedron Lett. 40, 8359-8360.
    • (1999) Tetrahedron Lett. , vol.40 , pp. 8359-8360
    • Di Guardia, S.1    Valls, R.2    Mesguiche, V.3    Brunei, J.-M.4    Culioli, G.5
  • 29
    • 84989479993 scopus 로고
    • Selenium dioxide oxidation of substrates with acid labile groups
    • Camps, F., Coll, J., and Parente, A. (1978) Selenium dioxide oxidation of substrates with acid labile groups. Synthesis 3, 215-216.
    • (1978) Synthesis , vol.3 , pp. 215-216
    • Camps, F.1    Coll, J.2    Parente, A.3
  • 30
    • 2042524507 scopus 로고
    • Useful procedures for the oxidation of alcohols involving pyridinium dichromate in approtic media
    • Corey, E. J. and Schmidt, G. (1979) Useful procedures for the oxidation of alcohols involving pyridinium dichromate in approtic media. Tetrahedron Lett. 20, 399-402.
    • (1979) Tetrahedron Lett. , vol.20 , pp. 399-402
    • Corey, E.J.1    Schmidt, G.2
  • 31
    • 37049068726 scopus 로고
    • Rhodium carbenoid mediated cyclisations. Part 4. Synthetic approaches to oxepanes related to zoapatanol
    • Davies, M. J., Heslin, J. C., and Moody, C. J. (1989) Rhodium carbenoid mediated cyclisations. Part 4. Synthetic approaches to oxepanes related to zoapatanol. J. Chem. Soc., Perkin Trans, 1 12, 2473-2484.
    • (1989) J. Chem. Soc., Perkin Trans. 1 , vol.12 , pp. 2473-2484
    • Davies, M.J.1    Heslin, J.C.2    Moody, C.J.3
  • 32
    • 0034102478 scopus 로고    scopus 로고
    • Synthesis of allylic isoprenoid diphosphates by SN2 displacement of diethyl phosphate
    • Ravn, M. M., Jin, Q., and Coates, R. M. (2000) Synthesis of allylic isoprenoid diphosphates by SN2 displacement of diethyl phosphate. Eur. J. Org. Chem. 2000, 1401-1410.
    • (2000) Eur. J. Org. Chem. , vol.2000 , pp. 1401-1410
    • Ravn, M.M.1    Jin, Q.2    Coates, R.M.3
  • 34
    • 22144485495 scopus 로고    scopus 로고
    • Evolutions in science triggered by green fluorescent protein (GFP)
    • Schmid, J. A. and Neumeier, H. (2005) Evolutions in science triggered by green fluorescent protein (GFP). ChemBioChem. 6, 1149-1156.
    • (2005) ChemBioChem. , vol.6 , pp. 1149-1156
    • Schmid, J.A.1    Neumeier, H.2
  • 35
    • 4644370323 scopus 로고    scopus 로고
    • Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity
    • Reid, T. S., Terry, K. L., Casey, P. J., and Beese, L. S. (2004) Crystallographic analysis of CaaX prenyltransferases complexed with substrates defines rules of protein substrate selectivity. J. Mol. Biol. 343, 417-433.
    • (2004) J. Mol. Biol. , vol.343 , pp. 417-433
    • Reid, T.S.1    Terry, K.L.2    Casey, P.J.3    Beese, L.S.4
  • 36
    • 0031577175 scopus 로고    scopus 로고
    • Photoaffinity labeling of yeast farnesyl protein transferase and enzymatic synthesis of a Ras protein incorporating a photoactive isoprenoid
    • Edelstem, R. L. and Distefano, M. D. (1997) Photoaffinity labeling of yeast farnesyl protein transferase and enzymatic synthesis of a Ras protein incorporating a photoactive isoprenoid. Biochem. Biophys. Res. Commun. 235, 377-382.
    • (1997) Biochem. Biophys. Res. Commun. , vol.235 , pp. 377-382
    • Edelstem, R.L.1    Distefano, M.D.2
  • 37
    • 0035906468 scopus 로고    scopus 로고
    • Synthesis of farnesyl diphosphate analogues containing ether-linked photoactive benzophenones and their application in studies of protein prenyltransferases
    • Turek, T. C., Gaon, I., Distefano, M. D., and Strickland, C. L. (2001) Synthesis of farnesyl diphosphate analogues containing ether-linked photoactive benzophenones and their application in studies of protein prenyltransferases. J. Org. Chem. 66, 3253-3264.
    • (2001) J. Org. Chem. , vol.66 , pp. 3253-3264
    • Turek, T.C.1    Gaon, I.2    Distefano, M.D.3    Strickland, C.L.4
  • 38
    • 0034685976 scopus 로고    scopus 로고
    • Design and synthesis of a transferable farnesyl pyrophosphate analogue to Ras by protein farnesyltransferase
    • Chehade, K. A. H., Andres, D. A., Morimoto, H., and Spielmann, H. P. (2000) Design and synthesis of a transferable farnesyl pyrophosphate analogue to Ras by protein farnesyltransferase. J. Org. Chem. 65, 3027-3033.
    • (2000) J. Org. Chem. , vol.65 , pp. 3027-3033
    • Chehade, K.A.H.1    Andres, D.A.2    Morimoto, H.3    Spielmann, H.P.4
  • 39
    • 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
  • 40
    • 4444324951 scopus 로고    scopus 로고
    • Polytriazoles as copper(I)-stabilizing ligands in catalysis
    • Chan, T. R., Hilgraf, R., Sharpless, K. B., and Fokin, V. V. (2004) Polytriazoles as copper(I)-stabilizing ligands in catalysis. Org. Lett. 6, 2853-2855.
    • (2004) Org. Lett. , vol.6 , pp. 2853-2855
    • Chan, T.R.1    Hilgraf, R.2    Sharpless, K.B.3    Fokin, V.V.4
  • 41
    • 1942522084 scopus 로고    scopus 로고
    • Profiling enzyme activities in vivo using click chemistry methods
    • Speers, A. E. and Cravatt, B. F. (2004) Profiling enzyme activities in vivo using click chemistry methods. Chem. Biol. 11, 535-546.
    • (2004) Chem. Biol. , vol.11 , pp. 535-546
    • Speers, A.E.1    Cravatt, B.F.2
  • 42
    • 0031105876 scopus 로고    scopus 로고
    • Expression of aggregation-prone recombinant proteins at low temperatures: A comparative study of the Escherichia coli cspA and tac promoter systems
    • Vasina, J. A. and Baneyx, F. (1997) Expression of aggregation-prone recombinant proteins at low temperatures: a comparative study of the Escherichia coli cspA and tac promoter systems. Prot. Expr. Purif. 9, 211-218.
    • (1997) Prot. Expr. Purif. , vol.9 , pp. 211-218
    • Vasina, J.A.1    Baneyx, F.2
  • 43
    • 0036362061 scopus 로고    scopus 로고
    • Differential effects of supplementary affinity tags on the solubility of MBP fusion proteins
    • Routzahn, K. M. and Waugh, D. S. (2002) Differential effects of supplementary affinity tags on the solubility of MBP fusion proteins. J. Struct. Funct. Gen. 2, 83-92.
    • (2002) J. Struct. Funct. Gen. , vol.2 , pp. 83-92
    • Routzahn, K.M.1    Waugh, D.S.2
  • 45
    • 0035083996 scopus 로고    scopus 로고
    • Total chemical synthesis of human matrix Gla protein
    • Hackeng, T. M., Rosing, J., Spronk, H. M., and Vermeer, C. (2001) Total chemical synthesis of human matrix Gla protein. Protein Sci. 10, 864-870.
    • (2001) Protein Sci. , vol.10 , pp. 864-870
    • Hackeng, T.M.1    Rosing, J.2    Spronk, H.M.3    Vermeer, C.4
  • 46
    • 0037039338 scopus 로고    scopus 로고
    • Soluble Fusion Proteins between single transmembrane photoreceptor guanylyl cyclases and their activators
    • Sokal, I., Alekseev, A., Baehr, W., Haeseleer, F., and Palczewski, K. (2002) Soluble Fusion Proteins between single transmembrane photoreceptor guanylyl cyclases and their activators. Biochemistry 41, 251-257.
    • (2002) Biochemistry , vol.41 , pp. 251-257
    • Sokal, I.1    Alekseev, A.2    Baehr, W.3    Haeseleer, F.4    Palczewski, K.5
  • 47
    • 0028932673 scopus 로고
    • Limitations to in vivo import of Hydrophobic proteins into yeast mitochondria. The case of a cytoplasmically synthesized apocytochrome b
    • Claros, M. G., Perea, J., Shu, Y., Samatey, F. A., Popot, J.-L., and Jacq, C. (1995) Limitations to in vivo import of Hydrophobic proteins into yeast mitochondria. The case of a cytoplasmically synthesized apocytochrome b. Eur. J. Biochem. 228, 162-111.
    • (1995) Eur. J. Biochem. , vol.228 , pp. 162-1111
    • Claros, M.G.1    Perea, J.2    Shu, Y.3    Samatey, F.A.4    Popot, J.-L.5    Jacq, C.6
  • 48
    • 0033946897 scopus 로고    scopus 로고
    • Limitations on the use of fused green fluorescent protein to investigate structure-function relationships for the cauliflower mosaic virus movement protein
    • Thomas, C. L. and Maule, A. J. (2000) Limitations on the use of fused green fluorescent protein to investigate structure-function relationships for the cauliflower mosaic virus movement protein. J. Gen. Virol. 81, 1851-1855.
    • (2000) J. Gen. Virol. , vol.81 , pp. 1851-1855
    • Thomas, C.L.1    Maule, A.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.