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Volumn 24, Issue 6, 2013, Pages 1094-1101

Clickable tyrosine binding bifunctional linkers for preparation of DNA-protein conjugates

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; PROTEINS;

EID: 84879335361     PISSN: 10431802     EISSN: 15204812     Source Type: Journal    
DOI: 10.1021/bc4001799     Document Type: Article
Times cited : (43)

References (36)
  • 1
    • 33645028600 scopus 로고    scopus 로고
    • Folding DNA to create nanoscale shapes and patterns
    • Rothemund, P. W. (2006) Folding DNA to create nanoscale shapes and patterns Nature 440, 297-302
    • (2006) Nature , vol.440 , pp. 297-302
    • Rothemund, P.W.1
  • 2
    • 85015106657 scopus 로고    scopus 로고
    • DNA in a material world
    • Seeman, N. C. (2003) DNA in a material world Nature 421, 427-31
    • (2003) Nature , vol.421 , pp. 427-431
    • Seeman, N.C.1
  • 3
    • 0037732852 scopus 로고    scopus 로고
    • Biochemistry and structural DNA nanotechnology: An evolving symbiotic relationship
    • Seeman, N. C. (2003) Biochemistry and structural DNA nanotechnology: an evolving symbiotic relationship Biochemistry 42, 7259-69
    • (2003) Biochemistry , vol.42 , pp. 7259-7269
    • Seeman, N.C.1
  • 4
    • 0035476388 scopus 로고    scopus 로고
    • DNA-directed functionalization of colloidal gold with proteins
    • Niemeyer, C. M. and Ceyhan, B. (2001) DNA-directed functionalization of colloidal gold with proteins Angew. Chem., Int. Ed. 40, 3685-3688
    • (2001) Angew. Chem., Int. Ed. , vol.40 , pp. 3685-3688
    • Niemeyer, C.M.1    Ceyhan, B.2
  • 5
    • 0043095428 scopus 로고    scopus 로고
    • A real-time immuno-PCR assay for routine ultrasensitive quantification of proteins
    • Adler, M., Wacker, R., and Niemeyer, C. M. (2003) A real-time immuno-PCR assay for routine ultrasensitive quantification of proteins Biochem. Biophys. Res. Commun. 308, 240-50
    • (2003) Biochem. Biophys. Res. Commun. , vol.308 , pp. 240-250
    • Adler, M.1    Wacker, R.2    Niemeyer, C.M.3
  • 6
    • 33644781739 scopus 로고    scopus 로고
    • DNA-directed protein immobilization for simultaneous detection of multiple analytes by surface plasmon resonance biosensor
    • Boozer, C., Ladd, J., Chen, S., and Jiang, S. (2006) DNA-directed protein immobilization for simultaneous detection of multiple analytes by surface plasmon resonance biosensor Anal. Chem. 78, 1515-9
    • (2006) Anal. Chem. , vol.78 , pp. 1515-1519
    • Boozer, C.1    Ladd, J.2    Chen, S.3    Jiang, S.4
  • 7
    • 67650361634 scopus 로고    scopus 로고
    • Toward multiprotein nanoarrays using nanografting and DNA directed immobilization of proteins
    • Bano, F., Fruk, L., Sanavio, B., Glettenberg, M., Casalis, L., Niemeyer, C. M., and Scoles, G. (2009) Toward multiprotein nanoarrays using nanografting and DNA directed immobilization of proteins Nano Lett. 9, 2614-8
    • (2009) Nano Lett. , vol.9 , pp. 2614-2618
    • Bano, F.1    Fruk, L.2    Sanavio, B.3    Glettenberg, M.4    Casalis, L.5    Niemeyer, C.M.6    Scoles, G.7
  • 8
    • 27744445693 scopus 로고    scopus 로고
    • Sensitive detection of proteins using difunctional DNA-gold nanoparticles
    • Hazarika, P., Ceyhan, B., and Niemeyer, C. M. (2005) Sensitive detection of proteins using difunctional DNA-gold nanoparticles Small 1, 844-8
    • (2005) Small , vol.1 , pp. 844-848
    • Hazarika, P.1    Ceyhan, B.2    Niemeyer, C.M.3
  • 9
    • 77955826786 scopus 로고    scopus 로고
    • Discrete and active nzyme nanoarrays on DNA origami scaffolds purified by affinity tag separation
    • Numajiri, K., Yamazaki, T., Kimura, M., Kuzuya, and A. Komiyama, M. (2010) Discrete and active nzyme nanoarrays on DNA origami scaffolds purified by affinity tag separation J. Am. Chem. Soc. 132, 9937-9
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 9937-9939
    • Numajiri, K.1    Yamazaki, T.2    Kimura, M.3    Kuzuya4    Komiyama, M.A.5
  • 10
    • 0032881724 scopus 로고    scopus 로고
    • Changing functionality of surfaces by directed self-assembly using oligonucleotides-The Oligo-Tag
    • 758, 760
    • Bier, F. F., Kleinjung, F., Ehrentreich-Forster, E., and Scheller, F. W. (1999) Changing functionality of surfaces by directed self-assembly using oligonucleotides-the Oligo-Tag Biotechniques 27, 752-756, 758, 760
    • (1999) Biotechniques , vol.27 , pp. 752-756
    • Bier, F.F.1    Kleinjung, F.2    Ehrentreich-Forster, E.3    Scheller, F.W.4
  • 11
    • 0028566558 scopus 로고
    • Oligonucleotide-directed self-assembly of proteins: Semisynthetic DNA - Streptavidin hybrid molecules as connectors for the generation of macroscopic arrays and the construction of supramolecular bioconjugates
    • Niemeyer, C. M., Sano, T., Smith, C. L., and Cantor, C. R. (1994) Oligonucleotide-directed self-assembly of proteins: semisynthetic DNA - streptavidin hybrid molecules as connectors for the generation of macroscopic arrays and the construction of supramolecular bioconjugates Nucleic Acids Res. 22, 5530-9
    • (1994) Nucleic Acids Res. , vol.22 , pp. 5530-5539
    • Niemeyer, C.M.1    Sano, T.2    Smith, C.L.3    Cantor, C.R.4
  • 13
    • 81255177825 scopus 로고    scopus 로고
    • Orthogonal protein decoration of DNA nanostructures
    • Meyer, R. and Niemeyer, C. M. (2011) Orthogonal protein decoration of DNA nanostructures Small 7, 3211-8
    • (2011) Small , vol.7 , pp. 3211-3218
    • Meyer, R.1    Niemeyer, C.M.2
  • 14
    • 76349083858 scopus 로고    scopus 로고
    • Semisynthetic DNA-protein conjugates for biosensing and nanofabrication
    • Niemeyer, C. M. (2010) Semisynthetic DNA-protein conjugates for biosensing and nanofabrication Angew. Chem., Int. Ed. 49, 1200-16
    • (2010) Angew. Chem., Int. Ed. , vol.49 , pp. 1200-1216
    • Niemeyer, C.M.1
  • 17
    • 60749134505 scopus 로고    scopus 로고
    • Apoenzyme reconstitution as a chemical tool for structural enzymology and biotechnology
    • Fruk, L., Kuo, C. H., Torres, E., and Niemeyer, C. M. (2009) Apoenzyme reconstitution as a chemical tool for structural enzymology and biotechnology Angew. Chem., Int. Ed. 48, 1550-74
    • (2009) Angew. Chem., Int. Ed. , vol.48 , pp. 1550-1574
    • Fruk, L.1    Kuo, C.H.2    Torres, E.3    Niemeyer, C.M.4
  • 18
    • 18144406582 scopus 로고    scopus 로고
    • Covalent hemin-DNA adducts for generating a novel class of artificial heme enzymes
    • Fruk, L. and Niemeyer, C. M. (2005) Covalent hemin-DNA adducts for generating a novel class of artificial heme enzymes Angew. Chem., Int. Ed. 44, 2603-6
    • (2005) Angew. Chem., Int. Ed. , vol.44 , pp. 2603-2606
    • Fruk, L.1    Niemeyer, C.M.2
  • 19
    • 18844403661 scopus 로고    scopus 로고
    • DNA detection through signal amplification by using NADH: Flavin oxidoreductase and oligonucleotide-flavin conjugates as cofactors
    • Simon, P., Dueymes, C., Fontecave, M., and Decout, J. L. (2005) DNA detection through signal amplification by using NADH: flavin oxidoreductase and oligonucleotide-flavin conjugates as cofactors Angew. Chem., Int. Ed. 44, 2764-7
    • (2005) Angew. Chem., Int. Ed. , vol.44 , pp. 2764-2767
    • Simon, P.1    Dueymes, C.2    Fontecave, M.3    Decout, J.L.4
  • 20
    • 33749250194 scopus 로고    scopus 로고
    • Kinetic analysis of semisynthetic peroxidase enzymes containing a covalent DNA-heme adduct as the cofactor
    • Fruk, L., Muller, J., and Niemeyer, C. M. (2006) Kinetic analysis of semisynthetic peroxidase enzymes containing a covalent DNA-heme adduct as the cofactor Chem.-Eur. J. 12, 7448-57
    • (2006) Chem. - Eur. J. , vol.12 , pp. 7448-7457
    • Fruk, L.1    Muller, J.2    Niemeyer, C.M.3
  • 21
    • 33846215935 scopus 로고    scopus 로고
    • Site-specific labeling of DNA-protein conjugates by means of expressed protein ligation
    • Lovrinovic, M., Fruk, L., Schroder, H., and Niemeyer, C. M. (2007) Site-specific labeling of DNA-protein conjugates by means of expressed protein ligation Chem. Commun. 353-5
    • (2007) Chem. Commun. , pp. 353-355
    • Lovrinovic, M.1    Fruk, L.2    Schroder, H.3    Niemeyer, C.M.4
  • 22
    • 36749055668 scopus 로고    scopus 로고
    • A universal method for the preparation of covalent protein-DNA conjugates for use in creating protein nanostructures
    • Duckworth, B. P., Chen, Y., Wollack, J. W., Sham, Y., Mueller, J. D., Taton, T. A., and Distefano, M. D. (2007) A universal method for the preparation of covalent protein-DNA conjugates for use in creating protein nanostructures Angew. Chem., Int. Ed. 46, 8819-22
    • (2007) Angew. Chem., Int. Ed. , vol.46 , pp. 8819-8822
    • Duckworth, B.P.1    Chen, Y.2    Wollack, J.W.3    Sham, Y.4    Mueller, J.D.5    Taton, T.A.6    Distefano, M.D.7
  • 24
    • 0035856963 scopus 로고    scopus 로고
    • Ketone-DNA: A versatile postsynthetic DNA decoration platform
    • Dey, S. and Sheppard, T. L. (2001) Ketone-DNA: a versatile postsynthetic DNA decoration platform Org. Lett. 3, 3983-6
    • (2001) Org. Lett. , vol.3 , pp. 3983-3986
    • Dey, S.1    Sheppard, T.L.2
  • 25
    • 33846245949 scopus 로고    scopus 로고
    • An enzymatic method for site-specific labeling of recombinant proteins with oligonucleotides
    • Tominaga, J., Kemori, Y., Tanaka, Y., Maruyama, T., Kamiya, N., and Goto, M. (2007) An enzymatic method for site-specific labeling of recombinant proteins with oligonucleotides Chem. Commun. 401-3
    • (2007) Chem. Commun. , pp. 401-403
    • Tominaga, J.1    Kemori, Y.2    Tanaka, Y.3    Maruyama, T.4    Kamiya, N.5    Goto, M.6
  • 26
    • 33646755397 scopus 로고    scopus 로고
    • Self-assembling protein arrays on DNA chips by auto-labeling fusion proteins with a single DNA address
    • Jongsma, M. A. and Litjens, R. H. (2006) Self-assembling protein arrays on DNA chips by auto-labeling fusion proteins with a single DNA address Proteomics 6, 2650-5
    • (2006) Proteomics , vol.6 , pp. 2650-2655
    • Jongsma, M.A.1    Litjens, R.H.2
  • 27
    • 68349146256 scopus 로고    scopus 로고
    • Protein-DNA photo-crosslinking with a genetically encoded benzophenone-containing amino acid
    • Lee, H. S., Dimla, R. D., and Schultz, P. G. (2009) Protein-DNA photo-crosslinking with a genetically encoded benzophenone-containing amino acid Bioorg. Med. Chem. Lett. 19, 5222-4
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 5222-5224
    • Lee, H.S.1    Dimla, R.D.2    Schultz, P.G.3
  • 28
    • 1942524457 scopus 로고    scopus 로고
    • Combination of DNA-directed immobilization and immuno-PCR: Very sensitive antigen detection by means of self-assembled DNA-protein conjugates
    • Niemeyer, C. M., Wacker, R., and Adler, M. (2003) Combination of DNA-directed immobilization and immuno-PCR: very sensitive antigen detection by means of self-assembled DNA-protein conjugates Nucleic Acids Res. 31, e90
    • (2003) Nucleic Acids Res. , vol.31 , pp. 90
    • Niemeyer, C.M.1    Wacker, R.2    Adler, M.3
  • 29
    • 76149123221 scopus 로고    scopus 로고
    • Tyrosine bioconjugation through aqueous ene-type reactions: A click-like reaction for tyrosine
    • Ban, H., Gavrilyuk, J., and Barbas, C. F., 3rd (2010) Tyrosine bioconjugation through aqueous ene-type reactions: a click-like reaction for tyrosine J. Am. Chem. Soc. 132, 1523-5
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 1523-1525
    • Ban, H.1    Gavrilyuk, J.2    Barbas III, C.F.3
  • 30
    • 59749100526 scopus 로고    scopus 로고
    • Synthesis and evaluation of a cyclic imine derivative conjugated to a fluorescent molecule for labeling of proteins
    • Guo, H. M., Minakawa, M., Ueno, L., and Tanaka, F. (2009) Synthesis and evaluation of a cyclic imine derivative conjugated to a fluorescent molecule for labeling of proteins Bioorg. Med. Chem. Lett. 19, 1210-3
    • (2009) Bioorg. Med. Chem. Lett. , vol.19 , pp. 1210-1213
    • Guo, H.M.1    Minakawa, M.2    Ueno, L.3    Tanaka, F.4
  • 31
    • 84871307240 scopus 로고    scopus 로고
    • Formylbenzene diazonium hexafluorophosphate reagent for tyrosine-selective modification of proteins and the introduction of a bioorthogonal aldehyde
    • Gavrilyuk, J., Ban, H., Nagano, M., Hakamata, W., and Barbas, C. F., 3rd (2012) Formylbenzene diazonium hexafluorophosphate reagent for tyrosine-selective modification of proteins and the introduction of a bioorthogonal aldehyde Bioconjugate Chem. 23, 2321-8
    • (2012) Bioconjugate Chem. , vol.23 , pp. 2321-2328
    • Gavrilyuk, J.1    Ban, H.2    Nagano, M.3    Hakamata, W.4    Barbas III, C.F.5
  • 32
    • 0035207160 scopus 로고    scopus 로고
    • A streptavidin mutant useful for directed immobilization on solid surfaces
    • Reznik, G. O., Vajda, S., Cantor, C. R., and Sano, T. (2001) A streptavidin mutant useful for directed immobilization on solid surfaces Bioconjugate Chem. 12, 1000-4
    • (2001) Bioconjugate Chem. , vol.12 , pp. 1000-1004
    • Reznik, G.O.1    Vajda, S.2    Cantor, C.R.3    Sano, T.4
  • 33
    • 0036523464 scopus 로고    scopus 로고
    • DNA-directed assembly of bienzymic complexes from in vivo biotinylated NAD(P)H:FMN oxidoreductase and luciferase
    • Niemeyer, C. M., Koehler, J., and Wuerdemann, C. (2002) DNA-directed assembly of bienzymic complexes from in vivo biotinylated NAD(P)H:FMN oxidoreductase and luciferase ChemBioChem 3, 242-5
    • (2002) ChemBioChem , vol.3 , pp. 242-245
    • Niemeyer, C.M.1    Koehler, J.2    Wuerdemann, C.3
  • 34
    • 1242292278 scopus 로고    scopus 로고
    • Engineering peroxidase activity in myoglobin: The haem cavity structure and peroxide activation in the T67R/S92D mutant and its derivative reconstituted with protohaemin-l-histidine
    • Roncone, R., Monzani, E., Murtas, M., Battaini, G., Pennati, A., Sanangelantoni, A. M., Zuccotti, S., Bolognesi, M., and Casella, L. (2004) Engineering peroxidase activity in myoglobin: the haem cavity structure and peroxide activation in the T67R/S92D mutant and its derivative reconstituted with protohaemin-l-histidine Biochem. J. 377, 717-24
    • (2004) Biochem. J. , vol.377 , pp. 717-724
    • Roncone, R.1    Monzani, E.2    Murtas, M.3    Battaini, G.4    Pennati, A.5    Sanangelantoni, A.M.6    Zuccotti, S.7    Bolognesi, M.8    Casella, L.9
  • 35
    • 0346456937 scopus 로고    scopus 로고
    • Hybridization of modified-heme reconstitution and distal histidine mutation to functionalize sperm whale myoglobin
    • Sato, H., Hayashi, T., Ando, T., Hisaeda, Y., Ueno, T., and Watanabe, Y. (2004) Hybridization of modified-heme reconstitution and distal histidine mutation to functionalize sperm whale myoglobin J. Am. Chem. Soc. 126, 436-7
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 436-437
    • Sato, H.1    Hayashi, T.2    Ando, T.3    Hisaeda, Y.4    Ueno, T.5    Watanabe, Y.6
  • 36
    • 66149185436 scopus 로고    scopus 로고
    • Tuning of peroxidase activity by covalently tethered DNA oligonucleotides
    • Glettenberg, M. and Niemeyer, C. M. (2009) Tuning of peroxidase activity by covalently tethered DNA oligonucleotides Bioconjugate Chem. 20, 969-75
    • (2009) Bioconjugate Chem. , vol.20 , pp. 969-975
    • Glettenberg, M.1    Niemeyer, C.M.2


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