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Volumn 2, Issue 2, 2005, Pages 99-104

Site-specific labeling of cell surface proteins with biophysical probes using biotin ligase

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; BACTERIAL ENZYME; BENZOPHENONE; BIOTIN; BIOTIN LIGASE; CELL SURFACE PROTEIN; EPIDERMAL GROWTH FACTOR RECEPTOR; FLUORESCEIN; HYDRAZIDE; HYDROXYLAMINE; KETONE; LIGASE; PEPTIDE; UNCLASSIFIED DRUG; BIRA PROTEIN, E COLI; ESCHERICHIA COLI PROTEIN; FLUORESCENT DYE; MEMBRANE PROTEIN; REPRESSOR PROTEIN; TRANSCRIPTION FACTOR;

EID: 18744401100     PISSN: 15487091     EISSN: None     Source Type: Journal    
DOI: 10.1038/nmeth735     Document Type: Article
Times cited : (559)

References (23)
  • 3
    • 3042793777 scopus 로고    scopus 로고
    • A general approach for chemical labeling and rapid, spatially controlled protein inactivation
    • Marks, K.M., Braun, P.D. & Nolan, G.P. A general approach for chemical labeling and rapid, spatially controlled protein inactivation. Proc. Natl. Acad. Sci. USA 101, 9982-9987 (2004).
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 9982-9987
    • Marks, K.M.1    Braun, P.D.2    Nolan, G.P.3
  • 4
    • 3242754218 scopus 로고    scopus 로고
    • Specific labeling of cell surface proteins with chemically diverse compounds
    • George, N., Pick, H., Vogel, H., Johnsson, N. & Johnsson, K. Specific labeling of cell surface proteins with chemically diverse compounds. J. Am. Chem. Soc. 126, 8896-8897 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 8896-8897
    • George, N.1    Pick, H.2    Vogel, H.3    Johnsson, N.4    Johnsson, K.5
  • 5
    • 3042546498 scopus 로고    scopus 로고
    • Labeling proteins with small molecules by site-specific posttranslational modification
    • Yin, J., Liu, F., Li, X. & Walsh, C.T. Labeling proteins with small molecules by site-specific posttranslational modification. J. Am. Chem. Soc. 126, 7754-7755 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 7754-7755
    • Yin, J.1    Liu, F.2    Li, X.3    Walsh, C.T.4
  • 6
    • 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. et al. 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).
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 6063-6076
    • Adams, S.R.1
  • 7
    • 3042826388 scopus 로고    scopus 로고
    • In vivo targeting of organic calcium sensors via genetically selected peptides
    • Marks, K.M., Rosinov, M. & Nolan, G.P. In vivo targeting of organic calcium sensors via genetically selected peptides. Chem. Biol. 11, 347-356 (2004).
    • (2004) Chem. Biol. , vol.11 , pp. 347-356
    • Marks, K.M.1    Rosinov, M.2    Nolan, G.P.3
  • 8
    • 1842582037 scopus 로고    scopus 로고
    • Reversible site-selective labeling of membrane proteins in live cells
    • Guignet, E.G., Hovius, R. & Vogel, H. Reversible site-selective labeling of membrane proteins in live cells. Nat. Biotechnol. 22, 440-444 (2004).
    • (2004) Nat. Biotechnol. , vol.22 , pp. 440-444
    • Guignet, E.G.1    Hovius, R.2    Vogel, H.3
  • 9
    • 85057633057 scopus 로고    scopus 로고
    • Site-specific labeling of proteins with small molecules in live cells
    • (in the press)
    • Chen, I. & Ting, A.Y. Site-specific labeling of proteins with small molecules in live cells. Curr. Opin. Biotech. (in the press).
    • Curr. Opin. Biotech.
    • Chen, I.1    Ting, A.Y.2
  • 10
    • 0032917076 scopus 로고    scopus 로고
    • A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation
    • Beckett, D., Kovaleva, E. & Schatz, P.J. A minimal peptide substrate in biotin holoenzyme synthetase-catalyzed biotinylation. Protein Sci. 8, 921-929 (1999).
    • (1999) Protein Sci. , vol.8 , pp. 921-929
    • Beckett, D.1    Kovaleva, E.2    Schatz, P.J.3
  • 11
    • 0038611015 scopus 로고    scopus 로고
    • Efficient biotinylation and single-step purification of tagged transcription factors in mammalian cells and transgenic mice
    • de Boer, E. et al. Efficient biotinylation and single-step purification of tagged transcription factors in mammalian cells and transgenic mice. Proc. Natl. Acad. Sci. USA 100, 7480-7485 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 7480-7485
    • de Boer, E.1
  • 12
    • 0030929377 scopus 로고    scopus 로고
    • Engineering chemical reactivity on cell surfaces through oligosaccharide biosynthesis
    • Mahal, L.K., Yarema, K.J. & Bertozzi, C.R. Engineering chemical reactivity on cell surfaces through oligosaccharide biosynthesis. Science 276, 1125-1128 (1997).
    • (1997) Science , vol.276 , pp. 1125-1128
    • Mahal, L.K.1    Yarema, K.J.2    Bertozzi, C.R.3
  • 13
    • 33645174152 scopus 로고
    • Synthesis of sulfur-containing carbaprostacyclin analogs
    • Baraldi, P.G. et al. Synthesis of sulfur-containing carbaprostacyclin analogs. Gazz. Chim. Ital. 114, 177-183 (1984).
    • (1984) Gazz. Chim. Ital. , vol.114 , pp. 177-183
    • Baraldi, P.G.1
  • 14
    • 33947094829 scopus 로고
    • Total synthesis of biotin based on stereoselective alkylation of sulfoxides
    • Lavielle, S., Bory, S., Moreau, B., Luche, M.J. & Marquet, A. Total synthesis of biotin based on stereoselective alkylation of sulfoxides. J. Am. Chem. Soc. 100, 1558-1563 (1978).
    • (1978) J. Am. Chem. Soc. , vol.100 , pp. 1558-1563
    • Lavielle, S.1    Bory, S.2    Moreau, B.3    Luche, M.J.4    Marquet, A.5
  • 15
    • 0033555541 scopus 로고    scopus 로고
    • Molecular recognition in a post-translational modification of exceptional specificity. Mutants of the biotinylated domain of acetyl-CoA carboxylase defective in recognition by biotin protein ligase
    • Chapman-Smith, A., Morris, T.W., Wallace, J.C. & Cronan, J.E., Jr. Molecular recognition in a post-translational modification of exceptional specificity. Mutants of the biotinylated domain of acetyl-CoA carboxylase defective in recognition by biotin protein ligase. J. Biol. Chem. 274, 1449-1457 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 1449-1457
    • Chapman-Smith, A.1    Morris, T.W.2    Wallace, J.C.3    Cronan Jr., J.E.4
  • 16
    • 0035814482 scopus 로고    scopus 로고
    • Kinetic parameters for small-molecule drug delivery by covalent cell surface targeting
    • Nauman, D.A. & Bertozzi, C.R. Kinetic parameters for small-molecule drug delivery by covalent cell surface targeting. Biochim. Biophys. Acta 1568, 147-154 (2001).
    • (2001) Biochim. Biophys. Acta , vol.1568 , pp. 147-154
    • Nauman, D.A.1    Bertozzi, C.R.2
  • 17
    • 0025873538 scopus 로고
    • Epidermal growth factor (EGF) induces oligomerization of soluble, extracellular, ligand-binding domain of EGF receptor. A low resolution projection structure of the ligand-binding domain
    • Lax, I. et al. Epidermal growth factor (EGF) induces oligomerization of soluble, extracellular, ligand-binding domain of EGF receptor. A low resolution projection structure of the ligand-binding domain. J. Biol. Chem. 266, 13828-13833 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 13828-13833
    • Lax, I.1
  • 18
    • 0033119241 scopus 로고    scopus 로고
    • Comparison of fixation protocols for adherent cultured cells applied to a GFP fusion protein of the epidermal growth factor receptor
    • Brock, R., Hamelers, I.H. & Jovin, T.M. Comparison of fixation protocols for adherent cultured cells applied to a GFP fusion protein of the epidermal growth factor receptor. Cytometry 35, 353-362 (1999).
    • (1999) Cytometry , vol.35 , pp. 353-362
    • Brock, R.1    Hamelers, I.H.2    Jovin, T.M.3
  • 19
    • 0038732770 scopus 로고    scopus 로고
    • EGFR activation coupled to inhibition of tyrosine phosphatases causes lateral signal propagation
    • Reynolds, A.R., Tischer, C., Verveer, P.J., Rocks, O. & Bastiaens, P.I. EGFR activation coupled to inhibition of tyrosine phosphatases causes lateral signal propagation. Nat. Cell Biol. 5, 447-453 (2003).
    • (2003) Nat. Cell Biol. , vol.5 , pp. 447-453
    • Reynolds, A.R.1    Tischer, C.2    Verveer, P.J.3    Rocks, O.4    Bastiaens, P.I.5
  • 20
    • 0038661197 scopus 로고    scopus 로고
    • A new strategy for the site-specific modification of proteins in vivo
    • Zhang, Z. et al. A new strategy for the site-specific modification of proteins in vivo. Biochemistry 42, 6735-6746 (2003).
    • (2003) Biochemistry , vol.42 , pp. 6735-6746
    • Zhang, Z.1
  • 21
    • 0033461172 scopus 로고    scopus 로고
    • Thymosin β(4) serves as a glutaminyl substrate of transglutaminase. Labeling with fluorescent dansylcadaverine does not abolish interaction with G-actin
    • Huff, T. et al. Thymosin β(4) serves as a glutaminyl substrate of transglutaminase. Labeling with fluorescent dansylcadaverine does not abolish interaction with G-actin. FEBS Lett 464, 14-20 (1999).
    • (1999) FEBS Lett. , vol.464 , pp. 14-20
    • Huff, T.1
  • 22
    • 0016743524 scopus 로고
    • Crosslinking and labeling of membrane proteins by transglutaminase-catalyzed reactions
    • Dutton, A. & Singer, S.J. Crosslinking and labeling of membrane proteins by transglutaminase-catalyzed reactions. Proc. Natl. Acad. Sci. USA 72, 2568-2571 (1975).
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 2568-2571
    • Dutton, A.1    Singer, S.J.2
  • 23
    • 1542317850 scopus 로고    scopus 로고
    • Sortase-mediated protein ligation: A new method for protein engineering
    • Mao, H., Hart, S.A., Schink, A. & Pollok, B.A. Sortase-mediated protein ligation: a new method for protein engineering. J. Am. Chem. Soc. 126, 2670-2671 (2004).
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 2670-2671
    • Mao, H.1    Hart, S.A.2    Schink, A.3    Pollok, B.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.