메뉴 건너뛰기




Volumn 8, Issue 8, 2013, Pages 1620-1634

Site-specific protein labeling using prime and chelation-assisted click chemistry

Author keywords

[No Author keywords available]

Indexed keywords

ALKYNE; AZIDE; CHELATING AGENT; COPPER; ESCHERICHIA COLI PROTEIN; LIGASE; LPLA PROTEIN, E COLI; MEMBRANE PROTEIN; PROTEIN;

EID: 84894443196     PISSN: 17542189     EISSN: 17502799     Source Type: Journal    
DOI: 10.1038/nprot.2013.096     Document Type: Article
Times cited : (72)

References (31)
  • 1
    • 84861912742 scopus 로고    scopus 로고
    • Fast, cell-compatible click chemistry with copper-chelating azides for biomolecular labeling
    • Uttamapinant, C. et al. Fast, cell-compatible click chemistry with copper-chelating azides for biomolecular labeling. Angew. Chem. Int. Ed. Engl.51, 5852–5856 (2012).
    • (2012) Angew. Chem. Int. Ed. Engl , vol.51 , pp. 5852-5856
    • Uttamapinant, C.1
  • 2
    • 77954633083 scopus 로고    scopus 로고
    • A fluorophore ligase for site-specific protein labeling inside living cells
    • Uttamapinant, C. et al. A fluorophore ligase for site-specific protein labeling inside living cells. Proc. Natl. Acad. Sci. USA 107, 10914–10919 (2010).
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 10914-10919
    • Uttamapinant, C.1
  • 3
    • 84862907995 scopus 로고    scopus 로고
    • Diels-Alder cycloaddition for fluorophore targeting to specific proteins inside living cells
    • Liu, D.S. et al. Diels-Alder cycloaddition for fluorophore targeting to specific proteins inside living cells. J. Am. Chem. Soc. 134, 792–795 (2012).
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 792-795
    • Liu, D.S.1
  • 4
    • 80053028232 scopus 로고    scopus 로고
    • Structure-guided engineering of a Pacific Blue fluorophore ligase for specific protein imaging in living cells
    • Cohen, J.D., Thompson, S., Ting, A.Y., Structure-guided engineering of a Pacific Blue fluorophore ligase for specific protein imaging in living cells. Biochemistry 50, 8221–8225 (2011).
    • (2011) Biochemistry , vol.50 , pp. 8221-8225
    • Cohen, J.D.1    Thompson, S.2    Ting, A.Y.3
  • 5
    • 78650688480 scopus 로고    scopus 로고
    • Synthesis of 7-aminocoumarin by Buchwald-Hartwig cross coupling for specific protein labeling in living cells
    • Jin, X., Uttamapinant, C., Ting, A.Y., Synthesis of 7-aminocoumarin by Buchwald-Hartwig cross coupling for specific protein labeling in living cells. Chembiochem 12, 65–70 (2011).
    • (2011) Chembiochem , vol.12 , pp. 65-70
    • Jin, X.1    Uttamapinant, C.2    Ting, A.Y.3
  • 6
    • 54749129835 scopus 로고    scopus 로고
    • An engineered aryl azide ligase for site-specific mapping of protein-protein interactions through photo-cross-linking
    • Baruah, H. et al. An engineered aryl azide ligase for site-specific mapping of protein-protein interactions through photo-cross-linking. Angew. Chem. Int. Ed. Engl. 47, 7018–7021 (2008).
    • (2008) Angew. Chem. Int. Ed. Engl , vol.47 , pp. 7018-7021
    • Baruah, H.1
  • 7
    • 84857779702 scopus 로고    scopus 로고
    • Fluorophore targeting to cellular proteins via enzyme-mediated azide ligation and strain-promoted cycloaddition
    • Yao, J.Z. et al. Fluorophore targeting to cellular proteins via enzyme-mediated azide ligation and strain-promoted cycloaddition. J. Am. Chem. Soc. 134, 3720–3728 (2012).
    • (2012) J. Am. Chem. Soc , vol.134 , pp. 3720-3728
    • Yao, J.Z.1
  • 8
    • 84871546842 scopus 로고    scopus 로고
    • Quantum dot targeting with lipoic acid ligase and HaloTag for single-molecule imaging on living cells
    • Liu, D.S. et al. Quantum dot targeting with lipoic acid ligase and HaloTag for single-molecule imaging on living cells. ACS Nano. 6, 11080–11087 (2012).
    • (2012) ACS Nano , vol.6 , pp. 11080-11087
    • Liu, D.S.1
  • 9
    • 84874008269 scopus 로고    scopus 로고
    • Imaging trans-cellular neurexin-neuroligin interactions by enzymatic probe ligation
    • Liu, D.S. et al. Imaging trans-cellular neurexin-neuroligin interactions by enzymatic probe ligation. PLoS ONE 8, e52823 (2013).
    • (2013) Plos ONE , vol.e52823 , pp. 8
    • Liu, D.S.1
  • 10
    • 72449154666 scopus 로고    scopus 로고
    • Analysis and optimization of copper-catalyzed azide-alkyne cycloaddition for bioconjugation
    • Hong, V. et al. Analysis and optimization of copper-catalyzed azide-alkyne cycloaddition for bioconjugation. Angew. Chem. Int. Ed. Engl. 48, 9879–9883 (2009).
    • (2009) Angew. Chem. Int. Ed. Engl , vol.48 , pp. 9879-9883
    • Hong, V.1
  • 11
    • 0033779765 scopus 로고    scopus 로고
    • Single-molecule imaging of EGFR signalling on the surface of living cells. Nat
    • Sako, Y., Minoghchi, S., Yanagida, T., Single-molecule imaging of EGFR signalling on the surface of living cells. Nat. Cell Biol. 2, 168–172 (2000).
    • (2000) Cell Biol , vol.2 , pp. 168-172
    • Sako, Y.1    Minoghchi, S.2    Yanagida, T.3
  • 12
    • 78649927344 scopus 로고    scopus 로고
    • Superresolution imaging of chemical synapses in the brain
    • Dani, A. et al. Superresolution imaging of chemical synapses in the brain. Neuron 68, 843–856 (2010).
    • (2010) Neuron , vol.68 , pp. 843-856
    • Dani, A.1
  • 13
    • 33751547691 scopus 로고    scopus 로고
    • Nanoscale organization of nicotinic acetylcholine receptors revealed by stimulated emission depletion microscopy
    • Kellner, R.R. et al. Nanoscale organization of nicotinic acetylcholine receptors revealed by stimulated emission depletion microscopy. Neuroscience 144, 135–143 (2007).
    • (2007) Neuroscience , vol.144 , pp. 135-143
    • Kellner, R.R.1
  • 14
    • 79954595064 scopus 로고    scopus 로고
    • Receptor oligomerization during endocytosis using a co-internalization assay. ACS
    • Zou, P., Ting, A.Y., Imaging LDL receptor oligomerization during endocytosis using a co-internalization assay. ACS Chem. Biol. 6, 308–313 (2011).
    • (2011) Chem. Biol , vol.6 , pp. 308-313
    • Zou, P.1    Ting, A.Y.2    Imaging, L.3
  • 15
    • 0035076478 scopus 로고    scopus 로고
    • Distribution of an NMDA receptor:GFP fusion protein in sensory neurons is altered by a C-terminal construct
    • Marsh, D.R. et al. Distribution of an NMDA receptor:GFP fusion protein in sensory neurons is altered by a C-terminal construct. J. Neurochem. 77, 23–33 (2001).
    • (2001) J. Neurochem , vol.77 , pp. 23-33
    • Marsh, D.R.1
  • 16
    • 39149145486 scopus 로고    scopus 로고
    • An engineered protein tag for multiprotein labeling in living cells
    • Gautier, A. et al. An engineered protein tag for multiprotein labeling in living cells. Chem. Biol. 15, 128–136 (2008).
    • (2008) Chem. Biol , vol.15 , pp. 128-136
    • Gautier, A.1
  • 17
    • 48049092838 scopus 로고    scopus 로고
    • HaloTag: A novel protein labeling technology for cell imaging and protein analysis. ACS
    • Los, G.V. et al. HaloTag: a novel protein labeling technology for cell imaging and protein analysis. ACS Chem. Biol. 3, 373–382 (2008).
    • (2008) Chem. Biol , vol.3 , pp. 373-382
    • Los, G.V.1
  • 18
    • 33645283107 scopus 로고    scopus 로고
    • A monovalent streptavidin with a single femtomolar biotin binding site. Nat
    • Howarth, M. et al. A monovalent streptavidin with a single femtomolar biotin binding site. Nat. Methods 3, 267–273 (2006).
    • (2006) Methods , vol.3 , pp. 267-273
    • Howarth, M.1
  • 19
    • 0031892994 scopus 로고    scopus 로고
    • Dimerization as a regulatory mechanism in signal transduction. Annu
    • Klemm, J.D., Schreiber, S.L., Crabtree, G.R., Dimerization as a regulatory mechanism in signal transduction. Annu. Rev. Immunol. 16, 569–592 (1998).
    • (1998) Rev. Immunol , vol.16 , pp. 569-592
    • Klemm, J.D.1    Schreiber, S.L.2    Crabtree, G.R.3
  • 20
    • 84860378415 scopus 로고    scopus 로고
    • Quantitative fluorescence labeling of aldehyde-tagged proteins for single-molecule imaging. Nat
    • Shi, X. et al. Quantitative fluorescence labeling of aldehyde-tagged proteins for single-molecule imaging. Nat. Methods 9, 499–503 (2012).
    • (2012) Methods , vol.9 , pp. 499-503
    • Shi, X.1
  • 21
    • 33845461876 scopus 로고    scopus 로고
    • Nucleophilic catalysis of hydrazone formation and transimination: Implications for dynamic covalent chemistry
    • Dirksen, A. et al. Nucleophilic catalysis of hydrazone formation and transimination: implications for dynamic covalent chemistry. J. Am. Chem. Soc. 128, 15602–15603 (2006).
    • (2006) J. Am. Chem. Soc , vol.128 , pp. 15602-15603
    • Dirksen, A.1
  • 22
    • 27144448780 scopus 로고    scopus 로고
    • Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity. Nat
    • Martin, B.R. et al. Mammalian cell-based optimization of the biarsenical-binding tetracysteine motif for improved fluorescence and affinity. Nat. Biotechnol. 23, 1308–1314 (2005).
    • (2005) Biotechnol , vol.23 , pp. 1308-1314
    • Martin, B.R.1
  • 23
    • 79751523257 scopus 로고    scopus 로고
    • Live-cell imaging of cellular proteins by a strain-promoted azide-alkyne cycloaddition
    • Beatty, K.E. et al. Live-cell imaging of cellular proteins by a strain-promoted azide-alkyne cycloaddition. Chembiochem 11, 2092–2095 (2010).
    • (2010) Chembiochem , vol.11 , pp. 2092-2095
    • Beatty, K.E.1
  • 24
    • 70450158888 scopus 로고    scopus 로고
    • Yeast display evolution of a kinetically efficient 13-amino acid substrate for lipoic acid ligase
    • Puthenveetil, S. et al. Yeast display evolution of a kinetically efficient 13-amino acid substrate for lipoic acid ligase. J. Am. Chem. Soc. 131, 16430–16438 (2009).
    • (2009) J. Am. Chem. Soc , vol.131 , pp. 16430-16438
    • Puthenveetil, S.1
  • 25
    • 42949085657 scopus 로고    scopus 로고
    • Monovalent, reduced-size quantum dots for imaging receptors on living cells. Nat
    • Howarth, M. et al. Monovalent, reduced-size quantum dots for imaging receptors on living cells. Nat. Methods 5, 397–399 (2008).
    • (2008) Methods , vol.5 , pp. 397-399
    • Howarth, M.1
  • 26
    • 0000167256 scopus 로고
    • A viral cleavage site cassette: Identification of amino acid sequences required for tobacco etch virus polyprotein processing
    • Carrington, J.C., Dougherty, W.G., A viral cleavage site cassette: identification of amino acid sequences required for tobacco etch virus polyprotein processing. Proc. Natl. Acad. Sci. USA 85, 3391–3395 (1988).
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 3391-3395
    • Carrington, J.C.1    Dougherty, W.G.2
  • 27
    • 80051727754 scopus 로고    scopus 로고
    • Increasing the efficacy of bioorthogonal click reactions for bioconjugation: A comparative study
    • Besanceney-Webler, C. et al. Increasing the efficacy of bioorthogonal click reactions for bioconjugation: a comparative study. Angew. Chem. Int. Ed. Engl. 50, 8051–8056 (2011).
    • (2011) Angew. Chem. Int. Ed. Engl , vol.50 , pp. 8051-8056
    • Besanceney-Webler, C.1
  • 28
    • 4444324951 scopus 로고    scopus 로고
    • Polytriazoles as copper(I)-stabilizing ligands in catalysis. Org
    • Chan, T.R. et al. Polytriazoles as copper(I)-stabilizing ligands in catalysis. Org. Lett. 6, 2853–2855 (2004).
    • (2004) Lett , vol.6 , pp. 2853-2855
    • Chan, T.R.1
  • 29
    • 40649128835 scopus 로고    scopus 로고
    • Imaging proteins in live mammalian cells with biotin ligase and monovalent streptavidin. Nat
    • Howarth, M., Ting, A.Y., Imaging proteins in live mammalian cells with biotin ligase and monovalent streptavidin. Nat. Protoc. 3, 534–545 (2008).
    • (2008) Protoc , vol.3 , pp. 534-545
    • Howarth, M.1    Ting, A.Y.2
  • 30
    • 0030755709 scopus 로고    scopus 로고
    • Microtubule interaction site of the kinesin motor
    • Woehlke, G. et al. Microtubule interaction site of the kinesin motor. Cell 90, 207–216 (1997).
    • (1997) Cell , vol.90 , pp. 207-216
    • Woehlke, G.1
  • 31
    • 84878781230 scopus 로고    scopus 로고
    • Copper-catalyzed azide-alkyne click chemistry for bioconjugation
    • Presolski, S.I., Hong, V.P., Finn, M.G., Copper-catalyzed azide-alkyne click chemistry for bioconjugation. Curr. Protoc. Chem. Biol. 3, 153–162 (2011).
    • (2011) Curr. Protoc. Chem. Biol , vol.3 , pp. 153-162
    • Presolski, S.I.1    Hong, V.P.2    Finn, M.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.