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Volumn 6, Issue 4, 2014, Pages 352-361

Palladium-triggered deprotection chemistry for protein activation in living cells

Author keywords

[No Author keywords available]

Indexed keywords

GREEN FLUORESCENT PROTEIN; PALLADIUM; PROTEIN;

EID: 84896965494     PISSN: 17554330     EISSN: 17554349     Source Type: Journal    
DOI: 10.1038/nchem.1887     Document Type: Article
Times cited : (338)

References (46)
  • 1
    • 77249169281 scopus 로고    scopus 로고
    • Turning enzymes ON with small molecules
    • Zorn, J. A. & Wells, J. A. Turning enzymes ON with small molecules. Nature Chem. Biol. 6, 179-188 (2010).
    • (2010) Nature Chem. Biol. , vol.6 , pp. 179-188
    • Zorn, J.A.1    Wells, J.A.2
  • 2
    • 65149094024 scopus 로고    scopus 로고
    • Brought to life: Targeted activation of enzyme function with small molecules
    • Bishop, A. & Chen, V. Brought to life: Targeted activation of enzyme function with small molecules. J. Chem. Biol., 2, 1-9 (2009).
    • (2009) J. Chem. Biol. , vol.2 , pp. 1-9
    • Bishop, A.1    Chen, V.2
  • 3
    • 77955844090 scopus 로고    scopus 로고
    • Recent advances in the photochemical control of protein function
    • Riggsbee, C. W. & Deiters, A. Recent advances in the photochemical control of protein function. Trends Biotechnol. 28, 468-475 (2010).
    • (2010) Trends Biotechnol. , vol.28 , pp. 468-475
    • Riggsbee, C.W.1    Deiters, A.2
  • 4
    • 33748195107 scopus 로고    scopus 로고
    • A rapid, reversible, and tunable method to regulate protein function in living cells using synthetic small molecules
    • Banaszynski, L. A., Chen, L-C., Maynard-Smith, L. A., Ooi, A. G. L. & Wandless, T. J. A rapid, reversible, and tunable method to regulate protein function in living cells using synthetic small molecules. Cell 126, 995-1004 (2006).
    • (2006) Cell , vol.126 , pp. 995-1004
    • Banaszynski, L.A.1    Chen, L.-C.2    Maynard-Smith, L.A.3    Ooi, A.G.L.4    Wandless, T.J.5
  • 5
    • 2342436150 scopus 로고    scopus 로고
    • Cofilin promotes actin polymerization and defines the direction of cell motility
    • Ghosh M. et al. Cofilin promotes actin polymerization and defines the direction of cell motility. Science 304, 743-746 (2004).
    • (2004) Science , vol.304 , pp. 743-746
    • Ghosh, M.1
  • 6
    • 70449372265 scopus 로고    scopus 로고
    • Small-molecule activators of a proenzyme
    • Wolan, D.W., Zorn, J. A., Gray, D. C. &Wells, J. A. Small-molecule activators of a proenzyme. Science 326, 853-858 (2009).
    • (2009) Science , vol.326 , pp. 853-858
    • Wolan, D.W.1    Zorn, J.A.2    Gray, D.C.3    Wells, J.A.4
  • 7
    • 34250177582 scopus 로고    scopus 로고
    • Ligand interaction scan: A general method for engineering ligand-sensitive protein alleles
    • Erster O., Eisenstein, M. & Liscovitch, M. Ligand interaction scan: A general method for engineering ligand-sensitive protein alleles. Nature Methods 4, 393-395 (2007).
    • (2007) Nature Methods , vol.4 , pp. 393-395
    • Erster, O.1    Eisenstein, M.2    Liscovitch, M.3
  • 8
    • 33644684486 scopus 로고    scopus 로고
    • Chemical rescue of a mutant enzyme in living cells
    • Qiao, Y., Molina, H., Pandey, A., Zhang. J. & Cole, P. A. Chemical rescue of a mutant enzyme in living cells. Science 311, 1293-1297 (2006).
    • (2006) Science , vol.311 , pp. 1293-1297
    • Qiao, Y.1    Molina, H.2    Pandey, A.3    Zhang, J.4    Cole, P.A.5
  • 9
    • 34547406152 scopus 로고    scopus 로고
    • Small-molecule-mediated rescue of protein function by an inducible proteolytic shunt
    • Pratt, M. R, Schwartz, E. C. & Muir, T. W. Small-molecule-mediated rescue of protein function by an inducible proteolytic shunt. Proc. Natl Acad. Sci. USA 104, 11209-11214 (2007).
    • (2007) Proc. Natl Acad. Sci. USA , vol.104 , pp. 11209-11214
    • Pratt, M.R.1    Schwartz, E.C.2    Muir, T.W.3
  • 10
    • 49449113694 scopus 로고    scopus 로고
    • Light-mediated liberation of enzymatic activity: 'Small molecule' caged protein equivalents
    • Li, H., Hah, J-M. & Lawrence, D. S. Light-mediated liberation of enzymatic activity: 'small molecule' caged protein equivalents. J. Am. Chem. Soc. 130, 10474-10475 (2008).
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 10474-10475
    • Li, H.1    Hah, J.-M.2    Lawrence, D.S.3
  • 11
    • 0037125492 scopus 로고    scopus 로고
    • Catalytic subunit of protein kinase a caged at the activating phosphothreonine
    • Zou, K., Cheley, S., Givens, R. S. & Bayley, H. Catalytic subunit of protein kinase a caged at the activating phosphothreonine. J. Am. Chem. Soc. 124, 8220-8229 (2002).
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 8220-8229
    • Zou, K.1    Cheley, S.2    Givens, R.S.3    Bayley, H.4
  • 12
    • 70349783657 scopus 로고    scopus 로고
    • A facile system for encoding unnatural amino acids in mammalian cells
    • Chen, P. R. et al. A facile system for encoding unnatural amino acids in mammalian cells. Angew. Chem. Int. Ed. 48, 4052-4055 (2009).
    • (2009) Angew. Chem. Int. Ed. , vol.48 , pp. 4052-4055
    • Chen, P.R.1
  • 13
    • 84857451064 scopus 로고    scopus 로고
    • Designer proteins: Applications of genetic code expansion in cell biology
    • Davis, L. & Chin, J.W. Designer proteins: Applications of genetic code expansion in cell biology. Nature Rev. Mol. Cell Biol. 13, 168-182 (2012).
    • (2012) Nature Rev. Mol. Cell Biol. , vol.13 , pp. 168-182
    • Davis, L.1    Chin, J.W.2
  • 14
    • 84864276237 scopus 로고    scopus 로고
    • Photocontrol of tyrosine phosphorylation in mammalian cells via genetic encoding of photocaged tyrosine
    • Arbely, E., Torres-Kolbus, J., Deiters, A. & Chin, J. W. Photocontrol of tyrosine phosphorylation in mammalian cells via genetic encoding of photocaged tyrosine. J. Am. Chem. Soc. 134, 11912-11915 (2012).
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 11912-11915
    • Arbely, E.1    Torres-Kolbus, J.2    Deiters, A.3    Chin, J.W.4
  • 15
    • 0037084496 scopus 로고    scopus 로고
    • UV induces tyrosine kinase-independent internalisation and endosome arrest of the EGF receptor
    • Oksvold, M. P., Huitfeldt, H. S., Østvold, A. C. & Skarpen, E. UV induces tyrosine kinase-independent internalisation and endosome arrest of the EGF receptor. J. Cell Sci. 115, 793-803 (2002).
    • (2002) J. Cell Sci. , vol.115 , pp. 793-803
    • Oksvold, M.P.1    Huitfeldt, H.S.2    Østvold, A.C.3    Skarpen, E.4
  • 17
    • 0027439438 scopus 로고
    • The conserved lysine of the catalytic domain of protein kinases is actively involved in the phosphotransfer reaction and not required for anchoring ATP
    • Carrera, A. C., Alexandrov, K. & Roberts, T. M. The conserved lysine of the catalytic domain of protein kinases is actively involved in the phosphotransfer reaction and not required for anchoring ATP. Proc. Natl Acad. Sci. USA 90, 442-446 (1993).
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 442-446
    • Carrera, A.C.1    Alexandrov, K.2    Roberts, T.M.3
  • 18
    • 33748620928 scopus 로고    scopus 로고
    • Ruthenium-induced allylcarbamate cleavage in living cells
    • Streu, C. & Meggers, E. Ruthenium-induced allylcarbamate cleavage in living cells. Angew. Chem. Int. Ed. 45, 5645-5648 (2006).
    • (2006) Angew. Chem. Int. Ed. , vol.45 , pp. 5645-5648
    • Streu, C.1    Meggers, E.2
  • 19
    • 67849104049 scopus 로고    scopus 로고
    • Enhancement of a catalysis-based fluorometric detection method for palladium through rational fine-Tuning of the palladium species
    • Garner, A. L., Song, F. & Koide, K. Enhancement of a catalysis-based fluorometric detection method for palladium through rational fine-Tuning of the palladium species. J. Am. Chem. Soc. 131, 5163-5171 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 5163-5171
    • Garner, A.L.1    Song, F.2    Koide, K.3
  • 21
    • 77954802263 scopus 로고    scopus 로고
    • A method to site-specifically introduce methyllysine into proteins in E coli
    • Ai, H-W., Lee, J. W. & Schultz, P. G. A method to site-specifically introduce methyllysine into proteins in E. coli. Chem. Commun. 46, 5506-5508 (2010).
    • (2010) Chem. Commun. , vol.46 , pp. 5506-5508
    • Ai, H.-W.1    Lee, J.W.2    Schultz, P.G.3
  • 22
    • 77952753941 scopus 로고    scopus 로고
    • Fluorescent detection of palladium species with an O-propargylated fluorescein
    • Santra, M., Ko, S-K., Shin, I & Ahn, K. H. Fluorescent detection of palladium species with an O-propargylated fluorescein. Chem. Commun. 46, 3964-3966 (2010).
    • (2010) Chem. Commun. , vol.46 , pp. 3964-3966
    • Santra, M.1    Ko, S.-K.2    Shin, I.3    Ahn, K.H.4
  • 24
    • 84873279753 scopus 로고    scopus 로고
    • Metal complex catalysis in living biological systems
    • Sasmal, P. K., Streu, C. N. & Meggers, E. Metal complex catalysis in living biological systems. Chem. Commun. 49, 1581-1587 (2013).
    • (2013) Chem. Commun. , vol.49 , pp. 1581-1587
    • Sasmal, P.K.1    Streu, C.N.2    Meggers, E.3
  • 25
    • 84877815387 scopus 로고    scopus 로고
    • Ligand-free palladium-mediated site-specific protein labeling inside gram-negative bacterial pathogens
    • Li. J. et al. Ligand-free palladium-mediated site-specific protein labeling inside gram-negative bacterial pathogens. J. Am. Chem. Soc. 135, 7330-7338 (2013).
    • (2013) J. Am. Chem. Soc. , vol.135 , pp. 7330-7338
    • Li, J.1
  • 26
    • 70450158907 scopus 로고    scopus 로고
    • A convenient catalyst for aqueous and protein Suzuki-Miyaura cross-coupling
    • Chalker, J. M., Wood, C. S. C. & Davis, B. G. A convenient catalyst for aqueous and protein Suzuki-Miyaura cross-coupling. J. Am. Chem. Soc. 131, 16346-16347 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 16346-16347
    • Chalker, J.M.1    Wood, C.S.C.2    Davis, B.G.3
  • 27
    • 53849112496 scopus 로고    scopus 로고
    • Water-mediated catalyst preactivation: An efficient protocol for C-N cross-coupling reactions
    • Fors, B. P., Krattiger, P., Strieter, E. & Buchwald, S. L. Water-mediated catalyst preactivation: An efficient protocol for C-N cross-coupling reactions. Org. Lett. 3505-3508 (2008).
    • (2008) Org. Lett. , pp. 3505-3508
    • Fors, B.P.1    Krattiger, P.2    Strieter, E.3    Buchwald, S.L.4
  • 28
    • 37049122988 scopus 로고
    • Convenient preparation of novel palladium-polefin complexes from bis(dibenzylideneacetone) palladium (0)
    • Ito, T., Takahashi, Y. & Ishii Y. Convenient preparation of novel palladium-polefin complexes from bis(dibenzylideneacetone)palladium(0). Chem. Commun. 629a-629a (1972).
    • (1972) Chem. Commun.
    • Ito, T.1    Takahashi, Y.2    Ishii, Y.3
  • 29
    • 84878113601 scopus 로고    scopus 로고
    • The impact of palladium(II) reduction pathways on the structure and activity of palladium (0) catalysts
    • Wei, C.S. et al. The impact of palladium(II) reduction pathways on the structure and activity of palladium(0) catalysts. Angew. Chem. Int. Ed. 52, 5822-5826 (2013).
    • (2013) Angew. Chem. Int. Ed. , vol.52 , pp. 5822-5826
    • Wei, C.S.1
  • 30
    • 80053319803 scopus 로고    scopus 로고
    • Copper-free Sonogashira crosscoupling for functionalization of alkyne-encoded proteins in aqueous medium and in bacterial cells
    • Li, N., Lim, R. K. V., Edwardraja, S. & Lin, Q. Copper-free Sonogashira crosscoupling for functionalization of alkyne-encoded proteins in aqueous medium and in bacterial cells. J. Am. Chem. Soc. 133, 15316-15319 (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 15316-15319
    • Li, N.1    Lim, R.K.V.2    Edwardraja, S.3    Lin, Q.4
  • 32
    • 0037165964 scopus 로고    scopus 로고
    • A new UAG-encoded residue in the structure of a methanogen methyltransferase
    • Hao, B. et al. A new UAG-encoded residue in the structure of a methanogen methyltransferase. Science 296, 1462-1466 (2002).
    • (2002) Science , vol.296 , pp. 1462-1466
    • Hao, B.1
  • 33
    • 44149083513 scopus 로고    scopus 로고
    • Adding L-lysine derivatives to the genetic code of mammalian cells with engineered pyrrolysyl-TRNA synthetases
    • Mukai T et al. Adding L-lysine derivatives to the genetic code of mammalian cells with engineered pyrrolysyl-TRNA synthetases. Biochem. Biophys. Res. Commun. 371, 818-822 (2008).
    • (2008) Biochem. Biophys. Res. Commun. , vol.371 , pp. 818-822
    • Mukai, T.1
  • 34
    • 77953643054 scopus 로고    scopus 로고
    • Adding new chemistries to the genetic code
    • Liu, C. C. & Schultz, P. G. Adding new chemistries to the genetic code. Annu. Rev. Biochem. 79, 413-444 (2010).
    • (2010) Annu. Rev. Biochem. , vol.79 , pp. 413-444
    • Liu, C.C.1    Schultz, P.G.2
  • 36
    • 67649625295 scopus 로고    scopus 로고
    • Genetic encoding and labeling of aliphatic azides and alkynes in recombinant proteins via a pyrrolysyl-TRNA synthetase/tRNACUA pair and click chemistry
    • Nguyen, D. P. et al. Genetic encoding and labeling of aliphatic azides and alkynes in recombinant proteins via a pyrrolysyl-TRNA synthetase/tRNACUA pair and click chemistry. J. Am. Chem. Soc. 131, 8720-8721 (2009).
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 8720-8721
    • Nguyen, D.P.1
  • 37
    • 80455129305 scopus 로고    scopus 로고
    • Cellular consequences of copper complexes used to catalyze bioorthogonal click reactions
    • Kennedy, D. C. et al. Cellular consequences of copper complexes used to catalyze bioorthogonal click reactions. J. Am. Chem. Soc. 133, 17993-18001 (2011).
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 17993-18001
    • Kennedy, D.C.1
  • 38
    • 33847154642 scopus 로고    scopus 로고
    • The phosphothreonine lyase activity of a bacterial Type III effector family
    • Li, H. et al. The phosphothreonine lyase activity of a bacterial Type III effector family. Science 315, 1000-1003 (2007).
    • (2007) Science , vol.315 , pp. 1000-1003
    • Li, H.1
  • 39
    • 33846958783 scopus 로고    scopus 로고
    • An injected bacterial effector targets chromatin access for transcription factor NF-kB to alter transcription of host genes involved in immune responses
    • Arbibe, L. et al. An injected bacterial effector targets chromatin access for transcription factor NF-kB to alter transcription of host genes involved in immune responses. Nature Immunol. 8, 47-56 (2007).
    • (2007) Nature Immunol. , vol.8 , pp. 47-56
    • Arbibe, L.1
  • 40
    • 36749011295 scopus 로고    scopus 로고
    • Structural insights into the enzymatic mechanism of the pathogenic MAPK phosphothreonine lyase
    • Zhu, Y. et al. Structural insights into the enzymatic mechanism of the pathogenic MAPK phosphothreonine lyase. Mol. Cell 28, 899-913 (2007).
    • (2007) Mol. Cell , vol.28 , pp. 899-913
    • Zhu, Y.1
  • 41
    • 77449122749 scopus 로고    scopus 로고
    • ERK nuclear translocation is dimerization-independent but controlled by the rate of phosphorylation
    • Lidke, D. S. et al. ERK nuclear translocation is dimerization-independent but controlled by the rate of phosphorylation. J. Biol. Chem. 285, 3092-3102 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 3092-3102
    • Lidke, D.S.1
  • 42
    • 0034757776 scopus 로고    scopus 로고
    • The nucleus, a site for signal termination by sequestration and inactivation of p42/p44 MAP kinases
    • Volmat, V., Camps, M., Arkinstall, S., Pouysségur, J. & Lenormand, P. The nucleus, a site for signal termination by sequestration and inactivation of p42/p44 MAP kinases. J. Cell Sci. 114, 3433-3443 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 3433-3443
    • Volmat, V.1    Camps, M.2    Arkinstall, S.3    Pouysségur, J.4    Lenormand, P.5
  • 43
    • 84865135567 scopus 로고    scopus 로고
    • Bacterial virulence proteins as tools to rewire kinase pathways in yeast and immune cells
    • Wei, P. et al. Bacterial virulence proteins as tools to rewire kinase pathways in yeast and immune cells. Nature 488, 384-388 (2012).
    • (2012) Nature , vol.488 , pp. 384-388
    • Wei, P.1
  • 44
    • 9244247669 scopus 로고    scopus 로고
    • Regulation of p53 activity through lysine methylation
    • Chuikov, S. et al. Regulation of p53 activity through lysine methylation. Nature 432, 353-360 (2004).
    • (2004) Nature , vol.432 , pp. 353-360
    • Chuikov, S.1
  • 45
    • 79951816315 scopus 로고    scopus 로고
    • Architects at the bacterial surface-sortases and the assembly of pili with isopeptide bonds
    • Hendrickx, A. P. A., Budzik, J. M., Oh, S-Y. & Schneewind, O. Architects at the bacterial surface-sortases and the assembly of pili with isopeptide bonds. Nature Rev. Micro. 9, 166-176 (2011).
    • (2011) Nature Rev. Micro. , vol.9 , pp. 166-176
    • Hendrickx, A.P.A.1    Budzik, J.M.2    Oh, S.-Y.3    Schneewind, O.4
  • 46
    • 84864770769 scopus 로고    scopus 로고
    • Moving Pd-mediated protein cross coupling to living systems
    • Li, J. & Chen, P. R. Moving Pd-mediated protein cross coupling to living systems. Chembiochem 13, 1728-1731 (2012).
    • (2012) Chembiochem , vol.13 , pp. 1728-1731
    • Li, J.1    Chen, P.R.2


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