메뉴 건너뛰기




Volumn 28, Issue 9, 2010, Pages 468-475

Recent advances in the photochemical control of protein function

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID RESIDUES; BIOLOGICAL LABORATORY; BIOLOGICAL PROCESS; CELLULAR CONTEXTS; PHOTOCHEMICAL CONTROL; PROTEIN FUNCTIONS; REGULATORY ELEMENTS; SMALL MOLECULES; STANDARD EQUIPMENTS; TEMPORAL RESOLUTION;

EID: 77955844090     PISSN: 01677799     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tibtech.2010.06.001     Document Type: Review
Times cited : (107)

References (72)
  • 1
    • 75649114249 scopus 로고    scopus 로고
    • Principles and applications of the photochemical control of cellular processes
    • Deiters A. Principles and applications of the photochemical control of cellular processes. ChemBioChem 2010, 11:47-53.
    • (2010) ChemBioChem , vol.11 , pp. 47-53
    • Deiters, A.1
  • 2
    • 70549102321 scopus 로고    scopus 로고
    • Light activation as a method of regulating and studying gene expression
    • Deiters A. Light activation as a method of regulating and studying gene expression. Curr. Opin. Chem. Biol. 2009, 13:678-686.
    • (2009) Curr. Opin. Chem. Biol. , vol.13 , pp. 678-686
    • Deiters, A.1
  • 3
    • 67649243556 scopus 로고    scopus 로고
    • Illuminating the chemistry of life: design, synthesis, and applications of " caged" and related photoresponsive compounds
    • Lee H.M., et al. Illuminating the chemistry of life: design, synthesis, and applications of " caged" and related photoresponsive compounds. ACS Chem. Biol. 2009, 4:409-427.
    • (2009) ACS Chem. Biol. , vol.4 , pp. 409-427
    • Lee, H.M.1
  • 4
    • 33947504848 scopus 로고    scopus 로고
    • Photochemical control of biological processes
    • Young D.D., Deiters A. Photochemical control of biological processes. Org. Biomol. Chem. 2007, 5:999-1005.
    • (2007) Org. Biomol. Chem. , vol.5 , pp. 999-1005
    • Young, D.D.1    Deiters, A.2
  • 5
    • 33746734322 scopus 로고    scopus 로고
    • Biologically active molecules with a " light switch"
    • Mayer G., Heckel A. Biologically active molecules with a " light switch" Angew. Chem. Int. Ed. 2006, 45:4900-4921.
    • (2006) Angew. Chem. Int. Ed. , vol.45 , pp. 4900-4921
    • Mayer, G.1    Heckel, A.2
  • 6
    • 77951683196 scopus 로고    scopus 로고
    • Oligonucleotide-based tools for studying zebrafish development
    • Shestopalov I.A., Chen J.K. Oligonucleotide-based tools for studying zebrafish development. Zebrafish 2010, 7:31-40.
    • (2010) Zebrafish , vol.7 , pp. 31-40
    • Shestopalov, I.A.1    Chen, J.K.2
  • 7
    • 77955843051 scopus 로고    scopus 로고
    • Light-responsive nucleic acids for the spatiotemporal control of biological processes
    • John Wiley & Sons, G. Mayer (Ed.)
    • Heckel A., Mayer G. Light-responsive nucleic acids for the spatiotemporal control of biological processes. The Chemical Biology of Nucleic Acids 2010, 279-306. John Wiley & Sons. G. Mayer (Ed.).
    • (2010) The Chemical Biology of Nucleic Acids , pp. 279-306
    • Heckel, A.1    Mayer, G.2
  • 8
    • 67249113148 scopus 로고    scopus 로고
    • Caged siRNAs for spatiotemporal control of gene silencing
    • Casey J.P., et al. Caged siRNAs for spatiotemporal control of gene silencing. Mol. Pharm. 2009, 6:669-685.
    • (2009) Mol. Pharm. , vol.6 , pp. 669-685
    • Casey, J.P.1
  • 9
    • 34547863548 scopus 로고    scopus 로고
    • Taking control of gene expression with light-activated oligonucleotides
    • Dmochowski I.J., Tang X. Taking control of gene expression with light-activated oligonucleotides. BioTechniques 2007, 43:161-171.
    • (2007) BioTechniques , vol.43 , pp. 161-171
    • Dmochowski, I.J.1    Tang, X.2
  • 10
    • 33846539799 scopus 로고    scopus 로고
    • Regulating gene expression with light-activated oligonucleotides
    • Tang X., Dmochowski I.J. Regulating gene expression with light-activated oligonucleotides. Mol. Biosyst. 2007, 3:100-110.
    • (2007) Mol. Biosyst. , vol.3 , pp. 100-110
    • Tang, X.1    Dmochowski, I.J.2
  • 11
    • 0027480532 scopus 로고
    • Controlling cell chemistry with caged compounds
    • Adams S.R., Tsien R.Y. Controlling cell chemistry with caged compounds. Annu. Rev. Physiol. 1993, 55:755-784.
    • (1993) Annu. Rev. Physiol. , vol.55 , pp. 755-784
    • Adams, S.R.1    Tsien, R.Y.2
  • 12
    • 33645472593 scopus 로고    scopus 로고
    • 8-Bromo-7-hydroxyquinoline as a photoremovable protecting group for physiological use: mechanism and scope
    • Zhu Y., et al. 8-Bromo-7-hydroxyquinoline as a photoremovable protecting group for physiological use: mechanism and scope. J. Am. Chem. Soc. 2006, 128:4267-4276.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 4267-4276
    • Zhu, Y.1
  • 13
    • 31344464915 scopus 로고    scopus 로고
    • The nitrodibenzofuran chromophore: a new caging group for ultra-efficient photolysis in living cells
    • Momotake A., et al. The nitrodibenzofuran chromophore: a new caging group for ultra-efficient photolysis in living cells. Nat. Methods 2006, 3:35-40.
    • (2006) Nat. Methods , vol.3 , pp. 35-40
    • Momotake, A.1
  • 14
    • 4444300242 scopus 로고    scopus 로고
    • Controlling cellular systems using Bhc-caged compounds
    • Furuta T., Noguchi K. Controlling cellular systems using Bhc-caged compounds. Trends Anal. Chem. 2004, 23:501-509.
    • (2004) Trends Anal. Chem. , vol.23 , pp. 501-509
    • Furuta, T.1    Noguchi, K.2
  • 15
    • 0033574057 scopus 로고    scopus 로고
    • Brominated 7-hydroxycoumarin-4-ylmethyls: photolabile protecting groups with biologically useful cross-sections for two photon photolysis
    • Furuta T., et al. Brominated 7-hydroxycoumarin-4-ylmethyls: photolabile protecting groups with biologically useful cross-sections for two photon photolysis. Proc. Natl. Acad. Sci. U. S. A. 1999, 96:1193-1200.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , pp. 1193-1200
    • Furuta, T.1
  • 16
    • 54249105941 scopus 로고    scopus 로고
    • Surface sites for engineering allosteric control in proteins
    • Lee J., et al. Surface sites for engineering allosteric control in proteins. Science 2008, 322:438-442.
    • (2008) Science , vol.322 , pp. 438-442
    • Lee, J.1
  • 17
    • 76249109093 scopus 로고    scopus 로고
    • Differential regulation of protrusion and polarity by PI3K during neutrophil motility in live zebrafish
    • Yoo S.K., et al. Differential regulation of protrusion and polarity by PI3K during neutrophil motility in live zebrafish. Dev. Cell 2010, 18:226-236.
    • (2010) Dev. Cell , vol.18 , pp. 226-236
    • Yoo, S.K.1
  • 18
    • 69949104482 scopus 로고    scopus 로고
    • A genetically encoded photoactivatable Rac controls the motility of living cells
    • Wu Y.I., et al. A genetically encoded photoactivatable Rac controls the motility of living cells. Nature 2009, 461:104-108.
    • (2009) Nature , vol.461 , pp. 104-108
    • Wu, Y.I.1
  • 19
    • 49449118042 scopus 로고    scopus 로고
    • Light-activated DNA binding in a designed allosteric protein
    • Strickland D., et al. Light-activated DNA binding in a designed allosteric protein. Proc. Natl. Acad. Sci. U. S. A. 2008, 105:10709-10714.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 10709-10714
    • Strickland, D.1
  • 20
    • 67649625533 scopus 로고    scopus 로고
    • Doxycycline-dependent photoactivated gene expression in eukaryotic systems
    • Cambridge S.B., et al. Doxycycline-dependent photoactivated gene expression in eukaryotic systems. Nat. Methods 2009, 6:527-531.
    • (2009) Nat. Methods , vol.6 , pp. 527-531
    • Cambridge, S.B.1
  • 21
    • 0036909269 scopus 로고    scopus 로고
    • Spatially discrete, light-driven protein expression
    • Lin W., et al. Spatially discrete, light-driven protein expression. Chem. Biol. 2002, 9:1347-1353.
    • (2002) Chem. Biol. , vol.9 , pp. 1347-1353
    • Lin, W.1
  • 22
    • 0034644439 scopus 로고    scopus 로고
    • Light-activated gene expression
    • Cruz F.G., et al. Light-activated gene expression. J. Am. Chem. Soc. 2000, 122:8777-8778.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 8777-8778
    • Cruz, F.G.1
  • 23
    • 25444480818 scopus 로고    scopus 로고
    • Light activated recombination
    • Link K.H., et al. Light activated recombination. J. Am. Chem. Soc. 2005, 127:13088-13089.
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 13088-13089
    • Link, K.H.1
  • 24
    • 34447281731 scopus 로고    scopus 로고
    • Photochemical activation of protein expression in bacterial cells
    • Young D.D., Deiters A. Photochemical activation of protein expression in bacterial cells. Angew. Chem. Int. Ed. 2007, 46:4290-4292.
    • (2007) Angew. Chem. Int. Ed. , vol.46 , pp. 4290-4292
    • Young, D.D.1    Deiters, A.2
  • 25
    • 28544442417 scopus 로고    scopus 로고
    • Synthetic biology: engineering Escherichia coli to see light
    • Levskaya A., et al. Synthetic biology: engineering Escherichia coli to see light. Nature 2005, 438:441-442.
    • (2005) Nature , vol.438 , pp. 441-442
    • Levskaya, A.1
  • 26
    • 77949872445 scopus 로고    scopus 로고
    • Light-activated gene expression directs segregation of co-cultured cells in vitro
    • Sauers D.J., et al. Light-activated gene expression directs segregation of co-cultured cells in vitro. ACS Chem. Biol. 2010, 5:313-320.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 313-320
    • Sauers, D.J.1
  • 27
    • 0031740332 scopus 로고    scopus 로고
    • Tetracycline-regulatable factors with distinct dimerization domains allow reversible growth inhibition by p16
    • Rossi F.M., et al. Tetracycline-regulatable factors with distinct dimerization domains allow reversible growth inhibition by p16. Nat. Genet. 1998, 20:389-393.
    • (1998) Nat. Genet. , vol.20 , pp. 389-393
    • Rossi, F.M.1
  • 28
    • 70450207816 scopus 로고    scopus 로고
    • New photochemical tools for controlling neuronal activity
    • Kramer R.H., et al. New photochemical tools for controlling neuronal activity. Curr. Opin. Neurobiol. 2009, 19:544-552.
    • (2009) Curr. Opin. Neurobiol. , vol.19 , pp. 544-552
    • Kramer, R.H.1
  • 30
    • 23644461168 scopus 로고    scopus 로고
    • Synthesis of a caged glutamate for efficient one- and two-photon photorelease on living cells
    • Fedoryak O.D., et al. Synthesis of a caged glutamate for efficient one- and two-photon photorelease on living cells. Chem. Commun. 2005, 29:3664-3666.
    • (2005) Chem. Commun. , vol.29 , pp. 3664-3666
    • Fedoryak, O.D.1
  • 31
    • 0027220694 scopus 로고
    • Photostimulation using caged glutamate reveals functional circuitry in living brain slices
    • Callaway E.M., Katz L.C. Photostimulation using caged glutamate reveals functional circuitry in living brain slices. Proc. Natl. Acad. Sci. U. S. A. 1993, 90:7661-7665.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 7661-7665
    • Callaway, E.M.1    Katz, L.C.2
  • 32
    • 44849095806 scopus 로고    scopus 로고
    • Neurobiology with caged calcium
    • Ellis-Davies G.C. Neurobiology with caged calcium. Chem. Rev. 2008, 108:1603-1613.
    • (2008) Chem. Rev. , vol.108 , pp. 1603-1613
    • Ellis-Davies, G.C.1
  • 33
    • 0034816479 scopus 로고    scopus 로고
    • Incorporation of caged cysteine and caged tyrosine into a transmembrane segment of the nicotinic ACh receptor
    • Philipson K.D., et al. Incorporation of caged cysteine and caged tyrosine into a transmembrane segment of the nicotinic ACh receptor. Am. J. Physiol. Cell Physiol. 2001, 281:C195-206.
    • (2001) Am. J. Physiol. Cell Physiol. , vol.281
    • Philipson, K.D.1
  • 34
    • 12344309164 scopus 로고    scopus 로고
    • Light-activated ion channels for remote control of neuronal firing
    • Banghart M., et al. Light-activated ion channels for remote control of neuronal firing. Nat. Neurosci. 2004, 1381-1386.
    • (2004) Nat. Neurosci. , pp. 1381-1386
    • Banghart, M.1
  • 35
    • 33645218213 scopus 로고    scopus 로고
    • Allosteric control of an ionotropic glutamate receptor with an optical switch
    • Volgraf M., et al. Allosteric control of an ionotropic glutamate receptor with an optical switch. Nat. Chem. Biol. 2006, 2:47-52.
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 47-52
    • Volgraf, M.1
  • 36
    • 34247222730 scopus 로고    scopus 로고
    • Multimodal fast optical interrogation of neural circuitry
    • Zhang F., et al. Multimodal fast optical interrogation of neural circuitry. Nature 2007, 446:633-639.
    • (2007) Nature , vol.446 , pp. 633-639
    • Zhang, F.1
  • 37
    • 0029310574 scopus 로고
    • A photogenerated pore-forming protein
    • Chang C.Y., et al. A photogenerated pore-forming protein. Chem. Biol. 1995, 2:391-400.
    • (1995) Chem. Biol. , vol.2 , pp. 391-400
    • Chang, C.Y.1
  • 38
    • 33845685983 scopus 로고    scopus 로고
    • Optogenetics. Shining new light on neural circuits
    • Miller G. Optogenetics. Shining new light on neural circuits. Science 2006, 314:1674-1676.
    • (2006) Science , vol.314 , pp. 1674-1676
    • Miller, G.1
  • 39
    • 70350104716 scopus 로고    scopus 로고
    • The optogenetic catechism
    • Miesenbock G. The optogenetic catechism. Science 2009, 326:395-399.
    • (2009) Science , vol.326 , pp. 395-399
    • Miesenbock, G.1
  • 40
    • 77749323191 scopus 로고    scopus 로고
    • Optogenetic interrogation of neural circuits: technology for probing mammalian brain structures
    • Zhang F., et al. Optogenetic interrogation of neural circuits: technology for probing mammalian brain structures. Nat. Protoc. 2010, 5:439-456.
    • (2010) Nat. Protoc. , vol.5 , pp. 439-456
    • Zhang, F.1
  • 41
    • 65249126727 scopus 로고    scopus 로고
    • The dawning of primate optogenetics
    • Berdyyeva T.K., Reynolds J.H. The dawning of primate optogenetics. Neuron 2009, 62:159-160.
    • (2009) Neuron , vol.62 , pp. 159-160
    • Berdyyeva, T.K.1    Reynolds, J.H.2
  • 42
    • 41449113929 scopus 로고    scopus 로고
    • Photochemical control of endogenous ion channels and cellular excitability
    • Fortin D.L., et al. Photochemical control of endogenous ion channels and cellular excitability. Nat. Methods 2008, 5:331-338.
    • (2008) Nat. Methods , vol.5 , pp. 331-338
    • Fortin, D.L.1
  • 44
    • 27744567862 scopus 로고    scopus 로고
    • The preparation and in vivo applications of caged peptides and proteins
    • Lawrence D.S. The preparation and in vivo applications of caged peptides and proteins. Curr. Opin. Chem. Biol. 2005, 9:570-575.
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 570-575
    • Lawrence, D.S.1
  • 45
    • 0037274664 scopus 로고    scopus 로고
    • Caging proteins through unnatural amino acid mutagenesis
    • Petersson E.J., et al. Caging proteins through unnatural amino acid mutagenesis. Methods Enzymol. 2003, 360:258-273.
    • (2003) Methods Enzymol. , vol.360 , pp. 258-273
    • Petersson, E.J.1
  • 46
    • 54749102251 scopus 로고    scopus 로고
    • Activation of protein splicing by protease- or light-triggered O to N acyl migration
    • Vila-Perelló M., et al. Activation of protein splicing by protease- or light-triggered O to N acyl migration. Angew. Chem. Int. Ed. Engl. 2008, 47:7764-7767.
    • (2008) Angew. Chem. Int. Ed. Engl. , vol.47 , pp. 7764-7767
    • Vila-Perelló, M.1
  • 47
    • 77952977698 scopus 로고    scopus 로고
    • Photocontrol of coiled-coil proteins in living cells
    • Zhang F., et al. Photocontrol of coiled-coil proteins in living cells. Angew. Chem. Int. Ed. Engl. 2010, 49:3943-3946.
    • (2010) Angew. Chem. Int. Ed. Engl. , vol.49 , pp. 3943-3946
    • Zhang, F.1
  • 48
    • 27744485401 scopus 로고    scopus 로고
    • Adding amino acids to the genetic repertoire
    • Xie J., Schultz P.G. Adding amino acids to the genetic repertoire. Curr. Opin. Chem. Biol. 2005, 9:548-554.
    • (2005) Curr. Opin. Chem. Biol. , vol.9 , pp. 548-554
    • Xie, J.1    Schultz, P.G.2
  • 50
    • 7444263987 scopus 로고    scopus 로고
    • An expanding genetic code
    • Cropp T.A., Schultz P.G. An expanding genetic code. Trends Genet. 2004, 20:625-630.
    • (2004) Trends Genet. , vol.20 , pp. 625-630
    • Cropp, T.A.1    Schultz, P.G.2
  • 51
    • 77951755582 scopus 로고    scopus 로고
    • Photocaged T7 RNA polymerase for the light activation of transcription and gene function in pro- and eukaryotic cells
    • Chou C., et al. Photocaged T7 RNA polymerase for the light activation of transcription and gene function in pro- and eukaryotic cells. ChemBioChem 2010, 11:972-977.
    • (2010) ChemBioChem , vol.11 , pp. 972-977
    • Chou, C.1
  • 52
    • 70349902858 scopus 로고    scopus 로고
    • A light-activated DNA polymerase
    • Chou C., et al. A light-activated DNA polymerase. Angew. Chem. Int. Ed. 2009, 48:5950-5953.
    • (2009) Angew. Chem. Int. Ed. , vol.48 , pp. 5950-5953
    • Chou, C.1
  • 53
    • 67649280374 scopus 로고    scopus 로고
    • Light-activated Cre recombinase as a tool for the spatial and temporal control of gene function in mammalian cells
    • Edwards W.F., et al. Light-activated Cre recombinase as a tool for the spatial and temporal control of gene function in mammalian cells. ACS Chem. Biol. 2009, 4:441-445.
    • (2009) ACS Chem. Biol. , vol.4 , pp. 441-445
    • Edwards, W.F.1
  • 54
    • 33746044574 scopus 로고    scopus 로고
    • A genetically encoded photocaged tyrosine
    • Deiters A., et al. A genetically encoded photocaged tyrosine. Angew. Chem. Int. Ed. 2006, 45:2728-2731.
    • (2006) Angew. Chem. Int. Ed. , vol.45 , pp. 2728-2731
    • Deiters, A.1
  • 55
    • 7744222751 scopus 로고    scopus 로고
    • A genetically encoded photocaged amino acid
    • Wu N., et al. A genetically encoded photocaged amino acid. J. Am. Chem. Soc. 2004, 126:14306-14307.
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 14306-14307
    • Wu, N.1
  • 56
    • 36249000015 scopus 로고    scopus 로고
    • Control of protein phosphorylation with a genetically encoded photocaged amino acid
    • Lemke E.A., et al. Control of protein phosphorylation with a genetically encoded photocaged amino acid. Nat. Chem. Biol. 2007, 3:769-772.
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 769-772
    • Lemke, E.A.1
  • 57
    • 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. 2009, 48:4052-4055.
    • (2009) Angew. Chem. Int. Ed. , vol.48 , pp. 4052-4055
    • Chen, P.R.1
  • 58
    • 77950279568 scopus 로고    scopus 로고
    • Genetically encoded photo-control of protein localization in mammalian cells
    • Gautier A., et al. Genetically encoded photo-control of protein localization in mammalian cells. J. Am. Chem. Soc. 2010, 132:4086-4088.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 4086-4088
    • Gautier, A.1
  • 59
    • 40949099577 scopus 로고    scopus 로고
    • e{open}-acetyllysine in recombinant proteins
    • e{open}-acetyllysine in recombinant proteins. Nat. Chem. Biol. 2008, 4:232-234.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 232-234
    • Neumann, H.1
  • 60
    • 0036016438 scopus 로고    scopus 로고
    • Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch
    • Crosson S., Moffat K. Photoexcited structure of a plant photoreceptor domain reveals a light-driven molecular switch. Plant Cell 2002, 14:1067-1075.
    • (2002) Plant Cell , vol.14 , pp. 1067-1075
    • Crosson, S.1    Moffat, K.2
  • 61
    • 58549105950 scopus 로고    scopus 로고
    • Design and signaling mechanism of light-regulated histidine kinases
    • Moglich A., et al. Design and signaling mechanism of light-regulated histidine kinases. J. Mol. Biol. 2009, 385:1433-1444.
    • (2009) J. Mol. Biol. , vol.385 , pp. 1433-1444
    • Moglich, A.1
  • 62
    • 0036484368 scopus 로고    scopus 로고
    • Phytochrome photosensory signalling networks
    • Quail P.H. Phytochrome photosensory signalling networks. Nat. Rev. Mol. Cell Biol. 2002, 3:85-93.
    • (2002) Nat. Rev. Mol. Cell Biol. , vol.3 , pp. 85-93
    • Quail, P.H.1
  • 63
    • 0033584359 scopus 로고    scopus 로고
    • Binding of phytochrome B to its nuclear signalling partner PIF3 is reversibly induced by light
    • Ni M., et al. Binding of phytochrome B to its nuclear signalling partner PIF3 is reversibly induced by light. Nature 1999, 400:781-784.
    • (1999) Nature , vol.400 , pp. 781-784
    • Ni, M.1
  • 64
    • 76649121542 scopus 로고    scopus 로고
    • Reversible light switching of cell signalling by genetically encoded protein dimerization
    • Georgianna W.E., Deiters A. Reversible light switching of cell signalling by genetically encoded protein dimerization. ChemBioChem 2010, 11:301-303.
    • (2010) ChemBioChem , vol.11 , pp. 301-303
    • Georgianna, W.E.1    Deiters, A.2
  • 65
    • 67549145283 scopus 로고    scopus 로고
    • A synthetic edge detection program
    • Tabor J.J., et al. A synthetic edge detection program. Cell 2009, 137:1272-1281.
    • (2009) Cell , vol.137 , pp. 1272-1281
    • Tabor, J.J.1
  • 66
    • 53749091743 scopus 로고    scopus 로고
    • Bacterial bilin- and flavin-binding photoreceptors
    • Losi A., Gartner W. Bacterial bilin- and flavin-binding photoreceptors. Photochem. Photobiol. Sci. 2008, 7:1168-1178.
    • (2008) Photochem. Photobiol. Sci. , vol.7 , pp. 1168-1178
    • Losi, A.1    Gartner, W.2
  • 67
    • 0036789439 scopus 로고    scopus 로고
    • A light-switchable gene promoter system
    • Shimizu-Sato S., et al. A light-switchable gene promoter system. Nat. Biotechnol. 2002, 20:1041-1044.
    • (2002) Nat. Biotechnol. , vol.20 , pp. 1041-1044
    • Shimizu-Sato, S.1
  • 68
    • 70350070364 scopus 로고    scopus 로고
    • Spatiotemporal control of cell signalling using a light-switchable protein interaction
    • Levskaya A., et al. Spatiotemporal control of cell signalling using a light-switchable protein interaction. Nature 2009, 461:997-1001.
    • (2009) Nature , vol.461 , pp. 997-1001
    • Levskaya, A.1
  • 69
    • 41449091908 scopus 로고    scopus 로고
    • Activation of protein splicing with light in yeast
    • Tyszkiewicz A.B., Muir T.W. Activation of protein splicing with light in yeast. Nat. Methods 2008, 5:303-305.
    • (2008) Nat. Methods , vol.5 , pp. 303-305
    • Tyszkiewicz, A.B.1    Muir, T.W.2
  • 70
    • 77949872727 scopus 로고    scopus 로고
    • Two-photon uncaging of gamma-aminobutyric acid in intact brain tissue
    • Matsuzaki M., et al. Two-photon uncaging of gamma-aminobutyric acid in intact brain tissue. Nat. Chem. Biol. 2010, 6:255-257.
    • (2010) Nat. Chem. Biol. , vol.6 , pp. 255-257
    • Matsuzaki, M.1
  • 71
    • 36749078085 scopus 로고    scopus 로고
    • 2+-sensor model for neurotransmitter release in a central synapse
    • 2+-sensor model for neurotransmitter release in a central synapse. Nature 2007, 450:676-682.
    • (2007) Nature , vol.450 , pp. 676-682
    • Sun, J.1
  • 72
    • 70350746490 scopus 로고    scopus 로고
    • Astrocyte-mediated distributed plasticity at hypothalamic glutamate synapses
    • Gordon G.R., et al. Astrocyte-mediated distributed plasticity at hypothalamic glutamate synapses. Neuron 2009, 64:391-403.
    • (2009) Neuron , vol.64 , pp. 391-403
    • Gordon, G.R.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.