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Volumn 8, Issue 12, 2011, Pages 1083-1091

A gene-fusion strategy for stoichiometric and co-localized expression of light-gated membrane proteins

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; HALORHODOPSIN; LIGHT GATED MEMBRANE PROTEIN; MEMBRANE PROTEIN; RHODOPSIN; UNCLASSIFIED DRUG;

EID: 82355175134     PISSN: 15487091     EISSN: 15491676     Source Type: Journal    
DOI: 10.1038/nmeth.1766     Document Type: Article
Times cited : (73)

References (34)
  • 1
    • 29044433616 scopus 로고    scopus 로고
    • Light activation of Channelrhodopsin-2 in excitable cells of caenorhabditis elegans triggers rapid behavioral responses
    • DOI 10.1016/j.cub.2005.11.032, PII S0960982205014077
    • Nagel, G. et al. Light activation of channelrhodopsin-2 in excitable cells of Caenorhabditis elegans triggers rapid behavioral responses. Curr. Biol. 15, 2279-2284 (2005). (Pubitemid 41790623)
    • (2005) Current Biology , vol.15 , Issue.24 , pp. 2279-2284
    • Nagel, G.1    Brauner, M.2    Liewald, J.F.3    Adeishvili, N.4    Bamberg, E.5    Gottschalk, A.6
  • 2
    • 55849136898 scopus 로고    scopus 로고
    • Multiple-color optical activation, silencing, and desynchronization of neural activity, with single-spike temporal resolution
    • Han, X. & Boyden, E. Multiple-color optical activation, silencing, and desynchronization of neural activity, with single-spike temporal resolution. PLoS ONE 2, e299 (2007).
    • (2007) PLoS ONE , vol.2
    • Han, X.1    Boyden, E.2
  • 4
    • 13244262697 scopus 로고    scopus 로고
    • Use and comparison of different internal ribosomal entry sites (IRES) in tricistronic retroviral vectors
    • Douin, V. et al. Use and comparison of different internal ribosomal entry sites (IRES) in tricistronic retroviral vectors. BMC Biotechnol. 4, 16 (2004).
    • (2004) BMC Biotechnol. , vol.4 , pp. 16
    • Douin, V.1
  • 5
    • 77950935182 scopus 로고    scopus 로고
    • Informational lesions: Optical perturbation of spike timing and neural synchrony via microbial opsin gene fusions
    • Han, X., Qian, X., Stern, P., Chuong, A. & Boyden, E. Informational lesions: optical perturbation of spike timing and neural synchrony via microbial opsin gene fusions. Front. Mol. Neurosci. 2, 12 (2009).
    • (2009) Front. Mol. Neurosci. , vol.2 , pp. 12
    • Han, X.1    Qian, X.2    Stern, P.3    Chuong, A.4    Boyden, E.5
  • 6
    • 67650487803 scopus 로고    scopus 로고
    • Faithful expression of multiple proteins via 2A-peptide self-processing: A versatile and reliable method for manipulating brain circuits
    • Tang, W. et al. Faithful expression of multiple proteins via 2A-peptide self-processing: a versatile and reliable method for manipulating brain circuits. J. Neurosci. 29, 8621-8629 (2009).
    • (2009) J. Neurosci. , vol.29 , pp. 8621-8629
    • Tang, W.1
  • 8
    • 77950930288 scopus 로고    scopus 로고
    • Molecular and cellular approaches for diversifying and extending optogenetics
    • Gradinaru, V. et al. Molecular and cellular approaches for diversifying and extending optogenetics. Cell 141, 154-165 (2009).
    • (2009) Cell , vol.141 , pp. 154-165
    • Gradinaru, V.1
  • 9
    • 0034805052 scopus 로고    scopus 로고
    • The voltage-dependent proton pumping in bacteriorhodopsin is characterized by optoelectric behavior
    • Geibel, S. et al. The voltage-dependent proton pumping in bacteriorhodopsin is characterized by optoelectic behavior. Biophys. J. 81, 2059-2068 (2001). (Pubitemid 32917156)
    • (2001) Biophysical Journal , vol.81 , Issue.4 , pp. 2059-2068
    • Geibel, S.1    Friedrich, T.2    Ormos, P.3    Wood, P.G.4    Nagel, G.5    Bamberg, E.6
  • 11
    • 0029591347 scopus 로고
    • + pumping
    • DOI 10.1016/0014-5793(95)01356-3
    • Nagel, G., Möckel, B., Büldt, G. & Bamberg, E. Functional expression of bacteriorhodopsin in oocytes allows direct measurement of voltage dependence of light induced H+ pumping. FEBS Lett. 377, 263-266 (1995). (Pubitemid 26015079)
    • (1995) FEBS Letters , vol.377 , Issue.2 , pp. 263-266
    • Nagel, G.1    Mockel, B.2    Buldt, G.3    Bamberg, E.4
  • 13
    • 68149145775 scopus 로고    scopus 로고
    • Channelrhodopsin-2 is a leaky proton pump
    • Feldbauer, K. et al. Channelrhodopsin-2 is a leaky proton pump. Proc. Natl. Acad. Sci. USA 106, 12317-12322 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 12317-12322
    • Feldbauer, K.1
  • 15
    • 75349085542 scopus 로고    scopus 로고
    • Structural guidance of the photocycle of channelrhodopsin-2 by an interhelical hydrogen bond
    • Bamann, C., Gueta, R., Kleinlogel, S., Nagel, G. & Bamberg, E. Structural guidance of the photocycle of channelrhodopsin-2 by an interhelical hydrogen bond. Biochemistry 49, 267-278 (2010).
    • (2010) Biochemistry , vol.49 , pp. 267-278
    • Bamann, C.1    Gueta, R.2    Kleinlogel, S.3    Nagel, G.4    Bamberg, E.5
  • 18
    • 0034874537 scopus 로고    scopus 로고
    • Temperature and halide dependence of the photocycle of halorhodopsin from Natronobacterium pharaonis
    • Chizhov, I. & Engelhard, M. Temperature and halide dependence of the photocycle of halorhodopsin from Natronobacterium pharaonis. Biophys. J. 81, 1600-1612 (2001). (Pubitemid 32783600)
    • (2001) Biophysical Journal , vol.81 , Issue.3 , pp. 1600-1612
    • Chizhov, I.1    Engelhard, M.2
  • 19
    • 0022484888 scopus 로고
    • Halorhodopsin: A light-driven chloride ion pump
    • Lanyi, J. Halorhodopsin: A light-driven chloride ion pump. Annu. Rev. Biophys. Biophys. Chem. 15, 11-28 (1986).
    • (1986) Annu. Rev. Biophys. Biophys. Chem. , vol.15 , pp. 11-28
    • Lanyi, J.1
  • 20
    • 0016811990 scopus 로고
    • Flash photometric experiments on the photochemical cycle of bacteriorhodopsin
    • Dencher, N. & Wilms, M. Flash photometric experiments on the photochemical cycle of bacteriorhodopsin. Biophys. Struct. Mech. 1, 259-271 (1975).
    • (1975) Biophys. Struct. Mech. , vol.1 , pp. 259-271
    • Dencher, N.1    Wilms, M.2
  • 21
    • 73849143150 scopus 로고    scopus 로고
    • High-performance genetically targetable optical neural silencing by light-driven proton pumps
    • Chow, B. et al. High-performance genetically targetable optical neural silencing by light-driven proton pumps. Nature 463, 98-102 (2010).
    • (2010) Nature , vol.463 , pp. 98-102
    • Chow, B.1
  • 22
    • 79953230429 scopus 로고    scopus 로고
    • 2+-permeable channelrhodopsin CatCh
    • 2+-permeable channelrhodopsin CatCh. Nat. Neurosci. 14, 513-518 (2011).
    • (2011) Nat. Neurosci. , vol.14 , pp. 513-518
    • Kleinlogel, S.1
  • 23
    • 0029780351 scopus 로고    scopus 로고
    • The molecular structure of green fluorescent protein
    • Yang, F., Moss, L. & Phillips, G. The molecular structure of green fluorescent protein. Nat. Biotechnol. 14, 1246-1251 (1996). (Pubitemid 26332784)
    • (1996) Nature Biotechnology , vol.14 , Issue.10 , pp. 1246-1251
    • Yang, F.1    Moss, L.G.2    Phillips Jr., G.N.3
  • 24
    • 0037072602 scopus 로고    scopus 로고
    • A photoactivatable GFP for selective photolabeling of proteins and cells
    • DOI 10.1126/science.1074952
    • Patterson, G. & Lippincott-Schwartz, J. A photoactivatable GFP for selective photolabeling of proteins and cells. Science 297, 1873-1877 (2002). (Pubitemid 35024347)
    • (2002) Science , vol.297 , Issue.5588 , pp. 1873-1877
    • Patterson, G.H.1    Lippincott-Schwartz, J.2
  • 26
    • 0034957766 scopus 로고    scopus 로고
    • Static and time-resolved step-scan fourier transform infrared investigations of the photoreaction of halorhodopsin from Natronobacterium pharaonis: Consequences for models of the anion translocation mechanism
    • Hackmann, C. et al. Static and time-resolved step-scan Fourier transform infrared investigations of the photoreaction of halorhodopsin from Natronobacterium pharaonis: consequences for models of the anion translocation mechanism. Biophys. J. 81, 394-406 (2001). (Pubitemid 32605979)
    • (2001) Biophysical Journal , vol.81 , Issue.1 , pp. 394-406
    • Hackmann, C.1    Guijarro, J.2    Chizhov, I.3    Engelhard, M.4    Rodig, C.5    Siebert, F.6
  • 27
    • 0022369592 scopus 로고
    • The transport activity of the light-driven chloride pump halorhodopsin is regulated by green and blue light
    • DOI 10.1016/0005-2736(85)90174-9
    • Hegemann, P., Oesterhelt, D. & Bamberg, E. The transport activity of the light-driven chloride pump halorhodopsin is regulated by green and blue light. Biochim. Biophys. Acta 819, 195-205 (1985). (Pubitemid 16238672)
    • (1985) Biochimica et Biophysica Acta - Biomembranes , vol.819 , Issue.2 , pp. 195-205
    • Hegemann, P.1    Oesterhelt, D.2    Bamberg, E.3
  • 28
    • 57649231182 scopus 로고    scopus 로고
    • A crystallographic study of bright far-red fluorescent protein mKate reveals pH-induced cis-trans isomerization of the chromophore
    • Pletnev, S. et al. A crystallographic study of bright far-red fluorescent protein mKate reveals pH-induced cis-trans isomerization of the chromophore. J. Biol. Chem. 283, 28980-28987 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 28980-28987
    • Pletnev, S.1
  • 32
    • 34147126914 scopus 로고    scopus 로고
    • In vivo light-induced activation of neural circuitry in transgenic mice expressing channelrhodopsin-2
    • Arenkiel, B. et al. In vivo light-induced activation of neural circuitry in transgenic mice expressing channelrhodopsin-2. Neuron 54, 205 (2007).
    • (2007) Neuron , vol.54 , pp. 205
    • Arenkiel, B.1
  • 33
    • 77954408920 scopus 로고    scopus 로고
    • Visual function in mice with photoreceptor degeneration and transgenic expression of channelrhodopsin 2 in ganglion cells
    • Thyagarajan, S. et al. Visual function in mice with photoreceptor degeneration and transgenic expression of channelrhodopsin 2 in ganglion cells. J. Neurosci. 30, 8745 (2010).
    • (2010) J. Neurosci. , vol.30 , pp. 8745
    • Thyagarajan, S.1
  • 34
    • 41149162022 scopus 로고    scopus 로고
    • Effects on capacitance by overexpression of membrane proteins
    • Zimmermann, D. et al. Effects on capacitance by overexpression of membrane proteins. Biochem. Biophys. Res. Commun. 369, 1022-1026 (2008).
    • (2008) Biochem. Biophys. Res. Commun. , vol.369 , pp. 1022-1026
    • Zimmermann, D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.