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Volumn 14, Issue 11, 2006, Pages 480-487

The multitalented microbial sensory rhodopsins

Author keywords

[No Author keywords available]

Indexed keywords

CHEA KINASE; ION CHANNEL; MEMBRANE RECEPTOR; RETINAL; SCHIFF BASE; SENSORY RHODOPSIN;

EID: 33749580770     PISSN: 0966842X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tim.2006.09.005     Document Type: Review
Times cited : (161)

References (69)
  • 1
    • 0020320163 scopus 로고
    • Control of transmembrane ion fluxes to select halorhodopsin-deficient and other energy transduction mutants of Halobacterium halobium
    • Spudich E.N., and Spudich J.L. Control of transmembrane ion fluxes to select halorhodopsin-deficient and other energy transduction mutants of Halobacterium halobium. Proc. Natl. Acad. Sci. U. S. A. 79 (1982) 4308-4312
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 4308-4312
    • Spudich, E.N.1    Spudich, J.L.2
  • 2
    • 0000373165 scopus 로고
    • Identification of a third rhodopsin-like pigment in phototactic Halobacterium halobium
    • Bogomolni R.A., and Spudich J.L. Identification of a third rhodopsin-like pigment in phototactic Halobacterium halobium. Proc. Natl. Acad. Sci. U. S. A. 79 (1982) 6250-6254
    • (1982) Proc. Natl. Acad. Sci. U. S. A. , vol.79 , pp. 6250-6254
    • Bogomolni, R.A.1    Spudich, J.L.2
  • 4
    • 0034519206 scopus 로고    scopus 로고
    • Retinylidene proteins: structures and functions from Archaea to humans
    • Spudich J.L., et al. Retinylidene proteins: structures and functions from Archaea to humans. Annu. Rev. Cell Dev. Biol. 16 (2000) 365-392
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 365-392
    • Spudich, J.L.1
  • 5
    • 1842531691 scopus 로고    scopus 로고
    • New insights into the evolutionary history of type 1 rhodopsins
    • Ruiz-Gonzalez M.X., and Marin I. New insights into the evolutionary history of type 1 rhodopsins. J. Mol. Evol. 58 (2004) 348-358
    • (2004) J. Mol. Evol. , vol.58 , pp. 348-358
    • Ruiz-Gonzalez, M.X.1    Marin, I.2
  • 6
    • 84889439782 scopus 로고    scopus 로고
    • Microbial rhodopsins: phylogenetic and functional diversity
    • Briggs W., and Spudich J.L. (Eds), Wiley-VCH
    • Spudich J.L., and Jung K.-H. Microbial rhodopsins: phylogenetic and functional diversity. In: Briggs W., and Spudich J.L. (Eds). Handbook of Photosensory Receptors (2005), Wiley-VCH 1-24
    • (2005) Handbook of Photosensory Receptors , pp. 1-24
    • Spudich, J.L.1    Jung, K.-H.2
  • 7
    • 3242797479 scopus 로고    scopus 로고
    • Fungal rhodopsins and opsin-related proteins: eukaryotic homologues of bacteriorhodopsin with unknown functions
    • Brown L.S. Fungal rhodopsins and opsin-related proteins: eukaryotic homologues of bacteriorhodopsin with unknown functions. Photochem. Photobiol. Sci. 3 (2004) 555-565
    • (2004) Photochem. Photobiol. Sci. , vol.3 , pp. 555-565
    • Brown, L.S.1
  • 8
    • 33749557420 scopus 로고    scopus 로고
    • Microbial rhodopsins: functional versatility plus genetic mobility
    • Sharma A.K., et al. Microbial rhodopsins: functional versatility plus genetic mobility. Trends Microbiol. 14 (2006) 463-469
    • (2006) Trends Microbiol. , vol.14 , pp. 463-469
    • Sharma, A.K.1
  • 9
    • 0030906654 scopus 로고    scopus 로고
    • Molecular mechanism of photosignaling by archaeal sensory rhodopsins
    • Hoff W.D., et al. Molecular mechanism of photosignaling by archaeal sensory rhodopsins. Annu. Rev. Biophys. Biomol. Struct. 26 (1997) 223-258
    • (1997) Annu. Rev. Biophys. Biomol. Struct. , vol.26 , pp. 223-258
    • Hoff, W.D.1
  • 10
    • 0035498353 scopus 로고    scopus 로고
    • Photochemistry and photoinduced proton-transfer by pharaonis phoborhodopsin
    • Kamo N., et al. Photochemistry and photoinduced proton-transfer by pharaonis phoborhodopsin. Biochemistry (Mosc.) 66 (2001) 1277-1282
    • (2001) Biochemistry (Mosc.) , vol.66 , pp. 1277-1282
    • Kamo, N.1
  • 11
    • 1942436349 scopus 로고    scopus 로고
    • The archaeal sensory rhodopsin II/transducer complex: a model for transmembrane signal transfer
    • Klare J.P., et al. The archaeal sensory rhodopsin II/transducer complex: a model for transmembrane signal transfer. FEBS Lett. 564 (2004) 219-224
    • (2004) FEBS Lett. , vol.564 , pp. 219-224
    • Klare, J.P.1
  • 12
    • 0021756564 scopus 로고
    • The mechanism of colour discrimination by a bacterial sensory rhodopsin
    • Spudich J.L., and Bogomolni R.A. The mechanism of colour discrimination by a bacterial sensory rhodopsin. Nature 312 (1984) 509-513
    • (1984) Nature , vol.312 , pp. 509-513
    • Spudich, J.L.1    Bogomolni, R.A.2
  • 13
    • 29144485325 scopus 로고    scopus 로고
    • The genome of Salinibacter ruber: convergence and gene exchange among hyperhalophilic bacteria and archaea
    • Mongodin E.F., et al. The genome of Salinibacter ruber: convergence and gene exchange among hyperhalophilic bacteria and archaea. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 18147-18152
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 18147-18152
    • Mongodin, E.F.1
  • 14
    • 25444463058 scopus 로고    scopus 로고
    • Xanthorhodopsin: a proton pump with a light-harvesting carotenoid antenna
    • Balashov S.P., et al. Xanthorhodopsin: a proton pump with a light-harvesting carotenoid antenna. Science 309 (2005) 2061-2064
    • (2005) Science , vol.309 , pp. 2061-2064
    • Balashov, S.P.1
  • 15
    • 0035943457 scopus 로고    scopus 로고
    • Crystal structure of sensory rhodopsin II at 2.4 Å: insights into color tuning and transducer interaction
    • Luecke H., et al. Crystal structure of sensory rhodopsin II at 2.4 Å: insights into color tuning and transducer interaction. Science 293 (2001) 1499-1503
    • (2001) Science , vol.293 , pp. 1499-1503
    • Luecke, H.1
  • 16
    • 0035964365 scopus 로고    scopus 로고
    • X-ray structure of sensory rhodopsin II at 2.1-Å resolution
    • Royant A., et al. X-ray structure of sensory rhodopsin II at 2.1-Å resolution. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 10131-10136
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 10131-10136
    • Royant, A.1
  • 17
    • 0141592427 scopus 로고    scopus 로고
    • Conformational changes detected in a sensory rhodopsin II-transducer complex
    • Bergo V., et al. Conformational changes detected in a sensory rhodopsin II-transducer complex. J. Biol. Chem. 278 (2003) 36556-36562
    • (2003) J. Biol. Chem. , vol.278 , pp. 36556-36562
    • Bergo, V.1
  • 18
    • 0345492028 scopus 로고    scopus 로고
    • Hydrogen bonding alteration of Thr-204 in the complex between pharaonis phoborhodopsin and its transducer protein
    • Sudo Y., et al. Hydrogen bonding alteration of Thr-204 in the complex between pharaonis phoborhodopsin and its transducer protein. Biochemistry 42 (2003) 14166-14172
    • (2003) Biochemistry , vol.42 , pp. 14166-14172
    • Sudo, Y.1
  • 19
    • 0942268923 scopus 로고    scopus 로고
    • Consequences of counterion mutation in sensory rhodopsin II of Natronobacterium pharaonis for photoreaction and receptor activation: an FTIR study
    • Hein M., et al. Consequences of counterion mutation in sensory rhodopsin II of Natronobacterium pharaonis for photoreaction and receptor activation: an FTIR study. Biochemistry 43 (2004) 995-1002
    • (2004) Biochemistry , vol.43 , pp. 995-1002
    • Hein, M.1
  • 20
    • 14344261575 scopus 로고    scopus 로고
    • Structural changes of the complex between pharaonis phoborhodopsin and its cognate transducer upon formation of the M photointermediate
    • Furutani Y., et al. Structural changes of the complex between pharaonis phoborhodopsin and its cognate transducer upon formation of the M photointermediate. Biochemistry 44 (2005) 2909-2915
    • (2005) Biochemistry , vol.44 , pp. 2909-2915
    • Furutani, Y.1
  • 21
    • 33645913545 scopus 로고    scopus 로고
    • Temperature-dependent interactions between photoactivated pharaonis phoborhodopsin and its transducer
    • Kamada K., et al. Temperature-dependent interactions between photoactivated pharaonis phoborhodopsin and its transducer. Biochemistry 45 (2006) 4859-4866
    • (2006) Biochemistry , vol.45 , pp. 4859-4866
    • Kamada, K.1
  • 22
    • 23344432363 scopus 로고    scopus 로고
    • Photoactivation perturbs the membrane-embedded contacts between sensory rhodopsin II and its transducer
    • Bergo V.B., et al. Photoactivation perturbs the membrane-embedded contacts between sensory rhodopsin II and its transducer. J. Biol. Chem. 280 (2005) 28365-28369
    • (2005) J. Biol. Chem. , vol.280 , pp. 28365-28369
    • Bergo, V.B.1
  • 23
    • 0036667744 scopus 로고    scopus 로고
    • Sensory rhodopsin II: functional insights from structure
    • Spudich J.L., and Luecke H. Sensory rhodopsin II: functional insights from structure. Curr. Opin. Struct. Biol. 12 (2002) 540-546
    • (2002) Curr. Opin. Struct. Biol. , vol.12 , pp. 540-546
    • Spudich, J.L.1    Luecke, H.2
  • 24
    • 0037064214 scopus 로고    scopus 로고
    • Structural basis for sensory rhodopsin function
    • Pebay-Peyroula E., et al. Structural basis for sensory rhodopsin function. Biochim. Biophys. Acta 1565 (2002) 196-205
    • (2002) Biochim. Biophys. Acta , vol.1565 , pp. 196-205
    • Pebay-Peyroula, E.1
  • 25
    • 3242804523 scopus 로고    scopus 로고
    • Sensory rhodopsin II and bacteriorhodopsin: light activated helix F movement
    • Klare J.P., et al. Sensory rhodopsin II and bacteriorhodopsin: light activated helix F movement. Photochem. Photobiol. Sci. 3 (2004) 543-547
    • (2004) Photochem. Photobiol. Sci. , vol.3 , pp. 543-547
    • Klare, J.P.1
  • 26
    • 0037015619 scopus 로고    scopus 로고
    • Molecular basis of transmembrane signalling by sensory rhodopsin II-transducer complex
    • Gordeliy V.I., et al. Molecular basis of transmembrane signalling by sensory rhodopsin II-transducer complex. Nature 419 (2002) 484-487
    • (2002) Nature , vol.419 , pp. 484-487
    • Gordeliy, V.I.1
  • 27
    • 0036829632 scopus 로고    scopus 로고
    • Spotlight on receptor/transducer interaction
    • Spudich J.L. Spotlight on receptor/transducer interaction. Nat. Struct. Biol. 9 (2002) 797-799
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 797-799
    • Spudich, J.L.1
  • 28
    • 5644247396 scopus 로고    scopus 로고
    • The cytoplasmic membrane-proximal domain of the HtrII transducer interacts with the E-F loop of photoactivated Natronomonas pharaonis sensory rhodopsin II
    • Yang C.-S., et al. The cytoplasmic membrane-proximal domain of the HtrII transducer interacts with the E-F loop of photoactivated Natronomonas pharaonis sensory rhodopsin II. J. Biol. Chem. 279 (2004) 42970-42976
    • (2004) J. Biol. Chem. , vol.279 , pp. 42970-42976
    • Yang, C.-S.1
  • 29
    • 32044450659 scopus 로고    scopus 로고
    • Structural analysis of a HAMP domain: the linker region of the phototransducer in complex with sensory rhodopsin II
    • Bordignon E., et al. Structural analysis of a HAMP domain: the linker region of the phototransducer in complex with sensory rhodopsin II. J. Biol. Chem. 280 (2005) 38767-38775
    • (2005) J. Biol. Chem. , vol.280 , pp. 38767-38775
    • Bordignon, E.1
  • 30
    • 17644401016 scopus 로고    scopus 로고
    • Linker region of a halobacterial transducer protein interacts directly with its sensor retinal protein
    • Sudo Y., et al. Linker region of a halobacterial transducer protein interacts directly with its sensor retinal protein. Biochemistry 44 (2005) 6144-6152
    • (2005) Biochemistry , vol.44 , pp. 6144-6152
    • Sudo, Y.1
  • 31
    • 0031747352 scopus 로고    scopus 로고
    • Variations on a molecular switch: transport and sensory signaling by archaeal rhodopsins
    • Spudich J.L. Variations on a molecular switch: transport and sensory signaling by archaeal rhodopsins. Mol. Microbiol. 28 (1998) 1051-1058
    • (1998) Mol. Microbiol. , vol.28 , pp. 1051-1058
    • Spudich, J.L.1
  • 32
    • 0034632864 scopus 로고    scopus 로고
    • Molecular mechanism of vectorial proton translocation by bacteriorhodopsin
    • Subramaniam S., and Henderson R. Molecular mechanism of vectorial proton translocation by bacteriorhodopsin. Nature 406 (2000) 653-657
    • (2000) Nature , vol.406 , pp. 653-657
    • Subramaniam, S.1    Henderson, R.2
  • 33
    • 0034714097 scopus 로고    scopus 로고
    • Time-resolved detection of transient movement of helix F in spin-labelled pharaonis sensory rhodopsin II
    • Wegener A., et al. Time-resolved detection of transient movement of helix F in spin-labelled pharaonis sensory rhodopsin II. J. Mol. Biol. 301 (2000) 881-891
    • (2000) J. Mol. Biol. , vol.301 , pp. 881-891
    • Wegener, A.1
  • 34
    • 0035477798 scopus 로고    scopus 로고
    • Structural insights into the early steps of receptor-transducer signal transfer in archaeal phototaxis
    • Wegener A., et al. Structural insights into the early steps of receptor-transducer signal transfer in archaeal phototaxis. EMBO J. 20 (2001) 5312-5319
    • (2001) EMBO J. , vol.20 , pp. 5312-5319
    • Wegener, A.1
  • 35
    • 33644771099 scopus 로고    scopus 로고
    • Development of the signal in sensory rhodopsin and its transfer to the cognate transducer
    • Moukhametzianov R., et al. Development of the signal in sensory rhodopsin and its transfer to the cognate transducer. Nature 440 (2006) 115-119
    • (2006) Nature , vol.440 , pp. 115-119
    • Moukhametzianov, R.1
  • 36
    • 0035960642 scopus 로고    scopus 로고
    • Light-induced structural changes occur in the transmembrane helices of the Natronobacterium pharaonis HtrII transducer
    • Yang C.-S., and Spudich J.L. Light-induced structural changes occur in the transmembrane helices of the Natronobacterium pharaonis HtrII transducer. Biochemistry 40 (2001) 14207-14214
    • (2001) Biochemistry , vol.40 , pp. 14207-14214
    • Yang, C.-S.1    Spudich, J.L.2
  • 37
    • 33749564907 scopus 로고    scopus 로고
    • Sudo, Y. et al. Functional importance of the interhelical hydrogen bond between Thr204 and Tyr174 of sensory rhodopsin II and its alteration during the signaling process. J. Biol. Chem. (in press)
  • 38
    • 0037346546 scopus 로고    scopus 로고
    • Demonstration of a sensory rhodopsin in eubacteria
    • Jung K.-H., et al. Demonstration of a sensory rhodopsin in eubacteria. Mol. Microbiol. 47 (2003) 1513-1522
    • (2003) Mol. Microbiol. , vol.47 , pp. 1513-1522
    • Jung, K.-H.1
  • 39
    • 33645796433 scopus 로고    scopus 로고
    • Crystallization, X-ray diffraction analysis and SIRAS/molecular-replacement phasing of three crystal forms of Anabaena sensory rhodopsin transducer
    • Vogeley L., and Luecke H. Crystallization, X-ray diffraction analysis and SIRAS/molecular-replacement phasing of three crystal forms of Anabaena sensory rhodopsin transducer. Acta Crystallograph. Sect. F. Struct. Biol. Cryst. Commun. 62 (2006) 388-391
    • (2006) Acta Crystallograph. Sect. F. Struct. Biol. Cryst. Commun. , vol.62 , pp. 388-391
    • Vogeley, L.1    Luecke, H.2
  • 40
    • 8844250818 scopus 로고    scopus 로고
    • Anabaena sensory rhodopsin: A photochromic color sensor at 2.0 Å
    • Vogeley L., et al. Anabaena sensory rhodopsin: A photochromic color sensor at 2.0 Å. Science 306 (2004) 1390-1393
    • (2004) Science , vol.306 , pp. 1390-1393
    • Vogeley, L.1
  • 41
    • 33646056953 scopus 로고    scopus 로고
    • Cytoplasmic shuttling of protons in anabaena sensory rhodopsin: implications for signaling mechanism
    • Shi L., et al. Cytoplasmic shuttling of protons in anabaena sensory rhodopsin: implications for signaling mechanism. J. Mol. Biol. 358 (2006) 686-700
    • (2006) J. Mol. Biol. , vol.358 , pp. 686-700
    • Shi, L.1
  • 42
    • 33744959429 scopus 로고    scopus 로고
    • Conformational changes in the photocycle of Anabaena sensory rhodopsin
    • Bergo V.B., et al. Conformational changes in the photocycle of Anabaena sensory rhodopsin. J. Biol. Chem. 281 (2006) 15208-15214
    • (2006) J. Biol. Chem. , vol.281 , pp. 15208-15214
    • Bergo, V.B.1
  • 43
    • 3242801403 scopus 로고    scopus 로고
    • Light-induced intramolecular charge movements in microbial rhodopsins in intact E. coli cells
    • Sineshchekov O.A., and Spudich J.L. Light-induced intramolecular charge movements in microbial rhodopsins in intact E. coli cells. Photochem. Photobiol. Sci. 3 (2004) 548-554
    • (2004) Photochem. Photobiol. Sci. , vol.3 , pp. 548-554
    • Sineshchekov, O.A.1    Spudich, J.L.2
  • 44
    • 17644387239 scopus 로고    scopus 로고
    • Photochromicity of Anabaena sensory rhodopsin, an atypical microbial receptor with a cis-retinal light-adapted form
    • Sineshchekov O.A., et al. Photochromicity of Anabaena sensory rhodopsin, an atypical microbial receptor with a cis-retinal light-adapted form. J. Biol. Chem. 280 (2005) 14663-14668
    • (2005) J. Biol. Chem. , vol.280 , pp. 14663-14668
    • Sineshchekov, O.A.1
  • 45
    • 0037173051 scopus 로고    scopus 로고
    • Two rhodopsins mediate phototaxis to low and high intensity light in Chlamydomonas reinhardtii
    • Sineshchekov O.A., et al. Two rhodopsins mediate phototaxis to low and high intensity light in Chlamydomonas reinhardtii. Proc. Natl. Acad. Sci. U. S. A. 99 (2002) 8689-8694
    • (2002) Proc. Natl. Acad. Sci. U. S. A. , vol.99 , pp. 8689-8694
    • Sineshchekov, O.A.1
  • 46
    • 18744369621 scopus 로고    scopus 로고
    • Leptosphaeria rhodopsin: bacteriorhodopsin-like proton pump from a eukaryote
    • Waschuk S.A., et al. Leptosphaeria rhodopsin: bacteriorhodopsin-like proton pump from a eukaryote. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 6879-6883
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 6879-6883
    • Waschuk, S.A.1
  • 47
    • 33746784332 scopus 로고    scopus 로고
    • + pumping rhodopsin from the marine alga Acetabularia
    • + pumping rhodopsin from the marine alga Acetabularia. Biophys. J. 91 (2006) 1471-1479
    • (2006) Biophys. J. , vol.91 , pp. 1471-1479
    • Tsunoda, S.P.1
  • 48
    • 0033042090 scopus 로고    scopus 로고
    • Rhodopsin-mediated photosensing in green flagellated algae
    • Sineshchekov O.A., and Govorunova E.G. Rhodopsin-mediated photosensing in green flagellated algae. Trends Plant Sci. 4 (1999) 58-63
    • (1999) Trends Plant Sci. , vol.4 , pp. 58-63
    • Sineshchekov, O.A.1    Govorunova, E.G.2
  • 49
    • 1942519407 scopus 로고    scopus 로고
    • Chlamydomonas sensory rhodopsins A and B: cellular content and role in photophobic responses
    • Govorunova E.G., et al. Chlamydomonas sensory rhodopsins A and B: cellular content and role in photophobic responses. Biophys. J. 86 (2004) 2342-2349
    • (2004) Biophys. J. , vol.86 , pp. 2342-2349
    • Govorunova, E.G.1
  • 50
    • 84889393168 scopus 로고    scopus 로고
    • Sensory Rhodopsin Signaling in Green Flagellate Algae
    • Briggs W., and Spudich J.L. (Eds), Wiley-VCH
    • Sineshchekov O.A., and Spudich J.L. Sensory Rhodopsin Signaling in Green Flagellate Algae. In: Briggs W., and Spudich J.L. (Eds). Handbook of Photosensory Receptors (2005), Wiley-VCH 25-42
    • (2005) Handbook of Photosensory Receptors , pp. 25-42
    • Sineshchekov, O.A.1    Spudich, J.L.2
  • 51
    • 28444454100 scopus 로고    scopus 로고
    • Rhodopsin-mediated photoreception in cryptophyte flagellates
    • Sineshchekov O.A., et al. Rhodopsin-mediated photoreception in cryptophyte flagellates. Biophys. J. 89 (2005) 4310-4319
    • (2005) Biophys. J. , vol.89 , pp. 4310-4319
    • Sineshchekov, O.A.1
  • 52
    • 3042762373 scopus 로고    scopus 로고
    • "Vision" in single-celled algae
    • Kateriya S., et al. "Vision" in single-celled algae. News Physiol. Sci. 19 (2004) 133-137
    • (2004) News Physiol. Sci. , vol.19 , pp. 133-137
    • Kateriya, S.1
  • 53
    • 0037189362 scopus 로고    scopus 로고
    • Channelrhodopsin-1: a light-gated proton channel in green algae
    • Nagel G., et al. Channelrhodopsin-1: a light-gated proton channel in green algae. Science 296 (2002) 2395-2398
    • (2002) Science , vol.296 , pp. 2395-2398
    • Nagel, G.1
  • 54
    • 0345133280 scopus 로고    scopus 로고
    • Channelrhodopsin-2, a directly light-gated cation-selective membrane channel
    • Nagel G., et al. Channelrhodopsin-2, a directly light-gated cation-selective membrane channel. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 13940-13945
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 13940-13945
    • Nagel, G.1
  • 55
    • 29044433616 scopus 로고    scopus 로고
    • Light activation of channelrhodopsin-2 in excitable cells of Caenorhabditis elegans triggers rapid behavioral responses
    • Nagel G., et al. Light activation of channelrhodopsin-2 in excitable cells of Caenorhabditis elegans triggers rapid behavioral responses. Curr. Biol. 15 (2005) 2279-2284
    • (2005) Curr. Biol. , vol.15 , pp. 2279-2284
    • Nagel, G.1
  • 56
    • 29144480494 scopus 로고    scopus 로고
    • Fast noninvasive activation and inhibition of neural and network activity by vertebrate rhodopsin and green algae channelrhodopsin
    • Li X., et al. Fast noninvasive activation and inhibition of neural and network activity by vertebrate rhodopsin and green algae channelrhodopsin. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 17816-17821
    • (2005) Proc. Natl. Acad. Sci. U. S. A. , vol.102 , pp. 17816-17821
    • Li, X.1
  • 57
    • 33645974269 scopus 로고    scopus 로고
    • Ectopic expression of a microbial-type rhodopsin restores visual responses in mice with photoreceptor degeneration
    • Bi A., et al. Ectopic expression of a microbial-type rhodopsin restores visual responses in mice with photoreceptor degeneration. Neuron 50 (2006) 23-33
    • (2006) Neuron , vol.50 , pp. 23-33
    • Bi, A.1
  • 58
    • 0034665853 scopus 로고    scopus 로고
    • Bacterial rhodopsin: evidence for a new type of phototrophy in the sea
    • Béjà O., et al. Bacterial rhodopsin: evidence for a new type of phototrophy in the sea. Science 289 (2000) 1902-1906
    • (2000) Science , vol.289 , pp. 1902-1906
    • Béjà, O.1
  • 59
    • 0035859080 scopus 로고    scopus 로고
    • Proteorhodopsin phototrophy in the ocean
    • Béjà O., et al. Proteorhodopsin phototrophy in the ocean. Nature 411 (2001) 786-789
    • (2001) Nature , vol.411 , pp. 786-789
    • Béjà, O.1
  • 60
    • 0038391981 scopus 로고    scopus 로고
    • Diversification and spectral tuning in marine proteorhodopsins
    • Man D., et al. Diversification and spectral tuning in marine proteorhodopsins. EMBO J. 22 (2003) 1725-1731
    • (2003) EMBO J. , vol.22 , pp. 1725-1731
    • Man, D.1
  • 61
    • 0141676335 scopus 로고    scopus 로고
    • Novel proteorhodopsin variants from the Mediterranean and Red Seas
    • Sabehi G., et al. Novel proteorhodopsin variants from the Mediterranean and Red Seas. Environ. Microbiol. 5 (2003) 842-849
    • (2003) Environ. Microbiol. , vol.5 , pp. 842-849
    • Sabehi, G.1
  • 62
    • 0242331634 scopus 로고    scopus 로고
    • Proteorhodopsin genes are widely distributed among divergent bacterial taxa
    • de la Torre J.R., et al. Proteorhodopsin genes are widely distributed among divergent bacterial taxa. Proc. Natl. Acad. Sci. U. S. A. 100 (2003) 12830-12835
    • (2003) Proc. Natl. Acad. Sci. U. S. A. , vol.100 , pp. 12830-12835
    • de la Torre, J.R.1
  • 63
    • 4344584482 scopus 로고    scopus 로고
    • Different SAR86 subgroups harbour divergent proteorhodopsins
    • Sabehi G., et al. Different SAR86 subgroups harbour divergent proteorhodopsins. Environ. Microbiol. 6 (2004) 903-910
    • (2004) Environ. Microbiol. , vol.6 , pp. 903-910
    • Sabehi, G.1
  • 64
    • 11144354360 scopus 로고    scopus 로고
    • Environmental genome shotgun sequencing of the Sargasso Sea
    • Venter J.C., et al. Environmental genome shotgun sequencing of the Sargasso Sea. Science 304 (2004) 66-74
    • (2004) Science , vol.304 , pp. 66-74
    • Venter, J.C.1
  • 65
    • 23944505538 scopus 로고    scopus 로고
    • New insights into metabolic properties of marine bacteria encoding proteorhodopsins
    • Sabehi G., et al. New insights into metabolic properties of marine bacteria encoding proteorhodopsins. PLoS Biol. 3 (2005) e273
    • (2005) PLoS Biol. , vol.3
    • Sabehi, G.1
  • 66
    • 0141817991 scopus 로고    scopus 로고
    • Spectroscopic and photochemical characterization of a deep ocean proteorhodopsin
    • Wang W.-W., et al. Spectroscopic and photochemical characterization of a deep ocean proteorhodopsin. J. Biol. Chem. 278 (2003) 33985-33991
    • (2003) J. Biol. Chem. , vol.278 , pp. 33985-33991
    • Wang, W.-W.1
  • 67
    • 0035423908 scopus 로고    scopus 로고
    • Crystal structure of rhodopsin: implications for vision and beyond
    • Okada T., and Palczewski K. Crystal structure of rhodopsin: implications for vision and beyond. Curr. Opin. Struct. Biol. 11 (2001) 420-426
    • (2001) Curr. Opin. Struct. Biol. , vol.11 , pp. 420-426
    • Okada, T.1    Palczewski, K.2
  • 68
    • 33745114416 scopus 로고    scopus 로고
    • Bacteriorhodopsin-like proteins of eubacteria and fungi: the extent of conservation of the haloarchaeal proton-pumping mechanism
    • Brown L.S., and Jung K.H. Bacteriorhodopsin-like proteins of eubacteria and fungi: the extent of conservation of the haloarchaeal proton-pumping mechanism. Photochem. Photobiol. Sci. 5 (2006) 538-546
    • (2006) Photochem. Photobiol. Sci. , vol.5 , pp. 538-546
    • Brown, L.S.1    Jung, K.H.2
  • 69
    • 33749563719 scopus 로고    scopus 로고
    • Sudo, Y. and Spudich, J.L. Three strategically placed hydrogen-bonding residues convert a proton pump into a sensory receptor. Proc. Natl. Acad. Sci. U.S.A. (in press)


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.