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Volumn 3, Issue 6, 2004, Pages 555-565

Fungal rhodopsins and opsin-related proteins: Eukaryotic homologues of bacteriorhodopsin with unknown functions

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIORHODOPSIN; FUNGAL PROTEIN; LYSINE; OPSIN RELATED KINASE; PROTEIN KINASE; RHODOPSIN; UNCLASSIFIED DRUG;

EID: 3242797479     PISSN: 1474905X     EISSN: 14749092     Source Type: Journal    
DOI: 10.1039/b315527g     Document Type: Article
Times cited : (79)

References (87)
  • 1
    • 0034519206 scopus 로고    scopus 로고
    • Retinylidene proteins: Structures and functions from archaea to humans
    • J. L. Spudich C. Yang K. Jung E. N. Spudich Retinylidene proteins: structures and functions from archaea to humans Annu. Rev. Cell Dev. Biol. 2000 16 365-392.
    • (2000) Annu. Rev. Cell Dev. Biol. , vol.16 , pp. 365-392
    • Spudich, J.L.1    Yang, C.2    Jung, K.3    Spudich, E.N.4
  • 2
    • 0033529279 scopus 로고    scopus 로고
    • The nop-1 gene of Neurospora crassa encodes a seven transmembrane helix retinal-binding protein homologous to archaeal rhodopsins
    • J. A. Bieszke E. L. Braun L. E. Bean S. Kang D. O. Natvig K. A. Borkovich The nop-1 gene of Neurospora crassa encodes a seven transmembrane helix retinal-binding protein homologous to archaeal rhodopsins Proc. Natl. Acad. Sci. USA 1999 96 8034-8039.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8034-8039
    • Bieszke, J.A.1    Braun, E.L.2    Bean, L.E.3    Kang, S.4    Natvig, D.O.5    Borkovich, K.A.6
  • 4
    • 0014339898 scopus 로고
    • Rapid photoelectric effect in the alga Acetabularia
    • C. Schilde Rapid photoelectric effect in the alga Acetabularia Z. Naturforsch. B 1968 23 1369-1376.
    • (1968) Z. Naturforsch. B , vol.23 , pp. 1369-1376
    • Schilde, C.1
  • 5
    • 0019166329 scopus 로고
    • Light antennas in phototactic algae
    • K. W. Foster R. D. Smyth Light antennas in phototactic algae Microbiol. Rev. 1980 44 572-630.
    • (1980) Microbiol. Rev. , vol.44 , pp. 572-630
    • Foster, K.W.1    Smyth, R.D.2
  • 6
    • 0021143119 scopus 로고
    • A rhodopsin is the functional photoreceptor for phototaxis in the unicellular eukaryote Chlamydomonas
    • K. W. Foster J. Saranak N. Patel G. Zarilli M. Okabe T. Kline K. Nakanishi A rhodopsin is the functional photoreceptor for phototaxis in the unicellular eukaryote Chlamydomonas Nature 1984 311 756-759.
    • (1984) Nature , vol.311 , pp. 756-759
    • Foster, K.W.1    Saranak, J.2    Patel, N.3    Zarilli, G.4    Okabe, M.5    Kline, T.6    Nakanishi, K.7
  • 7
    • 0027516533 scopus 로고
    • A biological point of view on photoreception (No-imaging vision) in algae
    • P. Gualtieri A biological point of view on photoreception (no-imaging vision) in algae J. Photochem. Photobiol. B 1993 18 95-97.
    • (1993) J. Photochem. Photobiol. B , vol.18 , pp. 95-97
    • Gualtieri, P.1
  • 8
    • 0030829631 scopus 로고    scopus 로고
    • Vision in microalgae
    • P. Hegemann Vision in microalgae Planta 1997 203 265-274.
    • (1997) Planta , vol.203 , pp. 265-274
    • Hegemann, P.1
  • 10
    • 0025874704 scopus 로고
    • In vitro identification of rhodopsin in the green alga Chlamydomonas
    • M. Beckmann P. Hegemann In vitro identification of rhodopsin in the green alga Chlamydomonas Biochemistry 1991 30 3692-3697.
    • (1991) Biochemistry , vol.30 , pp. 3692-3697
    • Beckmann, M.1    Hegemann, P.2
  • 11
    • 0026283324 scopus 로고
    • All-trans-retinal is the chromophore bound to the photoreceptor of the alga Chlamydomonas reinhardtii
    • F. Derguini P. Mazur K. Nakanishi D. M. Starace J. Saranak K. W. Foster All-trans-retinal is the chromophore bound to the photoreceptor of the alga Chlamydomonas reinhardtii Photochem. Photobiol. 1991 54 1017-1021.
    • (1991) Photochem. Photobiol. , vol.54 , pp. 1017-1021
    • Derguini, F.1    Mazur, P.2    Nakanishi, K.3    Starace, D.M.4    Saranak, J.5    Foster, K.W.6
  • 12
    • 0026320894 scopus 로고
    • Retinal analog restoration of photophobic responses in a blind Chlamydomonas reinhardtii mutant. Evidence for an archaebacterial like chromophore in a eukaryotic rhodopsin
    • M. A. Lawson D. N. Zacks F. Derguini K. Nakanishi J. L. Spudich Retinal analog restoration of photophobic responses in a blind Chlamydomonas reinhardtii mutant. Evidence for an archaebacterial like chromophore in a eukaryotic rhodopsin Biophys. J. 1991 60 1490-1498.
    • (1991) Biophys. J. , vol.60 , pp. 1490-1498
    • Lawson, M.A.1    Zacks, D.N.2    Derguini, F.3    Nakanishi, K.4    Spudich, J.L.5
  • 14
    • 0037173051 scopus 로고    scopus 로고
    • Two rhodopsins mediate phototaxis to low- and high-intensity light in Chlamydomonas reinhardtii
    • O. A. Sineshchekov K. H. Jung J. L. Spudich Two rhodopsins mediate phototaxis to low- and high-intensity light in Chlamydomonas reinhardtii Proc. Natl. Acad. Sci. USA 2002 99 8689-8694.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 8689-8694
    • Sineshchekov, O.A.1    Jung, K.H.2    Spudich, J.L.3
  • 16
    • 85056356471 scopus 로고    scopus 로고
    • Microbial rhodopsins: Transport and sensory proteins throughout the three domains of life
    • W. M. Horspool and F. Lenci, CRC Press, 2nd edn
    • K. H. Jung and J. L. Spudich, Microbial rhodopsins: Transport and sensory proteins throughout the three domains of life, in CRC Handbook of Organic Photochemistry and Photobiology, ed. W. M. Horspool and F. Lenci, CRC Press, 2nd edn., 2004, 124/1-124/11.
    • (2004) CRC Handbook of Organic Photochemistry and Photobiology , pp. 1-124
    • Jung, K.H.1    Spudich, J.L.2
  • 18
    • 3242795017 scopus 로고    scopus 로고
    • Rhodopsin-like-proteins: Light detection pigments in Leptolyngbya, Euglena, Ochromonas, Pelvetia
    • P. Gualtieri Rhodopsin-like-proteins: light detection pigments in Leptolyngbya, Euglena, Ochromonas, Pelvetia Compr. Ser. Photosci. 2001 1 281-295.
    • (2001) Compr. Ser. Photosci. , vol.1 , pp. 281-295
    • Gualtieri, P.1
  • 19
    • 0037346546 scopus 로고    scopus 로고
    • Demonstration of a sensory rhodopsin in eubacteria
    • K. H. Jung V. D. Trivedi J. L. Spudich Demonstration of a sensory rhodopsin in eubacteria Mol. Microbiol. 2003 47 1513-1522.
    • (2003) Mol. Microbiol. , vol.47 , pp. 1513-1522
    • Jung, K.H.1    Trivedi, V.D.2    Spudich, J.L.3
  • 21
    • 0038009383 scopus 로고    scopus 로고
    • Novel dinoflagellate clock-related genes identified through microarray analysis
    • O. K. Okamoto J. Woodland Hastings Novel dinoflagellate clock-related genes identified through microarray analysis J. Phycol. 2003 39 519-526.
    • (2003) J. Phycol. , vol.39 , pp. 519-526
    • Okamoto, O.K.1    Woodland Hastings, J.2
  • 22
    • 0031008374 scopus 로고    scopus 로고
    • Rhodopsin guides fungal phototaxis
    • J. Saranak K. W. Foster Rhodopsin guides fungal phototaxis Nature 1997 387 465-466.
    • (1997) Nature , vol.387 , pp. 465-466
    • Saranak, J.1    Foster, K.W.2
  • 23
    • 0036363930 scopus 로고    scopus 로고
    • A rhodopsin-like protein in the plasma membrane of Silvetia compressa eggs
    • P. Gualtieri K. R. Robinson A rhodopsin-like protein in the plasma membrane of Silvetia compressa eggs Photochem. Photobiol. 2002 75 76-78.
    • (2002) Photochem. Photobiol. , vol.75 , pp. 76-78
    • Gualtieri, P.1    Robinson, K.R.2
  • 24
    • 0025940190 scopus 로고
    • Identification of 11-cis and all-trans-retinal in the photoreceptive organelle of a flagellate green alga
    • G. Kreimer F. J. Marner U. Brohsonn M. Melkonian Identification of 11-cis and all-trans-retinal in the photoreceptive organelle of a flagellate green alga FEBS Lett. 1991 293 49-52.
    • (1991) FEBS Lett. , vol.293 , pp. 49-52
    • Kreimer, G.1    Marner, F.J.2    Brohsonn, U.3    Melkonian, M.4
  • 25
    • 0034122433 scopus 로고    scopus 로고
    • Presence of rhodopsin-like proteins in Sorghum bicolor and Pisum sativum
    • C. A. O. Ricart A. Wise J. B. C. Findlay P. A. Millner Presence of rhodopsin-like proteins in Sorghum bicolor and Pisum sativum J. Plant Physiol. 2000 156 300-305.
    • (2000) J. Plant Physiol. , vol.156 , pp. 300-305
    • Ricart, C.A.O.1    Wise, A.2    Findlay, J.B.C.3    Millner, P.A.4
  • 26
    • 0035683447 scopus 로고    scopus 로고
    • Do plants have rhodopsin after all? A mystery of plant G protein-coupled signalling
    • A. V. Andreeva M. A. Kutuzov Do plants have rhodopsin after all? A mystery of plant G protein-coupled signalling Plant Physiol. Biochem. 2001 39 1027-1035.
    • (2001) Plant Physiol. Biochem. , vol.39 , pp. 1027-1035
    • Andreeva, A.V.1    Kutuzov, M.A.2
  • 27
    • 0026634082 scopus 로고
    • The plasma membrane of yeast acquires a novel heat-shock protein (Hsp30) and displays a decline in proton-pumping ATPase levels in response to both heat shock and the entry to stationary phase
    • B. Panaretou P. W. Piper The plasma membrane of yeast acquires a novel heat-shock protein (hsp30) and displays a decline in proton-pumping ATPase levels in response to both heat shock and the entry to stationary phase Eur. J. Biochem. 1992 206 635-640.
    • (1992) Eur. J. Biochem. , vol.206 , pp. 635-640
    • Panaretou, B.1    Piper, P.W.2
  • 28
    • 0027196110 scopus 로고
    • Isolation and sequence of HSP30, a yeast heat-shock gene coding for a hydrophobic membrane protein
    • M. Regnacq H. Boucherie Isolation and sequence of HSP30, a yeast heat-shock gene coding for a hydrophobic membrane protein Curr. Genet. 1993 23 435-442.
    • (1993) Curr. Genet. , vol.23 , pp. 435-442
    • Regnacq, M.1    Boucherie, H.2
  • 30
    • 0031459371 scopus 로고    scopus 로고
    • Evolutionary relationships among proteins probed by an iterative neighborhood cluster analysis (INCA). Alignment of bacteriorhodopsins with the yeast sequence YRO2
    • R. C. Graul W. Sadee Evolutionary relationships among proteins probed by an iterative neighborhood cluster analysis (INCA). Alignment of bacteriorhodopsins with the yeast sequence YRO2 Pharm. Res. 1997 14 1533-1541.
    • (1997) Pharm. Res. , vol.14 , pp. 1533-1541
    • Graul, R.C.1    Sadee, W.2
  • 31
    • 0035795114 scopus 로고    scopus 로고
    • Homologues of archaeal rhodopsins in plants, animals and fungi: Structural and functional predications for a putative fungal chaperone protein
    • Y.-F. Zhai W. H. M. Heijne D. W. Smith M. H. Saier, Jr. Homologues of archaeal rhodopsins in plants, animals and fungi: structural and functional predications for a putative fungal chaperone protein Biochim. Biophys. Acta 2001 1511 206-223.
    • (2001) Biochim. Biophys. Acta , vol.1511 , pp. 206-223
    • Zhai, Y.-F.1    Heijne, W.H.M.2    Smith, D.W.3    Saier, M.H.4
  • 33
    • 0035058358 scopus 로고    scopus 로고
    • Characterization of an opsin gene from the ascomycete Leptosphaeria maculans
    • A. Idnurm B. J. Howlett Characterization of an opsin gene from the ascomycete Leptosphaeria maculans Genome 2001 44 167-171.
    • (2001) Genome , vol.44 , pp. 167-171
    • Idnurm, A.1    Howlett, B.J.2
  • 34
    • 0027968068 scopus 로고
    • CLUSTALW: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • J. D. Thompson D. G. Higgins T. J. Gibson CLUSTALW: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice Nucl. Acids Res. 1994 22 4673-4680.
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 35
    • 0032964297 scopus 로고    scopus 로고
    • BLAST 2 Sequences, a new tool for comparing protein and nucleotide sequences
    • T. A. Tatusova T. L. Madden BLAST 2 Sequences, a new tool for comparing protein and nucleotide sequences FEMS Microbiol. Lett. 1999 174 247-250.
    • (1999) FEMS Microbiol. Lett. , vol.174 , pp. 247-250
    • Tatusova, T.A.1    Madden, T.L.2
  • 36
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • N. Saitou M. Nei The neighbor-joining method: a new method for reconstructing phylogenetic trees Mol. Biol. Evol. 1987 4 406-425.
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 37
    • 0031574072 scopus 로고    scopus 로고
    • The ClustalX windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • J. D. Thompson T. J. Gibson F. Plewniak F. Jeanmougin D. G. Higgins The ClustalX windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools Nucl. Acids Res. 1997 24 4876-4882.
    • (1997) Nucl. Acids Res. , vol.24 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 38
    • 0030203863 scopus 로고    scopus 로고
    • TREEVIEW: An application to display phylogenetic trees on personal computers
    • R. D. M. Page TREEVIEW: An application to display phylogenetic trees on personal computers Comput. Appl. Biosci. 1996 12 357-358.
    • (1996) Comput. Appl. Biosci. , vol.12 , pp. 357-358
    • Page, R.D.M.1
  • 39
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling
    • N. Guex M. C. Peitsch SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modeling Electrophoresis 1997 18 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 40
    • 85034383598 scopus 로고    scopus 로고
    • Washington University GSC Histoplasma BLAST Search Service
    • Washington University GSC Histoplasma BLAST Search Service (http://genome.wustl.edu/blast/histo_client.cgi).
  • 41
    • 85034367243 scopus 로고    scopus 로고
    • Aspergillus flavus sequencing project
    • Aspergillus flavus sequencing project, D. Kupfer, L. Hern, Y. Tang and N. Keller, http://www.genome.ou.edu/flavus_blast.html.
    • Kupfer, D.1    Hern, L.2    Tang, Y.3    Keller, N.4
  • 42
    • 85034314963 scopus 로고    scopus 로고
    • Personal communication, Génolevures project
    • Personal communication, Génolevures project http://cbi.labri.fr/Genolevures/.
  • 44
    • 85034343097 scopus 로고    scopus 로고
    • These sequence data were produced by the US Department of Energy Joint Genome Institute
    • These sequence data were produced by the US Department of Energy Joint Genome Institute http://www.jgi.doe.gov/.
  • 45
    • 85034355775 scopus 로고    scopus 로고
    • The TIGR Gene Index Databases, The Institute for Genomic Research, Rockville, MD 20850 (URL
    • The TIGR Gene Index Databases, The Institute for Genomic Research, Rockville, MD 20850 (URL: http://www.tigr.org/tdb/tgi).
  • 46
    • 25344447670 scopus 로고    scopus 로고
    • Modeling of eukaryotic homologs of the bacteriorhodopsin superfamily reveals a possible retinoid binding site
    • M. S. Hutson M. S. Braiman Modeling of eukaryotic homologs of the bacteriorhodopsin superfamily reveals a possible retinoid binding site Biophys. J. 1999 76 A123.
    • (1999) Biophys. J. , vol.76 , pp. A123
    • Hutson, M.S.1    Braiman, M.S.2
  • 47
    • 0141480266 scopus 로고    scopus 로고
    • An ordered collection of expressed sequences from Cryphonectria parasitica and evidence of genomic microsynteny with Neurospora crassa and Magnaporthe grisea
    • A. L. Dawe V. C. McMains M. Panglao S. Kasahara B. Chen D. L. Nuss An ordered collection of expressed sequences from Cryphonectria parasitica and evidence of genomic microsynteny with Neurospora crassa and Magnaporthe grisea Microbiol. 2003 149 2373-2384.
    • (2003) Microbiol. , vol.149 , pp. 2373-2384
    • Dawe, A.L.1    McMains, V.C.2    Panglao, M.3    Kasahara, S.4    Chen, B.5    Nuss, D.L.6
  • 48
    • 0033947041 scopus 로고    scopus 로고
    • A group of expressed cDNA sequences from the wheat fungal leaf blotch pathogen, Mycosphaerella graminicola (Septoria tritici)
    • J. Keon A. Bailey J. Hargreaves A group of expressed cDNA sequences from the wheat fungal leaf blotch pathogen, Mycosphaerella graminicola(Septoria tritici) Fungal Genet. Biol. 2000 29 118-133.
    • (2000) Fungal Genet. Biol. , vol.29 , pp. 118-133
    • Keon, J.1    Bailey, A.2    Hargreaves, J.3
  • 49
    • 0033534585 scopus 로고    scopus 로고
    • Evolution of the archaeal rhodopsins: Evolution rate changes by gene duplication and functional differentiation
    • K. Ihara T. Umemura I. Katagiri T. Kitajima-Ihara Y. Sugiyama Y. Kimura Y. Mukohata Evolution of the archaeal rhodopsins: evolution rate changes by gene duplication and functional differentiation J. Mol. Biol. 1999 285 163-174.
    • (1999) J. Mol. Biol. , vol.285 , pp. 163-174
    • Ihara, K.1    Umemura, T.2    Katagiri, I.3    Kitajima-Ihara, T.4    Sugiyama, Y.5    Kimura, Y.6    Mukohata, Y.7
  • 50
    • 0035498346 scopus 로고    scopus 로고
    • Proton transport mechanism of bacteriorhodopsin as revealed by site-specific mutagenesis and protein sequence variability
    • L. S. Brown Proton transport mechanism of bacteriorhodopsin as revealed by site-specific mutagenesis and protein sequence variability Biochemistry (Moscow) 2001 66 1249-1255.
    • (2001) Biochemistry (Moscow) , vol.66 , pp. 1249-1255
    • Brown, L.S.1
  • 52
    • 0037015032 scopus 로고    scopus 로고
    • Continued evolutionary surprises among dinoflagellates
    • C. W. Morden A. R. Sherwood Continued evolutionary surprises among dinoflagellates Proc. Natl. Acad. Sci. USA 2002 99 11558-11560.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11558-11560
    • Morden, C.W.1    Sherwood, A.R.2
  • 54
    • 0032546920 scopus 로고    scopus 로고
    • Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution
    • H. Luecke H.-T. Richter J. K. Lanyi Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution Science 1998 280 1934-1937.
    • (1998) Science , vol.280 , pp. 1934-1937
    • Luecke, H.1    Richter, H.-T.2    Lanyi, J.K.3
  • 55
    • 0032987478 scopus 로고    scopus 로고
    • Membrane protein folding and stability: Physical principles
    • S. H. White W. C. Wimley Membrane protein folding and stability: physical principles Annu. Rev. Biophys. Biomol. Struct. 1999 28 319-365.
    • (1999) Annu. Rev. Biophys. Biomol. Struct. , vol.28 , pp. 319-365
    • White, S.H.1    Wimley, W.C.2
  • 57
    • 0032578378 scopus 로고    scopus 로고
    • Lipid patches in membrane protein oligomers: Crystal structure of the bacteriorhodopsin-lipid complex
    • L.-O. Essen R. Siegert W. D. Lehmann D. Oesterhelt Lipid patches in membrane protein oligomers: crystal structure of the bacteriorhodopsin-lipid complex Proc. Natl. Acad. Sci. USA 1998 95 11673-11678.
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 11673-11678
    • Essen, L.-O.1    Siegert, R.2    Lehmann, W.D.3    Oesterhelt, D.4
  • 58
    • 0029665673 scopus 로고    scopus 로고
    • a’s of Asp-85 and Glu-204 forms part of the reprotonation switch of bacteriorhodopsin
    • a’s of Asp-85 and Glu-204 forms part of the reprotonation switch of bacteriorhodopsin Biochemistry 1996 35 4054-4062.
    • (1996) Biochemistry , vol.35 , pp. 4054-4062
    • Richter, H.-T.1    Brown, L.S.2    Needleman, R.3    Lanyi, J.K.4
  • 59
    • 0035949633 scopus 로고    scopus 로고
    • Coupling of the reisomerization of the retinal, proton uptake, and reprotonation of Asp-96 in the N photointermediate of bacteriorhodopsin
    • A. K. Dioumaev L. S. Brown R. Needleman J. K. Lanyi Coupling of the reisomerization of the retinal, proton uptake, and reprotonation of Asp-96 in the N photointermediate of bacteriorhodopsin Biochemistry 2001 40 11308-11317.
    • (2001) Biochemistry , vol.40 , pp. 11308-11317
    • Dioumaev, A.K.1    Brown, L.S.2    Needleman, R.3    Lanyi, J.K.4
  • 60
    • 0033972499 scopus 로고    scopus 로고
    • Expression and subcellular localization of a membrane protein related to Hsp30p in Saccharomyces cerevisiae
    • K. Wu J. H. Dawe J. P. Aris Expression and subcellular localization of a membrane protein related to Hsp30p in Saccharomyces cerevisiae Biochim. Biophys. Acta 2000 1463 477-482.
    • (2000) Biochim. Biophys. Acta , vol.1463 , pp. 477-482
    • Wu, K.1    Dawe, J.H.2    Aris, J.P.3
  • 61
    • 0028274849 scopus 로고
    • Covalent link between the chromophore and the protein backbone of bacteriorhodopsin is not required for forming a photochemically active pigment analogous to the wild type
    • N. Friedman S. Druckmann J. Lanyi R. Needleman A. Lewis M. Ottolenghi M. Sheves Covalent link between the chromophore and the protein backbone of bacteriorhodopsin is not required for forming a photochemically active pigment analogous to the wild type Biochemistry 1994 33 1971-1976.
    • (1994) Biochemistry , vol.33 , pp. 1971-1976
    • Friedman, N.1    Druckmann, S.2    Lanyi, J.3    Needleman, R.4    Lewis, A.5    Ottolenghi, M.6    Sheves, M.7
  • 62
    • 0027958155 scopus 로고
    • Bacteriorhodopsin can function without a covalent linkage between retinal and protein
    • U. Schweiger J. Tittor D. Oesterhelt Bacteriorhodopsin can function without a covalent linkage between retinal and protein Biochemistry 1994 33 535-541.
    • (1994) Biochemistry , vol.33 , pp. 535-541
    • Schweiger, U.1    Tittor, J.2    Oesterhelt, D.3
  • 63
    • 0033607149 scopus 로고    scopus 로고
    • A eukaryotic protein, NOP-1, binds retinal to form an archaeal rhodopsin-like photochemically reactive pigment
    • J. A. Bieszke E. N. Spudich K. L. Scott K. A. Borkovich J. L. Spudich A eukaryotic protein, NOP-1, binds retinal to form an archaeal rhodopsin-like photochemically reactive pigment Biochemistry 1999 38 14138-14145.
    • (1999) Biochemistry , vol.38 , pp. 14138-14145
    • Bieszke, J.A.1    Spudich, E.N.2    Scott, K.L.3    Borkovich, K.A.4    Spudich, J.L.5
  • 64
    • 0035979995 scopus 로고    scopus 로고
    • Photochemical reaction cycle and proton transfers in Neurospora rhodopsin
    • L. S. Brown A. K. Dioumaev J. K. Lanyi E. N. Spudich and J. L. Spudich Photochemical reaction cycle and proton transfers in Neurospora rhodopsin J. Biol. Chem. 2001 276 32495-32505.
    • (2001) J. Biol. Chem. , vol.276 , pp. 32495-32505
    • Brown, L.S.1    Dioumaev, A.K.2    Lanyi, J.K.3    Spudich, E.N.4    Spudich, J.L.5
  • 65
    • 0036727510 scopus 로고    scopus 로고
    • A Fourier transform infrared study of Neurospora rhodopsin: Similarities with archaeal rhodopsins
    • V. Bergo E. N. Spudich J. L. Spudich K. J. Rothschild A Fourier transform infrared study of Neurospora rhodopsin: similarities with archaeal rhodopsins Photochem. Photobiol. 2002 73 341-349.
    • (2002) Photochem. Photobiol. , vol.73 , pp. 341-349
    • Bergo, V.1    Spudich, E.N.2    Spudich, J.L.3    Rothschild, K.J.4
  • 67
    • 0037015268 scopus 로고    scopus 로고
    • Algal rhodopsins: Phototaxis receptors found at last
    • K. D. Ridge Algal rhodopsins: phototaxis receptors found at last Curr. Biol. 2002 12 R588-R590.
    • (2002) Curr. Biol. , vol.12 , pp. R588-R590
    • Ridge, K.D.1
  • 69
    • 0032834867 scopus 로고    scopus 로고
    • Updated map of duplicated regions in the yeast genome
    • C. Seoighe K. H. Wolfe Updated map of duplicated regions in the yeast genome Gene 1999 238 253-261.
    • (1999) Gene , vol.238 , pp. 253-261
    • Seoighe, C.1    Wolfe, K.H.2
  • 70
    • 0037047141 scopus 로고    scopus 로고
    • Gene order evolution and paleopolyploidy in hemiascomycete yeasts
    • S. Wong G. Butler K. H. Wolfe Gene order evolution and paleopolyploidy in hemiascomycete yeasts Proc. Natl. Acad. Sci. USA 2002 99 9272-9277.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 9272-9277
    • Wong, S.1    Butler, G.2    Wolfe, K.H.3
  • 71
    • 0027218962 scopus 로고
    • Hydrophobic amino acids in the retinal-binding pocket of bacteriorhodopsin
    • D. A. Greenhalgh D. L. Farrens S. Subramaniam H. G. Khorana Hydrophobic amino acids in the retinal-binding pocket of bacteriorhodopsin J. Biol. Chem. 1993 268 20305-20311.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20305-20311
    • Greenhalgh, D.A.1    Farrens, D.L.2    Subramaniam, S.3    Khorana, H.G.4
  • 72
    • 0028016119 scopus 로고
    • Met-145 is a key residue in the dark adaptation of bacteriorhodopsin homologs
    • K. Ihara T. Amemiya Y. Miyashita Y. Mukohata Met-145 is a key residue in the dark adaptation of bacteriorhodopsin homologs Biophys. J. 1994 67 1187-1191.
    • (1994) Biophys. J. , vol.67 , pp. 1187-1191
    • Ihara, K.1    Amemiya, T.2    Miyashita, Y.3    Mukohata, Y.4
  • 73
    • 0024978461 scopus 로고
    • Structure-function studies on bacteriorhodopsin. 9. Substitutions of tryptophan residues affect protein–retinal interactions in bacteriorhodopsin
    • T. Mogi T. Marti H. G. Khorana Structure-function studies on bacteriorhodopsin. 9. Substitutions of tryptophan residues affect protein–retinal interactions in bacteriorhodopsin J. Biol. Chem. 1989 264 14197-14201.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14197-14201
    • Mogi, T.1    Marti, T.2    Khorana, H.G.3
  • 74
    • 0034922262 scopus 로고    scopus 로고
    • Functional analysis of six ORFs from Saccharomyces cerevisiae chromosome IV: Two-spored asci produced by disruptant of YDR027c and strain-dependent DNA heterogeneity around YDR036c
    • M. Aittamaa H. Turakainen M. Korhola Functional analysis of six ORFs from Saccharomyces cerevisiae chromosome IV: two-spored asci produced by disruptant of YDR027c and strain-dependent DNA heterogeneity around YDR036c Yeast 2001 18 931-941.
    • (2001) Yeast , vol.18 , pp. 931-941
    • Aittamaa, M.1    Turakainen, H.2    Korhola, M.3
  • 75
    • 0036852128 scopus 로고    scopus 로고
    • Characterization of a gene (Sp1) encoding a secreted protein from Leptosphaeria maculans, the blackleg pathogen of Brassica napus
    • L. M. Wilson A. Idnurm B. J. Howlett Characterization of a gene (sp1) encoding a secreted protein from Leptosphaeria maculans, the blackleg pathogen of Brassica napus Mol. Plant Pathol. 2002 3 487-493.
    • (2002) Mol. Plant Pathol. , vol.3 , pp. 487-493
    • Wilson, L.M.1    Idnurm, A.2    Howlett, B.J.3
  • 76
    • 0035852672 scopus 로고    scopus 로고
    • Electrophysiological characterization of specific interactions between bacterial sensory rhodopsins and their transducers
    • G. Schmies M. Engelhard P. G. Wood G. Nagel E. Bamberg Electrophysiological characterization of specific interactions between bacterial sensory rhodopsins and their transducers Proc. Natl. Acad. Sci. USA 2001 98 1555-1559.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 1555-1559
    • Schmies, G.1    Engelhard, M.2    Wood, P.G.3    Nagel, G.4    Bamberg, E.5
  • 77
    • 0024317089 scopus 로고
    • Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin
    • H. Otto T. Marti M. Holz T. Mogi M. Lindau H. G. Khorana M. P. Heyn Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin Proc. Natl. Acad. Sci. USA 1989 86 9228-9232.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 9228-9232
    • Otto, H.1    Marti, T.2    Holz, M.3    Mogi, T.4    Lindau, M.5    Khorana, H.G.6    Heyn, M.P.7
  • 79
    • 3242762201 scopus 로고    scopus 로고
    • Identification of photoreceptors that sense light and inhibit differentiation of Cryptococcus neoformans
    • (S), abstract #69
    • A. Idnurm J. Heitman Identification of photoreceptors that sense light and inhibit differentiation of Cryptococcus neoformans Fungal Genet. Newsl. 2003 50.(S), abstract #69.
    • (2003) Fungal Genet. Newsl. , vol.50
    • Idnurm, A.1    Heitman, J.2
  • 80
    • 0028867333 scopus 로고
    • The heat shock and ethanol stress responses of yeast exhibit extensive similarity and functional overlap
    • P. W. Piper The heat shock and ethanol stress responses of yeast exhibit extensive similarity and functional overlap FEMS Microbiol. Lett. 1995 134 121-127.
    • (1995) FEMS Microbiol. Lett. , vol.134 , pp. 121-127
    • Piper, P.W.1
  • 81
    • 0030838741 scopus 로고    scopus 로고
    • Isolation of mRNAs induced by a hazardous chemical in white-rot fungus, Coriolus versicolor, by differential display
    • Y. Iimura K. Tatsumi Isolation of mRNAs induced by a hazardous chemical in white-rot fungus, Coriolus versicolor, by differential display FEBS Lett. 1997 412 370-374.
    • (1997) FEBS Lett. , vol.412 , pp. 370-374
    • Iimura, Y.1    Tatsumi, K.2
  • 82
    • 0030797707 scopus 로고    scopus 로고
    • Identification of genes with nutrient-controlled expression by PCR-mapping in the yeast Saccharomyces cerevisiae
    • M. Crauwels J. Winderickx J. H. de Winde J. M. Thevelein Identification of genes with nutrient-controlled expression by PCR-mapping in the yeast Saccharomyces cerevisiae Yeast 1997 13 973-984.
    • (1997) Yeast , vol.13 , pp. 973-984
    • Crauwels, M.1    Winderickx, J.2    de Winde, J.H.3    Thevelein, J.M.4
  • 83
    • 0037474301 scopus 로고    scopus 로고
    • The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur
    • V. M. Boer J. H. de Winde J. T. Pronk M. D. Piper The genome-wide transcriptional responses of Saccharomyces cerevisiae grown on glucose in aerobic chemostat cultures limited for carbon, nitrogen, phosphorus, or sulfur J. Biol. Chem. 2003 278 3265-3274.
    • (2003) J. Biol. Chem. , vol.278 , pp. 3265-3274
    • Boer, V.M.1    de Winde, J.H.2    Pronk, J.T.3    Piper, M.D.4
  • 84
    • 3242759828 scopus 로고    scopus 로고
    • Orp-1, an Opsin Related Protein of Neurospora crassa
    • (S), abstract #99
    • M. Nemcovic K. A. Borkovich Orp-1, an Opsin Related Protein of Neurospora crassa Fungal Genet. Newsl. 2003 50.(S), abstract #99.
    • (2003) Fungal Genet. Newsl. , vol.50
    • Nemcovic, M.1    Borkovich, K.A.2
  • 85
    • 0030935908 scopus 로고    scopus 로고
    • Hsp30, the integral plasma membrane heat shock protein of Saccharomyces cerevisiae, is a stress-inducible regulator of plasma membrane H(+)-ATPase
    • P. W. Piper C. Ortiz-Calderon C. Holyoak P. Coote M. Cole Hsp30, the integral plasma membrane heat shock protein of Saccharomyces cerevisiae, is a stress-inducible regulator of plasma membrane H(+)-ATPase Cell Stress Chaperones 1997 2 12-24.
    • (1997) Cell Stress Chaperones , vol.2 , pp. 12-24
    • Piper, P.W.1    Ortiz-Calderon, C.2    Holyoak, C.3    Coote, P.4    Cole, M.5
  • 86
    • 0033764930 scopus 로고    scopus 로고
    • The yeast model for batten disease: Mutations in BTN1, BTN2, and HSP30 alter pH homeostasis
    • S. Chattopadhyay N. E. Muzaffar F. Sherman D. A. Pearce The yeast model for batten disease: mutations in BTN1, BTN2, and HSP30 alter pH homeostasis J. Bacteriol. 2000 182 6418-6423.
    • (2000) J. Bacteriol. , vol.182 , pp. 6418-6423
    • Chattopadhyay, S.1    Muzaffar, N.E.2    Sherman, F.3    Pearce, D.A.4


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