메뉴 건너뛰기




Volumn 165, Issue 5, 2014, Pages 662-675

Proteomics Analysis of Heterogeneous Flagella in Brown Algae (Stramenopiles)

Author keywords

Blue light receptor; Brown algae; Creatine kinase; Flagella; Phototaxis; Proteomics

Indexed keywords

ALGAL PROTEIN; PROTEOME;

EID: 84908120732     PISSN: 14344610     EISSN: 16180941     Source Type: Journal    
DOI: 10.1016/j.protis.2014.07.007     Document Type: Article
Times cited : (34)

References (77)
  • 2
    • 56849114016 scopus 로고    scopus 로고
    • An overview of the phylogeny and diversity of eukaryotes
    • Baldauf S.L. An overview of the phylogeny and diversity of eukaryotes. J Syst Evol 2008, 46:263-273.
    • (2008) J Syst Evol , vol.46 , pp. 263-273
    • Baldauf, S.L.1
  • 3
    • 33847370317 scopus 로고    scopus 로고
    • Functional genomics in Trypanosoma brucei identifies evolutionarily conserved components of motile flagella
    • Baron D.M., Ralston K.S., Kabututu Z.P., Hill K.L. Functional genomics in Trypanosoma brucei identifies evolutionarily conserved components of motile flagella. J Cell Sci 2007, 120:478-491.
    • (2007) J Cell Sci , vol.120 , pp. 478-491
    • Baron, D.M.1    Ralston, K.S.2    Kabututu, Z.P.3    Hill, K.L.4
  • 4
    • 33751526052 scopus 로고    scopus 로고
    • The roles of cilia in developmental disorders and disease
    • Bisgrove B.W., Yost H.J. The roles of cilia in developmental disorders and disease. Development 2006, 133:4131-4143.
    • (2006) Development , vol.133 , pp. 4131-4143
    • Bisgrove, B.W.1    Yost, H.J.2
  • 5
    • 0028867374 scopus 로고
    • Identification of a molecular chaperone in the eukaryotic flagellum and its localization to the site of microtubule assembly
    • Bloch M.A., Johnson K.A. Identification of a molecular chaperone in the eukaryotic flagellum and its localization to the site of microtubule assembly. J Cell Sci 1995, 108:3541-3545.
    • (1995) J Cell Sci , vol.108 , pp. 3541-3545
    • Bloch, M.A.1    Johnson, K.A.2
  • 8
    • 0036208071 scopus 로고    scopus 로고
    • The phagotrophic origin of eukaryotes and phylogenetic classification of Protozoa
    • Cavalier-Smith T. The phagotrophic origin of eukaryotes and phylogenetic classification of Protozoa. Int J Syst Evol Microbiol 2002, 52:297-354.
    • (2002) Int J Syst Evol Microbiol , vol.52 , pp. 297-354
    • Cavalier-Smith, T.1
  • 9
    • 0011962966 scopus 로고
    • Brown Algae and Chromophyte Phylogeny
    • Clarendon Press, Oxford, J.C. Green, B.S.C. Leadbeater, W.L. Diver (Eds.)
    • Clayton M.N. Brown Algae and Chromophyte Phylogeny. The Chromophyte Alge: Problems and Perspectives 1989, 229-254. Clarendon Press, Oxford. J.C. Green, B.S.C. Leadbeater, W.L. Diver (Eds.).
    • (1989) The Chromophyte Alge: Problems and Perspectives , pp. 229-254
    • Clayton, M.N.1
  • 11
    • 0035853139 scopus 로고    scopus 로고
    • Structure of a flavin-binding plant photoreceptor domain: insights into light-mediated signal transduction
    • Crosson S., Moffat K. Structure of a flavin-binding plant photoreceptor domain: insights into light-mediated signal transduction. Proc Natl Acad Sci USA 2001, 98:2995-3000.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 2995-3000
    • Crosson, S.1    Moffat, K.2
  • 12
    • 0037435618 scopus 로고    scopus 로고
    • The LOV domain family: photoresponsive signaling modules coupled to diverse output domains
    • Crosson S., Rajagopal S., Moffat K. The LOV domain family: photoresponsive signaling modules coupled to diverse output domains. Biochemistry 2003, 42:2-10.
    • (2003) Biochemistry , vol.42 , pp. 2-10
    • Crosson, S.1    Rajagopal, S.2    Moffat, K.3
  • 13
    • 27944469172 scopus 로고    scopus 로고
    • An incredible decade for the primary cilium: a look at a once-forgotten organelle
    • Davenport J.R., Yoder B.K. An incredible decade for the primary cilium: a look at a once-forgotten organelle. Am J Physiol-Renal 2005, 289:F1159-F1169.
    • (2005) Am J Physiol-Renal , vol.289
    • Davenport, J.R.1    Yoder, B.K.2
  • 14
    • 0038778365 scopus 로고    scopus 로고
    • Congenital hydrocephalus in hy3 mice is caused by a frameshift mutation in Hydin, a large novel gene
    • Davy B.E., Robinson M.L. Congenital hydrocephalus in hy3 mice is caused by a frameshift mutation in Hydin, a large novel gene. Hum Mol Genet 2003, 12:1163-1170.
    • (2003) Hum Mol Genet , vol.12 , pp. 1163-1170
    • Davy, B.E.1    Robinson, M.L.2
  • 15
    • 41749112440 scopus 로고    scopus 로고
    • The conserved PA14 domain of cell wall-associated fungal adhesins governs their glycan-binding specificity
    • de Groot P.W.J., Klis F.M. The conserved PA14 domain of cell wall-associated fungal adhesins governs their glycan-binding specificity. Mol Microbiol 2008, 68:535-537.
    • (2008) Mol Microbiol , vol.68 , pp. 535-537
    • de Groot, P.W.J.1    Klis, F.M.2
  • 16
    • 67349218869 scopus 로고    scopus 로고
    • The RJL family of small GTPases is an ancient eukaryotic invention probably functionally associated with the flagellar apparatus
    • Elias M., Archibald J.M. The RJL family of small GTPases is an ancient eukaryotic invention probably functionally associated with the flagellar apparatus. Gene 2009, 442:63-72.
    • (2009) Gene , vol.442 , pp. 63-72
    • Elias, M.1    Archibald, J.M.2
  • 17
    • 4444291840 scopus 로고    scopus 로고
    • Mutations in a member of the Ras superfamily of small GTP-binding proteins causes Bardet-Biedl syndrome
    • Fan Y., Esmail M.A., Ansley S.J., Blacque O.E., Boroevich K., Ross A.J., et al. Mutations in a member of the Ras superfamily of small GTP-binding proteins causes Bardet-Biedl syndrome. Nat Genet 2004, 36:989-993.
    • (2004) Nat Genet , vol.36 , pp. 989-993
    • Fan, Y.1    Esmail, M.A.2    Ansley, S.J.3    Blacque, O.E.4    Boroevich, K.5    Ross, A.J.6
  • 18
    • 7944237936 scopus 로고    scopus 로고
    • The many faces of filamin: a versatile molecular scaffold for cell motility and signalling
    • Feng Y., Walsh C.A. The many faces of filamin: a versatile molecular scaffold for cell motility and signalling. Nat Cell Biol 2004, 6:1034-1038.
    • (2004) Nat Cell Biol , vol.6 , pp. 1034-1038
    • Feng, Y.1    Walsh, C.A.2
  • 19
    • 35448961665 scopus 로고    scopus 로고
    • When cilia go bad: cilia defects and ciliopathies
    • Fliegauf M., Benzing T., Omran H. When cilia go bad: cilia defects and ciliopathies. Nat Rev Mol Cell Biol 2007, 11:880-893.
    • (2007) Nat Rev Mol Cell Biol , vol.11 , pp. 880-893
    • Fliegauf, M.1    Benzing, T.2    Omran, H.3
  • 20
    • 0036496289 scopus 로고    scopus 로고
    • Photomovement of the swarmers of the brown algae Scytosiphon lomentaria and Petalonia fascia: effect of photon irradiance, spectral composition and UV dose
    • Flores-Moya A., Posudin Y.I., Fernández J.A., Figueroa F.L., Kawai H. Photomovement of the swarmers of the brown algae Scytosiphon lomentaria and Petalonia fascia: effect of photon irradiance, spectral composition and UV dose. J Photochem Photobiol B 2002, 66:134-140.
    • (2002) J Photochem Photobiol B , vol.66 , pp. 134-140
    • Flores-Moya, A.1    Posudin, Y.I.2    Fernández, J.A.3    Figueroa, F.L.4    Kawai, H.5
  • 21
    • 84873083334 scopus 로고    scopus 로고
    • Ultrastructural analysis of flagellar development in plurilocular sporangia of Ectocarpus siliculosus (Phaeophyceae)
    • Fu G., Nagasato C., Ito T., Müller D.G., Motomura T. Ultrastructural analysis of flagellar development in plurilocular sporangia of Ectocarpus siliculosus (Phaeophyceae). Protoplasma 2013, 250:261-272.
    • (2013) Protoplasma , vol.250 , pp. 261-272
    • Fu, G.1    Nagasato, C.2    Ito, T.3    Müller, D.G.4    Motomura, T.5
  • 22
    • 21244464338 scopus 로고    scopus 로고
    • Identification and characterization of a fluorescent flagellar protein from the brown alga Scytosiphon lomentaria (Scytosiphonales, Phaeophyceae): A flavoprotein homologous to Old Yellow Enzyme
    • Fujita S., Iseki M., Yoshikawa S., Makino Y., Watanabe M., Motomura T., Kawai H., Murakami A. Identification and characterization of a fluorescent flagellar protein from the brown alga Scytosiphon lomentaria (Scytosiphonales, Phaeophyceae): A flavoprotein homologous to Old Yellow Enzyme. Eur J Phycol 2005, 40:159-167.
    • (2005) Eur J Phycol , vol.40 , pp. 159-167
    • Fujita, S.1    Iseki, M.2    Yoshikawa, S.3    Makino, Y.4    Watanabe, M.5    Motomura, T.6    Kawai, H.7    Murakami, A.8
  • 23
    • 0036796467 scopus 로고    scopus 로고
    • CDART: protein homology by domain architecture
    • Geer L.Y. CDART: protein homology by domain architecture. Genome Res 2002, 12:1619-1623.
    • (2002) Genome Res , vol.12 , pp. 1619-1623
    • Geer, L.Y.1
  • 24
    • 0000176188 scopus 로고
    • Analysis of the flagellar beat pattern of male Ectocarpus siliculosus gametes (Phaeophyta) in relation to chemotactic stimulation by female cells
    • Geller A., Müller D.G. Analysis of the flagellar beat pattern of male Ectocarpus siliculosus gametes (Phaeophyta) in relation to chemotactic stimulation by female cells. J Exp Biol 1981, 92:53-66.
    • (1981) J Exp Biol , vol.92 , pp. 53-66
    • Geller, A.1    Müller, D.G.2
  • 25
    • 33748335482 scopus 로고    scopus 로고
    • The ciliary proteome database: an integrated community resource for the genetic and functional dissection of cilia
    • Gherman A., Davis E.E., Katsanis N. The ciliary proteome database: an integrated community resource for the genetic and functional dissection of cilia. Nat Genet 2006, 38:961-962.
    • (2006) Nat Genet , vol.38 , pp. 961-962
    • Gherman, A.1    Davis, E.E.2    Katsanis, N.3
  • 26
    • 54149116728 scopus 로고    scopus 로고
    • Swimming with protists: perception, motility and flagellum assembly
    • Ginger M.L., Portman N., McKean P.G. Swimming with protists: perception, motility and flagellum assembly. Nat Rev Microbiol 2008, 6:838-850.
    • (2008) Nat Rev Microbiol , vol.6 , pp. 838-850
    • Ginger, M.L.1    Portman, N.2    McKean, P.G.3
  • 27
    • 1942519407 scopus 로고    scopus 로고
    • Chlamydomonas sensory rhodopsins A and B: cellular content and role in photophobic responses
    • Govorunova E.G., Jung K.H., Sineshchekov O.A., Spudich J.L. Chlamydomonas sensory rhodopsins A and B: cellular content and role in photophobic responses. Biophys J 2004, 86:2342-2349.
    • (2004) Biophys J , vol.86 , pp. 2342-2349
    • Govorunova, E.G.1    Jung, K.H.2    Sineshchekov, O.A.3    Spudich, J.L.4
  • 28
    • 67549126280 scopus 로고    scopus 로고
    • World-wide electronic publication, National University of Ireland, Galway.
    • Guiry MD, Guiry GM (2014) AlgaeBase. World-wide electronic publication, National University of Ireland, Galway. http://www.algaebase.org/.
    • (2014) AlgaeBase
    • Guiry, M.D.1    Guiry, G.M.2
  • 29
    • 84985279785 scopus 로고
    • Ultrastructure of swarmers in the Laminariales (Phaeophyceae). I. Zoospores
    • Henry E.C., Cole K.M. Ultrastructure of swarmers in the Laminariales (Phaeophyceae). I. Zoospores. J Phycol 1982, 18:550-569.
    • (1982) J Phycol , vol.18 , pp. 550-569
    • Henry, E.C.1    Cole, K.M.2
  • 30
    • 84985209703 scopus 로고
    • Ultrastructure of swarmers in the Laminariales (Phaeophyceae). II. Sperms
    • Henry E.C., Cole K.M. Ultrastructure of swarmers in the Laminariales (Phaeophyceae). II. Sperms. J Phycol 1982, 18:570-579.
    • (1982) J Phycol , vol.18 , pp. 570-579
    • Henry, E.C.1    Cole, K.M.2
  • 31
    • 84880980811 scopus 로고    scopus 로고
    • Sperm ultrastructure in the diatoms Melosira and Thalassiosira and the significance of the 9 + 0 configuration
    • Idei M., Osada K., Sato S., Nakayama T., Nagumo T., Mann D.G. Sperm ultrastructure in the diatoms Melosira and Thalassiosira and the significance of the 9 + 0 configuration. Protoplasma 2013, 250:833-850.
    • (2013) Protoplasma , vol.250 , pp. 833-850
    • Idei, M.1    Osada, K.2    Sato, S.3    Nakayama, T.4    Nagumo, T.5    Mann, D.G.6
  • 33
    • 84867508935 scopus 로고    scopus 로고
    • Decay of genes encoding the oomycete flagellar proteome in the downy mildew Hyaloperonospora arabidopsidis
    • Judelson H.S., Shrivastava J., Manson J. Decay of genes encoding the oomycete flagellar proteome in the downy mildew Hyaloperonospora arabidopsidis. PLoS ONE 2012, 7:e47624.
    • (2012) PLoS ONE , vol.7
    • Judelson, H.S.1    Shrivastava, J.2    Manson, J.3
  • 34
    • 84986840358 scopus 로고
    • A flavin-like autofluorescent substance in the posterior flagellum of golden and brown algae
    • Kawai H. A flavin-like autofluorescent substance in the posterior flagellum of golden and brown algae. J Phycol 1988, 24:114-117.
    • (1988) J Phycol , vol.24 , pp. 114-117
    • Kawai, H.1
  • 35
    • 51249163514 scopus 로고
    • Green flagellar autofluorescence in brown algal swarmers and their phototactic responses
    • Kawai H. Green flagellar autofluorescence in brown algal swarmers and their phototactic responses. Bot Mag Tokyo 1992, 105:171-184.
    • (1992) Bot Mag Tokyo , vol.105 , pp. 171-184
    • Kawai, H.1
  • 36
    • 0002916815 scopus 로고
    • Flagellar autofluorescence in forty-four chlorophyll c-containing algae
    • Kawai H., Inouye I. Flagellar autofluorescence in forty-four chlorophyll c-containing algae. Phycologia 1989, 28:222-227.
    • (1989) Phycologia , vol.28 , pp. 222-227
    • Kawai, H.1    Inouye, I.2
  • 37
    • 0001087591 scopus 로고
    • Phototactic responses in the gametes of the brown alga, Ectocarpus siliculosus
    • Kawai H., Müller D., Fölster E., Häder D.-P. Phototactic responses in the gametes of the brown alga, Ectocarpus siliculosus. Planta 1990, 182:292-297.
    • (1990) Planta , vol.182 , pp. 292-297
    • Kawai, H.1    Müller, D.2    Fölster, E.3    Häder, D.-P.4
  • 38
    • 0006393781 scopus 로고    scopus 로고
    • Microspectrofluorometry of the autofluorescent flagellum in phototactic brown algal zoids
    • Kawai H., Nakamura S., Mimuro M., Furuya M., Watanabe M. Microspectrofluorometry of the autofluorescent flagellum in phototactic brown algal zoids. Protoplasma 1996, 191:172-177.
    • (1996) Protoplasma , vol.191 , pp. 172-177
    • Kawai, H.1    Nakamura, S.2    Mimuro, M.3    Furuya, M.4    Watanabe, M.5
  • 39
    • 0032509129 scopus 로고    scopus 로고
    • The fibronectin type III domain as a scaffold for novel binding proteins
    • Koide A., Bailey C.W., Huang X., Koide S. The fibronectin type III domain as a scaffold for novel binding proteins. J Mol Biol 1998, 284:1141-1151.
    • (1998) J Mol Biol , vol.284 , pp. 1141-1151
    • Koide, A.1    Bailey, C.W.2    Huang, X.3    Koide, S.4
  • 41
    • 33846962482 scopus 로고    scopus 로고
    • Chlamydomonas reinhardtii hydin is a central pair protein required for flagellar motility
    • Lechtreck K.-F., Witman G.B. Chlamydomonas reinhardtii hydin is a central pair protein required for flagellar motility. J Cell Biol 2007, 176:473-482.
    • (2007) J Cell Biol , vol.176 , pp. 473-482
    • Lechtreck, K.-F.1    Witman, G.B.2
  • 43
    • 2942592126 scopus 로고    scopus 로고
    • Deletion of the Parkin coregulated gene causes male sterility in the quakingviable mouse mutant
    • Lorenzetti D., Bishop C.E., Justice M.J. Deletion of the Parkin coregulated gene causes male sterility in the quakingviable mouse mutant. Proc Natl Acad Sci USA 2004, 101:8402-8407.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 8402-8407
    • Lorenzetti, D.1    Bishop, C.E.2    Justice, M.J.3
  • 44
    • 84872256330 scopus 로고    scopus 로고
    • The evolution of flavin-binding photoreceptors: an ancient chromophore serving trendy blue-light sensors
    • Losi A., Gärtner W. The evolution of flavin-binding photoreceptors: an ancient chromophore serving trendy blue-light sensors. Annu Rev Plant Biol 2012, 63:49-72.
    • (2012) Annu Rev Plant Biol , vol.63 , pp. 49-72
    • Losi, A.1    Gärtner, W.2
  • 45
    • 33645904854 scopus 로고    scopus 로고
    • NIMA-related kinases defective in murine models of polycystic kidney diseases localize to primary cilia and centrosomes
    • Mahjoub M.R., Trapp M.L., Quarmby L.M. NIMA-related kinases defective in murine models of polycystic kidney diseases localize to primary cilia and centrosomes. J Am Soc Nephrol 2005, 16:3485-3489.
    • (2005) J Am Soc Nephrol , vol.16 , pp. 3485-3489
    • Mahjoub, M.R.1    Trapp, M.L.2    Quarmby, L.M.3
  • 46
    • 0031475076 scopus 로고    scopus 로고
    • The fine structure of the male gamete of Ectocarpus siliculosus (Ectocarpales
    • Maier I. The fine structure of the male gamete of Ectocarpus siliculosus (Ectocarpales. Phaeophyceae). I. General structure of the cell. Eur J Phycol 1997, 32:241-325.
    • (1997) Phaeophyceae). I. General structure of the cell. Eur J Phycol , vol.32 , pp. 241-325
    • Maier, I.1
  • 47
    • 0031475077 scopus 로고    scopus 로고
    • The fine structure of the male gamete of Ectocarpus siliculosus (Ectocarpales
    • Maier I. The fine structure of the male gamete of Ectocarpus siliculosus (Ectocarpales. Phaeophyceae). II. The flagellar apparatus. Eur J Phycol 1997, 32:255-266.
    • (1997) Phaeophyceae). II. The flagellar apparatus. Eur J Phycol , vol.32 , pp. 255-266
    • Maier, I.1
  • 48
    • 2642678540 scopus 로고
    • Electron microscope observations on the zoospores of Pylaiella and Laminaria
    • Manton I., Clarke B. Electron microscope observations on the zoospores of Pylaiella and Laminaria. J Exp Bot 1951, 2:242-243.
    • (1951) J Exp Bot , vol.2 , pp. 242-243
    • Manton, I.1    Clarke, B.2
  • 49
    • 0344111695 scopus 로고
    • Further observations with the electron microscope on spermatozoids in the brown algae
    • Manton I., Clarke B., Greenwood A.D. Further observations with the electron microscope on spermatozoids in the brown algae. J Exp Bot 1953, 4:319-329.
    • (1953) J Exp Bot , vol.4 , pp. 319-329
    • Manton, I.1    Clarke, B.2    Greenwood, A.D.3
  • 50
    • 38349018369 scopus 로고    scopus 로고
    • The cell biological basis of ciliary disease
    • Marshall W.F. The cell biological basis of ciliary disease. J Cell Biol 2008, 180:17-21.
    • (2008) J Cell Biol , vol.180 , pp. 17-21
    • Marshall, W.F.1
  • 51
    • 33746528106 scopus 로고    scopus 로고
    • Cilia: Tuning in to the cell's antenna
    • Marshall W.F., Nonaka S. Cilia: Tuning in to the cell's antenna. Curr Biol 2006, 16:R604-R614.
    • (2006) Curr Biol , vol.16
    • Marshall, W.F.1    Nonaka, S.2
  • 53
    • 84934439875 scopus 로고    scopus 로고
    • The evolution of eukaryotic cilia and flagella as motile and sensory organelles
    • Mitchell D.R. The evolution of eukaryotic cilia and flagella as motile and sensory organelles. Adv Exp Med Biol 2007, 607:130-140.
    • (2007) Adv Exp Med Biol , vol.607 , pp. 130-140
    • Mitchell, D.R.1
  • 55
    • 84989741615 scopus 로고
    • Flagellum autofluorescence and photoaccumulation in heterokont algae
    • Müller D.G., Maier I., Müller H. Flagellum autofluorescence and photoaccumulation in heterokont algae. Photochem Photobiol 1987, 46:1003-1008.
    • (1987) Photochem Photobiol , vol.46 , pp. 1003-1008
    • Müller, D.G.1    Maier, I.2    Müller, H.3
  • 56
    • 79957838808 scopus 로고    scopus 로고
    • Spag16, an axonemal central apparatus gene, encodes a male germ cell nuclear speckle protein that regulates SPAG16 mRNA expression
    • Nagarkatti-Gude D.R., Jaimez R., Henderson S.C., Teves M.E., Zhang Z., Strauss J.F. Spag16, an axonemal central apparatus gene, encodes a male germ cell nuclear speckle protein that regulates SPAG16 mRNA expression. PLoS ONE 2011, 6:e20625.
    • (2011) PLoS ONE , vol.6
    • Nagarkatti-Gude, D.R.1    Jaimez, R.2    Henderson, S.C.3    Teves, M.E.4    Zhang, Z.5    Strauss, J.F.6
  • 57
    • 0037096166 scopus 로고    scopus 로고
    • Influence of the centrosome in cytokinesis of brown algae: polyspermic zygotes of Scytosiphon lomentaria (Scytosiphonales, Phaeophyceae)
    • Nagasato C., Motomura T. Influence of the centrosome in cytokinesis of brown algae: polyspermic zygotes of Scytosiphon lomentaria (Scytosiphonales, Phaeophyceae). J Cell Sci 2002, 115:2541-2548.
    • (2002) J Cell Sci , vol.115 , pp. 2541-2548
    • Nagasato, C.1    Motomura, T.2
  • 58
    • 27644477833 scopus 로고    scopus 로고
    • 3D structure of eukaryotic flagella in a quiescent state revealed by cryo-electron tomography
    • Nicastro D., McIntosh J.R., Baumeister W. 3D structure of eukaryotic flagella in a quiescent state revealed by cryo-electron tomography. Proc Nat Acad Sci USA 2005, 102:15889-15894.
    • (2005) Proc Nat Acad Sci USA , vol.102 , pp. 15889-15894
    • Nicastro, D.1    McIntosh, J.R.2    Baumeister, W.3
  • 59
    • 0000077720 scopus 로고
    • The Evolutionary Origin of the Brown Algae: Information from Studies of Motile Cell Ultrastructure
    • Oxford University Press, Oxford, J.C. Green, B.S.C. Leadbeater, W.L. Diver (Eds.)
    • O'Kelly C.J. The Evolutionary Origin of the Brown Algae: Information from Studies of Motile Cell Ultrastructure. The Chromophyte Algae: Problems and Perspectives 1989, 255-278. Oxford University Press, Oxford. J.C. Green, B.S.C. Leadbeater, W.L. Diver (Eds.).
    • (1989) The Chromophyte Algae: Problems and Perspectives , pp. 255-278
    • O'Kelly, C.J.1
  • 60
    • 14644388135 scopus 로고    scopus 로고
    • Phototactic activity in Chlamydomonas "non-phototactic" mutants deficient in Ca2+-dependent control of flagellar dominance or in inner-arm dynein
    • Okita N., Isogai N., Hirono M., Kamiya R., Yoshimura K. Phototactic activity in Chlamydomonas "non-phototactic" mutants deficient in Ca2+-dependent control of flagellar dominance or in inner-arm dynein. J Cell Sci 2005, 118:529-537.
    • (2005) J Cell Sci , vol.118 , pp. 529-537
    • Okita, N.1    Isogai, N.2    Hirono, M.3    Kamiya, R.4    Yoshimura, K.5
  • 61
    • 0020332838 scopus 로고
    • Immunofluorescence and Immunocytochemical Procedures with Affinity Purified Antibodies: Tubulin-containing Structures
    • Academic Press, New York
    • Osborn M., Weber K. Immunofluorescence and Immunocytochemical Procedures with Affinity Purified Antibodies: Tubulin-containing Structures. Methods in Cell Biology 1982, 24:97-132. Academic Press, New York.
    • (1982) Methods in Cell Biology , vol.24 , pp. 97-132
    • Osborn, M.1    Weber, K.2
  • 62
    • 58149485065 scopus 로고    scopus 로고
    • Targeting proteins to the ciliary membrane
    • Pazour G.J., Bloodgood R.A. Targeting proteins to the ciliary membrane. Curr Top Dev Biol 2008, 85:115-149.
    • (2008) Curr Top Dev Biol , vol.85 , pp. 115-149
    • Pazour, G.J.1    Bloodgood, R.A.2
  • 64
    • 0002733010 scopus 로고
    • Media and Prospects for the Cultivation of Marine Algae
    • Watanabe A, Hattori A (eds) Hakone, Sep 1996, Jan Soc Plant Physiol.
    • Provasoli L (1968) Media and Prospects for the Cultivation of Marine Algae. In Watanabe A, Hattori A (eds) Culture and Collection of Algae. Proc US - Japan Conf, Hakone, Sep 1996, Jan Soc Plant Physiol, pp 63-75.
    • (1968) Culture and Collection of Algae. Proc US - Japan Conf , pp. 63-75
    • Provasoli, L.1
  • 67
    • 25144494636 scopus 로고    scopus 로고
    • Characterization of a molecular chaperone present in the eukaryotic flagellum
    • Shapiro J., Ingram J., Johnson K.A. Characterization of a molecular chaperone present in the eukaryotic flagellum. Eukaryot Cell 2005, 4:1591-1594.
    • (2005) Eukaryot Cell , vol.4 , pp. 1591-1594
    • Shapiro, J.1    Ingram, J.2    Johnson, K.A.3
  • 68
    • 77953324852 scopus 로고    scopus 로고
    • A multi-locus time-calibrated phylogeny of the brown algae (Heterokonta, Ochrophyta, Phaeophyceae): Investigating the evolutionary nature of the "brown algal crown radiation"
    • Silberfeld T., Leigh J.W., Verbruggen H., Cruaud C., De Reviers B., Rousseau F. A multi-locus time-calibrated phylogeny of the brown algae (Heterokonta, Ochrophyta, Phaeophyceae): Investigating the evolutionary nature of the "brown algal crown radiation". Mol Phylogenet Evol 2010, 56:659-674.
    • (2010) Mol Phylogenet Evol , vol.56 , pp. 659-674
    • Silberfeld, T.1    Leigh, J.W.2    Verbruggen, H.3    Cruaud, C.4    De Reviers, B.5    Rousseau, F.6
  • 69
    • 0032740537 scopus 로고    scopus 로고
    • Molecular chaperones in cilia and flagella: implications for protein turnover
    • Stephens R.E., Lemieux N.A. Molecular chaperones in cilia and flagella: implications for protein turnover. Cell Motil Cytoskeleton 1999, 44:274-283.
    • (1999) Cell Motil Cytoskeleton , vol.44 , pp. 274-283
    • Stephens, R.E.1    Lemieux, N.A.2
  • 70
    • 0021843865 scopus 로고
    • Metabolite channeling: a phosphorylcreatine shuttle to mediate high energy phosphate transport between sperm mitochondrion and tail
    • Tombes R.M., Shapiro B.M. Metabolite channeling: a phosphorylcreatine shuttle to mediate high energy phosphate transport between sperm mitochondrion and tail. Cell 1985, 41:325-334.
    • (1985) Cell , vol.41 , pp. 325-334
    • Tombes, R.M.1    Shapiro, B.M.2
  • 71
    • 0023372480 scopus 로고
    • Creatine kinase-dependent energy transport in sea urchin spermatozoa. Flagellar wave attenuation and theoretical analysis of high energy phosphate diffusion
    • Tombes R.M., Brokaw C., Shapiro B.M. Creatine kinase-dependent energy transport in sea urchin spermatozoa. Flagellar wave attenuation and theoretical analysis of high energy phosphate diffusion. Biophys J 1987, 52:75-86.
    • (1987) Biophys J , vol.52 , pp. 75-86
    • Tombes, R.M.1    Brokaw, C.2    Shapiro, B.M.3
  • 72
    • 80054949733 scopus 로고    scopus 로고
    • Protein kinase A acts at the basal body of the primary cilium to prevent Gli2 activation and ventralization of the mouse neural tube
    • Tuson M., He M., Anderson K.V. Protein kinase A acts at the basal body of the primary cilium to prevent Gli2 activation and ventralization of the mouse neural tube. Development 2011, 138:4921-4930.
    • (2011) Development , vol.138 , pp. 4921-4930
    • Tuson, M.1    He, M.2    Anderson, K.V.3
  • 73
    • 0032944179 scopus 로고    scopus 로고
    • Spermiogenesis is impaired in mice bearing a targeted mutation in the protein phosphatase 1cgamma gene
    • Varmuza S., Jurisicova A., Okano K., Hudson J., Boekelheide K., Shipp E.B. Spermiogenesis is impaired in mice bearing a targeted mutation in the protein phosphatase 1cgamma gene. Devel Biol 1999, 205:98-110.
    • (1999) Devel Biol , vol.205 , pp. 98-110
    • Varmuza, S.1    Jurisicova, A.2    Okano, K.3    Hudson, J.4    Boekelheide, K.5    Shipp, E.B.6
  • 74
    • 56849118127 scopus 로고    scopus 로고
    • Pix proteins and the evolution of centrioles
    • Woodland H.R., Fry A.M. Pix proteins and the evolution of centrioles. PLoS ONE 2008, 3:e3778.
    • (2008) PLoS ONE , vol.3
    • Woodland, H.R.1    Fry, A.M.2
  • 75
    • 0025287976 scopus 로고
    • The phosphocreatine shuttle of sea urchin sperm: flagellar creatine kinase resulted from a gene triplication
    • Wothe D.D., Charbonneau H., Shapiro B.M. The phosphocreatine shuttle of sea urchin sperm: flagellar creatine kinase resulted from a gene triplication. Proc Natl Acad Sci USA 1990, 87:5203-5207.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 5203-5207
    • Wothe, D.D.1    Charbonneau, H.2    Shapiro, B.M.3
  • 76
    • 4444326525 scopus 로고    scopus 로고
    • Haploinsufficiency for the murine orthologue of Chlamydomonas PF20 disrupts spermatogenesis
    • Zhang Z., Kostetskii I., Moss S.B., Jones B.H., Ho C., Wang H., et al. Haploinsufficiency for the murine orthologue of Chlamydomonas PF20 disrupts spermatogenesis. Proc Natl Acad Sci USA 2004, 101:12946-12951.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 12946-12951
    • Zhang, Z.1    Kostetskii, I.2    Moss, S.B.3    Jones, B.H.4    Ho, C.5    Wang, H.6
  • 77
    • 0036841725 scopus 로고    scopus 로고
    • A sperm-associated WD repeat protein orthologous to Chlamydomonas PF20 associates with Spag6, the mammalian orthologue of Chlamydomonas PF16
    • Zhang Z., Sapiro R., Kapfhamer D., Bucan M., Bray J., Chennathukuzhi V., et al. A sperm-associated WD repeat protein orthologous to Chlamydomonas PF20 associates with Spag6, the mammalian orthologue of Chlamydomonas PF16. Mol Cell Biol 2002, 22:7993-8004.
    • (2002) Mol Cell Biol , vol.22 , pp. 7993-8004
    • Zhang, Z.1    Sapiro, R.2    Kapfhamer, D.3    Bucan, M.4    Bray, J.5    Chennathukuzhi, V.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.