메뉴 건너뛰기




Volumn 42, Issue 12, 2004, Pages 989-1001

Chlamydomonas reinhardtii proteomics

Author keywords

Mass spectrometry; Proteomics; Quantitative proteomics; Subproteome analysis

Indexed keywords

CHLAMYDOMONAS; CHLAMYDOMONAS REINHARDTII;

EID: 13444266075     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2004.09.008     Document Type: Short Survey
Times cited : (34)

References (79)
  • 1
    • 1642382766 scopus 로고    scopus 로고
    • A new approach that allows identification of intron-split peptides from mass spectrometric data in genomic databases
    • J. Allmer, C. Markert, E.J. Stauber, and M. Hippler A new approach that allows identification of intron-split peptides from mass spectrometric data in genomic databases FEBS Lett 562 2004 202 206
    • (2004) FEBS Lett , vol.562 , pp. 202-206
    • Allmer, J.1    Markert, C.2    Stauber, E.J.3    Hippler, M.4
  • 2
    • 19944428191 scopus 로고    scopus 로고
    • Establishment of publicly available cDNA material and information resource of Chlamydomonas reinhardtii (Chlorophyta), to facilitate gene function analysis
    • E. Asamizu, Y. Nakamura, K. Miura, H. Fukuzawa, S. Fujiwara, and M. Hirono Establishment of publicly available cDNA material and information resource of Chlamydomonas reinhardtii (Chlorophyta), to facilitate gene function analysis Phycologia 2004
    • (2004) Phycologia
    • Asamizu, E.1    Nakamura, Y.2    Miura, K.3    Fukuzawa, H.4    Fujiwara, S.5    Hirono, M.6
  • 3
    • 0027070688 scopus 로고
    • Characterization of chlorophyll a/b proteins of photosystem I from Chlamydomonas reinhardtii
    • R. Bassi, S.Y. Soen, G. Frank, H. Zuber, and J.D. Rochaix Characterization of chlorophyll a/b proteins of photosystem I from Chlamydomonas reinhardtii J. Biol. Chem. 267 1992 25714 25721
    • (1992) J. Biol. Chem. , vol.267 , pp. 25714-25721
    • Bassi, R.1    Soen, S.Y.2    Frank, G.3    Zuber, H.4    Rochaix, J.D.5
  • 4
    • 0033123490 scopus 로고    scopus 로고
    • Polarities of the centriolar structure: Morphogenetic consequences
    • J. Beisson, and M. Jerka-Dziadosz Polarities of the centriolar structure: morphogenetic consequences Biol. Cell. 91 1999 367 378
    • (1999) Biol. Cell. , vol.91 , pp. 367-378
    • Beisson, J.1    Jerka-Dziadosz, M.2
  • 5
    • 0028783663 scopus 로고
    • Etiolated cells of Chlamydomonas reinhardtii: Choice material for characterization of mitochondrial membrane polypeptides
    • P. Bennoun, A. Atteia, Y. Pierre, and M. Delosme Etiolated cells of Chlamydomonas reinhardtii: choice material for characterization of mitochondrial membrane polypeptides Proc. Natl. Acad. Sci. USA 92 1995 10202 10206
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10202-10206
    • Bennoun, P.1    Atteia, A.2    Pierre, Y.3    Delosme, M.4
  • 6
    • 0348148910 scopus 로고    scopus 로고
    • Crystal structure of plant photosystem I
    • A. Ben-Shem, F. Frolow, and N. Nelson Crystal structure of plant photosystem I Nature 426 2003 630 635
    • (2003) Nature , vol.426 , pp. 630-635
    • Ben-Shem, A.1    Frolow, F.2    Nelson, N.3
  • 7
    • 0037744859 scopus 로고    scopus 로고
    • The intraflagellar transport machinery of Chlamydomonas reinhardti
    • D.G. Cole The intraflagellar transport machinery of Chlamydomonas reinhardti Traffic 4 2003 435 442
    • (2003) Traffic , vol.4 , pp. 435-442
    • Cole, D.G.1
  • 8
    • 0031750484 scopus 로고    scopus 로고
    • Chlamydomonas kinesin-II-dependent intraflagellar transport (IFT): IFT particles contain proteins required for ciliary assembly in Caenorhabditis elegans sensory neurons
    • D.G. Cole, D.R. Diener, A.L. Himelblau, P.L. Beech, J.C. Fuster, and J.L. Rosenbaum Chlamydomonas kinesin-II-dependent intraflagellar transport (IFT): IFT particles contain proteins required for ciliary assembly in Caenorhabditis elegans sensory neurons J. Cell Biol. 141 1998 993 1008
    • (1998) J. Cell Biol. , vol.141 , pp. 993-1008
    • Cole, D.G.1    Diener, D.R.2    Himelblau, A.L.3    Beech, P.L.4    Fuster, J.C.5    Rosenbaum, J.L.6
  • 9
    • 0026706874 scopus 로고
    • Sequence analysis reveals homology between two proteins of the flagellar radial spoke
    • A.M. Curry, B.D. Williams, and J.L. Rosenbaum Sequence analysis reveals homology between two proteins of the flagellar radial spoke Mol. Cell. Biol. 12 1992 3967 3977
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3967-3977
    • Curry, A.M.1    Williams, B.D.2    Rosenbaum, J.L.3
  • 10
    • 0029187094 scopus 로고
    • Purification of basal bodies and basal body complexes from Chlamydomonas reinhardtii
    • S. Dutcher Purification of basal bodies and basal body complexes from Chlamydomonas reinhardtii Methods Cell Biol. 47 1995 323 334
    • (1995) Methods Cell Biol. , vol.47 , pp. 323-334
    • Dutcher, S.1
  • 11
    • 1442301640 scopus 로고    scopus 로고
    • A genomes-eye view of the light-harvesting polypeptides of Chlamydomonas reinhardtii
    • D. Elrad, and A.R. Grossman A genomes-eye view of the light-harvesting polypeptides of Chlamydomonas reinhardtii Curr. Genet 45 2004 61 75
    • (2004) Curr. Genet , vol.45 , pp. 61-75
    • Elrad, D.1    Grossman, A.R.2
  • 12
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localization of proteins based on their N-terminal amino acid sequence
    • O. Emanuelsson, H. Nielsen, S. Brunak, and G. Von Heijne Predicting subcellular localization of proteins based on their N-terminal amino acid sequence J. Mol. Biol. 300 2000 1005 1016
    • (2000) J. Mol. Biol. , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Von Heijne, G.4
  • 13
    • 0000857494 scopus 로고
    • An approach to corrrelate tandem mass spectral data of peptides with amino acid sequences in a protein database
    • J.K. Eng, A.L. McCormack, and J.R. Yates An approach to corrrelate tandem mass spectral data of peptides with amino acid sequences in a protein database J. Am. Soc. Mass Spectrom. 5 1994 976 989
    • (1994) J. Am. Soc. Mass Spectrom. , vol.5 , pp. 976-989
    • Eng, J.K.1    McCormack, A.L.2    Yates, J.R.3
  • 14
    • 0029110550 scopus 로고
    • Isolation, purification, and characterization of mitochondria from Chlamydomonas reinhardtii
    • M. Eriksson, P. Gardestrom, and G. Samuelsson Isolation, purification, and characterization of mitochondria from Chlamydomonas reinhardtii Plant Physiol. 107 1995 479 483
    • (1995) Plant Physiol. , vol.107 , pp. 479-483
    • Eriksson, M.1    Gardestrom, P.2    Samuelsson, G.3
  • 16
    • 45149135688 scopus 로고
    • Chloroplast transit peptides from the green alga Chlamydomonas reinhardtii share features with both mitochondrial and higher plant chloroplast presequences
    • L. Franzen, J. Rochaix, and G. Von Heijne Chloroplast transit peptides from the green alga Chlamydomonas reinhardtii share features with both mitochondrial and higher plant chloroplast presequences FEBS Lett. 260 1990 165 168
    • (1990) FEBS Lett. , vol.260 , pp. 165-168
    • Franzen, L.1    Rochaix, J.2    Von Heijne, G.3
  • 17
    • 1042279117 scopus 로고    scopus 로고
    • In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts: New proteins, new functions, and a plastid proteome database
    • G. Friso, L. Giacomelli, A.J. Ytterberg, J.-B. Peltier, A. Rudella, and Q. Sun In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts: new proteins, new functions, and a plastid proteome database Plant Cell 16 2004 478 499
    • (2004) Plant Cell , vol.16 , pp. 478-499
    • Friso, G.1    Giacomelli, L.2    Ytterberg, A.J.3    Peltier, J.-B.4    Rudella, A.5    Sun, Q.6
  • 18
    • 0041733229 scopus 로고    scopus 로고
    • Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis
    • J. Froehlich, C. Wilkerson, W. Ray, R. McAndrew, K. Osteryoung, and D. Gage Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis J. Proteome Res. 2 2003 413 425
    • (2003) J. Proteome Res. , vol.2 , pp. 413-425
    • Froehlich, J.1    Wilkerson, C.2    Ray, W.3    McAndrew, R.4    Osteryoung, K.5    Gage, D.6
  • 19
    • 3242885644 scopus 로고    scopus 로고
    • The ultrastructure of the Chlamydomonas reinhardtii basal apparatus: Identification of an early marker of radial asymmetry inherent in the basal body
    • S. Geimer, and M. Melkonian The ultrastructure of the Chlamydomonas reinhardtii basal apparatus: identification of an early marker of radial asymmetry inherent in the basal body J. Cell. Sci. 117 2004 2663 2674
    • (2004) J. Cell. Sci. , vol.117 , pp. 2663-2674
    • Geimer, S.1    Melkonian, M.2
  • 20
    • 0026660307 scopus 로고
    • Green yeast
    • U.W. Goodenough Green yeast Cell 70 1992 533 538
    • (1992) Cell , vol.70 , pp. 533-538
    • Goodenough, U.W.1
  • 22
    • 0032875697 scopus 로고    scopus 로고
    • Quantitative analysis of complex protein mixtures using isotope-coded affinity tags
    • S.P. Gygi, B. Rist, S.A. Gerber, F. Turecek, M.H. Gelb, and R. Aebersold Quantitative analysis of complex protein mixtures using isotope-coded affinity tags Nat. Biotechnol. 17 1999 994 999
    • (1999) Nat. Biotechnol. , vol.17 , pp. 994-999
    • Gygi, S.P.1    Rist, B.2    Gerber, S.A.3    Turecek, F.4    Gelb, M.H.5    Aebersold, R.6
  • 23
    • 0016285694 scopus 로고
    • Characterization of chloroplast and cytoplasmic ribosomal proteins of Chlamydomonas reinhardi by two-dimensional gel electrophoresis
    • M. Hanson, J. Davidson, and L.B. Mets Characterization of chloroplast and cytoplasmic ribosomal proteins of Chlamydomonas reinhardi by two-dimensional gel electrophoresis Mol. Gen. Genet. 132 1974 105 118
    • (1974) Mol. Gen. Genet. , vol.132 , pp. 105-118
    • Hanson, M.1    Davidson, J.2    Mets, L.B.3
  • 25
    • 0842270043 scopus 로고    scopus 로고
    • Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins
    • J.L. Heazlewood, J.S. Tonti-Filippini, A.M. Gout, D.A. Day, J. Whelan, and A.H. Millar Experimental analysis of the Arabidopsis mitochondrial proteome highlights signaling and regulatory components, provides assessment of targeting prediction programs, and indicates plant-specific mitochondrial proteins Plant Cell 16 2004 241 256
    • (2004) Plant Cell , vol.16 , pp. 241-256
    • Heazlewood, J.L.1    Tonti-Filippini, J.S.2    Gout, A.M.3    Day, D.A.4    Whelan, J.5    Millar, A.H.6
  • 26
    • 0030990023 scopus 로고    scopus 로고
    • Fast electron transfer from cytochrome c6 and plastocyanin to photosystem I of Chlamydomonas reinhardtii requires PsaF
    • M. Hippler, F. Drepper, J. Farah, and J.D. Rochaix Fast electron transfer from cytochrome c6 and plastocyanin to photosystem I of Chlamydomonas reinhardtii requires PsaF Biochemistry 36 1997 6343 6349
    • (1997) Biochemistry , vol.36 , pp. 6343-6349
    • Hippler, M.1    Drepper, F.2    Farah, J.3    Rochaix, J.D.4
  • 27
    • 0035543903 scopus 로고    scopus 로고
    • Towards functional proteomics of membrane protein complexes: Analysis of thylakoid membranes from Chlamydomonas reinhardtii
    • M. Hippler, J. Klein, A. Fink, T. Allinger, and P. Hoerth Towards functional proteomics of membrane protein complexes: analysis of thylakoid membranes from Chlamydomonas reinhardtii Plant J. 28 2001 595 606
    • (2001) Plant J. , vol.28 , pp. 595-606
    • Hippler, M.1    Klein, J.2    Fink, A.3    Allinger, T.4    Hoerth, P.5
  • 28
    • 0032487367 scopus 로고    scopus 로고
    • Chlamydomonas genetics, a tool for the study of bioenergetic pathways
    • M. Hippler, K. Redding, and J. Rochaix Chlamydomonas genetics, a tool for the study of bioenergetic pathways Biochim. Biophys. Acta 1367 1998 1 62
    • (1998) Biochim. Biophys. Acta , vol.1367 , pp. 1-62
    • Hippler, M.1    Redding, K.2    Rochaix, J.3
  • 29
    • 0035805255 scopus 로고    scopus 로고
    • Integrated genomic and proteomic analyses of a systematically perturbed metabolic network
    • T. Ideker, V. Thorsson, J.A. Ranish, R. Christmas, J. Buhler, and J.K. Eng Integrated genomic and proteomic analyses of a systematically perturbed metabolic network Science 292 2001 929 934
    • (2001) Science , vol.292 , pp. 929-934
    • Ideker, T.1    Thorsson, V.2    Ranish, J.A.3    Christmas, R.4    Buhler, J.5    Eng, J.K.6
  • 30
    • 1942435934 scopus 로고    scopus 로고
    • Precise circadian clocks in prokaryotic cyanobacteria
    • C.H. Johnson Precise circadian clocks in prokaryotic cyanobacteria Curr. Issues Mol. Biol. 6 2004 103 110
    • (2004) Curr. Issues Mol. Biol. , vol.6 , pp. 103-110
    • Johnson, C.H.1
  • 33
    • 0142245713 scopus 로고    scopus 로고
    • Alternative splicing and proteome diversity in plants: The tip of the iceberg has just emerged
    • K. Kazan Alternative splicing and proteome diversity in plants: the tip of the iceberg has just emerged Trends Plant Sci. 8 2003 468 471
    • (2003) Trends Plant Sci. , vol.8 , pp. 468-471
    • Kazan, K.1
  • 34
    • 0031452439 scopus 로고    scopus 로고
    • Protein disulfide isomerase as a regulator of chloroplast translational activation
    • J. Kim, and S.P. Mayfield Protein disulfide isomerase as a regulator of chloroplast translational activation Science 278 1997 1954 1957
    • (1997) Science , vol.278 , pp. 1954-1957
    • Kim, J.1    Mayfield, S.P.2
  • 37
    • 0032895578 scopus 로고    scopus 로고
    • Chlamydomonas: The cell and its genomes
    • P.A. Lefebvre, and C.D. Silflow Chlamydomonas: the cell and its genomes Genetics 151 1999 9 14
    • (1999) Genetics , vol.151 , pp. 9-14
    • Lefebvre, P.A.1    Silflow, C.D.2
  • 39
    • 2342501364 scopus 로고    scopus 로고
    • Comparative genomics identifies a flagellar and basal body proteome that includes the BBS5 human disease gene
    • J. Li, J. Gerdes, C. Haycraft, Y. Fan, T. Teslovich, and H. May-Simera Comparative genomics identifies a flagellar and basal body proteome that includes the BBS5 human disease gene Cell 117 2004 541 552
    • (2004) Cell , vol.117 , pp. 541-552
    • Li, J.1    Gerdes, J.2    Haycraft, C.3    Fan, Y.4    Teslovich, T.5    May-Simera, H.6
  • 40
    • 0034255836 scopus 로고    scopus 로고
    • Maturation of cellular Fe-S proteins: An essential function of mitochondria
    • R. Lill, and G. Kispal Maturation of cellular Fe-S proteins: an essential function of mitochondria Trends Biochem. Sci. 25 2000 352 356
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 352-356
    • Lill, R.1    Kispal, G.2
  • 41
    • 1342296319 scopus 로고
    • Flagellar mutants of Chlamydomonas: Studies of radial spoke-defective strains by dikaryon and revertant analysis
    • D. Luck, G. Piperno, Z. Ramanis, and B. Huang Flagellar mutants of Chlamydomonas: studies of radial spoke-defective strains by dikaryon and revertant analysis Proc. Natl. Acad. Sci. USA 74 1977 3456 3460
    • (1977) Proc. Natl. Acad. Sci. USA , vol.74 , pp. 3456-3460
    • Luck, D.1    Piperno, G.2    Ramanis, Z.3    Huang, B.4
  • 42
    • 0028575316 scopus 로고
    • Error-tolerant identification of peptides in sequence databases by peptide sequence tags
    • M. Mann, and M. Wilm Error-tolerant identification of peptides in sequence databases by peptide sequence tags Anal. Chem. 66 1994 4390 4399
    • (1994) Anal. Chem. , vol.66 , pp. 4390-4399
    • Mann, M.1    Wilm, M.2
  • 43
    • 0033952311 scopus 로고    scopus 로고
    • How centrioles work: Lessons from green yeast
    • W. Marshall, and J. Rosenbaum How centrioles work: lessons from green yeast Curr. Opin. Cell Biol. 12 2000 119 125
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 119-125
    • Marshall, W.1    Rosenbaum, J.2
  • 44
    • 0036845754 scopus 로고    scopus 로고
    • The Chlamydomonas reinhardtii plastid chromosome: Islands of genes in a sea of repeats
    • J.E. Maul, J.W. Lilly, L. Cui, C.W. Depamphilis, W. Miller, and E.H. Harris The Chlamydomonas reinhardtii plastid chromosome: islands of genes in a sea of repeats Plant Cell 14 2002 2659 2679
    • (2002) Plant Cell , vol.14 , pp. 2659-2679
    • Maul, J.E.1    Lilly, J.W.2    Cui, L.3    Depamphilis, C.W.4    Miller, W.5    Harris, E.H.6
  • 45
    • 0038617729 scopus 로고    scopus 로고
    • Alternative splicing in the human, mouse and rat genomes is associated with an increased frequency of exon creation and/or loss
    • B. Modrek, and C.J. Lee Alternative splicing in the human, mouse and rat genomes is associated with an increased frequency of exon creation and/or loss Nat. Genet. 34 2003 177 180
    • (2003) Nat. Genet. , vol.34 , pp. 177-180
    • Modrek, B.1    Lee, C.J.2
  • 46
    • 12244262259 scopus 로고    scopus 로고
    • Adaptation to Fe-deficiency requires remodeling of the photosynthetic apparatus
    • J.L. Moseley, T. Allinger, S. Herzog, P. Hoerth, E. Wehinger, and S. Merchant Adaptation to Fe-deficiency requires remodeling of the photosynthetic apparatus EMBO J. 21 2002 6709 6720
    • (2002) EMBO J. , vol.21 , pp. 6709-6720
    • Moseley, J.L.1    Allinger, T.2    Herzog, S.3    Hoerth, P.4    Wehinger, E.5    Merchant, S.6
  • 47
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • K. Nakai, and P. Horton PSORT: a program for detecting sorting signals in proteins and predicting their subcellular localization Trends Biochem. Sci. 24 1999 34 35
    • (1999) Trends Biochem. Sci. , vol.24 , pp. 34-35
    • Nakai, K.1    Horton, P.2
  • 48
    • 1042266254 scopus 로고    scopus 로고
    • Analysis, statistical validation and dissemination of large-scale proteomics datasets generated by tandem MS
    • A.I. Nesvizhskii, and R. Aebersold Analysis, statistical validation and dissemination of large-scale proteomics datasets generated by tandem MS Drug Discov. Today 9 2004 173 181
    • (2004) Drug Discov. Today , vol.9 , pp. 173-181
    • Nesvizhskii, A.I.1    Aebersold, R.2
  • 49
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • S.-E. Ong, B. Blagoev, I. Kratchmarova, D.B. Kristensen, H. Steen, and A. Pandey Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics Mol. Cell Proteomics 1 2002 376 386
    • (2002) Mol. Cell Proteomics , vol.1 , pp. 376-386
    • Ong, S.-E.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6
  • 51
    • 0036007922 scopus 로고    scopus 로고
    • Central functions of the lumenal and peripheral thylakoid proteome of Arabidopsis determined by experimentation and genome-wide prediction
    • J.-B. Peltier, O. Emanuelsson, D.E. Kalume, J. Ytterberg, G. Friso, and A. Rudella Central functions of the lumenal and peripheral thylakoid proteome of Arabidopsis determined by experimentation and genome-wide prediction Plant Cell 14 2002 211 236
    • (2002) Plant Cell , vol.14 , pp. 211-236
    • Peltier, J.-B.1    Emanuelsson, O.2    Kalume, D.E.3    Ytterberg, J.4    Friso, G.5    Rudella, A.6
  • 52
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • D.N. Perkins, D.J.C. Pappin, D.M. Creasy, and J.S. Cottrell Probability-based protein identification by searching sequence databases using mass spectrometry data Electrophoresis 20 1999 3551 3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.C.2    Creasy, D.M.3    Cottrell, J.S.4
  • 53
    • 0036007665 scopus 로고    scopus 로고
    • Computational gene finding in plants
    • M. Pertea, and S. Salzberg Computational gene finding in plants Plant Mol. Biol. 48 2002 39 48
    • (2002) Plant Mol. Biol. , vol.48 , pp. 39-48
    • Pertea, M.1    Salzberg, S.2
  • 54
    • 0024694921 scopus 로고
    • Electrophoretic and immunological comparisons of chloroplast and prokaryotic ribosomal proteins reveal that certain families of large subunit proteins are evolutionarily conserved
    • B. Randolph-Anderson, N. Gillham, and J. Boynton Electrophoretic and immunological comparisons of chloroplast and prokaryotic ribosomal proteins reveal that certain families of large subunit proteins are evolutionarily conserved J. Mol. Evol. 29 1989 68 88
    • (1989) J. Mol. Evol. , vol.29 , pp. 68-88
    • Randolph-Anderson, B.1    Gillham, N.2    Boynton, J.3
  • 55
    • 0038708337 scopus 로고    scopus 로고
    • C. elegans ORFeome version 1.1: Experimental verification of the genome annotation and resource for proteome-scale protein expression
    • J. Reboul, P. Vaglio, J.-F. Rual, P. Lamesch, M. Martinez, and C.M. Armstrong C. elegans ORFeome version 1.1: experimental verification of the genome annotation and resource for proteome-scale protein expression Nat. Genet. 34 2003 35 41
    • (2003) Nat. Genet. , vol.34 , pp. 35-41
    • Reboul, J.1    Vaglio, P.2    Rual, J.-F.3    Lamesch, P.4    Martinez, M.5    Armstrong, C.M.6
  • 56
    • 0347134600 scopus 로고    scopus 로고
    • Thylakoid membrane at altered metabolic state: Challenging the forgotten realms of the proteome
    • S. Rexroth, J.M.W.M.z. Tittingdorf, F. Krause, N.A. Dencher, and H. Seelert Thylakoid membrane at altered metabolic state: challenging the forgotten realms of the proteome Electrophoresis 24 2003 2814 2823
    • (2003) Electrophoresis , vol.24 , pp. 2814-2823
    • Rexroth, S.1    Tittingdorf, J.M.W.M.Z.2    Krause, F.3    Dencher, N.A.4    Seelert, H.5
  • 57
    • 1642276286 scopus 로고    scopus 로고
    • An improved prediction of chloroplast proteins reveals diversities and commonalities in the chloroplast proteomes of Arabidopsis and rice
    • E. Richly, and D. Leister An improved prediction of chloroplast proteins reveals diversities and commonalities in the chloroplast proteomes of Arabidopsis and rice Gene 329 2004 11 16
    • (2004) Gene , vol.329 , pp. 11-16
    • Richly, E.1    Leister, D.2
  • 58
    • 85047685989 scopus 로고    scopus 로고
    • Assembly, function, and dynamics of the photosynthetic machinery in Chlamydomonas reinhardtii
    • J.-D. Rochaix Assembly, function, and dynamics of the photosynthetic machinery in Chlamydomonas reinhardtii Plant Physiol. 127 2001 1394 1398
    • (2001) Plant Physiol. , vol.127 , pp. 1394-1398
    • Rochaix, J.-D.1
  • 60
    • 0031784934 scopus 로고    scopus 로고
    • Endogenous fluctuations of DNA topology in the chloroplast of Chlamydomonas reinhardtii
    • M.L. Salvador, U. Klein, and L. Bogorad Endogenous fluctuations of DNA topology in the chloroplast of Chlamydomonas reinhardtii Mol. Cell. Biol. 18 1998 7235 7242
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7235-7242
    • Salvador, M.L.1    Klein, U.2    Bogorad, L.3
  • 61
    • 0030292843 scopus 로고    scopus 로고
    • The Chlamydomonas reinhardtii LI818 gene represents a distant relative of the cabI/II genes that is regulated during the cell cycle and in response to illumination
    • F. Savard, C. Richard, and M. Guertin The Chlamydomonas reinhardtii LI818 gene represents a distant relative of the cabI/II genes that is regulated during the cell cycle and in response to illumination Plant Mol. Biol. 32 1996 461 473
    • (1996) Plant Mol. Biol. , vol.32 , pp. 461-473
    • Savard, F.1    Richard, C.2    Guertin, M.3
  • 64
    • 12244286739 scopus 로고    scopus 로고
    • Chlamydomonas reinhardtii genome project. A guide to the generation and use of the cDNA information
    • J. Shrager, C. Hauser, C.-W. Chang, E.H. Harris, J. Davies, and J. McDermott Chlamydomonas reinhardtii genome project. A guide to the generation and use of the cDNA information Plant Physiol. 131 2003 401 408
    • (2003) Plant Physiol. , vol.131 , pp. 401-408
    • Shrager, J.1    Hauser, C.2    Chang, C.-W.3    Harris, E.H.4    Davies, J.5    McDermott, J.6
  • 66
    • 85047681474 scopus 로고    scopus 로고
    • Assembly and motility of eukaryotic cilia and flagella. Lessons from Chlamydomonas reinhardtii
    • C.D. Silflow, and P.A. Lefebvre Assembly and motility of eukaryotic cilia and flagella. Lessons from Chlamydomonas reinhardtii Plant Physiol. 127 2001 1500 1507
    • (2001) Plant Physiol. , vol.127 , pp. 1500-1507
    • Silflow, C.D.1    Lefebvre, P.A.2
  • 67
    • 2942589051 scopus 로고    scopus 로고
    • Predotar: A tool for rapidly screening proteomes for N-terminal targeting sequences
    • I. Small, N. Peeters, F. Legeai, and C. Lurin Predotar: a tool for rapidly screening proteomes for N-terminal targeting sequences Proteomics 4 2004 1581 1590
    • (2004) Proteomics , vol.4 , pp. 1581-1590
    • Small, I.1    Peeters, N.2    Legeai, F.3    Lurin, C.4
  • 69
    • 3042581458 scopus 로고    scopus 로고
    • Analysis of curated and predicted plastid subproteomes of Arabidopsis. Subcellular compartmentalization leads to distinctive proteome properties
    • Q. Sun, O. Emanuelsson, and K.J. Van Wijk Analysis of curated and predicted plastid subproteomes of Arabidopsis. Subcellular compartmentalization leads to distinctive proteome properties Plant Physiol. 135 2004 723 734
    • (2004) Plant Physiol. , vol.135 , pp. 723-734
    • Sun, Q.1    Emanuelsson, O.2    Van Wijk, K.J.3
  • 70
    • 0025911941 scopus 로고
    • Directed chloroplast transformation in Chlamydomonas reinhardtii: Insertional inactivation of the psaC gene encoding the iron sulfur protein destabilizes photosystem I
    • Y. Takahashi, M. Goldschmidt-Clermont, S.Y. Soen, L.G. Franzen, and J.D. Rochaix Directed chloroplast transformation in Chlamydomonas reinhardtii: insertional inactivation of the psaC gene encoding the iron sulfur protein destabilizes photosystem I EMBO J. 10 1991 2033 2040
    • (1991) EMBO J. , vol.10 , pp. 2033-2040
    • Takahashi, Y.1    Goldschmidt-Clermont, M.2    Soen, S.Y.3    Franzen, L.G.4    Rochaix, J.D.5
  • 71
    • 2942750314 scopus 로고    scopus 로고
    • Comparison of the subunit compositions of the PSI-LHCI supercomplex and the LHCI in the green alga Chlamydomonas reinhardtii
    • Y. Takahashi, T.A. Yasui, E.J. Stauber, and M. Hippler Comparison of the subunit compositions of the PSI-LHCI supercomplex and the LHCI in the green alga Chlamydomonas reinhardtii Biochemistry 43 2004 7816 7823
    • (2004) Biochemistry , vol.43 , pp. 7816-7823
    • Takahashi, Y.1    Yasui, T.A.2    Stauber, E.J.3    Hippler, M.4
  • 72
    • 1842861617 scopus 로고    scopus 로고
    • The transit peptide of CP29 thylakoid protein in Chlamydomonas reinhardtii is not removed but undergoes acetylation and phosphorylation
    • M.V. Turkina, A. Villarejo, and A.V. Vener The transit peptide of CP29 thylakoid protein in Chlamydomonas reinhardtii is not removed but undergoes acetylation and phosphorylation FEBS Lett. 564 2004 104 108
    • (2004) FEBS Lett. , vol.564 , pp. 104-108
    • Turkina, M.V.1    Villarejo, A.2    Vener, A.V.3
  • 73
    • 0037434980 scopus 로고    scopus 로고
    • From genomics to proteomics
    • M. Tyers, and M. Mann From genomics to proteomics Nature 422 2003 193 197
    • (2003) Nature , vol.422 , pp. 193-197
    • Tyers, M.1    Mann, M.2
  • 74
    • 0037986673 scopus 로고    scopus 로고
    • Identification of novel mitochondrial protein components of Chlamydomonas reinhardtii. A proteomic approach
    • R. Van Lis, A. Atteia, G. Mendoza-Hernandez, and D. Gonzalez-Halphen Identification of novel mitochondrial protein components of Chlamydomonas reinhardtii. A proteomic approach Plant Physiol. 132 2003 318 330
    • (2003) Plant Physiol. , vol.132 , pp. 318-330
    • Van Lis, R.1    Atteia, A.2    Mendoza-Hernandez, G.3    Gonzalez-Halphen, D.4
  • 75
    • 0442323440 scopus 로고    scopus 로고
    • Functional proteomics of circadian expressed proteins from Chlamydomonas reinhardtii
    • V. Wagner, M. Fiedler, C. Markert, M. Hippler, and M. Mittag Functional proteomics of circadian expressed proteins from Chlamydomonas reinhardtii FEBS Lett. 559 2004 129 135
    • (2004) FEBS Lett. , vol.559 , pp. 129-135
    • Wagner, V.1    Fiedler, M.2    Markert, C.3    Hippler, M.4    Mittag, M.5
  • 76
    • 0024706870 scopus 로고
    • Molecular cloning and sequence analysis of the Chlamydomonas gene coding for radial spoke protein 3: Flagellar mutation pf-14 is an ochre allele
    • B. Williams, M. Velleca, A. Curry, and J. Rosenbaum Molecular cloning and sequence analysis of the Chlamydomonas gene coding for radial spoke protein 3: flagellar mutation pf-14 is an ochre allele J. Cell Biol. 109 1989 235 245
    • (1989) J. Cell Biol. , vol.109 , pp. 235-245
    • Williams, B.1    Velleca, M.2    Curry, A.3    Rosenbaum, J.4
  • 77
    • 2542500559 scopus 로고    scopus 로고
    • Oda5p, a novel axonemal protein required for assembly of the outer dynein arm and an associated adenylate kinase
    • M. Wirschell, G. Pazour, A. Yoda, M. Hirono, R. Kamiya, and G.B. Witman Oda5p, a novel axonemal protein required for assembly of the outer dynein arm and an associated adenylate kinase Mol. Biol. Cell 15 2004 2729 2741
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2729-2741
    • Wirschell, M.1    Pazour, G.2    Yoda, A.3    Hirono, M.4    Kamiya, R.5    Witman, G.B.6
  • 78
    • 0141817918 scopus 로고    scopus 로고
    • Proteomic characterization of the Chlamydomonas reinhardtii chloroplast ribosome: Identification of proteins unique to the 70S ribosome
    • K. Yamaguchi, M.V. Beligni, S. Prieto, P.A. Haynes, W.H. McDonald, and J.R. Yates Proteomic characterization of the Chlamydomonas reinhardtii chloroplast ribosome: identification of proteins unique to the 70S ribosome J. Biol. Chem. 278 2003 33774 33785
    • (2003) J. Biol. Chem. , vol.278 , pp. 33774-33785
    • Yamaguchi, K.1    Beligni, M.V.2    Prieto, S.3    Haynes, P.A.4    McDonald, W.H.5    Yates, J.R.6
  • 79
    • 2942692262 scopus 로고    scopus 로고
    • The circadian RNA-binding protein CHLAMY 1 represents a novel type heteromer of RNA recognition motif and lysine homology domain-containing subunits
    • B. Zhao, C. Schneid, D. Iliev, E.-M. Schmidt, V. Wagner, F. Wollnik, and M. Mittag The circadian RNA-binding protein CHLAMY 1 represents a novel type heteromer of RNA recognition motif and lysine homology domain-containing subunits Eukaryotic Cell 3 2004 815 825
    • (2004) Eukaryotic Cell , vol.3 , pp. 815-825
    • Zhao, B.1    Schneid, C.2    Iliev, D.3    Schmidt, E.-M.4    Wagner, V.5    Wollnik, F.6    Mittag, M.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.