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Volumn 42, Issue 12, 2004, Pages 963-977

Plastid proteomics

Author keywords

Chloroplast; Mass spectrometry; Proteomics

Indexed keywords

ALGAE; CHLOROPHYTA;

EID: 13444267478     PISSN: 09819428     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.plaphy.2004.10.015     Document Type: Short Survey
Times cited : (111)

References (102)
  • 3
    • 10344242448 scopus 로고    scopus 로고
    • New functions of the thylakoid membrane proteome of Arabidopsis thaliana revealed by a simple, fast and versatile fractionation strategy
    • J.B. Peltier, A.J. Ytterberg, Q. Sun, and K.J. Van Wijk New functions of the thylakoid membrane proteome of Arabidopsis thaliana revealed by a simple, fast and versatile fractionation strategy J. Biol. Chem. 279 2004 49367 49383
    • (2004) J. Biol. Chem. , vol.279 , pp. 49367-49383
    • Peltier, J.B.1    Ytterberg, A.J.2    Sun, Q.3    Van Wijk, K.J.4
  • 5
    • 0034193582 scopus 로고    scopus 로고
    • Solute pores, ion channels, and metabolite transporters in the outer and inner envelope membranes of higher plant plastids
    • H.E. Neuhaus, and R. Wagner Solute pores, ion channels, and metabolite transporters in the outer and inner envelope membranes of higher plant plastids Biochim. Biophys. Acta 1465 2000 307 323
    • (2000) Biochim. Biophys. Acta , vol.1465 , pp. 307-323
    • Neuhaus, H.E.1    Wagner, R.2
  • 6
    • 2442480656 scopus 로고    scopus 로고
    • Solute transporters as connecting elements between cytosol and plastid stroma
    • A.P. Weber Solute transporters as connecting elements between cytosol and plastid stroma Curr. Opin. Plant Biol. 7 2004 247 253
    • (2004) Curr. Opin. Plant Biol. , vol.7 , pp. 247-253
    • Weber, A.P.1
  • 8
    • 0037446849 scopus 로고    scopus 로고
    • Intracellular signalling: The language of the chloroplast
    • P. Jarvis Intracellular signalling: the language of the chloroplast Curr. Biol. 13 2003 R314 R316
    • (2003) Curr. Biol. , vol.13
    • Jarvis, P.1
  • 9
    • 0037143630 scopus 로고    scopus 로고
    • Integral membrane proteins of the chloroplast envelope: Identification and subcellular localization of new transporters
    • M. Ferro, D. Salvi, H. Riviere-Rolland, T. Vermat, D. Seigneurin-Berny, and D. Grunwald Integral membrane proteins of the chloroplast envelope: identification and subcellular localization of new transporters Proc. Natl. Acad. Sci. USA 99 2002 11487 11492
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11487-11492
    • Ferro, M.1    Salvi, D.2    Riviere-Rolland, H.3    Vermat, T.4    Seigneurin-Berny, D.5    Grunwald, D.6
  • 10
    • 0032881817 scopus 로고    scopus 로고
    • Technical advance: Differential extraction of hydrophobic proteins from chloroplast envelope membranes: A subcellular-specific proteomic approach to identify rare intrinsic membrane proteins
    • D. Seigneurin-Berny, N. Rolland, J. Garin, and J. Joyard Technical advance: differential extraction of hydrophobic proteins from chloroplast envelope membranes: a subcellular-specific proteomic approach to identify rare intrinsic membrane proteins Plant J. 19 1999 217 228
    • (1999) Plant J. , vol.19 , pp. 217-228
    • Seigneurin-Berny, D.1    Rolland, N.2    Garin, J.3    Joyard, J.4
  • 12
    • 0041733229 scopus 로고    scopus 로고
    • Proteomic study of the Arabidopsis thaliana chloroplastic envelope membrane utilizing alternatives to traditional two-dimensional electrophoresis
    • J.E. Froehlich, C.G. Wilkerson, W.K. Ray, R.S. McAndrew, K.W. Osteryoung, and D.A. 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.E.1    Wilkerson, C.G.2    Ray, W.K.3    McAndrew, R.S.4    Osteryoung, K.W.5    Gage, D.A.6
  • 13
    • 85030828241 scopus 로고    scopus 로고
    • Profiling protein expression changes in monocytic U97 cells exposed to PMA using a twodimensional LC-MS/MS on a hybrid quadropole orthogonal acceleration time-of-flight (Q-TOF) mass spectrometer
    • San Francisco
    • A. Millar, S. Brunet, C. Hughes, E. Bonneil, M. Dominguez, J. Lanoix, et al., Profiling protein expression changes in monocytic U97 cells exposed to PMA using a twodimensional LC-MS/MS on a hybrid quadropole orthogonal acceleration time-of-flight (Q-TOF) mass spectrometer, in: Fifth International Symposium on Mass Spectrometry, San Francisco, 2001.
    • (2001) Fifth International Symposium on Mass Spectrometry
    • Millar, A.1    Brunet, S.2    Hughes, C.3    Bonneil, E.4    Dominguez, M.5    Lanoix, J.6
  • 14
    • 0037379183 scopus 로고    scopus 로고
    • Prediction of the plant beta-barrel proteome: A case study of the chloroplast outer envelope
    • E. Schleiff, L.A. Eichacker, K. Eckart, T. Becker, O. Mirus, and T. Stahl Prediction of the plant beta-barrel proteome: A case study of the chloroplast outer envelope Protein Sci. 12 2003 748 759
    • (2003) Protein Sci. , vol.12 , pp. 748-759
    • Schleiff, E.1    Eichacker, L.A.2    Eckart, K.3    Becker, T.4    Mirus, O.5    Stahl, T.6
  • 15
    • 12144291195 scopus 로고    scopus 로고
    • MAPMAN: A user-driven tool to display genomics data sets onto diagrams of metabolic pathways and other biological processes
    • O. Thimm, O. Blasing, Y. Gibon, A. Nagel, S. Meyer, and P. Kruger MAPMAN: a user-driven tool to display genomics data sets onto diagrams of metabolic pathways and other biological processes Plant J. 37 2004 914 939
    • (2004) Plant J. , vol.37 , pp. 914-939
    • Thimm, O.1    Blasing, O.2    Gibon, Y.3    Nagel, A.4    Meyer, S.5    Kruger, P.6
  • 17
    • 0032549515 scopus 로고    scopus 로고
    • The thylakoid lumen of chloroplasts. Isolation and characterization
    • T. Kieselbach, A. Hagman, B. Andersson, and W.P. Schroder The thylakoid lumen of chloroplasts. Isolation and characterization J. Biol. Chem. 273 1998 6710 6716
    • (1998) J. Biol. Chem. , vol.273 , pp. 6710-6716
    • Kieselbach, T.1    Hagman, A.2    Andersson, B.3    Schroder, W.P.4
  • 18
    • 0034026047 scopus 로고    scopus 로고
    • Proteomics of the chloroplast. Systematic identification and targeting analysis of lumenal and peripheral thylakoid proteins
    • J.B. Peltier, G. Friso, D.E. Kalume, P. Roepstorff, F. Nilsson, and I. Adamska Proteomics of the chloroplast. Systematic identification and targeting analysis of lumenal and peripheral thylakoid proteins Plant Cell 12 2000 319 342
    • (2000) Plant Cell , vol.12 , pp. 319-342
    • Peltier, J.B.1    Friso, G.2    Kalume, D.E.3    Roepstorff, P.4    Nilsson, F.5    Adamska, I.6
  • 19
    • 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
  • 20
    • 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
  • 21
    • 0034072182 scopus 로고    scopus 로고
    • Over-expression of a pepper plastid lipid-associated protein in tobacco leads to changes in plastid ultrastructure and plant development upon stress
    • P. Rey, B. Gillet, S. Romer, F. Eymery, J. Massimino, and G. Peltier Over-expression of a pepper plastid lipid-associated protein in tobacco leads to changes in plastid ultrastructure and plant development upon stress Plant J. 21 2000 483 494 [In Process Citation]
    • (2000) Plant J. , vol.21 , pp. 483-494
    • Rey, P.1    Gillet, B.2    Romer, S.3    Eymery, F.4    Massimino, J.5    Peltier, G.6
  • 22
    • 0033103281 scopus 로고    scopus 로고
    • Identification of proteins associated with plastoglobules isolated from pea (Pisum sativum L.) chloroplasts
    • F. Kessler, D. Schnell, and G. Blobel Identification of proteins associated with plastoglobules isolated from pea (Pisum sativum L.) chloroplasts Planta 208 1999 107 113
    • (1999) Planta , vol.208 , pp. 107-113
    • Kessler, F.1    Schnell, D.2    Blobel, G.3
  • 23
    • 0036051481 scopus 로고    scopus 로고
    • The chloroplast grana proteome defined by intact mass measurements from liquid chromatography mass spectrometry
    • S.M. Gomez, J.N. Nishio, K.F. Faull, and J.P. Whitelegge The chloroplast grana proteome defined by intact mass measurements from liquid chromatography mass spectrometry Mol. Cell. Proteom. 1 2002 46 59
    • (2002) Mol. Cell. Proteom. , vol.1 , pp. 46-59
    • Gomez, S.M.1    Nishio, J.N.2    Faull, K.F.3    Whitelegge, J.P.4
  • 26
    • 0035018583 scopus 로고    scopus 로고
    • Multiple pathways used for the targeting of thylakoid proteins in chloroplasts
    • C. Robinson, S.J. Thompson, and C. Woolhead Multiple pathways used for the targeting of thylakoid proteins in chloroplasts Traffic 2 2001 245 251
    • (2001) Traffic , vol.2 , pp. 245-251
    • Robinson, C.1    Thompson, S.J.2    Woolhead, C.3
  • 27
    • 0035852345 scopus 로고    scopus 로고
    • Function of a chloroplast SRP in thylakoid protein export
    • L.A. Eichacker, and R. Henry Function of a chloroplast SRP in thylakoid protein export Biochim. Biophys. Acta 1541 2001 120 134
    • (2001) Biochim. Biophys. Acta , vol.1541 , pp. 120-134
    • Eichacker, L.A.1    Henry, R.2
  • 28
    • 0036929475 scopus 로고    scopus 로고
    • Proteomics of light-harvesting proteins in different plant species. Analysis and comparison by liquid chromatography-electrospray ionization mass spectrometry. Photosystem I
    • L. Zolla, S. Rinalducci, A.M. Timperio, and C.G. Huber Proteomics of light-harvesting proteins in different plant species. Analysis and comparison by liquid chromatography-electrospray ionization mass spectrometry. Photosystem I Plant Physiol. 130 2002 1938 1950
    • (2002) Plant Physiol. , vol.130 , pp. 1938-1950
    • Zolla, L.1    Rinalducci, S.2    Timperio, A.M.3    Huber, C.G.4
  • 29
    • 0037249679 scopus 로고    scopus 로고
    • Proteomics of light-harvesting proteins in different plant species. Analysis and comparison by liquid chromatography-electrospray ionization mass spectrometry
    • L. Zolla, A.M. Timperio, W. Walcher, and C.G. Huber Proteomics of light-harvesting proteins in different plant species. Analysis and comparison by liquid chromatography-electrospray ionization mass spectrometry Photosystem II, Plant Physiol. 131 2003 198 214
    • (2003) Photosystem II, Plant Physiol. , vol.131 , pp. 198-214
    • Zolla, L.1    Timperio, A.M.2    Walcher, W.3    Huber, C.G.4
  • 30
    • 0842263994 scopus 로고    scopus 로고
    • Is each light-harvesting complex protein important for plant fitness?
    • U. Ganeteg, C. Kulheim, J. Andersson, and S. Jansson Is each light-harvesting complex protein important for plant fitness? Plant Physiol. 134 2004 502 509
    • (2004) Plant Physiol. , vol.134 , pp. 502-509
    • Ganeteg, U.1    Kulheim, C.2    Andersson, J.3    Jansson, S.4
  • 31
    • 0033773868 scopus 로고    scopus 로고
    • Organic solvent extraction as a versatile procedure to identify hydrophobic chloroplast membrane proteins
    • M. Ferro, D. Seigneurin-Berny, N. Rolland, A. Chapel, D. Salvi, and J. Garin Organic solvent extraction as a versatile procedure to identify hydrophobic chloroplast membrane proteins Electrophoresis 21 2000 3517 3526
    • (2000) Electrophoresis , vol.21 , pp. 3517-3526
    • Ferro, M.1    Seigneurin-Berny, D.2    Rolland, N.3    Chapel, A.4    Salvi, D.5    Garin, J.6
  • 32
    • 0037047381 scopus 로고    scopus 로고
    • PGR5 is involved in cyclic electron flow around photosystem I and is essential for photoprotection in Arabidopsis
    • Y. Munekage, M. Hojo, J. Meurer, T. Endo, M. Tasaka, and T. Shikanai PGR5 is involved in cyclic electron flow around photosystem I and is essential for photoprotection in Arabidopsis Cell 110 2002 361
    • (2002) Cell , vol.110 , pp. 361
    • Munekage, Y.1    Hojo, M.2    Meurer, J.3    Endo, T.4    Tasaka, M.5    Shikanai, T.6
  • 33
    • 0031281935 scopus 로고    scopus 로고
    • Three phase partitioning: Concentration and purification of proteins
    • C. Dennison, and R. Lovrien Three phase partitioning: concentration and purification of proteins Protein Exp. Purif. 11 1997 149 161
    • (1997) Protein Exp. Purif. , vol.11 , pp. 149-161
    • Dennison, C.1    Lovrien, R.2
  • 35
    • 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
  • 36
    • 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
  • 37
    • 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
  • 38
    • 3042815334 scopus 로고    scopus 로고
    • Trypsin cleaves exclusively C-terminal to Arginine and lysine residues
    • J.V. Olsen, S.E. Ong, and M. Mann Trypsin cleaves exclusively C-terminal to Arginine and lysine residues Mol. Cell. Proteom 3 2004 608 614
    • (2004) Mol. Cell. Proteom , vol.3 , pp. 608-614
    • Olsen, J.V.1    Ong, S.E.2    Mann, M.3
  • 39
    • 0041920588 scopus 로고    scopus 로고
    • The Arabidopsis ppi1 mutant is specifically defective in the expression, chloroplast import, and accumulation of photosynthetic proteins
    • S. Kubis, A. Baldwin, R. Patel, A. Razzaq, P. Dupree, and K. Lilley The Arabidopsis ppi1 mutant is specifically defective in the expression, chloroplast import, and accumulation of photosynthetic proteins Plant Cell 15 2003 1859 1871
    • (2003) Plant Cell , vol.15 , pp. 1859-1871
    • Kubis, S.1    Baldwin, A.2    Patel, R.3    Razzaq, A.4    Dupree, P.5    Lilley, K.6
  • 40
    • 0043166918 scopus 로고    scopus 로고
    • Evaluation of saturation labelling two-dimensional difference gel electrophoresis fluorescent dyes
    • J. Shaw, R. Rowlinson, J. Nickson, T. Stone, A. Sweet, and K. Williams Evaluation of saturation labelling two-dimensional difference gel electrophoresis fluorescent dyes Proteomics 3 2003 1181 1195
    • (2003) Proteomics , vol.3 , pp. 1181-1195
    • Shaw, J.1    Rowlinson, R.2    Nickson, J.3    Stone, T.4    Sweet, A.5    Williams, K.6
  • 41
    • 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
  • 42
    • 0034066471 scopus 로고    scopus 로고
    • Membrane proteins and proteomics: Un amour impossible?
    • V. Santoni, M. Molloy, and T. Rabilloud Membrane proteins and proteomics: un amour impossible? Electrophoresis 21 2000 1054 1070
    • (2000) Electrophoresis , vol.21 , pp. 1054-1070
    • Santoni, V.1    Molloy, M.2    Rabilloud, T.3
  • 43
    • 0028214450 scopus 로고
    • Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis
    • H. Schägger, W.A. Cramer, and G. Von Jagow Analysis of molecular masses and oligomeric states of protein complexes by blue native electrophoresis and isolation of membrane protein complexes by two-dimensional native electrophoresis Anal. Biochem. 217 1994 220 230
    • (1994) Anal. Biochem. , vol.217 , pp. 220-230
    • Schägger, H.1    Cramer, W.A.2    Von Jagow, G.3
  • 44
    • 1642580518 scopus 로고    scopus 로고
    • Protein assembly of photosystem II and accumulation of subcomplexes in the absence of low molecular mass subunits PsbL and PsbJ
    • M. Suorsa, R.E. Regel, V. Paakkarinen, N. Battchikova, R.G. Herrmann, and E.M. Aro Protein assembly of photosystem II and accumulation of subcomplexes in the absence of low molecular mass subunits PsbL and PsbJ Eur. J. Biochem. 271 2004 96 107
    • (2004) Eur. J. Biochem. , vol.271 , pp. 96-107
    • Suorsa, M.1    Regel, R.E.2    Paakkarinen, V.3    Battchikova, N.4    Herrmann, R.G.5    Aro, E.M.6
  • 45
    • 3142653751 scopus 로고    scopus 로고
    • Subunit composition of NDH-1 complexes of Synechocystis sp. PCC 6803: Identification of two new ndh gene products with nuclear-encoded homologues in the chloroplast Ndh complex
    • P. Prommeenate, A.M. Lennon, C. Markert, M. Hippler, and P.J. Nixon Subunit composition of NDH-1 complexes of Synechocystis sp. PCC 6803: identification of two new ndh gene products with nuclear-encoded homologues in the chloroplast Ndh complex J. Biol. Chem. 279 2004 28165 28173
    • (2004) J. Biol. Chem. , vol.279 , pp. 28165-28173
    • Prommeenate, P.1    Lennon, A.M.2    Markert, C.3    Hippler, M.4    Nixon, P.J.5
  • 47
    • 0031744191 scopus 로고    scopus 로고
    • Cellular differentiation in the leaf
    • J.A. Langdale Cellular differentiation in the leaf Curr. Opin. Cell Biol. 10 1998 734 738
    • (1998) Curr. Opin. Cell Biol. , vol.10 , pp. 734-738
    • Langdale, J.A.1
  • 49
    • 0032910388 scopus 로고    scopus 로고
    • The biogenesis and assembly of photosynthetic proteins in thylakoid membranes 1
    • F.A. Wollman, L. Minai, and R. Nechushtai The biogenesis and assembly of photosynthetic proteins in thylakoid membranes 1 Biochim. Biophys. Acta 1411 1999 21 85
    • (1999) Biochim. Biophys. Acta , vol.1411 , pp. 21-85
    • Wollman, F.A.1    Minai, L.2    Nechushtai, R.3
  • 50
    • 0032481317 scopus 로고    scopus 로고
    • Identification of a functional respiratory complex in chloroplasts through analysis of tobacco mutants containing disrupted plastid ndh genes
    • P.A. Burrows, L.A. Sazanov, Z. Svab, P. Maliga, and P.J. Nixon Identification of a functional respiratory complex in chloroplasts through analysis of tobacco mutants containing disrupted plastid ndh genes EMBO J. 17 1998 868 876
    • (1998) EMBO J. , vol.17 , pp. 868-876
    • Burrows, P.A.1    Sazanov, L.A.2    Svab, Z.3    Maliga, P.4    Nixon, P.J.5
  • 51
    • 0035851111 scopus 로고    scopus 로고
    • Ferredoxin:NADP+ oxidoreductase is a subunit of the chloroplast cytochrome b6f complex
    • H. Zhang, J.P. Whitelegge, and W.A. Cramer Ferredoxin:NADP+ oxidoreductase is a subunit of the chloroplast cytochrome b6f complex J. Biol. Chem. 276 2001 38159 38165
    • (2001) J. Biol. Chem. , vol.276 , pp. 38159-38165
    • Zhang, H.1    Whitelegge, J.P.2    Cramer, W.A.3
  • 52
    • 0037067133 scopus 로고    scopus 로고
    • Toc, tic, and chloroplast protein import
    • P. Jarvis, and J. Soll Toc, tic, and chloroplast protein import Biochim. Biophys. Acta 1590 2002 177 189
    • (2002) Biochim. Biophys. Acta , vol.1590 , pp. 177-189
    • Jarvis, P.1    Soll, J.2
  • 53
    • 0036166363 scopus 로고    scopus 로고
    • A GTPase gate for protein import into chloroplasts
    • F. Kessler, and D.J. Schnell A GTPase gate for protein import into chloroplasts Nat. Struct. Biol. 9 2002 81 83
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 81-83
    • Kessler, F.1    Schnell, D.J.2
  • 54
    • 0035852296 scopus 로고    scopus 로고
    • Molecular chaperones involved in chloroplast protein import
    • D. Jackson-Constan, M. Akita, and K. Keegstra Molecular chaperones involved in chloroplast protein import Biochim. Biophys. Acta 1541 2001 102 113
    • (2001) Biochim. Biophys. Acta , vol.1541 , pp. 102-113
    • Jackson-Constan, D.1    Akita, M.2    Keegstra, K.3
  • 55
    • 0036845834 scopus 로고    scopus 로고
    • Proteomic characterization of the small subunit of Chlamydomonas reinhardtii chloroplast ribosome: Identification of a novel S1 domain-containing protein and unusually large orthologs of bacterial S2, S3, and S5
    • K. Yamaguchi, S. Prieto, M.V. Beligni, P.A. Haynes, W.H. McDonald, and J.R. Yates 3rd Proteomic characterization of the small subunit of Chlamydomonas reinhardtii chloroplast ribosome: identification of a novel S1 domain-containing protein and unusually large orthologs of bacterial S2, S3, and S5 Plant Cell 14 2002 2957 2974
    • (2002) Plant Cell , vol.14 , pp. 2957-2974
    • Yamaguchi, K.1    Prieto, S.2    Beligni, M.V.3    Haynes, P.A.4    McDonald, W.H.5    Yates III, J.R.6
  • 56
    • 0037238202 scopus 로고    scopus 로고
    • Proteomic identification of all plastid-specific ribosomal proteins in higher plant chloroplast 30S ribosomal subunit
    • K. Yamaguchi, and A.R. Subramanian Proteomic identification of all plastid-specific ribosomal proteins in higher plant chloroplast 30S ribosomal subunit Eur. J. Biochem. 270 2003 190 205
    • (2003) Eur. J. Biochem. , vol.270 , pp. 190-205
    • Yamaguchi, K.1    Subramanian, A.R.2
  • 57
    • 0034665988 scopus 로고    scopus 로고
    • The plastid ribosomal proteins. Identification of all the proteins in the 50S subunit of an organelle ribosome (chloroplast)
    • K. Yamaguchi, and A.R. Subramanian The plastid ribosomal proteins. Identification of all the proteins in the 50S subunit of an organelle ribosome (chloroplast) J. Biol. Chem. 275 2000 28466 28482
    • (2000) J. Biol. Chem. , vol.275 , pp. 28466-28482
    • Yamaguchi, K.1    Subramanian, A.R.2
  • 58
    • 0034666124 scopus 로고    scopus 로고
    • The plastid ribosomal proteins. Identification of all the proteins in the 30S subunit of an organelle ribosome (chloroplast)
    • K. Yamaguchi, K. Von Knoblauch, and A.R. Subramanian The plastid ribosomal proteins. Identification of all the proteins in the 30S subunit of an organelle ribosome (chloroplast) J. Biol. Chem. 275 2000 28455 28465
    • (2000) J. Biol. Chem. , vol.275 , pp. 28455-28465
    • Yamaguchi, K.1    Von Knoblauch, K.2    Subramanian, A.R.3
  • 59
    • 0037899997 scopus 로고    scopus 로고
    • The life of ribulose 1,5-bisphosphate carboxylase/oxygenase - Posttranslational facts and mysteries
    • R.L. Houtz, and A.R. Portis Jr. The life of ribulose 1,5-bisphosphate carboxylase/oxygenase - posttranslational facts and mysteries Arch. Biochem. Biophys. 414 2003 150 158
    • (2003) Arch. Biochem. Biophys. , vol.414 , pp. 150-158
    • Houtz, R.L.1    Portis Jr., A.R.2
  • 60
    • 0033102499 scopus 로고    scopus 로고
    • A multisubunit acetyl coenzyme a carboxylase from soybean
    • S. Reverdatto, V. Beilinson, and N.C. Nielsen A multisubunit acetyl coenzyme A carboxylase from soybean Plant Physiol. 119 1999 961 978
    • (1999) Plant Physiol. , vol.119 , pp. 961-978
    • Reverdatto, S.1    Beilinson, V.2    Nielsen, N.C.3
  • 61
    • 5144222512 scopus 로고    scopus 로고
    • Affinity purification of the tobacco plastid RNA polymerase and in vitro reconstitution of the holoenzyme
    • J.Y. Suzuki, A.J. Ytterberg, T.A. Beardslee, L.A. Allison, K.J. Van Wijk, and P. Maliga Affinity purification of the tobacco plastid RNA polymerase and in vitro reconstitution of the holoenzyme Plant J. 40 2004 164 172
    • (2004) Plant J. , vol.40 , pp. 164-172
    • Suzuki, J.Y.1    Ytterberg, A.J.2    Beardslee, T.A.3    Allison, L.A.4    Van Wijk, K.J.5    Maliga, P.6
  • 62
    • 0034029659 scopus 로고    scopus 로고
    • Stability determinants in the chloroplast psbB/T/H mRNAs of Chlamydomonas reinhardtii
    • F.E. Vaistij, M. Goldschmidt-Clermont, K. Wostrikoff, and J.D. Rochaix Stability determinants in the chloroplast psbB/T/H mRNAs of Chlamydomonas reinhardtii Plant J. 21 2000 469 482
    • (2000) Plant J. , vol.21 , pp. 469-482
    • Vaistij, F.E.1    Goldschmidt-Clermont, M.2    Wostrikoff, K.3    Rochaix, J.D.4
  • 63
    • 0035794689 scopus 로고    scopus 로고
    • Identification of an RNA-protein complex involved in chloroplast group II intron trans-splicing in Chlamydomonas reinhardtii
    • C. Rivier, M. Goldschmidt-Clermont, and J.D. Rochaix Identification of an RNA-protein complex involved in chloroplast group II intron trans-splicing in Chlamydomonas reinhardtii EMBO J. 20 2001 1765 1773
    • (2001) EMBO J. , vol.20 , pp. 1765-1773
    • Rivier, C.1    Goldschmidt-Clermont, M.2    Rochaix, J.D.3
  • 64
    • 1642488239 scopus 로고    scopus 로고
    • A multiprotein complex involved in chloroplast group II intron splicing
    • K. Perron, M. Goldschmidt-Clermont, and J.D. Rochaix A multiprotein complex involved in chloroplast group II intron splicing RNA 10 2004 704 711
    • (2004) RNA , vol.10 , pp. 704-711
    • Perron, K.1    Goldschmidt-Clermont, M.2    Rochaix, J.D.3
  • 65
    • 0037054542 scopus 로고    scopus 로고
    • Characterization of Tbc2, a nucleus-encoded factor specifically required for translation of the chloroplast psbC mRNA in Chlamydomonas reinhardtii
    • A.H. Auchincloss, W. Zerges, K. Perron, J. Girard-Bascou, and J.D. Rochaix Characterization of Tbc2, a nucleus-encoded factor specifically required for translation of the chloroplast psbC mRNA in Chlamydomonas reinhardtii J. Cell Biol. 157 2002 953 962
    • (2002) J. Cell Biol. , vol.157 , pp. 953-962
    • Auchincloss, A.H.1    Zerges, W.2    Perron, K.3    Girard-Bascou, J.4    Rochaix, J.D.5
  • 66
    • 1042289735 scopus 로고    scopus 로고
    • Clp protease complexes from photosynthetic and non-photosynthetic plastids and mitochondria of plants, their predicted three-dimensional structures, and functional implications
    • J.B. Peltier, D.R. Ripoll, G. Friso, A. Rudella, Y. Cai, and J. Ytterberg Clp protease complexes from photosynthetic and non-photosynthetic plastids and mitochondria of plants, their predicted three-dimensional structures, and functional implications J. Biol. Chem. 279 2004 4768 4781
    • (2004) J. Biol. Chem. , vol.279 , pp. 4768-4781
    • Peltier, J.B.1    Ripoll, D.R.2    Friso, G.3    Rudella, A.4    Cai, Y.5    Ytterberg, J.6
  • 67
    • 0035844248 scopus 로고    scopus 로고
    • Identification of a 350-kDa ClpP protease complex with 10 different Clp isoforms in chloroplasts of Arabidopsis thaliana
    • J.B. Peltier, J. Ytterberg, D.A. Liberles, P. Roepstorff, and K.J. Van Wijk Identification of a 350-kDa ClpP protease complex with 10 different Clp isoforms in chloroplasts of Arabidopsis thaliana J. Biol. Chem. 276 2001 16318 16327
    • (2001) J. Biol. Chem. , vol.276 , pp. 16318-16327
    • Peltier, J.B.1    Ytterberg, J.2    Liberles, D.A.3    Roepstorff, P.4    Van Wijk, K.J.5
  • 68
    • 0017819391 scopus 로고
    • Carbonic anhydrase from spinach leaves. Isolation and some chemical properties
    • M. Kandel, A.G. Gornall, D.L. Cybulsky, and S.I. Kandel Carbonic anhydrase from spinach leaves. Isolation and some chemical properties J. Biol. Chem. 253 1978 679 685
    • (1978) J. Biol. Chem. , vol.253 , pp. 679-685
    • Kandel, M.1    Gornall, A.G.2    Cybulsky, D.L.3    Kandel, S.I.4
  • 71
    • 0033214591 scopus 로고    scopus 로고
    • Localization of labile posttranslational modifications by electron capture dissociation: The case of gamma-carboxyglutamic acid
    • N.L. Kelleher, R.A. Zubarev, K. Bush, B. Furie, B.C. Furie, and F.W. McLafferty Localization of labile posttranslational modifications by electron capture dissociation: the case of gamma-carboxyglutamic acid Anal. Chem. 71 1999 4250 4253 [In Process Citation]
    • (1999) Anal. Chem. , vol.71 , pp. 4250-4253
    • Kelleher, N.L.1    Zubarev, R.A.2    Bush, K.3    Furie, B.4    Furie, B.C.5    McLafferty, F.W.6
  • 72
    • 0037196338 scopus 로고    scopus 로고
    • Top down characterization of larger proteins (45:kDa) by electron capture dissociation mass spectrometry
    • Y. Ge, B.G. Lawhorn, M. ElNaggar, E. Strauss, J.H. Park, and T.P. Begley Top down characterization of larger proteins (45:kDa) by electron capture dissociation mass spectrometry J. Am. Chem. Soc. 124 2002 672 678
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 672-678
    • Ge, Y.1    Lawhorn, B.G.2    Elnaggar, M.3    Strauss, E.4    Park, J.H.5    Begley, T.P.6
  • 74
    • 2642520417 scopus 로고    scopus 로고
    • Top-down proteomics
    • N.L. Kelleher Top-down proteomics Anal. Chem. 76 2004 197A 203A
    • (2004) Anal. Chem. , vol.76
    • Kelleher, N.L.1
  • 75
    • 2642578319 scopus 로고    scopus 로고
    • A new approach for plant proteomics: Characterization of chloroplast proteins of Arabidopsis thaliana by top-down mass spectrometry
    • V. Zabrouskov, L. Giacomelli, K.J. Van Wijk, and F.W. McLafferty A new approach for plant proteomics: characterization of chloroplast proteins of Arabidopsis thaliana by top-down mass spectrometry Mol. Cell. Proteom. 2 2003 1253 1260
    • (2003) Mol. Cell. Proteom. , vol.2 , pp. 1253-1260
    • Zabrouskov, V.1    Giacomelli, L.2    Van Wijk, K.J.3    McLafferty, F.W.4
  • 76
    • 3242717090 scopus 로고    scopus 로고
    • Construction of a hybrid quadrupole/Fourier transform ion cyclotron resonance mass spectrometer for versatile MS/MS above 10:kDa
    • S.M. Patrie, J.P. Charlebois, D. Whipple, N.L. Kelleher, C.L. Hendrickson, and J.P. Quinn Construction of a hybrid quadrupole/Fourier transform ion cyclotron resonance mass spectrometer for versatile MS/MS above 10:kDa J. Am. Soc. Mass Spectrom. 15 2004 1099 1108
    • (2004) J. Am. Soc. Mass Spectrom. , vol.15 , pp. 1099-1108
    • Patrie, S.M.1    Charlebois, J.P.2    Whipple, D.3    Kelleher, N.L.4    Hendrickson, C.L.5    Quinn, J.P.6
  • 77
    • 0024296223 scopus 로고
    • Tandem mass spectrometry reveals that three photosystem II proteins of spinach chloroplasts contain N-acetyl-O-phosphothreonine at their NH2 termini
    • H. Michel, D.F. Hunt, J. Shabanowitz, and J. Bennett Tandem mass spectrometry reveals that three photosystem II proteins of spinach chloroplasts contain N-acetyl-O-phosphothreonine at their NH2 termini J. Biol. Chem. 263 1988 1123 1130
    • (1988) J. Biol. Chem. , vol.263 , pp. 1123-1130
    • Michel, H.1    Hunt, D.F.2    Shabanowitz, J.3    Bennett, J.4
  • 78
    • 0025951229 scopus 로고
    • Tandem mass spectrometry identifies sites of three post-translational modifications of spinach light-harvesting chlorophyll protein II. Proteolytic cleavage, acetylation, and phosphorylation
    • H. Michel, P.R. Griffin, J. Shabanowitz, D.F. Hunt, and J. Bennett Tandem mass spectrometry identifies sites of three post-translational modifications of spinach light-harvesting chlorophyll protein II. Proteolytic cleavage, acetylation, and phosphorylation J. Biol. Chem. 266 1991 17584 17591
    • (1991) J. Biol. Chem. , vol.266 , pp. 17584-17591
    • Michel, H.1    Griffin, P.R.2    Shabanowitz, J.3    Hunt, D.F.4    Bennett, J.5
  • 79
    • 0037413729 scopus 로고    scopus 로고
    • Control of protein life-span by N-terminal methionine excision
    • C. Giglione, O. Vallon, and T. Meinnel Control of protein life-span by N-terminal methionine excision EMBO J. 22 2003 13 23
    • (2003) EMBO J. , vol.22 , pp. 13-23
    • Giglione, C.1    Vallon, O.2    Meinnel, T.3
  • 80
    • 0035543404 scopus 로고    scopus 로고
    • Organellar peptide deformylases: Universality of the N-terminal methionine cleavage mechanism
    • C. Giglione, and T. Meinnel Organellar peptide deformylases: universality of the N-terminal methionine cleavage mechanism Trends Plant Sci. 6 2001 566 572
    • (2001) Trends Plant Sci. , vol.6 , pp. 566-572
    • Giglione, C.1    Meinnel, T.2
  • 81
    • 0035831456 scopus 로고    scopus 로고
    • Mass spectrometric resolution of reversible protein phosphorylation in photosynthetic membranes of Arabidopsis thaliana
    • A.V. Vener, A. Harms, M.R. Sussman, and R.D. Vierstra Mass spectrometric resolution of reversible protein phosphorylation in photosynthetic membranes of Arabidopsis thaliana J. Biol. Chem. 276 2001 6959 6966
    • (2001) J. Biol. Chem. , vol.276 , pp. 6959-6966
    • Vener, A.V.1    Harms, A.2    Sussman, M.R.3    Vierstra, R.D.4
  • 82
    • 1842546738 scopus 로고    scopus 로고
    • Identification of three previously unknown in vivo protein phosphorylation sites in thylakoid membranes of Arabidopsis thaliana
    • M. Hansson, and A.V. Vener Identification of three previously unknown in vivo protein phosphorylation sites in thylakoid membranes of Arabidopsis thaliana Mol. Cell. Proteom. 2 2003 550 559
    • (2003) Mol. Cell. Proteom. , vol.2 , pp. 550-559
    • Hansson, M.1    Vener, A.V.2
  • 83
    • 0023303085 scopus 로고
    • Intramembrane translocation and posttranslational palmitoylation of the chloroplast 32-kDa herbicide-binding protein
    • A.K. Mattoo, and M. Edelman Intramembrane translocation and posttranslational palmitoylation of the chloroplast 32-kDa herbicide-binding protein Proc. Natl. Acad. Sci. USA 84 1987 1497 1501
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1497-1501
    • Mattoo, A.K.1    Edelman, M.2
  • 84
    • 0032548785 scopus 로고    scopus 로고
    • Thylakoid protein phosphorylation in evolutionally divergent species with oxygenic photosynthesis
    • S. Pursiheimo, E. Rintamaki, E. Baena-Gonzalez, and E.M. Aro Thylakoid protein phosphorylation in evolutionally divergent species with oxygenic photosynthesis FEBS Lett. 423 1998 178 182
    • (1998) FEBS Lett. , vol.423 , pp. 178-182
    • Pursiheimo, S.1    Rintamaki, E.2    Baena-Gonzalez, E.3    Aro, E.M.4
  • 85
    • 0024542834 scopus 로고
    • Domain structure of mitochondrial and chloroplast targeting peptides
    • G. Von Heijne, J. Steppuhn, and S.G. Hermann Domain structure of mitochondrial and chloroplast targeting peptides Eur. J. Biochem. 80 1989 535 545
    • (1989) Eur. J. Biochem. , vol.80 , pp. 535-545
    • Von Heijne, G.1    Steppuhn, J.2    Hermann, S.G.3
  • 86
  • 87
    • 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
  • 88
    • 0037126071 scopus 로고    scopus 로고
    • Evolutionary analysis of Arabidopsis, cyanobacterial, and chloroplast genomes reveals plastid phylogeny and thousands of cyanobacterial genes in the nucleus
    • W. Martin, T. Rujan, E. Richly, A. Hansen, S. Cornelsen, and T. Lins Evolutionary analysis of Arabidopsis, cyanobacterial, and chloroplast genomes reveals plastid phylogeny and thousands of cyanobacterial genes in the nucleus Proc. Natl. Acad. Sci. USA 99 2002 11996 11997
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 11996-11997
    • Martin, W.1    Rujan, T.2    Richly, E.3    Hansen, A.4    Cornelsen, S.5    Lins, T.6
  • 89
    • 0033515448 scopus 로고    scopus 로고
    • TAKs, thylakoid membrane protein kinases associated with energy transduction
    • S. Snyders, and B.D. Kohorn TAKs, thylakoid membrane protein kinases associated with energy transduction J. Biol. Chem. 274 1999 9137 9140
    • (1999) J. Biol. Chem. , vol.274 , pp. 9137-9140
    • Snyders, S.1    Kohorn, B.D.2
  • 90
    • 0033759068 scopus 로고    scopus 로고
    • Interaction of a plant 14-3-3 protein with the signal peptide of a thylakoid-targeted chloroplast precursor protein and the presence of 14-3-3 isoforms in the chloroplast stroma
    • P.C. Sehnke, R. Henry, K. Cline, and R.J. Ferl Interaction of a plant 14-3-3 protein with the signal peptide of a thylakoid-targeted chloroplast precursor protein and the presence of 14-3-3 isoforms in the chloroplast stroma Plant Physiol. 122 2000 235 242
    • (2000) Plant Physiol. , vol.122 , pp. 235-242
    • Sehnke, P.C.1    Henry, R.2    Cline, K.3    Ferl, R.J.4
  • 92
    • 0036800808 scopus 로고    scopus 로고
    • The predicted candidates of Arabidopsis plastid inner envelope membrane proteins and their expression profiles
    • A.J. Koo, and J.B. Ohlrogge The predicted candidates of Arabidopsis plastid inner envelope membrane proteins and their expression profiles Plant Physiol. 130 2002 823 836
    • (2002) Plant Physiol. , vol.130 , pp. 823-836
    • Koo, A.J.1    Ohlrogge, J.B.2
  • 93
    • 0036763207 scopus 로고    scopus 로고
    • On filtering false positive transmembrane protein predictions
    • M. Cserzo, F. Eisenhaber, B. Eisenhaber, and I. Simon On filtering false positive transmembrane protein predictions Protein Eng. 15 2002 745 752
    • (2002) Protein Eng. , vol.15 , pp. 745-752
    • Cserzo, M.1    Eisenhaber, F.2    Eisenhaber, B.3    Simon, I.4
  • 94
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • A. Krogh, B. Larsson, G. Von Heijne, and E.L. Sonnhammer Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes J. Mol. Biol. 305 2001 567 580
    • (2001) J. Mol. Biol. , vol.305 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.4
  • 95
    • 0035852327 scopus 로고    scopus 로고
    • Post-translational protein translocation into thylakoids by the Sec and DeltapH-dependent pathways
    • H. Mori, and K. Cline Post-translational protein translocation into thylakoids by the Sec and DeltapH-dependent pathways Biochim. Biophys. Acta 1541 2001 80 90
    • (2001) Biochim. Biophys. Acta , vol.1541 , pp. 80-90
    • Mori, H.1    Cline, K.2
  • 96
    • 0000580602 scopus 로고    scopus 로고
    • The L18 domain of light-harvesting chlorophyll proteins binds to cpSRP43
    • C.J. Tu, E.C. Peterson, R. Henry, and N.E. Hoffman The L18 domain of light-harvesting chlorophyll proteins binds to cpSRP43 J. Biol. Chem. 275 2000 13187 13190
    • (2000) J. Biol. Chem. , vol.275 , pp. 13187-13190
    • Tu, C.J.1    Peterson, E.C.2    Henry, R.3    Hoffman, N.E.4
  • 97
    • 0141866809 scopus 로고    scopus 로고
    • AtTic110 functions as a scaffold for coordinating the stromal events of protein import into chloroplasts
    • T. Inaba, M. Li, M. Alvarez-Huerta, F. Kessler, and D.J. Schnell atTic110 functions as a scaffold for coordinating the stromal events of protein import into chloroplasts J. Biol. Chem. 278 2003 38617 39627
    • (2003) J. Biol. Chem. , vol.278 , pp. 38617-39627
    • Inaba, T.1    Li, M.2    Alvarez-Huerta, M.3    Kessler, F.4    Schnell, D.J.5
  • 98
  • 99
    • 0033117218 scopus 로고    scopus 로고
    • Protein import and routing systems of chloroplasts
    • K. Keegstra, and K. Cline Protein import and routing systems of chloroplasts Plant Cell 11 1999 557 570
    • (1999) Plant Cell , vol.11 , pp. 557-570
    • Keegstra, K.1    Cline, K.2
  • 100
    • 0141746356 scopus 로고    scopus 로고
    • LumenP - A neural network predictor for protein localization in the thylakoid lumen
    • I. Westerlund, G. Von Heijne, and O. Emanuelsson LumenP - a neural network predictor for protein localization in the thylakoid lumen Protein Sci. 12 2003 2360 2366
    • (2003) Protein Sci. , vol.12 , pp. 2360-2366
    • Westerlund, I.1    Von Heijne, G.2    Emanuelsson, O.3
  • 101
    • 1242339568 scopus 로고    scopus 로고
    • Common interchange standards for proteomics data: Public availability of tools and schema
    • S. Orchard, H. Hermjakob, R.K. Julian Jr., K. Runte, D. Sherman, and J. Wojcik Common interchange standards for proteomics data: public availability of tools and schema Proteomics 4 2004 490 491
    • (2004) Proteomics , vol.4 , pp. 490-491
    • Orchard, S.1    Hermjakob, H.2    Julian Jr., R.K.3    Runte, K.4    Sherman, D.5    Wojcik, J.6
  • 102


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