메뉴 건너뛰기




Volumn 134, Issue 2, 2004, Pages 777-789

A Transcriptomic and Proteomic Characterization of the Arabidopsis Mitochondrial Protein Import Apparatus and Its Response to Mitochondrial Dysfunction

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; CYTOLOGY; ELECTRON TRANSITIONS; GENES; PROTEINS;

EID: 1342265924     PISSN: 00320889     EISSN: None     Source Type: Journal    
DOI: 10.1104/pp.103.033910     Document Type: Article
Times cited : (124)

References (67)
  • 1
    • 0035999379 scopus 로고    scopus 로고
    • Genes for two mitochondrial ribosomal proteins in flowering plants are derived from their chloroplast or cytosolic counterparts
    • Adams KL, Daley DO, Whelan J, Palmer JD (2002) Genes for two mitochondrial ribosomal proteins in flowering plants are derived from their chloroplast or cytosolic counterparts. Plant Cell 14: 931-943
    • (2002) Plant Cell , vol.14 , pp. 931-943
    • Adams, K.L.1    Daley, D.O.2    Whelan, J.3    Palmer, J.D.4
  • 2
    • 0035844870 scopus 로고    scopus 로고
    • Tom40, the pore-forming component of the protein-conducting Tom channel in the outer membrane of mitochondria
    • Ahting U, Thieffry M, Engelhardt H, Hegerl R, Neupert W, Nussberger S (2001) Tom40, the pore-forming component of the protein-conducting Tom channel in the outer membrane of mitochondria. J Cell Biol 153: 1151-1160
    • (2001) J Cell Biol , vol.153 , pp. 1151-1160
    • Ahting, U.1    Thieffry, M.2    Engelhardt, H.3    Hegerl, R.4    Neupert, W.5    Nussberger, S.6
  • 3
    • 0037117569 scopus 로고    scopus 로고
    • A dynamin-like protein (ADL2b), rather than FtsZ, is involved in Arabidopsis mitochondrial division
    • Arimura S, Tsutsumi N (2002) A dynamin-like protein (ADL2b), rather than FtsZ, is involved in Arabidopsis mitochondrial division. Proc Natl Acad Sci USA 99: 5727-5731
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5727-5731
    • Arimura, S.1    Tsutsumi, N.2
  • 4
    • 0030008581 scopus 로고    scopus 로고
    • The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria
    • Arlt H, Tauer R, Feldmann H, Neupert W, Langer T (1996) The YTA10-12 complex, an AAA protease with chaperone-like activity in the inner membrane of mitochondria. Cell 85: 875-885
    • (1996) Cell , vol.85 , pp. 875-885
    • Arlt, H.1    Tauer, R.2    Feldmann, H.3    Neupert, W.4    Langer, T.5
  • 5
    • 0030934657 scopus 로고    scopus 로고
    • Metaxin is a component of a preprotein import complex in the outer membrane of the mammalian mitochondrion
    • Armstrong LC, Komiya T, Bergman BE, Mihara K, Bornstein P (1997) Metaxin is a component of a preprotein import complex in the outer membrane of the mammalian mitochondrion. J Biol Chem 272: 6510-6518
    • (1997) J Biol Chem , vol.272 , pp. 6510-6518
    • Armstrong, L.C.1    Komiya, T.2    Bergman, B.E.3    Mihara, K.4    Bornstein, P.5
  • 6
    • 0037008216 scopus 로고    scopus 로고
    • AtCOX17, an Arabidopsis homolog of the yeast copper chaperone COX17
    • Balandin T, Castresana C (2002) AtCOX17, an Arabidopsis homolog of the yeast copper chaperone COX17. Plant Physiol 129: 1852-1857
    • (2002) Plant Physiol , vol.129 , pp. 1852-1857
    • Balandin, T.1    Castresana, C.2
  • 8
    • 0029066902 scopus 로고
    • Are the "core" proteins of the mitochondrial bel complex evolutionary relics of a processing protease?
    • Braun HP, Schmitz UK (1995) Are the "core" proteins of the mitochondrial bel complex evolutionary relics of a processing protease? Trends Biochem Sci 20: 171-175
    • (1995) Trends Biochem Sci , vol.20 , pp. 171-175
    • Braun, H.P.1    Schmitz, U.K.2
  • 10
    • 0037278304 scopus 로고    scopus 로고
    • Two chloroplastic protein translocation components, Tic110 and Toc75, are conserved in different plastid types from multiple plant species
    • Davila-Aponte JA, Inoue K, Keegstra K (2003) Two chloroplastic protein translocation components, Tic110 and Toc75, are conserved in different plastid types from multiple plant species. Plant Mol Biol 51: 175-181
    • (2003) Plant Mol Biol , vol.51 , pp. 175-181
    • Davila-Aponte, J.A.1    Inoue, K.2    Keegstra, K.3
  • 11
    • 0030930621 scopus 로고    scopus 로고
    • Temporal regulation of in vitro import of precursor proteins into mitochondria
    • Dessi P, Whelan J (1997) Temporal regulation of in vitro import of precursor proteins into mitochondria. FEBS Lett 415: 173-178
    • (1997) FEBS Lett , vol.415 , pp. 173-178
    • Dessi, P.1    Whelan, J.2
  • 12
    • 0031741738 scopus 로고    scopus 로고
    • Preprotein translocase of the outer mitochondrial membrane: Molecular dissection and assembly of the general import pore complex
    • Dekker PJ, Ryan MT, Brix J, Muller H, Honlinger A, Pfanner N (1998) Preprotein translocase of the outer mitochondrial membrane: molecular dissection and assembly of the general import pore complex. Mol Cell Biol 18: 6515-6524
    • (1998) Mol Cell Biol , vol.18 , pp. 6515-6524
    • Dekker, P.J.1    Ryan, M.T.2    Brix, J.3    Muller, H.4    Honlinger, A.5    Pfanner, N.6
  • 13
    • 0030828201 scopus 로고    scopus 로고
    • Developmental regulation of the plant mitochondrial matrix located HSP70 chaperone and its role in protein import
    • Dudley P, Wood CK, Pratt JR, Moore AL (1997) Developmental regulation of the plant mitochondrial matrix located HSP70 chaperone and its role in protein import. FEBS Lett 417: 321-324
    • (1997) FEBS Lett , vol.417 , pp. 321-324
    • Dudley, P.1    Wood, C.K.2    Pratt, J.R.3    Moore, A.L.4
  • 14
    • 0038705126 scopus 로고    scopus 로고
    • Leaf mitochondria modulate whole cell redox homeostasis, set antioxidant capacity, and determine stress resistance through altered signaling and diurnal regulation
    • Dutilleul C, Garmier M, Noctor G, Mathieu C, Chetrit P, Foyer CH, de Paepe R (2003) Leaf mitochondria modulate whole cell redox homeostasis, set antioxidant capacity, and determine stress resistance through altered signaling and diurnal regulation. Plant Cell 15: 1212-1226
    • (2003) Plant Cell , vol.15 , pp. 1212-1226
    • Dutilleul, C.1    Garmier, M.2    Noctor, G.3    Mathieu, C.4    Chetrit, P.5    Foyer, C.H.6    De Paepe, R.7
  • 15
    • 0034697980 scopus 로고    scopus 로고
    • Predicting subcellular localisation of proteins based on their N-terminal amino acid sequence
    • Emanuelsson O, Nielsen H, Brunak S, von Heijne G (2000) Predicting subcellular localisation of proteins based on their N-terminal amino acid sequence. J Mol Biol 300: 1005-1016
    • (2000) J Mol Biol , vol.300 , pp. 1005-1016
    • Emanuelsson, O.1    Nielsen, H.2    Brunak, S.3    Von Heijne, G.4
  • 16
    • 0037566814 scopus 로고    scopus 로고
    • Tom40, the import channel of the mitochondrial outer membrane, plays an active role in sorting imported proteins
    • Gabriel K, Egan B, Lithgow T (2003) Tom40, the import channel of the mitochondrial outer membrane, plays an active role in sorting imported proteins. EMBO J 22: 2380-2386
    • (2003) EMBO J , vol.22 , pp. 2380-2386
    • Gabriel, K.1    Egan, B.2    Lithgow, T.3
  • 17
    • 0014276538 scopus 로고
    • Nutrient requirements of suspension cultures of soybean root cells
    • Gamborg OL, Miller RA, Ojima K (1968) Nutrient requirements of suspension cultures of soybean root cells. Exp Cell Res 50: 151-158
    • (1968) Exp Cell Res , vol.50 , pp. 151-158
    • Gamborg, O.L.1    Miller, R.A.2    Ojima, K.3
  • 20
    • 0030802910 scopus 로고    scopus 로고
    • COX15 codes for a mitochondrial protein essential for the assembly of yeast cytochrome oxidase
    • Glerum DM, Muroff I, Jin C, Tzagoloff A (1997) COX15 codes for a mitochondrial protein essential for the assembly of yeast cytochrome oxidase. J Biol Chem 272: 19088-19094
    • (1997) J Biol Chem , vol.272 , pp. 19088-19094
    • Glerum, D.M.1    Muroff, I.2    Jin, C.3    Tzagoloff, A.4
  • 21
    • 15844421373 scopus 로고    scopus 로고
    • Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase
    • Glerum DM, Shtanko A, Tzagoloff A (1996) Characterization of COX17, a yeast gene involved in copper metabolism and assembly of cytochrome oxidase. J Biol Chem 271: 14504-14509
    • (1996) J Biol Chem , vol.271 , pp. 14504-14509
    • Glerum, D.M.1    Shtanko, A.2    Tzagoloff, A.3
  • 23
    • 0035037171 scopus 로고    scopus 로고
    • Arabidopsis genes encoding components of the chloroplastic protein import apparatus
    • Jackson-Constan D, Keegstra K (2001) Arabidopsis genes encoding components of the chloroplastic protein import apparatus. Plant Physiol 125: 1567-1576
    • (2001) Plant Physiol , vol.125 , pp. 1567-1576
    • Jackson-Constan, D.1    Keegstra, K.2
  • 24
    • 0032479295 scopus 로고    scopus 로고
    • Unique composition of the preprotein translocase of the outer mitochondrial membrane from plants
    • Jansch L, Kruft V, Schmitz UK, Braun HP (1998) Unique composition of the preprotein translocase of the outer mitochondrial membrane from plants. J Biol Chem 273: 17251-17257
    • (1998) J Biol Chem , vol.273 , pp. 17251-17257
    • Jansch, L.1    Kruft, V.2    Schmitz, U.K.3    Braun, H.P.4
  • 25
    • 0033963688 scopus 로고    scopus 로고
    • Tim18p is a new component of the Tim54p-Tim22p translocon in the mitochondrial inner membrane
    • Kerscher O, Sepuri NB, Jensen RE (2000) Tim18p is a new component of the Tim54p-Tim22p translocon in the mitochondrial inner membrane. Mol Biol Cell 11: 103-116
    • (2000) Mol Biol Cell , vol.11 , pp. 103-116
    • Kerscher, O.1    Sepuri, N.B.2    Jensen, R.E.3
  • 26
    • 0033978123 scopus 로고    scopus 로고
    • Tim18p, a new subunit of the Tim22 complex that mediates insertion of imported proteins into the yeast mitochondrial inner membrane
    • Koehler CM, Murphy MP, Bally NA, Leuenberger D, Oppliger W, Dolfini L, Junne T, Schatz G, Or E (2000) Tim18p, a new subunit of the Tim22 complex that mediates insertion of imported proteins into the yeast mitochondrial inner membrane. Mol Cell Biol 20: 1187-1193
    • (2000) Mol Cell Biol , vol.20 , pp. 1187-1193
    • Koehler, C.M.1    Murphy, M.P.2    Bally, N.A.3    Leuenberger, D.4    Oppliger, W.5    Dolfini, L.6    Junne, T.7    Schatz, G.8    Or, E.9
  • 27
    • 0037113870 scopus 로고    scopus 로고
    • A higher plant mitochondrial homologue of the yeast m-AAA protease: Molecular cloning, localization, and putative function
    • Kolodziejczak M, Kolaczkowska A, Szczesny B, Urantowka A, Knorpp C, Kieleczawa J, Janska H (2002) A higher plant mitochondrial homologue of the yeast m-AAA protease: molecular cloning, localization, and putative function. J Biol Chem 277: 43792-43798
    • (2002) J Biol Chem , vol.277 , pp. 43792-43798
    • Kolodziejczak, M.1    Kolaczkowska, A.2    Szczesny, B.3    Urantowka, A.4    Knorpp, C.5    Kieleczawa, J.6    Janska, H.7
  • 28
    • 0036072543 scopus 로고    scopus 로고
    • Zinc-dependent intermembrane space proteins stimulate import of carrier proteins into plant mitochondria
    • Lister R, Mowday B, Whelan J, Millar AH (2002) Zinc-dependent intermembrane space proteins stimulate import of carrier proteins into plant mitochondria. Plant J 30: 555-566
    • (2002) Plant J , vol.30 , pp. 555-566
    • Lister, R.1    Mowday, B.2    Whelan, J.3    Millar, A.H.4
  • 29
    • 0037246883 scopus 로고    scopus 로고
    • The Mitochondrial Protein Import Machinery of Plants (MPIMP) database
    • Lister R, Murcha MW, Whelan J (2003) The Mitochondrial Protein Import Machinery of Plants (MPIMP) database. Nucleic Acids Res 31: 325-327
    • (2003) Nucleic Acids Res , vol.31 , pp. 325-327
    • Lister, R.1    Murcha, M.W.2    Whelan, J.3
  • 30
    • 0030968336 scopus 로고    scopus 로고
    • Tim23, a protein import component of the mitochondrial inner membrane, is required for normal activity of the multiple conductance channel, MCC
    • Lohret TA, Jensen RE, Kinnally KW (1997) Tim23, a protein import component of the mitochondrial inner membrane, is required for normal activity of the multiple conductance channel, MCC. J Cell Biol 137: 377-386
    • (1997) J Cell Biol , vol.137 , pp. 377-386
    • Lohret, T.A.1    Jensen, R.E.2    Kinnally, K.W.3
  • 31
    • 0035854694 scopus 로고    scopus 로고
    • YidC/Oxa1p/Alb3: Evolutionarily conserved mediators of membrane protein assembly
    • Luirink J, Samuelsson T, de Gier JW (2001) YidC/Oxa1p/Alb3: evolutionarily conserved mediators of membrane protein assembly. FEBS Lett 501: 1-5
    • (2001) FEBS Lett , vol.501 , pp. 1-5
    • Luirink, J.1    Samuelsson, T.2    De Gier, J.W.3
  • 32
    • 0033928908 scopus 로고    scopus 로고
    • How do plant mitochondria avoid importing chloroplast proteins? Components of the import apparatus Tom20 and Tom22 from Arabidopsis differ from their fungal counterparts
    • Mascasev D, Newbigin E, Whelan J, Lithgow T (2000) How do plant mitochondria avoid importing chloroplast proteins? Components of the import apparatus Tom20 and Tom22 from Arabidopsis differ from their fungal counterparts. Plant Physiol 123: 811-816
    • (2000) Plant Physiol , vol.123 , pp. 811-816
    • Mascasev, D.1    Newbigin, E.2    Whelan, J.3    Lithgow, T.4
  • 33
    • 0035854691 scopus 로고    scopus 로고
    • Modular structure of the Tim23 preprotein translocase of mitochondria
    • Milisav I, Moro F, W. N., Brunner M (2001) Modular structure of the Tim23 preprotein translocase of mitochondria. J Biol Chem 276: 25856-25861
    • (2001) J Biol Chem , vol.276 , pp. 25856-25861
    • Milisav, I.1    Moro, F.W.N.2    Brunner, M.3
  • 37
    • 0033168677 scopus 로고    scopus 로고
    • The TIM17.23 preprotein translocase of mitochondria: Composition and function in protein transport into the matrix
    • Moro F, Sirrenberg C, Schneider HC, Neupert W, Brunner M (1999) The TIM17.23 preprotein translocase of mitochondria: composition and function in protein transport into the matrix. EMBO J 18: 3667-3675
    • (1999) EMBO J , vol.18 , pp. 3667-3675
    • Moro, F.1    Sirrenberg, C.2    Schneider, H.C.3    Neupert, W.4    Brunner, M.5
  • 38
    • 0034676096 scopus 로고    scopus 로고
    • Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p
    • Mozdy AD, McCaffery JM, Shaw JM (2000) Dnm1p GTPase-mediated mitochondrial fission is a multi-step process requiring the novel integral membrane component Fis1p. J Cell Biol 151: 367-380
    • (2000) J Cell Biol , vol.151 , pp. 367-380
    • Mozdy, A.D.1    McCaffery, J.M.2    Shaw, J.M.3
  • 39
    • 0033452914 scopus 로고    scopus 로고
    • Import of precursor proteins into mitochondria from soybean tissues during development
    • Murcha MW, Huang T, Whelan J (1999) Import of precursor proteins into mitochondria from soybean tissues during development. FEBS Lett 464: 53-59
    • (1999) FEBS Lett , vol.464 , pp. 53-59
    • Murcha, M.W.1    Huang, T.2    Whelan, J.3
  • 40
    • 0037393286 scopus 로고    scopus 로고
    • Identification, expression, and import of components 17 and 23 of the inner mitochondrial membrane translocase from Arabidopsis
    • Murcha MW, Lister R, Ho AY, Whelan J (2003) Identification, expression, and import of components 17 and 23 of the inner mitochondrial membrane translocase from Arabidopsis. Plant Physiol 131: 1737-1747
    • (2003) Plant Physiol , vol.131 , pp. 1737-1747
    • Murcha, M.W.1    Lister, R.2    Ho, A.Y.3    Whelan, J.4
  • 41
    • 0037066703 scopus 로고    scopus 로고
    • The Oxal protein forms a homooligomeric complex and is an essential part of the mitochondrial export translocase in Neurospora crassa
    • Nargang FE, Preuss M, Neupert W, Herrmann JM (2002) The Oxal protein forms a homooligomeric complex and is an essential part of the mitochondrial export translocase in Neurospora crassa. J Biol Chem 277: 12846-12853
    • (2002) J Biol Chem , vol.277 , pp. 12846-12853
    • Nargang, F.E.1    Preuss, M.2    Neupert, W.3    Herrmann, J.M.4
  • 42
    • 0030969942 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Neupert W (1997) Protein import into mitochondria. Annu Rev Biochem 66: 863-917
    • (1997) Annu Rev Biochem , vol.66 , pp. 863-917
    • Neupert, W.1
  • 44
    • 0026702012 scopus 로고
    • BCS1, a novel gene required for the expression of functional Rieske iron-sulfur protein in Saccharomyces cerevisiae
    • Nobrega FG, Nobrega MP, Tzagoloff A (1992) BCS1, a novel gene required for the expression of functional Rieske iron-sulfur protein in Saccharomyces cerevisiae. EMBO J 11: 3821-3829
    • (1992) EMBO J , vol.11 , pp. 3821-3829
    • Nobrega, F.G.1    Nobrega, M.P.2    Tzagoloff, A.3
  • 45
    • 0035344460 scopus 로고    scopus 로고
    • Versatility of the mitochondrial protein import machinery
    • Pfanner N, Geissler A (2001) Versatility of the mitochondrial protein import machinery. Nat Rev Mol Cell Biol 2: 339-349
    • (2001) Nat Rev Mol Cell Biol , vol.2 , pp. 339-349
    • Pfanner, N.1    Geissler, A.2
  • 46
    • 0034756937 scopus 로고    scopus 로고
    • Structural requirements of Tom40 for assembly into preexisting Tom complexes of mitochondria
    • Rapaport D, Taylor RD, Kaser M, Langer T, Neupert W, Narang FE (2001) Structural requirements of Tom40 for assembly into preexisting Tom complexes of mitochondria. Mol Biol Cell 12: 1189-1198
    • (2001) Mol Biol Cell , vol.12 , pp. 1189-1198
    • Rapaport, D.1    Taylor, R.D.2    Kaser, M.3    Langer, T.4    Neupert, W.5    Narang, F.E.6
  • 48
    • 0037459118 scopus 로고    scopus 로고
    • Insertion of hydrophobic membrane proteins into the inner mitochondrial membrane: A guided tour
    • Rehling P, Pfanner N, Meisinger C (2003b) Insertion of hydrophobic membrane proteins into the inner mitochondrial membrane: a guided tour. J Mol Biol 326: 639-657
    • (2003) J Mol Biol , vol.326 , pp. 639-657
    • Rehling, P.1    Pfanner, N.2    Meisinger, C.3
  • 50
    • 0033729605 scopus 로고    scopus 로고
    • Mitochondrial localisation of AtOXA1, an Arabidopsis homologue of yeast Oxalp involved in the insertion and assembly of protein complexes in mitochondrial inner membrane
    • Sakamoto W, Spielewoy N, Bonnard G, Murata M, Wintz H (2000) Mitochondrial localisation of AtOXA1, an Arabidopsis homologue of yeast Oxalp involved in the insertion and assembly of protein complexes in mitochondrial inner membrane. Plant Cell Physiol 41: 1157-1163
    • (2000) Plant Cell Physiol , vol.41 , pp. 1157-1163
    • Sakamoto, W.1    Spielewoy, N.2    Bonnard, G.3    Murata, M.4    Wintz, H.5
  • 51
    • 0000301881 scopus 로고
    • SCO1, a yeast nuclear gene essential for accumulation of mitochondrial cytochrome c oxidase subunit II
    • Schulze M, Rodel G (1988) SCO1, a yeast nuclear gene essential for accumulation of mitochondrial cytochrome c oxidase subunit II. Mol Gen Genet 211: 492-498
    • (1988) Mol Gen Genet , vol.211 , pp. 492-498
    • Schulze, M.1    Rodel, G.2
  • 52
    • 0032055781 scopus 로고    scopus 로고
    • Mitochondrial targeting peptides in plants
    • Sjoling S, Glaser E (1998) Mitochondrial targeting peptides in plants. Trends Plant Sci 3: 136-140
    • (1998) Trends Plant Sci , vol.3 , pp. 136-140
    • Sjoling, S.1    Glaser, E.2
  • 53
    • 0036828801 scopus 로고    scopus 로고
    • Isolation and identification of a novel mitochondrial metalloprotease (PreP) that degrades targeting presequences in plants
    • Stahl A, Moberg P, Ytterberg J, Panfilov O, Brockenhuus Von Lowenhielm H, Nilsson F, Glaser E (2002) Isolation and identification of a novel mitochondrial metalloprotease (PreP) that degrades targeting presequences in plants. J Biol Chem 277: 41931-41939
    • (2002) J Biol Chem , vol.277 , pp. 41931-41939
    • Stahl, A.1    Moberg, P.2    Ytterberg, J.3    Panfilov, O.4    Brockenhuus Von Lowenhielm, H.5    Nilsson, F.6    Glaser, E.7
  • 55
    • 0035900433 scopus 로고    scopus 로고
    • Nucleoside diphosphate kinase III is localised to the inter-membrane space in plant mitochondria
    • Sweetlove LJ, Mowday B, Hebestreit HF, Leaver CJ, Millar AH (2001) Nucleoside diphosphate kinase III is localised to the inter-membrane space in plant mitochondria. FEBS Lett 254: 1-5
    • (2001) FEBS Lett , vol.254 , pp. 1-5
    • Sweetlove, L.J.1    Mowday, B.2    Hebestreit, H.F.3    Leaver, C.J.4    Millar, A.H.5
  • 58
    • 0037428379 scopus 로고    scopus 로고
    • Characterization of Neurospora crassa Tom40-deficient mutants and effect of specific mutations on Tom40 assembly
    • Taylor RD, McHale BJ, Nargang FE (2003b) Characterization of Neurospora crassa Tom40-deficient mutants and effect of specific mutations on Tom40 assembly. J Biol Chem 278: 765-775
    • (2003) J Biol Chem , vol.278 , pp. 765-775
    • Taylor, R.D.1    McHale, B.J.2    Nargang, F.E.3
  • 60
    • 0036119404 scopus 로고    scopus 로고
    • Biochemical dissection of the mitochondrial proteome from Arabidopsis thaliana by three-dimensional gel electrophoresis
    • Werhahn W, Braun HP (2002) Biochemical dissection of the mitochondrial proteome from Arabidopsis thaliana by three-dimensional gel electrophoresis. Electrophoresis 23: 640-646
    • (2002) Electrophoresis , vol.23 , pp. 640-646
    • Werhahn, W.1    Braun, H.P.2
  • 61
    • 0038687177 scopus 로고    scopus 로고
    • Identification of novel subunits of the TOM complex from Arabidopsis thaliana
    • Werhahn W, Jansch L, Braun H-P (2003) Identification of novel subunits of the TOM complex from Arabidopsis thaliana. Plant Physiol Biochem 41: 407-416
    • (2003) Plant Physiol Biochem , vol.41 , pp. 407-416
    • Werhahn, W.1    Jansch, L.2    Braun, H.-P.3
  • 62
    • 0035115121 scopus 로고    scopus 로고
    • Purification and characterisation of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis: Identification of multiple forms of Tom 20
    • Werhahn W, Niemeyer A, Jansch L, Kruft V, Schmitz UK, Braun H-P (2001) Purification and characterisation of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis: identification of multiple forms of Tom 20. Plant Physiol 125: 943-954
    • (2001) Plant Physiol , vol.125 , pp. 943-954
    • Werhahn, W.1    Niemeyer, A.2    Jansch, L.3    Kruft, V.4    Schmitz, U.K.5    Braun, H.-P.6
  • 63
    • 0029240442 scopus 로고
    • Studies on the import and processing of the alternative oxidase precursor by isolated soybean mitochondria
    • Whelan J, Hugosson M, Glaser E, Day DA (1995) Studies on the import and processing of the alternative oxidase precursor by isolated soybean mitochondria. Plant Mol Biol 27: 769-778
    • (1995) Plant Mol Biol , vol.27 , pp. 769-778
    • Whelan, J.1    Hugosson, M.2    Glaser, E.3    Day, D.A.4
  • 64
    • 0037111988 scopus 로고    scopus 로고
    • Tim50 is a subunit of the TIM23 complex that links protein translocation across the outer and inner mitochondrial membranes
    • Yamamoto H, Esaki M, Kanamori T, Tamura Y, Nishikawa S, Endo T (2002) Tim50 is a subunit of the TIM23 complex that links protein translocation across the outer and inner mitochondrial membranes. Cell 111: 519-528
    • (2002) Cell , vol.111 , pp. 519-528
    • Yamamoto, H.1    Esaki, M.2    Kanamori, T.3    Tamura, Y.4    Nishikawa, S.5    Endo, T.6
  • 65
    • 0035856567 scopus 로고    scopus 로고
    • Phylogenetic and structural analyses of the oxal family of protein translocases
    • Yen MR, Harley KT, Tseng YH, Saier MH Jr (2001) Phylogenetic and structural analyses of the oxal family of protein translocases. FEMS Microbiol Lett 204: 223-231
    • (2001) FEMS Microbiol Lett , vol.204 , pp. 223-231
    • Yen, M.R.1    Harley, K.T.2    Tseng, Y.H.3    Saier Jr., M.H.4
  • 66
    • 0035058478 scopus 로고    scopus 로고
    • A genome approach to mitochondrial-nuclear communication in Arabidopsis
    • Yu J, Nickels R, McIntosh L (2001) A genome approach to mitochondrial-nuclear communication in Arabidopsis. Plant Physiol Biochem 39: 345-353
    • (2001) Plant Physiol Biochem , vol.39 , pp. 345-353
    • Yu, J.1    Nickels, R.2    McIntosh, L.3
  • 67
    • 0034794778 scopus 로고    scopus 로고
    • Mutagenesis and computer modelling approach to study determinants for recognition of signal peptides by the mitochondrial processing peptidase
    • Zhang X-P, Sjoling S, Tanudji M, Somogyi L, Andreu D, Eriksson LEG, Graslund A, Whelan J, Glaser E (2001) Mutagenesis and computer modelling approach to study determinants for recognition of signal peptides by the mitochondrial processing peptidase. Plant J 27: 427-438
    • (2001) Plant J , vol.27 , pp. 427-438
    • Zhang, X.-P.1    Sjoling, S.2    Tanudji, M.3    Somogyi, L.4    Andreu, D.5    Eriksson, L.E.G.6    Graslund, A.7    Whelan, J.8    Glaser, E.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.