메뉴 건너뛰기




Volumn 157, Issue 2, 2011, Pages 587-598

Defining the protein complex proteome of plant mitochondria

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA; VASCONCELLEA CANDICANS;

EID: 80053594838     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.111.182352     Document Type: Article
Times cited : (154)

References (55)
  • 1
    • 0032534790 scopus 로고    scopus 로고
    • Yeast mitochondrial F1F0-ATP synthase exists as a dimer: Identification of three dimer-specific subunits
    • Arnold I, Pfeiffer K, Neupert W, Stuart RA, Schägger H (1998) Yeast mitochondrial F1F0-ATP synthase exists as a dimer: identification of three dimer-specific subunits. EMBO J 17: 7170-7178.
    • (1998) EMBO J , vol.17 , pp. 7170-7178
    • Arnold, I.1    Pfeiffer, K.2    Neupert, W.3    Stuart, R.A.4    Schägger, H.5
  • 3
    • 0026709336 scopus 로고
    • The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain
    • Braun HP, Emmermann M, Kruft V, Schmitz UK (1992) The general mitochondrial processing peptidase from potato is an integral part of cytochrome c reductase of the respiratory chain. EMBO J 11: 3219-3227.
    • (1992) EMBO J , vol.11 , pp. 3219-3227
    • Braun, H.P.1    Emmermann, M.2    Kruft, V.3    Schmitz, U.K.4
  • 4
    • 0028857080 scopus 로고
    • The bifunctional cytochrome c reductase/ processing peptidase complex from plant mitochondria
    • Braun HP, Schmitz UK (1995) The bifunctional cytochrome c reductase/ processing peptidase complex from plant mitochondria. J Bioenerg Biomembr 27: 423-436.
    • (1995) J Bioenerg Biomembr , vol.27 , pp. 423-436
    • Braun, H.P.1    Schmitz, U.K.2
  • 5
    • 0037431026 scopus 로고    scopus 로고
    • Identification of 14 new phosphoproteins involved in important plant mitochondrial processes
    • Bykova NV, Egsgaard H, Møller IM (2003a) Identification of 14 new phosphoproteins involved in important plant mitochondrial processes. FEBS Lett 540: 141-146.
    • (2003) FEBS Lett , vol.540 , pp. 141-146
    • Bykova, N.V.1    Egsgaard, H.2    Møller, I.M.3
  • 7
    • 0037184987 scopus 로고    scopus 로고
    • Definition of the nuclear encoded protein composition of bovine heart mitochondrial complex I: Identification of two new subunits
    • Carroll J, Shannon RJ, Fearnley IM, Walker JE, Hirst J (2002) Definition of the nuclear encoded protein composition of bovine heart mitochondrial complex I: identification of two new subunits. J Biol Chem 277: 50311-50317.
    • (2002) J Biol Chem , vol.277 , pp. 50311-50317
    • Carroll, J.1    Shannon, R.J.2    Fearnley, I.M.3    Walker, J.E.4    Hirst, J.5
  • 8
    • 37749036789 scopus 로고    scopus 로고
    • Pentatricopeptide repeat (PPR) proteins as sequence-specificity factors in post-transcriptional processes in organelles
    • Delannoy E, Stanley WA, Bond CS, Small ID (2007) Pentatricopeptide repeat (PPR) proteins as sequence-specificity factors in post-transcriptional processes in organelles. Biochem Soc Trans 35: 1643-1647.
    • (2007) Biochem Soc Trans , vol.35 , pp. 1643-1647
    • Delannoy, E.1    Stanley, W.A.2    Bond, C.S.3    Small, I.D.4
  • 10
    • 0026077266 scopus 로고
    • The ADP/ATP translocator from potato has a long amino-terminal extension
    • Emmermann M, Braun HP, Schmitz UK (1991) The ADP/ATP translocator from potato has a long amino-terminal extension. Curr Genet 20: 405-410.
    • (1991) Curr Genet , vol.20 , pp. 405-410
    • Emmermann, M.1    Braun, H.P.2    Schmitz, U.K.3
  • 11
    • 0141786914 scopus 로고    scopus 로고
    • New insights into the respiratory chain of plant mitochondria: Supercomplexes and a unique composition of complex II
    • Eubel H, Jänsch L, Braun HP (2003) New insights into the respiratory chain of plant mitochondria: supercomplexes and a unique composition of complex II. Plant Physiol 133: 274-286.
    • (2003) Plant Physiol , vol.133 , pp. 274-286
    • Eubel, H.1    Jänsch, L.2    Braun, H.P.3
  • 12
    • 0041379444 scopus 로고    scopus 로고
    • Identification of mitochondrial protein complexes in Arabidopsis using two-dimensional blue-native polyacrylamide gel electrophoresis
    • Giegé P, Sweetlove LJ, Leaver CJ (2003) Identification of mitochondrial protein complexes in Arabidopsis using two-dimensional blue-native polyacrylamide gel electrophoresis. Plant Mol Biol Rep 21: 133-144.
    • (2003) Plant Mol Biol Rep , vol.21 , pp. 133-144
    • Giegé, P.1    Sweetlove, L.J.2    Leaver, C.J.3
  • 13
    • 0035039711 scopus 로고    scopus 로고
    • Plant mitochondria contain proteolytic and regulatory subunits of the ATPdependent Clp protease
    • Halperin T, Zheng B, Itzhaki H, Clarke AK, Adam Z (2001) Plant mitochondria contain proteolytic and regulatory subunits of the ATPdependent Clp protease. Plant Mol Biol 45: 461-468.
    • (2001) Plant Mol Biol , vol.45 , pp. 461-468
    • Halperin, T.1    Zheng, B.2    Itzhaki, H.3    Clarke, A.K.4    Adam, Z.5
  • 14
    • 0038433229 scopus 로고    scopus 로고
    • Mitochondrial complex I from Arabidopsis and rice: Orthologs of mammalian and fungal components coupled with plant-specific subunits
    • Heazlewood JL, Howell KA, Millar AH (2003a) Mitochondrial complex I from Arabidopsis and rice: orthologs of mammalian and fungal components coupled with plant-specific subunits. Biochim Biophys Acta 1604: 159-169.
    • (2003) Biochim Biophys Acta , vol.1604 , pp. 159-169
    • Heazlewood, J.L.1    Howell, K.A.2    Millar, A.H.3
  • 16
    • 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
    • Heazlewood JL, Tonti-Filippini JS, Gout AM, Day DA, Whelan J, Millar AH (2004) 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: 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
  • 17
    • 33644649331 scopus 로고    scopus 로고
    • Combining experimental and predicted datasets for determination of the subcellular location of proteins in Arabidopsis
    • Heazlewood JL, Tonti-Filippini J, Verboom RE, Millar AH (2005) Combining experimental and predicted datasets for determination of the subcellular location of proteins in Arabidopsis. Plant Physiol 139: 598-609.
    • (2005) Plant Physiol , vol.139 , pp. 598-609
    • Heazlewood, J.L.1    Tonti-Filippini, J.2    Verboom, R.E.3    Millar, A.H.4
  • 19
    • 0037430978 scopus 로고    scopus 로고
    • The products of the mitochondrial orf25 and orfB genes are FO components in the plant F1FO ATP synthase
    • Heazlewood JL, Whelan J, Millar AH (2003c) The products of the mitochondrial orf25 and orfB genes are FO components in the plant F1FO ATP synthase. FEBS Lett 540: 201-205.
    • (2003) FEBS Lett , vol.540 , pp. 201-205
    • Heazlewood, J.L.1    Whelan, J.2    Millar, A.H.3
  • 20
    • 63349099933 scopus 로고    scopus 로고
    • Blue native DIGE as a tool for comparative analyses of protein complexes
    • Heinemeyer J, Scheibe B, Schmitz UK, Braun HP (2009) Blue native DIGE as a tool for comparative analyses of protein complexes. J Prot 72: 539-544.
    • (2009) J Prot , vol.72 , pp. 539-544
    • Heinemeyer, J.1    Scheibe, B.2    Schmitz, U.K.3    Braun, H.P.4
  • 21
    • 75949097168 scopus 로고    scopus 로고
    • Functional and composition differences between mitochondrial complex II in Arabidopsis and rice are correlated with the complex genetic history of the enzyme
    • Huang S, Taylor NL, Narsai R, Eubel H, Whelan J, Millar AH (2010) Functional and composition differences between mitochondrial complex II in Arabidopsis and rice are correlated with the complex genetic history of the enzyme. Plant Mol Biol 72: 331-342.
    • (2010) Plant Mol Biol , vol.72 , pp. 331-342
    • Huang, S.1    Taylor, N.L.2    Narsai, R.3    Eubel, H.4    Whelan, J.5    Millar, A.H.6
  • 22
    • 0030111226 scopus 로고    scopus 로고
    • New insights into the composition, molecular mass and stoichiometry of the protein complexes of plant mitochondria
    • Jänsch L, Kruft V, Schmitz UK, Braun HP (1996) New insights into the composition, molecular mass and stoichiometry of the protein complexes of plant mitochondria. Plant J 9: 357-368.
    • (1996) Plant J , vol.9 , pp. 357-368
    • Jänsch, L.1    Kruft, V.2    Schmitz, U.K.3    Braun, H.P.4
  • 23
    • 0032479295 scopus 로고    scopus 로고
    • Unique composition of the preprotein translocase of the outer mitochondrial membrane from plants
    • Jänsch 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
    • Jänsch, L.1    Kruft, V.2    Schmitz, U.K.3    Braun, H.P.4
  • 25
    • 79958144995 scopus 로고    scopus 로고
    • Proteomic approach to characterize mitochondrial complex I from plants
    • Klodmann J, Braun HP (2011) Proteomic approach to characterize mitochondrial complex I from plants. Phytochemistry 72: 1071-1080.
    • (2011) Phytochemistry , vol.72 , pp. 1071-1080
    • Klodmann, J.1    Braun, H.P.2
  • 26
    • 77953226426 scopus 로고    scopus 로고
    • Internal architecture of mitochondrial complex I from Arabidopsis thaliana
    • Klodmann J, Sunderhaus S, Nimtz M, Jänsch L, Braun HP (2010) Internal architecture of mitochondrial complex I from Arabidopsis thaliana. Plant Cell 22: 797-810.
    • (2010) Plant Cell , vol.22 , pp. 797-810
    • Klodmann, J.1    Sunderhaus, S.2    Nimtz, M.3    Jänsch, L.4    Braun, H.P.5
  • 27
    • 85047683107 scopus 로고    scopus 로고
    • Proteomic approach to identify novel mitochondrial functions in Arabidopsis thaliana
    • Kruft V, Eubel H, Werhahn WH, Jänsch L, Braun HP (2001) Proteomic approach to identify novel mitochondrial functions in Arabidopsis thaliana. Plant Physiol 127: 1694-1710.
    • (2001) Plant Physiol , vol.127 , pp. 1694-1710
    • Kruft, V.1    Eubel, H.2    Werhahn, W.H.3    Jänsch, L.4    Braun, H.P.5
  • 28
    • 79958172874 scopus 로고    scopus 로고
    • Combining proteomics of root and shoot mitochondria and transcript analysis to define constitutive and variable components in plant mitochondria
    • Lee CP, Eubel H, O'Toole N, Millar AH (2011) Combining proteomics of root and shoot mitochondria and transcript analysis to define constitutive and variable components in plant mitochondria. Phytochemistry 72: 1092-1108.
    • (2011) Phytochemistry , vol.72 , pp. 1092-1108
    • Lee, C.P.1    Eubel, H.2    O'Toole, N.3    Millar, A.H.4
  • 29
    • 37849017986 scopus 로고    scopus 로고
    • Functional definition of outer membrane proteins involved in preprotein import into mitochondria
    • Lister R, Carrie C, Duncan O, Ho LH, Howell KA, Murcha MW, Whelan J (2007) Functional definition of outer membrane proteins involved in preprotein import into mitochondria. Plant Cell 19: 3739-3759.
    • (2007) Plant Cell , vol.19 , pp. 3739-3759
    • Lister, R.1    Carrie, C.2    Duncan, O.3    Ho, L.H.4    Howell, K.A.5    Murcha, M.W.6    Whelan, J.7
  • 30
    • 18844421618 scopus 로고    scopus 로고
    • Protein import into mitochondria: Origins and functions today
    • Lister R, Hulett JM, Lithgow T, Whelan J (2005) Protein import into mitochondria: origins and functions today. Mol Membr Biol 22: 87-100.
    • (2005) Mol Membr Biol , vol.22 , pp. 87-100
    • Lister, R.1    Hulett, J.M.2    Lithgow, T.3    Whelan, J.4
  • 31
    • 34247513352 scopus 로고    scopus 로고
    • Mitochondrial acyl carrier proteins in Arabidopsis thaliana are predominantly soluble matrix proteins and none can be confirmed as subunits of respiratory complex I
    • Meyer EH, Heazlewood JL, Millar AH (2007) Mitochondrial acyl carrier proteins in Arabidopsis thaliana are predominantly soluble matrix proteins and none can be confirmed as subunits of respiratory complex I. Plant Mol Biol 64: 319-327.
    • (2007) Plant Mol Biol , vol.64 , pp. 319-327
    • Meyer, E.H.1    Heazlewood, J.L.2    Millar, A.H.3
  • 32
    • 39749155929 scopus 로고    scopus 로고
    • Resolving and identifying protein components of plant mitochondrial respiratory complexes using three dimensions of gel electrophoresis
    • Meyer EH, Taylor NL, Millar AH (2008) Resolving and identifying protein components of plant mitochondrial respiratory complexes using three dimensions of gel electrophoresis. J Proteome Res 2: 786-794.
    • (2008) J Proteome Res , vol.2 , pp. 786-794
    • Meyer, E.H.1    Taylor, N.L.2    Millar, A.H.3
  • 33
  • 34
    • 12344323931 scopus 로고    scopus 로고
    • Mitochondrial cytochrome c oxidase and succinate dehydrogenase contain plant-specific subunits
    • Millar AH, Eubel H, Jänsch L, Kruft V, Heazlewood L, Braun HP (2004a) Mitochondrial cytochrome c oxidase and succinate dehydrogenase contain plant-specific subunits. Plant Mol Biol 56: 77-89.
    • (2004) Plant Mol Biol , vol.56 , pp. 77-89
    • Millar, A.H.1    Eubel, H.2    Jänsch, L.3    Kruft, V.4    Heazlewood, L.5    Braun, H.P.6
  • 37
    • 4544230849 scopus 로고    scopus 로고
    • Changes in the mitochondrial proteome during the anoxia to air transition in rice focus around cytochrome-containing respiratory complexes
    • Millar AH, Trend AE, Heazlewood JL (2004b) Changes in the mitochondrial proteome during the anoxia to air transition in rice focus around cytochrome-containing respiratory complexes. J Biol Chem 279: 39471-39478.
    • (2004) J Biol Chem , vol.279 , pp. 39471-39478
    • Millar, A.H.1    Trend, A.E.2    Heazlewood, J.L.3
  • 38
    • 0029311313 scopus 로고
    • The N-terminal extension of the ADP/ATP translocator is not involved in targeting to plant mitochondria in vivo
    • Mozo T, Fischer K, Flügge UI, Schmitz UK (1995) The N-terminal extension of the ADP/ATP translocator is not involved in targeting to plant mitochondria in vivo. Plant J 7: 1015-1020.
    • (1995) Plant J , vol.7 , pp. 1015-1020
    • Mozo, T.1    Fischer, K.2    Schmitz, U.K.3
  • 39
    • 0023931883 scopus 로고
    • Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250
    • Neuhoff V, Arold N, Taube D, Ehrhardt W (1988) Improved staining of proteins in polyacrylamide gels including isoelectric focusing gels with clear background at nanogram sensitivity using Coomassie Brilliant Blue G-250 and R-250. Electrophoresis 6: 255-262.
    • (1988) Electrophoresis , vol.6 , pp. 255-262
    • Neuhoff, V.1    Arold, N.2    Taube, D.3    Ehrhardt, W.4
  • 40
    • 1042289735 scopus 로고    scopus 로고
    • Clp protease complexes from photosynthetic and non-photosynthetic plastids andmitochondria of plants, their predicted three-dimensional structures, and functional implications
    • Peltier JB, Ripoll DR, Friso G, Rudella A, Cai Y, Ytterberg J, Giacomelli L, Pillardy J, van Wijk KJ (2004) Clp protease complexes from photosynthetic and non-photosynthetic plastids andmitochondria of plants, their predicted three-dimensional structures, and functional implications. J Biol Chem 279: 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    Giacomelli, L.7    Pillardy, J.8    van Wijk, K.J.9
  • 41
    • 37549064026 scopus 로고    scopus 로고
    • A structural investigation of complex I and I+III2 supercomplex from Zea mays at 11-13. Å resolution: Assignment of the carbonic anhydrase domain and evidence for structural heterogeneity within complex I
    • Peters K, Dukina NV, Jänsch L, Braun HP, Boekema EJ (2008) A structural investigation of complex I and I+III2 supercomplex from Zea mays at 11-13. Å resolution: assignment of the carbonic anhydrase domain and evidence for structural heterogeneity within complex I. Biochim Biophys Acta (Bioenergetics) 1777: 84-93.
    • (2008) Biochim Biophys Acta (Bioenergetics) , vol.1777 , pp. 84-93
    • Peters, K.1    Dukina, N.V.2    Jänsch, L.3    Braun, H.P.4    Boekema, E.J.5
  • 42
    • 0035680135 scopus 로고    scopus 로고
    • Rotenone-insensitive NAD(P)H dehydrogenases in plants: Immunodetection and distribution of native proteins in mitochondria
    • Rasmusson AG, Agius SC (2001) Rotenone-insensitive NAD(P)H dehydrogenases in plants: immunodetection and distribution of native proteins in mitochondria. Plant Physiol Biochem 39: 1057-1066.
    • (2001) Plant Physiol Biochem , vol.39 , pp. 1057-1066
    • Rasmusson, A.G.1    Agius, S.C.2
  • 43
    • 80052032987 scopus 로고    scopus 로고
    • GelMap: A novel software tool for the creation and presentation of proteome reference maps
    • Rode C, Senkler M, Klodmann J, Winkelmann T, Braun HP (2011) GelMap: a novel software tool for the creation and presentation of proteome reference maps. J Proteomics 74: 2214-2219.
    • (2011) J Proteomics , vol.74 , pp. 2214-2219
    • Rode, C.1    Senkler, M.2    Klodmann, J.3    Winkelmann, T.4    Braun, H.P.5
  • 44
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger H, von Jagow G (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal Biochem 166: 368-379.
    • (1987) Anal Biochem , vol.166 , pp. 368-379
    • Schägger, H.1    von Jagow, G.2
  • 45
    • 0026409298 scopus 로고
    • Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form
    • Schägger H, von Jagow G (1991) Blue native electrophoresis for isolation of membrane protein complexes in enzymatically active form. Anal Biochem 199: 223-231.
    • (1991) Anal Biochem , vol.199 , pp. 223-231
    • Schägger, H.1    von Jagow, G.2
  • 47
    • 77949486574 scopus 로고    scopus 로고
    • Supramolecular structure of the OXPHOS system in highly thermogenic tissue of Arum maculatum
    • Sunderhaus S, Klodmann J, Lenz C, Braun HP (2010) Supramolecular structure of the OXPHOS system in highly thermogenic tissue of Arum maculatum. Plant Physiol Biochem 48: 265-272.
    • (2010) Plant Physiol Biochem , vol.48 , pp. 265-272
    • Sunderhaus, S.1    Klodmann, J.2    Lenz, C.3    Braun, H.P.4
  • 48
    • 79955022171 scopus 로고    scopus 로고
    • The Arabidopsis thaliana 2D gel mitochondrial proteome: Refining the value of reference maps for assessing protein abundance, contaminants and post-translational modifications
    • Taylor N, Heazlewood J, Millar AH (2011) The Arabidopsis thaliana 2D gel mitochondrial proteome: refining the value of reference maps for assessing protein abundance, contaminants and post-translational modifications. Proteomics 11: 1720-1733.
    • (2011) Proteomics , vol.11 , pp. 1720-1733
    • Taylor, N.1    Heazlewood, J.2    Millar, A.H.3
  • 49
    • 77953284896 scopus 로고    scopus 로고
    • Prohibitins: Mitochondrial partners in development and stress response
    • Van Aken O, Whelan J, van Breusegem F (2010) Prohibitins: mitochondrial partners in development and stress response. Trends Plant Sci 15: 275-282.
    • (2010) Trends Plant Sci , vol.15 , pp. 275-282
    • van Aken, O.1    Whelan, J.2    van Breusegem, F.3
  • 50
    • 0036119404 scopus 로고    scopus 로고
    • Biochemical dissection of the mitochondrial proteome of Arabidopsis thaliana by three-dimensional gel electrophoresis
    • Werhahn WH, Braun HP (2002) Biochemical dissection of the mitochondrial proteome of Arabidopsis thaliana by three-dimensional gel electrophoresis. Electrophoresis 23: 640-646.
    • (2002) Electrophoresis , vol.23 , pp. 640-646
    • Werhahn, W.H.1    Braun, H.P.2
  • 51
    • 0038687177 scopus 로고    scopus 로고
    • Identification of novel subunits of the TOMcomplex fromArabidopsis thaliana
    • WerhahnWH, Jänsch L, BraunHP
    • WerhahnWH, Jänsch L, BraunHP (2003) Identification of novel subunits of the TOMcomplex fromArabidopsis thaliana. Plant Physiol Biochem41: 407-416.
    • (2003) Plant Physiol Biochem , vol.41 , pp. 407-416
  • 52
    • 0035115121 scopus 로고    scopus 로고
    • Purification and characterization of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis thaliana: Identification of multiple forms of TOM20
    • Werhahn WH, Niemeyer A, Jänsch L, Kruft V, Schmitz UK, Braun HP (2001) Purification and characterization of the preprotein translocase of the outer mitochondrial membrane from Arabidopsis thaliana: identification of multiple forms of TOM20. Plant Physiol 125: 943-954.
    • (2001) Plant Physiol , vol.125 , pp. 943-954
    • Werhahn, W.H.1    Niemeyer, A.2    Jänsch, L.3    Kruft, V.4    Schmitz, U.K.5    Braun, H.P.6
  • 53
    • 0026920782 scopus 로고
    • The adenine nucleotide translocator of higher plants is synthesized as a large precursor that is processed upon import into mitochondria
    • Winning BM, Sarah CJ, Purdue PE, Day CD, Leaver CJ (1992) The adenine nucleotide translocator of higher plants is synthesized as a large precursor that is processed upon import into mitochondria. Plant J 2: 763-773.
    • (1992) Plant J , vol.2 , pp. 763-773
    • Winning, B.M.1    Sarah, C.J.2    Purdue, P.E.3    Day, C.D.4    Leaver, C.J.5
  • 55
    • 0035909958 scopus 로고    scopus 로고
    • The remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexes
    • Zhou ZH, McCarthy DB, O'Connor CM, Reed LJ, Stoops JK (2001) The remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexes. Proc Natl Acad Sci USA 98: 14802-14807.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14802-14807
    • Zhou, Z.H.1    McCarthy, D.B.2    O'Connor, C.M.3    Reed, L.J.4    Stoops, J.K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.