메뉴 건너뛰기




Volumn 253, Issue 5, 2016, Pages 1299-1308

Mitochondrial morphology and dynamics in Triticum aestivum roots in response to rotenone and antimycin A

Author keywords

Antimycin A; Megamitochondria; Mitochondrial morphology; Roots; Rotenone; Wheat

Indexed keywords

3-(2,4-DICHLORO-5-METHOXYPHENYL)-2-SULFANYL-4(3H)-QUINAZOLINONE; ANTIMYCIN A1; HYDROGEN PEROXIDE; QUINAZOLINONE DERIVATIVE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); ROTENONE; UBIQUINOL CYTOCHROME C REDUCTASE;

EID: 84944589315     PISSN: 0033183X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00709-015-0888-0     Document Type: Article
Times cited : (7)

References (51)
  • 1
    • 30344460650 scopus 로고    scopus 로고
    • Plant mitochondrial fission and fusion
    • COI: 1:CAS:528:DC%2BD28XhtVyms7Y%3D
    • Arimura S, Tsutsumi N (2005) Plant mitochondrial fission and fusion. Plant Biotechnol J 22:415–418
    • (2005) Plant Biotechnol J , vol.22 , pp. 415-418
    • Arimura, S.1    Tsutsumi, N.2
  • 2
    • 57749122081 scopus 로고    scopus 로고
    • Arabidopsis ELONGATED MITOCHONDRIA1 is required for localization of DYNAMIN-RELATED PROTEIN3A to mitochondrial fission sites
    • COI: 1:CAS:528:DC%2BD1cXpvVOisLY%3D, PID: 18559960
    • Arimura S, Fujimoto M, Doniwa Y, Kadoya N, Nakazono M, Sakamoto W, Tsutsumi N (2008) Arabidopsis ELONGATED MITOCHONDRIA1 is required for localization of DYNAMIN-RELATED PROTEIN3A to mitochondrial fission sites. Plant Cell 20(6):1555–1566
    • (2008) Plant Cell , vol.20 , Issue.6 , pp. 1555-1566
    • Arimura, S.1    Fujimoto, M.2    Doniwa, Y.3    Kadoya, N.4    Nakazono, M.5    Sakamoto, W.6    Tsutsumi, N.7
  • 3
    • 51749084230 scopus 로고    scopus 로고
    • Ultrastructure of the mitochondrion and its bearing on function and bioenergetics
    • COI: 1:CAS:528:DC%2BD1cXms1eqs7Y%3D, PID: 18435594
    • Benard G, Rossignol R (2008) Ultrastructure of the mitochondrion and its bearing on function and bioenergetics. Antioxid Redox Signal 10:1313–1343
    • (2008) Antioxid Redox Signal , vol.10 , pp. 1313-1343
    • Benard, G.1    Rossignol, R.2
  • 4
    • 77952055233 scopus 로고    scopus 로고
    • Reactive oxygen species and nitric oxide in plant mitochondria: origin and redundant regulatory systems
    • COI: 1:CAS:528:DC%2BC3cXktlOkt7c%3D, PID: 20059731
    • Blokhina O, Fagerstedt KV (2010) Reactive oxygen species and nitric oxide in plant mitochondria: origin and redundant regulatory systems. Physiol Plant 138(4):447–462
    • (2010) Physiol Plant , vol.138 , Issue.4 , pp. 447-462
    • Blokhina, O.1    Fagerstedt, K.V.2
  • 5
    • 77952541558 scopus 로고    scopus 로고
    • The sites and topology of mitochondrial superoxide production
    • COI: 1:CAS:528:DC%2BC3cXmslGjt70%3D, PID: 20064600
    • Brand MD (2010) The sites and topology of mitochondrial superoxide production. Exp Gerontol 45(7–8):466–472
    • (2010) Exp Gerontol , vol.45 , Issue.7-8 , pp. 466-472
    • Brand, M.D.1
  • 6
    • 57649211340 scopus 로고    scopus 로고
    • Megacomplex organization of the oxidative phosphorylation system by structural analysis of respiratory supercomplexes from potato
    • COI: 1:CAS:528:DC%2BD1cXhsFagu77F, PID: 19059196
    • Bultema JB, Braun HP, Boekema EJ, Kouril R (2009) Megacomplex organization of the oxidative phosphorylation system by structural analysis of respiratory supercomplexes from potato. Biochim Biophys Acta 1787(1):60–67
    • (2009) Biochim Biophys Acta , vol.1787 , Issue.1 , pp. 60-67
    • Bultema, J.B.1    Braun, H.P.2    Boekema, E.J.3    Kouril, R.4
  • 7
    • 38849099158 scopus 로고    scopus 로고
    • Chemical inhibition of the mitochondrial division dynamin reveals its role in Bax/Bak-dependent mitochondrial outer membrane permeabilization
    • COI: 1:CAS:528:DC%2BD1cXit1Ojs7w%3D, PID: 18267088
    • Cassidy-Stone A, Chipuk JE, Ingerman E, Song C, Yoo C, Kuwana T, Kurth MJ, Shaw JT, Hinshaw JE, Green DR, Nunnari J (2008) Chemical inhibition of the mitochondrial division dynamin reveals its role in Bax/Bak-dependent mitochondrial outer membrane permeabilization. Dev Cell 14(2):193–204
    • (2008) Dev Cell , vol.14 , Issue.2 , pp. 193-204
    • Cassidy-Stone, A.1    Chipuk, J.E.2    Ingerman, E.3    Song, C.4    Yoo, C.5    Kuwana, T.6    Kurth, M.J.7    Shaw, J.T.8    Hinshaw, J.E.9    Green, D.R.10    Nunnari, J.11
  • 8
    • 22544451586 scopus 로고    scopus 로고
    • Disruption of fusion results in mitochondrial heterogeneity and dysfunction
    • COI: 1:CAS:528:DC%2BD2MXlvFymt7s%3D, PID: 15899901
    • Chen HC, Chomyn A, Chan DC (2005) Disruption of fusion results in mitochondrial heterogeneity and dysfunction. J Biol Chem 280:26185–26192
    • (2005) J Biol Chem , vol.280 , pp. 26185-26192
    • Chen, H.C.1    Chomyn, A.2    Chan, D.C.3
  • 9
    • 77957358299 scopus 로고    scopus 로고
    • Mitochondrial dynamics in cell death and neurodegeneration
    • COI: 1:CAS:528:DC%2BC3cXhtFOrtb7E, PID: 20577776
    • Cho D-H, Nakamura T, Lipton SA (2010) Mitochondrial dynamics in cell death and neurodegeneration. Cell Mol Life Sci 67:3435–3447
    • (2010) Cell Mol Life Sci , vol.67 , pp. 3435-3447
    • Cho, D.-H.1    Nakamura, T.2    Lipton, S.A.3
  • 10
  • 12
    • 13444292066 scopus 로고    scopus 로고
    • Respiratory chain supercomplexes in plant mitochondria
    • COI: 1:CAS:528:DC%2BD2MXhtFGht7s%3D, PID: 15707832
    • Eubel H, Heinemeyer J, Sunderhaus S, Braun HP (2004) Respiratory chain supercomplexes in plant mitochondria. Plant Physiol Biochem 42(12):937–942
    • (2004) Plant Physiol Biochem , vol.42 , Issue.12 , pp. 937-942
    • Eubel, H.1    Heinemeyer, J.2    Sunderhaus, S.3    Braun, H.P.4
  • 13
    • 0006495655 scopus 로고
    • Inhibitor studies on formation of giant mitochondria in Nitella flexilis
    • COI: 1:CAS:528:DyaL3sXktVehs7o%3D
    • Foissner I (1983) Inhibitor studies on formation of giant mitochondria in Nitella flexilis. Phyton-Ann Rei Bot A 23(1):19–29
    • (1983) Phyton-Ann Rei Bot A , vol.23 , Issue.1 , pp. 19-29
    • Foissner, I.1
  • 14
    • 84870669523 scopus 로고    scopus 로고
    • Mitochondrial protein synthesis, import and assembly
    • COI: 1:CAS:528:DC%2BC3sXjt1eqsb0%3D, PID: 23212899
    • Fox TD (2012) Mitochondrial protein synthesis, import and assembly. Genetics 192(4):1203–1234
    • (2012) Genetics , vol.192 , Issue.4 , pp. 1203-1234
    • Fox, T.D.1
  • 15
    • 68949090311 scopus 로고    scopus 로고
    • Importance of lipid metabolism for intracellular and mitochondrial membrane fusion/fission processes
    • COI: 1:CAS:528:DC%2BD1MXhtVentbvP
    • Furt F, Moreau P (2009) Importance of lipid metabolism for intracellular and mitochondrial membrane fusion/fission processes. Biochem Cell Biol 41:1828–1836
    • (2009) Biochem Cell Biol , vol.41 , pp. 1828-1836
    • Furt, F.1    Moreau, P.2
  • 16
    • 0042233907 scopus 로고    scopus 로고
    • Structural organization of the mitochondrial respiratory chain
    • COI: 1:CAS:528:DC%2BD3sXmsFyntLc%3D, PID: 12833641
    • Genova ML, Bianchi C, Lenaz G (2003) Structural organization of the mitochondrial respiratory chain. Ital J Biochem 52(1):58–61
    • (2003) Ital J Biochem , vol.52 , Issue.1 , pp. 58-61
    • Genova, M.L.1    Bianchi, C.2    Lenaz, G.3
  • 17
    • 84985874191 scopus 로고
    • Effect of barbiturates and rotenone on respiration of intact plant tissues
    • COI: 1:CAS:528:DyaE2MXlsVantLg%3D
    • Gordon L, Alekseeva V, Bichurina A (1975a) Effect of barbiturates and rotenone on respiration of intact plant tissues. Russ Plant Physiol 22(4):849–851
    • (1975) Russ Plant Physiol , vol.22 , Issue.4 , pp. 849-851
    • Gordon, L.1    Alekseeva, V.2    Bichurina, A.3
  • 19
    • 34247641081 scopus 로고    scopus 로고
    • The influence of ascorbic acid on the oxygen consumption and the heat production by the cells of wheat seedlings roots with their mitochondrial electron transport chain inhibited at comlexes I and III
    • COI: 1:CAS:528:DC%2BD2sXkvFKqt7w%3D
    • Gordon L, Rakhmatullina D, Ogorodnikova T, Alyabyev A, Minibayeva F, Loseva N, Mityashina S (2007) The influence of ascorbic acid on the oxygen consumption and the heat production by the cells of wheat seedlings roots with their mitochondrial electron transport chain inhibited at comlexes I and III. Thermochim Acta 458:92–96
    • (2007) Thermochim Acta , vol.458 , pp. 92-96
    • Gordon, L.1    Rakhmatullina, D.2    Ogorodnikova, T.3    Alyabyev, A.4    Minibayeva, F.5    Loseva, N.6    Mityashina, S.7
  • 20
    • 84894410126 scopus 로고    scopus 로고
    • The energetic functions of plant mitochondria under stress
    • Grabelnych O (2005) The energetic functions of plant mitochondria under stress. J Stress Physiol Biochem 1(1):37–54
    • (2005) J Stress Physiol Biochem , vol.1 , Issue.1 , pp. 37-54
    • Grabelnych, O.1
  • 21
    • 0037768628 scopus 로고    scopus 로고
    • Spatial and temporal dymamics of budding yeast mitochondria lacking the division component Fis1p
    • Jacobs S, Martini N, Schauss AC, Egner A, Westermann B, Hell SW (2003) Spatial and temporal dymamics of budding yeast mitochondria lacking the division component Fis1p. J Cell Sci 116:2005–2014
    • (2003) J Cell Sci , vol.116 , pp. 2005-2014
    • Jacobs, S.1    Martini, N.2    Schauss, A.C.3    Egner, A.4    Westermann, B.5    Hell, S.W.6
  • 22
    • 84869221236 scopus 로고    scopus 로고
    • Mitochondrial composition, function and stress response in plants
    • COI: 1:CAS:528:DC%2BC3sXjtF2lu70%3D, PID: 23046139
    • Jacoby RP, Li L, Huang S, Pong Lee C, Millar AH, Taylor NL (2012) Mitochondrial composition, function and stress response in plants. J Integr Plant Biol 54(11):887–906
    • (2012) J Integr Plant Biol , vol.54 , Issue.11 , pp. 887-906
    • Jacoby, R.P.1    Li, L.2    Huang, S.3    Pong Lee, C.4    Millar, A.H.5    Taylor, N.L.6
  • 23
    • 0001465386 scopus 로고
    • Changes in lipid peroxidation and lipolytic and free-radical scavenging enzyme actvities during aging and sprouting of potato (Solanum tuberosum) seed-tubers
    • COI: 1:CAS:528:DyaK3sXks1yhtLo%3D, PID: 12231802
    • Kumar G, Knowles NR (1993) Changes in lipid peroxidation and lipolytic and free-radical scavenging enzyme actvities during aging and sprouting of potato (Solanum tuberosum) seed-tubers. Plant Physiol 102(1):115–124
    • (1993) Plant Physiol , vol.102 , Issue.1 , pp. 115-124
    • Kumar, G.1    Knowles, N.R.2
  • 24
    • 77953696905 scopus 로고    scopus 로고
    • Small molecule inhibitors of mitochondrial division: tools that translate basic biological research into medicine
    • COI: 1:CAS:528:DC%2BC3cXotVWqs7w%3D, PID: 20609407
    • Lackner L, Nunnari J (2010) Small molecule inhibitors of mitochondrial division: tools that translate basic biological research into medicine. Chem Biol 17(6):578–583
    • (2010) Chem Biol , vol.17 , Issue.6 , pp. 578-583
    • Lackner, L.1    Nunnari, J.2
  • 25
    • 68949107623 scopus 로고    scopus 로고
    • Structural and functional organization of the mitochondrial respiratory chain: a dynamic super-assembly
    • COI: 1:CAS:528:DC%2BD1MXhtVentbrL, PID: 19711505
    • Lenaz G, Genova ML (2009) Structural and functional organization of the mitochondrial respiratory chain: a dynamic super-assembly. Int J Biochem Cell Biol 41(10):1750–1772
    • (2009) Int J Biochem Cell Biol , vol.41 , Issue.10 , pp. 1750-1772
    • Lenaz, G.1    Genova, M.L.2
  • 26
    • 77949634569 scopus 로고    scopus 로고
    • Structure and organization of mitochondrial respiratory complexes: a new understanding of an old subject
    • COI: 1:CAS:528:DC%2BC3cXjtlGgs7k%3D, PID: 19739941
    • Lenaz G, Genova ML (2010) Structure and organization of mitochondrial respiratory complexes: a new understanding of an old subject. Antioxid Redox Signal 12(8):961–1008
    • (2010) Antioxid Redox Signal , vol.12 , Issue.8 , pp. 961-1008
    • Lenaz, G.1    Genova, M.L.2
  • 27
    • 33645745752 scopus 로고    scopus 로고
    • The mitochondrial compartment
    • Logan DC (2007) The mitochondrial compartment. J Exp Bot 57:1225–1243
    • (2007) J Exp Bot , vol.57 , pp. 1225-1243
    • Logan, D.C.1
  • 28
    • 77955280280 scopus 로고    scopus 로고
    • The dynamic plant chondriome
    • COI: 1:CAS:528:DC%2BC3cXpvVOhtrs%3D, PID: 20044013
    • Logan DC (2010) The dynamic plant chondriome. Semin Cell Dev Biol 21:550–557
    • (2010) Semin Cell Dev Biol , vol.21 , pp. 550-557
    • Logan, D.C.1
  • 29
    • 1542754695 scopus 로고    scopus 로고
    • ADL2a, like ADL2b, is involved in the control of higher plant mitochondrial morphology
    • COI: 1:CAS:528:DC%2BD2cXhvFSrtbs%3D, PID: 14754924
    • Logan DC, Scott I, Tobin AK (2004) ADL2a, like ADL2b, is involved in the control of higher plant mitochondrial morphology. J Exp Bot 55(397):783–785
    • (2004) J Exp Bot , vol.55 , Issue.397 , pp. 783-785
    • Logan, D.C.1    Scott, I.2    Tobin, A.K.3
  • 30
    • 0037265815 scopus 로고    scopus 로고
    • The alternative oxidase; in vivo regulation and function
    • COI: 1:CAS:528:DC%2BD3sXjsVWhsL4%3D
    • Millenaar FF, Lambers H (2003) The alternative oxidase; in vivo regulation and function. Plant Biol 5:2–15
    • (2003) Plant Biol , vol.5 , pp. 2-15
    • Millenaar, F.F.1    Lambers, H.2
  • 32
    • 0030924730 scopus 로고    scopus 로고
    • The oxidation of cytosolic NAD(P)H by external NAD(P)H dehydrogenases in the respiratory chain of plant mitochondria
    • Møller IM (1997) The oxidation of cytosolic NAD(P)H by external NAD(P)H dehydrogenases in the respiratory chain of plant mitochondria. Physiol Plant 100:85–90
    • (1997) Physiol Plant , vol.100 , pp. 85-90
    • Møller, I.M.1
  • 33
    • 0035781005 scopus 로고    scopus 로고
    • Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species
    • PID: 11337409
    • Møller IM (2001) Plant mitochondria and oxidative stress: electron transport, NADPH turnover, and metabolism of reactive oxygen species. Annu Rev Plant Physiol Plant Mol Biol 52:561–591
    • (2001) Annu Rev Plant Physiol Plant Mol Biol , vol.52 , pp. 561-591
    • Møller, I.M.1
  • 34
    • 84986974453 scopus 로고
    • Direct evidence for the presence of a rotenone-resistant NADH dehydrogenase on the inner surface of the inner membrane of plant mitochondria
    • Møller IM, Palmer JM (1982) Direct evidence for the presence of a rotenone-resistant NADH dehydrogenase on the inner surface of the inner membrane of plant mitochondria. Physiol Plant 54:267–274
    • (1982) Physiol Plant , vol.54 , pp. 267-274
    • Møller, I.M.1    Palmer, J.M.2
  • 35
    • 0038024175 scopus 로고    scopus 로고
    • A fuzzy mitochondrial fusion apparatus comes into focus
    • COI: 1:CAS:528:DC%2BD3sXktFOnsrg%3D, PID: 12778126
    • Mozdy AD, Shaw JM (2003) A fuzzy mitochondrial fusion apparatus comes into focus. Nat Rev Mol Cell Biol 4:468–478
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 468-478
    • Mozdy, A.D.1    Shaw, J.M.2
  • 36
    • 77955638748 scopus 로고    scopus 로고
    • Respiratory chain complexes in dynamic mitochondria display a patchy distribution in life cells
    • PID: 20689601
    • Muster B, Kohl W, Witting I, Strecker V, Joos F, Haase W, Bereiter-Hahn J, Busch K (2010) Respiratory chain complexes in dynamic mitochondria display a patchy distribution in life cells. PLoS ONE 5(7):e11910. doi:10.1371/journal. pone.0011910
    • (2010) PLoS ONE , vol.5 , Issue.7
    • Muster, B.1    Kohl, W.2    Witting, I.3    Strecker, V.4    Joos, F.5    Haase, W.6    Bereiter-Hahn, J.7    Busch, K.8
  • 37
    • 33846841016 scopus 로고    scopus 로고
    • Possible plant mitochondria involvement in cell adaptation to drought stress. A case study: durum wheat mitochondria
    • COI: 1:CAS:528:DC%2BD2sXhtlOltLs%3D, PID: 17261694
    • Pastore D, Trono D, Laus MN, Di Fonzo N, Flagella Z (2007) Possible plant mitochondria involvement in cell adaptation to drought stress. A case study: durum wheat mitochondria. J Exp Bot 58(2):195–210
    • (2007) J Exp Bot , vol.58 , Issue.2 , pp. 195-210
    • Pastore, D.1    Trono, D.2    Laus, M.N.3    Di Fonzo, N.4    Flagella, Z.5
  • 38
    • 84859738519 scopus 로고    scopus 로고
    • Changes in mitochondrial shape in wheat root cells exposed to mitochondrial poisons
    • COI: 1:CAS:528:DC%2BC38Xls1SgsrY%3D
    • Ponomareva AA, Polygalova OO (2012) Changes in mitochondrial shape in wheat root cells exposed to mitochondrial poisons. Russ Plant Physiol 59(3):428–433
    • (2012) Russ Plant Physiol , vol.59 , Issue.3 , pp. 428-433
    • Ponomareva, A.A.1    Polygalova, O.O.2
  • 39
    • 84989674612 scopus 로고
    • NAD(P)H dehydrogenases on the inner surface of the inner mitochondrial membrane studied using inside-out submitochondrial particles
    • COI: 1:CAS:528:DyaK38XhslKisg%3D%3D
    • Rasmusson AG, Møller IM (1991) NAD(P)H dehydrogenases on the inner surface of the inner mitochondrial membrane studied using inside-out submitochondrial particles. Physiol Plant 83:357–365
    • (1991) Physiol Plant , vol.83 , pp. 357-365
    • Rasmusson, A.G.1    Møller, I.M.2
  • 40
    • 0032490088 scopus 로고    scopus 로고
    • Physiological, biochemical and molecular aspects of mitochondrial complex I in plants
    • COI: 1:CAS:528:DyaK1cXis1ClsLk%3D, PID: 9593845
    • Rasmusson AG, Heiser V, Zabaleta E, Brennicke A, Grohmann L (1998) Physiological, biochemical and molecular aspects of mitochondrial complex I in plants. Biochim Biophys Acta 1364:101–111
    • (1998) Biochim Biophys Acta , vol.1364 , pp. 101-111
    • Rasmusson, A.G.1    Heiser, V.2    Zabaleta, E.3    Brennicke, A.4    Grohmann, L.5
  • 41
    • 0033213361 scopus 로고    scopus 로고
    • Homologues of yeast and bacterial rotenone-insensitive NADH dehydrogenases in higher eukaryotes: two enzymes are present in potato mitochondria
    • COI: 1:CAS:528:DyaK1MXnsVGru7Y%3D, PID: 10571867
    • Rasmusson AG, Svensson AS, Knoop V, Grohmann L, Brennicke A (1999) Homologues of yeast and bacterial rotenone-insensitive NADH dehydrogenases in higher eukaryotes: two enzymes are present in potato mitochondria. Plant J 20:79–87
    • (1999) Plant J , vol.20 , pp. 79-87
    • Rasmusson, A.G.1    Svensson, A.S.2    Knoop, V.3    Grohmann, L.4    Brennicke, A.5
  • 42
    • 0028862799 scopus 로고
    • Direct evidence for the presence of 2 external NAD(P)H dehydrogenases coupled to the electron transport chain in plant mitochondria
    • COI: 1:CAS:528:DyaK2MXovVynsr8%3D, PID: 7589489
    • Roberts TH, Fredlund KM, Møller IM (1995) Direct evidence for the presence of 2 external NAD(P)H dehydrogenases coupled to the electron transport chain in plant mitochondria. FEBS Lett 373(3):307–309
    • (1995) FEBS Lett , vol.373 , Issue.3 , pp. 307-309
    • Roberts, T.H.1    Fredlund, K.M.2    Møller, I.M.3
  • 43
    • 57749098549 scopus 로고    scopus 로고
    • The mitochondrial cycle of Arabidopsis shoot apical meristem leaf primordium meristematic cells is defined by a perinuclear tentaculate/cage-like mitochondrion
    • COI: 1:CAS:528:DC%2BD1cXhsVSnurjP, PID: 18799659
    • Segui-Simarro JM, Coronado MJ, Staehelin LA (2008) The mitochondrial cycle of Arabidopsis shoot apical meristem leaf primordium meristematic cells is defined by a perinuclear tentaculate/cage-like mitochondrion. Plant Physiol 148:1380–1393
    • (2008) Plant Physiol , vol.148 , pp. 1380-1393
    • Segui-Simarro, J.M.1    Coronado, M.J.2    Staehelin, L.A.3
  • 44
    • 0032564864 scopus 로고    scopus 로고
    • Uncoupling: new approaches to an old problem of bioenergetics
    • COI: 1:CAS:528:DyaK1cXht1WisL4%3D, PID: 9507078
    • Skulachev VP (1998) Uncoupling: new approaches to an old problem of bioenergetics. Biochem Biophys Acta 1363(2):100–124
    • (1998) Biochem Biophys Acta , vol.1363 , Issue.2 , pp. 100-124
    • Skulachev, V.P.1
  • 45
    • 77949486574 scopus 로고    scopus 로고
    • Supramolecular structure of the OXPHOS system in highly thermogenic tissue of Arum maculatum
    • COI: 1:CAS:528:DC%2BC3cXjs12lsbs%3D, PID: 20144873
    • Sunderhaus S, Klodmann J, Lenz C, Brawn H-P (2010) Supramolecular structure of the OXPHOS system in highly thermogenic tissue of Arum maculatum. Plant Physiol Biochem 48(4):265–272
    • (2010) Plant Physiol Biochem , vol.48 , Issue.4 , pp. 265-272
    • Sunderhaus, S.1    Klodmann, J.2    Lenz, C.3    Brawn, H.-P.4
  • 46
    • 49349102894 scopus 로고    scopus 로고
    • Mitochondrial fusion fission and autophagy as a quality control axis: the bioenergetic view
    • COI: 1:CAS:528:DC%2BD1cXpvF2qt7g%3D, PID: 18519024
    • Twig G, Hyde B, Shirihai OS (2008) Mitochondrial fusion fission and autophagy as a quality control axis: the bioenergetic view. Biochim Biophys Acta 1777(9):1092–1097
    • (2008) Biochim Biophys Acta , vol.1777 , Issue.9 , pp. 1092-1097
    • Twig, G.1    Hyde, B.2    Shirihai, O.S.3
  • 47
    • 0036011333 scopus 로고    scopus 로고
    • Giant mitochondria are a response to low oxygen pressure in cells of tabacco (Nicotiana tabacum L.)
    • PID: 11971932
    • Van Gestel K, Verbelen J-P (2002) Giant mitochondria are a response to low oxygen pressure in cells of tabacco (Nicotiana tabacum L.). J Exp Bot 53:1215–1218
    • (2002) J Exp Bot , vol.53 , pp. 1215-1218
    • Van Gestel, K.1    Verbelen, J.-P.2
  • 49
    • 84874575715 scopus 로고    scopus 로고
    • Mitochondrial metabolism of reactive oxygen species
    • COI: 1:CAS:528:DC%2BC3sXjvFCgtrY%3D, PID: 23376030
    • Venditti P, Di Stefano L, Di Meo S (2013) Mitochondrial metabolism of reactive oxygen species. Mitochondrion 13(2):71–82
    • (2013) Mitochondrion , vol.13 , Issue.2 , pp. 71-82
    • Venditti, P.1    Di Stefano, L.2    Di Meo, S.3
  • 50
    • 84864669289 scopus 로고    scopus 로고
    • Bioenergetic role of mitochondrial fusion and fission
    • COI: 1:CAS:528:DC%2BC38Xkt1GgsL0%3D, PID: 22409868
    • Westermann B (2012) Bioenergetic role of mitochondrial fusion and fission. Biochim Biophys Acta 1817(10):1833–1838
    • (2012) Biochim Biophys Acta , vol.1817 , Issue.10 , pp. 1833-1838
    • Westermann, B.1
  • 51
    • 0028306066 scopus 로고
    • Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides
    • Wolff S (1994) Ferrous ion oxidation in presence of ferric ion indicator xylenol orange for measurement of hydroperoxides. Method Enzymol 223:182–189
    • (1994) Method Enzymol , vol.223 , pp. 182-189
    • Wolff, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.