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Volumn 19, Issue 9, 2008, Pages 3934-3943

Erratum: The yeast Aac2 protein exists in physical association with the cytochrome bc1-COX supercomplex and the TIM23 machinery (Molecular Biology of the Cell (2008) 19 (3934-3943)DOI:10.1091/mbc.E08-04-0402);The yeast Aac2 protein exists in physical association with the cytochrome bc1-COX supercomplex and the TIM23 machinery

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE NUCLEOTIDE TRANSLOCASE; CYTOCHROME C OXIDASE; FUNGAL PROTEIN; MITOCHONDRIAL PROTEIN; PROTEIN AAC2; PROTEIN TIM23; UBIQUINOL CYTOCHROME C REDUCTASE; UNCLASSIFIED DRUG;

EID: 55549119296     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E08-04-0402     Document Type: Erratum
Times cited : (87)

References (56)
  • 2
    • 34447277172 scopus 로고    scopus 로고
    • Yeast mitochondrial ADP/ATP carriers are monomeric in detergents as demonstrated by differential affinity purification
    • Bamber, L., Slotboom, D. J., and Kunji, E. R. (2007a). Yeast mitochondrial ADP/ATP carriers are monomeric in detergents as demonstrated by differential affinity purification. J. Mol. Biol. 371, 388-395.
    • (2007) J. Mol. Biol , vol.371 , pp. 388-395
    • Bamber, L.1    Slotboom, D.J.2    Kunji, E.R.3
  • 3
    • 34547436185 scopus 로고    scopus 로고
    • The yeast mitochondrial ADP/ATP carrier functions as a monomer in mitochondrial membranes
    • Bamber, L., Harding, M., Monné, M., Slotboom, D. J., and Kunji, E. R. (2007b). The yeast mitochondrial ADP/ATP carrier functions as a monomer in mitochondrial membranes. Proc. Natl. Acad. Sci. USA 104, 10830-10834.
    • (2007) Proc. Natl. Acad. Sci. USA , vol.104 , pp. 10830-10834
    • Bamber, L.1    Harding, M.2    Monné, M.3    Slotboom, D.J.4    Kunji, E.R.5
  • 4
    • 4644319049 scopus 로고    scopus 로고
    • Mss51p and Cox14p jointly regulate mitochondrial Cox1p expression in Saccharomyces cerevisiae
    • Barrientos, A., Zambrano, A., and Tzagoloff, A. (2004). Mss51p and Cox14p jointly regulate mitochondrial Cox1p expression in Saccharomyces cerevisiae. EMBO J. 23, 3472-3482.
    • (2004) EMBO J , vol.23 , pp. 3472-3482
    • Barrientos, A.1    Zambrano, A.2    Tzagoloff, A.3
  • 5
    • 0033611057 scopus 로고    scopus 로고
    • Adenine nucleotide translocase-1, a component of the permeability transition pore, can dominantly induce apoptosis
    • Bauer, M.K.A., Schubert, A., Rocks, O., and Grimm, S., (1999). Adenine nucleotide translocase-1, a component of the permeability transition pore, can dominantly induce apoptosis. J. Cell Biol. 147, 1493-1501.
    • (1999) J. Cell Biol , vol.147 , pp. 1493-1501
    • Bauer, M.K.A.1    Schubert, A.2    Rocks, O.3    Grimm, S.4
  • 6
    • 33846968150 scopus 로고    scopus 로고
    • Supramolecular structure of the mitochondrial oxidative phosphorylation system
    • Boekema, E. J., and Braun, H. P. (2007). Supramolecular structure of the mitochondrial oxidative phosphorylation system. J. Biol. Chem. 282, 1-4.
    • (2007) J. Biol. Chem , vol.282 , pp. 1-4
    • Boekema, E.J.1    Braun, H.P.2
  • 7
    • 0032570865 scopus 로고    scopus 로고
    • The respiratory chain in yeast behaves as a single functional unit
    • Boumans, H., Grivell, L. A., and Berden, J. A. (1998). The respiratory chain in yeast behaves as a single functional unit. J. Biol. Chem. 273, 4872-4877.
    • (1998) J. Biol. Chem , vol.273 , pp. 4872-4877
    • Boumans, H.1    Grivell, L.A.2    Berden, J.A.3
  • 8
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72, 248-254.
    • (1976) Anal. Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 10
    • 20244373481 scopus 로고    scopus 로고
    • Mitochondrial presequence translocase: Switching between TOM tethering and motor recruitment involves Tim21 and Tim17
    • Chacinska, A. et al. (2005). Mitochondrial presequence translocase: switching between TOM tethering and motor recruitment involves Tim21 and Tim17. Cell 120, 817-829.
    • (2005) Cell , vol.120 , pp. 817-829
    • Chacinska, A.1
  • 11
    • 0036667983 scopus 로고    scopus 로고
    • Induction of an unregulated channel by mutations in adenine nucleotide translocase suggests an explanation for human ophthalmoplegia
    • Chen, X. J. (2002). Induction of an unregulated channel by mutations in adenine nucleotide translocase suggests an explanation for human ophthalmoplegia. Hum. Mol. Genet. 11, 1835-1843.
    • (2002) Hum. Mol. Genet , vol.11 , pp. 1835-1843
    • Chen, X.J.1
  • 12
    • 3142754128 scopus 로고    scopus 로고
    • Sal1p, a calcium-dependent carrier protein that suppresses an essential cellular function associated With the Aac2 isoform of ADP/ATP translocase in Saccharomyces cerevisiae
    • Chen, X. J. (2004). Sal1p, a calcium-dependent carrier protein that suppresses an essential cellular function associated With the Aac2 isoform of ADP/ATP translocase in Saccharomyces cerevisiae. Genetics 167, 607-617.
    • (2004) Genetics , vol.167 , pp. 607-617
    • Chen, X.J.1
  • 13
    • 0034674060 scopus 로고    scopus 로고
    • 1 and cytochrome c oxidase complexes associate to form a single supracomplex in yeast mitochondria
    • 1 and cytochrome c oxidase complexes associate to form a single supracomplex in yeast mitochondria. J. Biol. Chem. 275, 18093-18098.
    • (2000) J. Biol. Chem , vol.275 , pp. 18093-18098
    • Cruciat, C.1    Brunner, S.2    Baumann, F.3    Neupert, W.4    Stuart, R.A.5
  • 14
    • 0025915949 scopus 로고
    • ADP/ATP translocator is essential only for anaerobic growth of yeast Saccharomyces cerevisiae
    • Drgon, T., Sabová, L., Nelson, N., and Kolarov, J. (1991). ADP/ATP translocator is essential only for anaerobic growth of yeast Saccharomyces cerevisiae. FEBS Lett. 289, 159-162.
    • (1991) FEBS Lett , vol.289 , pp. 159-162
    • Drgon, T.1    Sabová, L.2    Nelson, N.3    Kolarov, J.4
  • 15
    • 0026689334 scopus 로고
    • Yeast ADP/ATP carrier (AAC) proteins exhibit similar enzymatic properties but their deletion produces different phenotypes
    • Drgon, T., Sabová, L., Gavurniková, G., and Kolarov, J. (1992). Yeast ADP/ATP carrier (AAC) proteins exhibit similar enzymatic properties but their deletion produces different phenotypes. FEBS Lett. 304, 277-280.
    • (1992) FEBS Lett , vol.304 , pp. 277-280
    • Drgon, T.1    Sabová, L.2    Gavurniková, G.3    Kolarov, J.4
  • 16
    • 14744270722 scopus 로고    scopus 로고
    • Structure of a mitochondrial supercomplex formed by respiratory-chain complexes I and III
    • Dudkina, N. V., Eubel, H., Keegstra, W., Boekema, E. J., and Braun, H. P. (2005). Structure of a mitochondrial supercomplex formed by respiratory-chain complexes I and III. Proc Natl Acad Sci USA 102, 3225-3229.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 3225-3229
    • Dudkina, N.V.1    Eubel, H.2    Keegstra, W.3    Boekema, E.J.4    Braun, H.P.5
  • 18
    • 0019879891 scopus 로고
    • Relationship between the energy cost of ATP transport and ATP synthesis in mitochondria
    • Duszyński, J., Bogucka, K., Letko, G., Küster, U., Kunz, W., and Wojtczak, L. (1981). Relationship between the energy cost of ATP transport and ATP synthesis in mitochondria. Biochim. Biophys. Acta 637, 217-223.
    • (1981) Biochim. Biophys. Acta , vol.637 , pp. 217-223
    • Duszyński, J.1    Bogucka, K.2    Letko, G.3    Küster, U.4    Kunz, W.5    Wojtczak, L.6
  • 19
    • 16544382212 scopus 로고    scopus 로고
    • Mutations in AAC2, equivalent to human adPEO-associated ANT1 mutations, lead to defective oxidative phosphorylation in Saccharomyces cerevisiae and affect mitochondrial DNA stability
    • Fontanesi, F., Palmieri, L., Scarcia, P., Lodi, T., Donnini, C., Limongelli, A., Tiranti, V., Zeviani, M., Ferrero, I., and Viola, A. M. (2004). Mutations in AAC2, equivalent to human adPEO-associated ANT1 mutations, lead to defective oxidative phosphorylation in Saccharomyces cerevisiae and affect mitochondrial DNA stability. Hum. Mol. Genet. 13, 923-934.
    • (2004) Hum. Mol. Genet , vol.13 , pp. 923-934
    • Fontanesi, F.1    Palmieri, L.2    Scarcia, P.3    Lodi, T.4    Donnini, C.5    Limongelli, A.6    Tiranti, V.7    Zeviani, M.8    Ferrero, I.9    Viola, A.M.10
  • 20
    • 33748108494 scopus 로고    scopus 로고
    • Characterization of Mmp37p, a Saccharomyces cerevisiae mitochondrial matrix protein with a role in mitochondrial protein import
    • Gallas, M. R., Dienhart, M. K. Stuart, R. A., and Long, R. M. (2006). Characterization of Mmp37p, a Saccharomyces cerevisiae mitochondrial matrix protein with a role in mitochondrial protein import. Mol. Biol. Cell 17, 4051-4062.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4051-4062
    • Gallas, M.R.1    Dienhart, M.K.2    Stuart, R.A.3    Long, R.M.4
  • 21
    • 20044386366 scopus 로고    scopus 로고
    • O-ATP synthase complex interactions in vivo can occur in the absence of the dimer specific subunit e
    • O-ATP synthase complex interactions in vivo can occur in the absence of the dimer specific subunit e. J. Bioenerg. Biomembr. 37, 55-66.
    • (2005) J. Bioenerg. Biomembr , vol.37 , pp. 55-66
    • Gavin, P.D.1    Prescott, M.2    Devenish, R.J.3
  • 22
    • 0025113386 scopus 로고
    • Structure-function studies of adenine nucleotide transport in mitochondria. II. Biochemical analysis of distinct AAC1 and AAC2 proteins in yeast
    • Gawaz, M., Douglas, M. G., and Klingenberg, M. (1990). Structure-function studies of adenine nucleotide transport in mitochondria. II. Biochemical analysis of distinct AAC1 and AAC2 proteins in yeast. J. Biol. Chem. 265, 14202-14208.
    • (1990) J. Biol. Chem , vol.265 , pp. 14202-14208
    • Gawaz, M.1    Douglas, M.G.2    Klingenberg, M.3
  • 23
    • 0029011611 scopus 로고
    • Cloning and characterization of COX14, whose product is required for assembly of yeast cytochrome oxidase
    • Glerum, D. M., Koerner, T. J., and Tzagoloff, A. (1995). Cloning and characterization of COX14, whose product is required for assembly of yeast cytochrome oxidase. J. Biol. Chem. 270, 15585-15590.
    • (1995) J. Biol. Chem , vol.270 , pp. 15585-15590
    • Glerum, D.M.1    Koerner, T.J.2    Tzagoloff, A.3
  • 25
    • 34249688217 scopus 로고    scopus 로고
    • A structural model of the cytochrome c reductase/oxidase supercomplex from yeast mitochondria
    • Heinemeyer, J., Braun, H. P., Boekema, E. J., and Kouril, R. (2007). A structural model of the cytochrome c reductase/oxidase supercomplex from yeast mitochondria. J. Biol. Chem. 282, 12240-12248.
    • (2007) J. Biol. Chem , vol.282 , pp. 12240-12248
    • Heinemeyer, J.1    Braun, H.P.2    Boekema, E.J.3    Kouril, R.4
  • 27
    • 0024600466 scopus 로고
    • Molecular aspects of the adenine nucleotide carrier from mitochondria
    • Klingenberg, M. (1989). Molecular aspects of the adenine nucleotide carrier from mitochondria. Arch. Biochem. Biophys. 270, 1-14.
    • (1989) Arch. Biochem. Biophys , vol.270 , pp. 1-14
    • Klingenberg, M.1
  • 28
    • 0037809232 scopus 로고    scopus 로고
    • Mitochondrial ATP synthasome. Cristae-enriched membranes and a multi-well detergent screening assay yield dispersed single complexes containing the ATP synthase and carriers for Pi and ADP/ATP
    • Ko, Y. H., Delannoy, M., Hullihen, J., Chiu, W., and Pedersen, P. L. (2003). Mitochondrial ATP synthasome. Cristae-enriched membranes and a multi-well detergent screening assay yield dispersed single complexes containing the ATP synthase and carriers for Pi and ADP/ATP. Biol. Chem. 278, 12305-12309.
    • (2003) Biol. Chem , vol.278 , pp. 12305-12309
    • Ko, Y.H.1    Delannoy, M.2    Hullihen, J.3    Chiu, W.4    Pedersen, P.L.5
  • 29
    • 0036225534 scopus 로고    scopus 로고
    • A novel D104G mutation in the adenine nucleotide translocator 1 gene in autosomal dominant progressive external ophthalmoplegia patients with mitochondrial DNA with multiple deletions
    • Komaki, H., Fukazawa, T., Houzen, H., Yoshida, K., Nonaka, I., and Goto, Y. (2002). A novel D104G mutation in the adenine nucleotide translocator 1 gene in autosomal dominant progressive external ophthalmoplegia patients with mitochondrial DNA with multiple deletions. Ann. Neurol. 51, 645-648.
    • (2002) Ann. Neurol , vol.51 , pp. 645-648
    • Komaki, H.1    Fukazawa, T.2    Houzen, H.3    Yoshida, K.4    Nonaka, I.5    Goto, Y.6
  • 30
    • 36349034613 scopus 로고    scopus 로고
    • Cooperation of translocase complexes in mitochondrial protein import
    • Kutik, S., Guiard, B., Meyer, H. E., Wiedemann, N., and Pfanner, N. (2007). Cooperation of translocase complexes in mitochondrial protein import. J. Cell Biol. 179, 585-591.
    • (2007) J. Cell Biol , vol.179 , pp. 585-591
    • Kutik, S.1    Guiard, B.2    Meyer, H.E.3    Wiedemann, N.4    Pfanner, N.5
  • 31
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 32
    • 37549019364 scopus 로고    scopus 로고
    • Supramolecular organization of the respiratory chain in Neurospora crassa mitochondria
    • Marques, I., Dencher, N. A., Videira, A., and Krause, F. (2007). Supramolecular organization of the respiratory chain in Neurospora crassa mitochondria. Eukaryot. Cell 6, 391-2405.
    • (2007) Eukaryot. Cell , vol.6 , pp. 391-2405
    • Marques, I.1    Dencher, N.A.2    Videira, A.3    Krause, F.4
  • 33
    • 0031009910 scopus 로고    scopus 로고
    • SHY1, the yeast homolog of the mammalian SURF-1 gene, encodes a mitochondrial protein required for respiration
    • Mashkevich, G., Repetto, B., Glerum, D. M., Jin, C., and Tzagoloff, A. (1997). SHY1, the yeast homolog of the mammalian SURF-1 gene, encodes a mitochondrial protein required for respiration. J. Biol. Chem. 272, 14356-14364.
    • (1997) J. Biol. Chem , vol.272 , pp. 14356-14364
    • Mashkevich, G.1    Repetto, B.2    Glerum, D.M.3    Jin, C.4    Tzagoloff, A.5
  • 34
    • 33746327466 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain supercomplexes are destabilized in Barth syndrome patients
    • McKenzie, M., Lazarou, M., Thorburn, D. R., and Ryan, M. T. (2006). Mitochondrial respiratory chain supercomplexes are destabilized in Barth syndrome patients. J. Mol. Biol. 361, 462-469.
    • (2006) J. Mol. Biol , vol.361 , pp. 462-469
    • McKenzie, M.1    Lazarou, M.2    Thorburn, D.R.3    Ryan, M.T.4
  • 36
  • 37
    • 0035956491 scopus 로고    scopus 로고
    • A novel missense adenine nucleotide translocator-1 gene mutation in a Greek adPEO family
    • Napoli, L. et al. (2001). A novel missense adenine nucleotide translocator-1 gene mutation in a Greek adPEO family. Neurology 57, 2295-2298.
    • (2001) Neurology , vol.57 , pp. 2295-2298
    • Napoli, L.1
  • 38
    • 27544484570 scopus 로고    scopus 로고
    • Structural basis for lipid-mediated interactions between mitochondrial ADP/ATP carrier monomers
    • Nury, H., Dahout-Gonzalez, C., Trézéguet, V., Lauquin, G., Brandolin, G., and Pebay-Peyroula, E. (2005). Structural basis for lipid-mediated interactions between mitochondrial ADP/ATP carrier monomers. FEBS Lett. 579, 6031-6036.
    • (2005) FEBS Lett , vol.579 , pp. 6031-6036
    • Nury, H.1    Dahout-Gonzalez, C.2    Trézéguet, V.3    Lauquin, G.4    Brandolin, G.5    Pebay-Peyroula, E.6
  • 42
    • 4143120198 scopus 로고    scopus 로고
    • Nucleotide exchange in mitochondria: Insight at a molecular level
    • Pebay-Peyroula, E., and Brandolin, G. (2004). Nucleotide exchange in mitochondria: insight at a molecular level Curr. Opin. Struct. Biol. 14, 420-425.
    • (2004) Curr. Opin. Struct. Biol , vol.14 , pp. 420-425
    • Pebay-Peyroula, E.1    Brandolin, G.2
  • 44
    • 35348842764 scopus 로고    scopus 로고
    • Coa1 links the Mss51 post-translational function to Cox1 cofactor insertion in cytochrome c oxidase assembly
    • Pierrel, F., Bestwick, M. L., Cobine, P. A., Khalimonchuk, O., Cricco, J. A., and Winge, D. R. (2007). Coa1 links the Mss51 post-translational function to Cox1 cofactor insertion in cytochrome c oxidase assembly. EMBO J. 26, 4335-4346.
    • (2007) EMBO J , vol.26 , pp. 4335-4346
    • Pierrel, F.1    Bestwick, M.L.2    Cobine, P.A.3    Khalimonchuk, O.4    Cricco, J.A.5    Winge, D.R.6
  • 45
    • 43749103377 scopus 로고    scopus 로고
    • 1-cytochrome oxidase supercomplex and its association with the TIM23 machinery
    • 1-cytochrome oxidase supercomplex and its association with the TIM23 machinery. J. Biol. Chem. 283, 6677-6686.
    • (2008) J. Biol. Chem , vol.283 , pp. 6677-6686
    • Saddar, S.1    Dienhart, M.K.2    Stuart, R.A.3
  • 46
    • 0033525924 scopus 로고    scopus 로고
    • Okidative phosphorylation at the fin de siècle
    • Saraste, M. (1999). Okidative phosphorylation at the fin de siècle. Science 283, 1488-1493.
    • (1999) Science , vol.283 , pp. 1488-1493
    • Saraste, M.1
  • 47
    • 0038230469 scopus 로고    scopus 로고
    • Supercomplexes in the respiratory chains of yeast and mammalian mitochondria
    • Schägger, H., and Pfeiffer, K. (2000). Supercomplexes in the respiratory chains of yeast and mammalian mitochondria. EMBO J. 19, 1777-1783.
    • (2000) EMBO J , vol.19 , pp. 1777-1783
    • Schägger, H.1    Pfeiffer, K.2
  • 48
    • 0037056045 scopus 로고    scopus 로고
    • Respiratory chain supercomplexes of mitochondria and bacteria
    • Schägger, H. (2002). Respiratory chain supercomplexes of mitochondria and bacteria. Biochim. Biophys. Acta 1555, 154-159.
    • (2002) Biochim. Biophys. Acta , vol.1555 , pp. 154-159
    • Schägger, H.1
  • 49
    • 0022404366 scopus 로고
    • Transport of proteins into mitochondria: Translocational intermediates spanning contact sites between outer and inner membranes
    • Schleyer, M., and Neupert, W. (1985). Transport of proteins into mitochondria: translocational intermediates spanning contact sites between outer and inner membranes. Cell 43, 339-350.
    • (1985) Cell , vol.43 , pp. 339-350
    • Schleyer, M.1    Neupert, W.2
  • 51
    • 0016795386 scopus 로고
    • Assembly of the mitochondrial membrane system: Isolation of nuclear and cytoplasmic mutants of Saccharomyces cerevisiae with specific defects in mitochondrial functions
    • Tzagoloff, A., Akai, A., Needleman, R. B. (1975). Assembly of the mitochondrial membrane system: isolation of nuclear and cytoplasmic mutants of Saccharomyces cerevisiae with specific defects in mitochondrial functions. J. Bacteriol. 122, 826-831.
    • (1975) J. Bacteriol , vol.122 , pp. 826-831
    • Tzagoloff, A.1    Akai, A.2    Needleman, R.B.3
  • 52
    • 33750949389 scopus 로고    scopus 로고
    • A role for Tim21 in membrane-potential-dependent preprotein sorting in mitochondria
    • van der Laan, M., Wiedemann, N., Mick, D. U., Guiard, B., Rehling, P., and Pfanner, N. (2006). A role for Tim21 in membrane-potential-dependent preprotein sorting in mitochondria. Curr. Biol. 16, 2271-2276.
    • (2006) Curr. Biol , vol.16 , pp. 2271-2276
    • van der Laan, M.1    Wiedemann, N.2    Mick, D.U.3    Guiard, B.4    Rehling, P.5    Pfanner, N.6
  • 53
    • 37249039150 scopus 로고    scopus 로고
    • Sorting switch of mitochondrial presequence translocase involves coupling of motor module to respiratory chain
    • Wiedemann, N., van der Laan, M., Hutu, D. P., Rehling, P., and Pfanner, N. (2007). Sorting switch of mitochondrial presequence translocase involves coupling of motor module to respiratory chain. J. Cell Biol. 179, 1115-1122.
    • (2007) J. Cell Biol , vol.179 , pp. 1115-1122
    • Wiedemann, N.1    van der Laan, M.2    Hutu, D.P.3    Rehling, P.4    Pfanner, N.5
  • 54
    • 0035229427 scopus 로고    scopus 로고
    • The mitochondrion in apoptosis: How Pandora's box opens
    • Zamzami, N., and Kroemer, G. (2001). The mitochondrion in apoptosis: how Pandora's box opens. Nat. Rev. Mol. Cell Biol. 2, 67-71.
    • (2001) Nat. Rev. Mol. Cell Biol , vol.2 , pp. 67-71
    • Zamzami, N.1    Kroemer, G.2
  • 55
    • 34548131150 scopus 로고    scopus 로고
    • Identification and characterization of cytochrome bc(1) subcomplexes in mitochondria from yeast with single and double deletions of genes encoding cytochrome bc(1) subunits
    • Zara, V., Conte, L., and Trumpower, B. L. (2007). Identification and characterization of cytochrome bc(1) subcomplexes in mitochondria from yeast with single and double deletions of genes encoding cytochrome bc(1) subunits. FEBS J. 274, 4526-4539.
    • (2007) FEBS J , vol.274 , pp. 4526-4539
    • Zara, V.1    Conte, L.2    Trumpower, B.L.3
  • 56
    • 0029116916 scopus 로고
    • The mitochondrial permeability transition
    • Zoratti, M., and Szabò I. (1995). The mitochondrial permeability transition Biochim. Biophys. Acta 1241, 139-176.
    • (1995) Biochim. Biophys. Acta , vol.1241 , pp. 139-176
    • Zoratti, M.1    Szabò, I.2


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