메뉴 건너뛰기




Volumn 18, Issue 9, 2007, Pages 3582-3590

OPA1 processing reconstituted in yeast depends on the subunit composition of the m-AAA protease in mitochondria

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; DYNAMIN; GUANOSINE TRIPHOSPHATASE; ISOPROTEIN; MITOCHONDRIAL ENZYME; OLIGOMER; PARAPLEGIN; PROTEIN AFGL1; PROTEIN AFGL2; PROTEIN MGM1; PROTEIN OPA1; PROTEIN PARL; PROTEIN PCP1; PROTEIN SUBUNIT; PROTEIN YTA10; PROTEIN YTA12; PROTEINASE; UNCLASSIFIED DRUG;

EID: 34548349869     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E07-02-0164     Document Type: Article
Times cited : (157)

References (45)
  • 1
    • 0033772264 scopus 로고    scopus 로고
    • OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28
    • Alexander, C. et al. (2000). OPA1, encoding a dynamin-related GTPase, is mutated in autosomal dominant optic atrophy linked to chromosome 3q28. Nat. Genet. 26, 211-215.
    • (2000) Nat. Genet , vol.26 , pp. 211-215
    • Alexander, C.1
  • 2
    • 0032541406 scopus 로고    scopus 로고
    • The formation of respiratory chain complexes in mitochondria is under the proteolytic control of the m-AAA protease
    • Arlt, H., Steglich, G., Perryman, R., Guiard, B., Neupert, W., and Langer, T. (1998). The formation of respiratory chain complexes in mitochondria is under the proteolytic control of the m-AAA protease. EMBO J. 17, 4837-4847.
    • (1998) EMBO J , vol.17 , pp. 4837-4847
    • Arlt, H.1    Steglich, G.2    Perryman, R.3    Guiard, B.4    Neupert, W.5    Langer, T.6
  • 3
    • 27444446030 scopus 로고    scopus 로고
    • Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation
    • Arnoult, D., Grodet, A., Lee, Y. J., Estaquier, J., and Blackstone, C. (2005). Release of OPA1 during apoptosis participates in the rapid and complete release of cytochrome c and subsequent mitochondrial fragmentation. J. Biol. Chem. 280, 35742-35750.
    • (2005) J. Biol. Chem , vol.280 , pp. 35742-35750
    • Arnoult, D.1    Grodet, A.2    Lee, Y.J.3    Estaquier, J.4    Blackstone, C.5
  • 4
    • 0344736798 scopus 로고    scopus 로고
    • Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia
    • Atorino, L., Silvestri, L., Koppen, M., Cassina, L., Ballabio, A., Marconi, R., Langer, T., and Casari, G. (2003). Loss of m-AAA protease in mitochondria causes complex I deficiency and increased sensitivity to oxidative stress in hereditary spastic paraplegia. J. Cell Biol. 163, 777-787.
    • (2003) J. Cell Biol , vol.163 , pp. 777-787
    • Atorino, L.1    Silvestri, L.2    Koppen, M.3    Cassina, L.4    Ballabio, A.5    Marconi, R.6    Langer, T.7    Casari, G.8
  • 5
    • 0032511186 scopus 로고    scopus 로고
    • Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease
    • Casari, G. et al. (1998). Spastic paraplegia and OXPHOS impairment caused by mutations in paraplegin, a nuclear-encoded mitochondrial metalloprotease. Cell 93, 973-983.
    • (1998) Cell , vol.93 , pp. 973-983
    • Casari, G.1
  • 6
    • 22544451586 scopus 로고    scopus 로고
    • Disruption of fusion results in mitochondrial heterogeneity and dysfunction
    • Chen, H., Chomyn, A., and Chan, D. C. (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.1    Chomyn, A.2    Chan, D.C.3
  • 8
    • 33745685054 scopus 로고    scopus 로고
    • Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling
    • Cipolat, S. et al. (2006). Mitochondrial rhomboid PARL regulates cytochrome c release during apoptosis via OPA1-dependent cristae remodeling. Cell 126, 163-175.
    • (2006) Cell , vol.126 , pp. 163-175
    • Cipolat, S.1
  • 10
    • 20244381365 scopus 로고    scopus 로고
    • Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy
    • Delettre, C. et al. (2000). Nuclear gene OPA1, encoding a mitochondrial dynamin-related protein, is mutated in dominant optic atrophy. Nat. Genet. 26, 207-210.
    • (2000) Nat. Genet , vol.26 , pp. 207-210
    • Delettre, C.1
  • 11
    • 33845976357 scopus 로고    scopus 로고
    • Proteolytic processing of OPA1 links mitochondrial dysfunction to alterations in mitochondrial morphology
    • Duvezin-Caubet, S. et al. (2006). Proteolytic processing of OPA1 links mitochondrial dysfunction to alterations in mitochondrial morphology. J. Biol. Chem. 281, 37972-37979.
    • (2006) J. Biol. Chem , vol.281 , pp. 37972-37979
    • Duvezin-Caubet, S.1
  • 12
    • 0036424840 scopus 로고    scopus 로고
    • Esser, K., Tursun, B., Ingenhoven, M., Michaelis, G., and E., P. (2002). A novel two-step mechanism for removal of a mitochondrial signal sequence involves the mAAA complex and the putative rhomboid protease pcp1. J. Mol. Biol. 323, 835-843.
    • Esser, K., Tursun, B., Ingenhoven, M., Michaelis, G., and E., P. (2002). A novel two-step mechanism for removal of a mitochondrial signal sequence involves the mAAA complex and the putative rhomboid protease pcp1. J. Mol. Biol. 323, 835-843.
  • 13
    • 1342310772 scopus 로고    scopus 로고
    • Axonal degeneration in paraplegin-deficient mice is associated with abnormal mitochondria and impairment of axonal transport
    • Ferreirinha, F. et al. (2004). Axonal degeneration in paraplegin-deficient mice is associated with abnormal mitochondria and impairment of axonal transport. J. Clin. Invest. 113, 231-242.
    • (2004) J. Clin. Invest , vol.113 , pp. 231-242
    • Ferreirinha, F.1
  • 15
    • 33745699393 scopus 로고    scopus 로고
    • OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion
    • Frezza, C. et al. (2006). OPA1 controls apoptotic cristae remodeling independently from mitochondrial fusion. Cell 126, 177-189.
    • (2006) Cell , vol.126 , pp. 177-189
    • Frezza, C.1
  • 16
    • 2442421118 scopus 로고    scopus 로고
    • Loss of the intermembrane space protein Mgm1/OPA1 induces swelling and localized constrictions along the lengths of mitochondria
    • Griparic, L., van der Wei, N. N., Orozco, I. J., Peters, P. J., and van der Bliek, A. M. (2004). Loss of the intermembrane space protein Mgm1/OPA1 induces swelling and localized constrictions along the lengths of mitochondria. J. Biol. Chem. 279, 18792-18798.
    • (2004) J. Biol. Chem , vol.279 , pp. 18792-18798
    • Griparic, L.1    van der Wei, N.N.2    Orozco, I.J.3    Peters, P.J.4    van der Bliek, A.M.5
  • 17
    • 0025994140 scopus 로고
    • Guide to yeast genetics and molecular biology
    • Guthrie, C., and Fink, G. R. (1991). Guide to yeast genetics and molecular biology. Methods Enzymol. 194, 1-270.
    • (1991) Methods Enzymol , vol.194 , pp. 1-270
    • Guthrie, C.1    Fink, G.R.2
  • 18
    • 2142710081 scopus 로고    scopus 로고
    • Alternative topogenesis of Mgm1 and mitochondrial morphology depend on ATP and a functional import motor
    • Herlan, M., Bornhovd, C., Hell, K., Neupert, W., and Reichert, A. S. (2004). Alternative topogenesis of Mgm1 and mitochondrial morphology depend on ATP and a functional import motor. J. Cell Biol. 165, 167-173.
    • (2004) J. Cell Biol , vol.165 , pp. 167-173
    • Herlan, M.1    Bornhovd, C.2    Hell, K.3    Neupert, W.4    Reichert, A.S.5
  • 19
    • 0042526632 scopus 로고    scopus 로고
    • Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA
    • Herlan, M., Vogel, F., Bornhövd, C., Neupert, W., and Reichert, A. S. (2003). Processing of Mgm1 by the rhomboid-type protease Pcp1 is required for maintenance of mitochondrial morphology and of mitochondrial DNA. J. Biol. Chem. 278, 27781-27788.
    • (2003) J. Biol. Chem , vol.278 , pp. 27781-27788
    • Herlan, M.1    Vogel, F.2    Bornhövd, C.3    Neupert, W.4    Reichert, A.S.5
  • 20
    • 33746299692 scopus 로고    scopus 로고
    • Regulation of mitochondrial morphology through proteolytic cleavage of OPA1
    • Ishihara, N., Fujita, Y., Oka, T., and Mihara, K. (2006). Regulation of mitochondrial morphology through proteolytic cleavage of OPA1. EMBO J. 25, 2966-2977.
    • (2006) EMBO J , vol.25 , pp. 2966-2977
    • Ishihara, N.1    Fujita, Y.2    Oka, T.3    Mihara, K.4
  • 21
    • 13944278072 scopus 로고    scopus 로고
    • DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans
    • Jagasia, R., Grote, P., Westermann, B., and Conradt, B. (2005). DRP-1-mediated mitochondrial fragmentation during EGL-1-induced cell death in C. elegans. Nature 433, 754-760.
    • (2005) Nature , vol.433 , pp. 754-760
    • Jagasia, R.1    Grote, P.2    Westermann, B.3    Conradt, B.4
  • 23
    • 33846127778 scopus 로고    scopus 로고
    • Variable and tissue-specific subunit composition of mitochondrial m-AAA protease complexes linked to hereditary spastic paraplegia
    • Koppen, M., Metodiev, M. D., Casari, G., Rugarli, E. I., and Langer, T. (2007). Variable and tissue-specific subunit composition of mitochondrial m-AAA protease complexes linked to hereditary spastic paraplegia. Mol. Cell. Biol. 27, 758-767.
    • (2007) Mol. Cell. Biol , vol.27 , pp. 758-767
    • Koppen, M.1    Metodiev, M.D.2    Casari, G.3    Rugarli, E.I.4    Langer, T.5
  • 24
    • 0035878402 scopus 로고    scopus 로고
    • Molecular and functional analyses of the human and mouse genes encoding AFG3L1, a mitochondrial metalloprotease homologous to the human spastic paraplegia protein
    • Kremmidiotis, G., Gardner, A. E., Settasatian, C., Savoia, A., Sutherland, G. R., and Callen, D. F. (2001). Molecular and functional analyses of the human and mouse genes encoding AFG3L1, a mitochondrial metalloprotease homologous to the human spastic paraplegia protein. Genomics 76, 58-65.
    • (2001) Genomics , vol.76 , pp. 58-65
    • Kremmidiotis, G.1    Gardner, A.E.2    Settasatian, C.3    Savoia, A.4    Sutherland, G.R.5    Callen, D.F.6
  • 25
    • 6344274848 scopus 로고    scopus 로고
    • Roles of the mammalian mitochondrial fission and fusion mediators fis1, drp1, and opa1 in apoptosis
    • Lee, Y. J., Jeong, S. Y., Karbowski, M., Smith, C. L., and Youle, R. J. (2004). Roles of the mammalian mitochondrial fission and fusion mediators fis1, drp1, and opa1 in apoptosis. Mol. Biol. Cell 15, 5001-5011.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 5001-5011
    • Lee, Y.J.1    Jeong, S.Y.2    Karbowski, M.3    Smith, C.L.4    Youle, R.J.5
  • 26
    • 0033639076 scopus 로고    scopus 로고
    • Membrane protein degradation by AAA proteases in mitochondria: Extraction of substrates from either membrane surface
    • Leonhard, K., Guiard, B., Pellecchia, G., Tzagoloff, A., Neupert, W., and Langer, T. (2000). Membrane protein degradation by AAA proteases in mitochondria: extraction of substrates from either membrane surface. Mol. Cell 5, 629-638.
    • (2000) Mol. Cell , vol.5 , pp. 629-638
    • Leonhard, K.1    Guiard, B.2    Pellecchia, G.3    Tzagoloff, A.4    Neupert, W.5    Langer, T.6
  • 27
    • 10944269186 scopus 로고    scopus 로고
    • The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses
    • Li, Z., Okamoto, K., Hayashi, Y., and Sheng, M. (2004). The importance of dendritic mitochondria in the morphogenesis and plasticity of spines and synapses. Cell 119, 873-887.
    • (2004) Cell , vol.119 , pp. 873-887
    • Li, Z.1    Okamoto, K.2    Hayashi, Y.3    Sheng, M.4
  • 28
    • 33646543714 scopus 로고    scopus 로고
    • Normal mitochondrial dynamics requires rhomboid-7 and affects Drosophila lifespan and neuronal function
    • McQuibban, G. A., Lee, J. R., Zheng, L., Juusola, M., and Freeman, M. (2006). Normal mitochondrial dynamics requires rhomboid-7 and affects Drosophila lifespan and neuronal function. Curr. Biol. 16, 982-989.
    • (2006) Curr. Biol , vol.16 , pp. 982-989
    • McQuibban, G.A.1    Lee, J.R.2    Zheng, L.3    Juusola, M.4    Freeman, M.5
  • 29
    • 0038700756 scopus 로고    scopus 로고
    • Mitochondrial membrane remodelling regulated by a conserved rhomboid protease
    • McQuibban, G. A., Saurya, S., and Freeman, M. (2003). Mitochondrial membrane remodelling regulated by a conserved rhomboid protease. Nature 423, 537-541.
    • (2003) Nature , vol.423 , pp. 537-541
    • McQuibban, G.A.1    Saurya, S.2    Freeman, M.3
  • 30
    • 0034881326 scopus 로고    scopus 로고
    • Inter-mitochondrial complementation: Mitochondria-specific system preventing mice from expression of disease phenotypes by mutant mtDNA
    • Nakada, K., Inoue, K., Ono, T., Isobe, K., Ogura, A., Goto, Y. I., Nonaka, I., and Hayashi, J. I. (2001). Inter-mitochondrial complementation: mitochondria-specific system preventing mice from expression of disease phenotypes by mutant mtDNA. Nat. Med. 7, 934-940.
    • (2001) Nat. Med , vol.7 , pp. 934-940
    • Nakada, K.1    Inoue, K.2    Ono, T.3    Isobe, K.4    Ogura, A.5    Goto, Y.I.6    Nonaka, I.7    Hayashi, J.I.8
  • 31
    • 25444514731 scopus 로고    scopus 로고
    • Ganglioside-induced differentiation associated protein 1 is a regulator of the mitochondrial network: New implications for Charcot-Marie-Tooth disease
    • Niemann, A., Ruegg, M., La Padula, V., Schenone, A., and Suter, U. (2005). Ganglioside-induced differentiation associated protein 1 is a regulator of the mitochondrial network: new implications for Charcot-Marie-Tooth disease. J. Cell Biol. 170, 1067-1078.
    • (2005) J. Cell Biol , vol.170 , pp. 1067-1078
    • Niemann, A.1    Ruegg, M.2    La Padula, V.3    Schenone, A.4    Suter, U.5
  • 32
    • 0030841103 scopus 로고    scopus 로고
    • Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA
    • Nunnari, J., Marshall, W. F., Straight, A., Murray, A., Sedat, J. W., and Walter, P. (1997). Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA. Mol. Biol. Cell 8, 1233-1242.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1233-1242
    • Nunnari, J.1    Marshall, W.F.2    Straight, A.3    Murray, A.4    Sedat, J.W.5    Walter, P.6
  • 33
    • 27544466847 scopus 로고    scopus 로고
    • Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes
    • Okamoto, K., and Shaw, J. M. (2005). Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes. Annu. Rev. Genet. 39, 503-536.
    • (2005) Annu. Rev. Genet , vol.39 , pp. 503-536
    • Okamoto, K.1    Shaw, J.M.2
  • 34
    • 0037424239 scopus 로고    scopus 로고
    • Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis
    • Olichon, A., Baricault, L., Gas, N., Guillou, E., Valette, A., Belenguer, P., and Lenaers, G. (2003). Loss of OPA1 perturbates the mitochondrial inner membrane structure and integrity, leading to cytochrome c release and apoptosis. J. Biol. Chem. 278, 7743-7746.
    • (2003) J. Biol. Chem , vol.278 , pp. 7743-7746
    • Olichon, A.1    Baricault, L.2    Gas, N.3    Guillou, E.4    Valette, A.5    Belenguer, P.6    Lenaers, G.7
  • 35
    • 33947434544 scopus 로고    scopus 로고
    • OPA1 alternate splicing uncouples an evolutionary conserved function in mitochondrial fusion from a vertebrate restricted function in apoptosis
    • Olichon, A., Elachouri, G., Baricault, L., Delettre, C., Belenguer, P., and Lenaers, G. (2006). OPA1 alternate splicing uncouples an evolutionary conserved function in mitochondrial fusion from a vertebrate restricted function in apoptosis. Cell Death Differ. 14, 682-692.
    • (2006) Cell Death Differ , vol.14 , pp. 682-692
    • Olichon, A.1    Elachouri, G.2    Baricault, L.3    Delettre, C.4    Belenguer, P.5    Lenaers, G.6
  • 36
    • 0037125183 scopus 로고    scopus 로고
    • The human dynamin-related protein OPA1 is anchored to the mitochondrial inner membrane facing the inter-membrane space
    • Olichon, A. et al. (2002). The human dynamin-related protein OPA1 is anchored to the mitochondrial inner membrane facing the inter-membrane space. FEBS Lett. 523, 171-176.
    • (2002) FEBS Lett , vol.523 , pp. 171-176
    • Olichon, A.1
  • 37
    • 0034938453 scopus 로고    scopus 로고
    • Human cells are protected from mitochondrial dysfunction by complementation of DNA products in fused mitochondria
    • Ono, T., Isobe, K., Nakada, K., and Hayashi, J. I. (2001). Human cells are protected from mitochondrial dysfunction by complementation of DNA products in fused mitochondria. Nat. Genet. 28, 272-275.
    • (2001) Nat. Genet , vol.28 , pp. 272-275
    • Ono, T.1    Isobe, K.2    Nakada, K.3    Hayashi, J.I.4
  • 38
    • 0037427529 scopus 로고    scopus 로고
    • Differential sublocalizarion of the dynamin-related protein OPA1 isoforms in mitochondria
    • Satoh, M., Hamamoto, T., Seo, N., Kagawa, Y., and Endo, H. (2003). Differential sublocalizarion of the dynamin-related protein OPA1 isoforms in mitochondria. Biochem. Biophys. Res. Commun. 300, 482-493.
    • (2003) Biochem. Biophys. Res. Commun , vol.300 , pp. 482-493
    • Satoh, M.1    Hamamoto, T.2    Seo, N.3    Kagawa, Y.4    Endo, H.5
  • 39
    • 0043095416 scopus 로고    scopus 로고
    • Cells lacking Pcp1p/Ugo2p, a rhomboid-like protease required for Mgm1p processing, lose mtDNA and mitochondrial structure in a Dnm1p-dependent manner, but remain competent for mitochondrial fusion
    • Sesaki, H., Southard, S. M., Hobbs, A. E., and Jensen, R. E. (2003). Cells lacking Pcp1p/Ugo2p, a rhomboid-like protease required for Mgm1p processing, lose mtDNA and mitochondrial structure in a Dnm1p-dependent manner, but remain competent for mitochondrial fusion. Biochem. Biophys Res. Commun. 308, 276-283.
    • (2003) Biochem. Biophys Res. Commun , vol.308 , pp. 276-283
    • Sesaki, H.1    Southard, S.M.2    Hobbs, A.E.3    Jensen, R.E.4
  • 40
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski, R. S., and Hieter, P. (1989). A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Generics 122, 19-27.
    • (1989) Generics , vol.122 , pp. 19-27
    • Sikorski, R.S.1    Hieter, P.2
  • 41
    • 33846490396 scopus 로고    scopus 로고
    • m-AAA protease-driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondria
    • Tatsuta, T., Augustin, S., Nolden, M., Friedrichs, B., and Langer, T. (2007). m-AAA protease-driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondria. EMBO J. 26, 325-335.
    • (2007) EMBO J , vol.26 , pp. 325-335
    • Tatsuta, T.1    Augustin, S.2    Nolden, M.3    Friedrichs, B.4    Langer, T.5
  • 42
    • 23044506102 scopus 로고    scopus 로고
    • Synaptic mitochondria are critical for mobilization of reserve pool vesicles at Drosophila neuromuscular junctions
    • Verstreken, P., Ly, C. V., Venken, K. J., Koh, T. W., Zhou, Y., and Bellen, H. J. (2005). Synaptic mitochondria are critical for mobilization of reserve pool vesicles at Drosophila neuromuscular junctions. Neuron 47, 365-378.
    • (2005) Neuron , vol.47 , pp. 365-378
    • Verstreken, P.1    Ly, C.V.2    Venken, K.J.3    Koh, T.W.4    Zhou, Y.5    Bellen, H.J.6
  • 43
    • 0033672549 scopus 로고    scopus 로고
    • Mitochondria-targeted green fluorescent proteins: Convenient tools for the study of organelle biogenesis in Saccharomyces cerevisiae
    • Westermann, B., and Neupert, W. (2000). Mitochondria-targeted green fluorescent proteins: convenient tools for the study of organelle biogenesis in Saccharomyces cerevisiae. Yeast 16, 1421-1427.
    • (2000) Yeast , vol.16 , pp. 1421-1427
    • Westermann, B.1    Neupert, W.2
  • 44
    • 33745012064 scopus 로고    scopus 로고
    • Evaluation of the association between OPA1 polymorphisms and primary open-angle glaucoma in Barbados families
    • Yao, W., Jiao, X., Hejtmancik, J. F., Leske, M. C., Hennis, A., and Nemesure, B. (2006). Evaluation of the association between OPA1 polymorphisms and primary open-angle glaucoma in Barbados families. Mol. Vis. 12, 649-654.
    • (2006) Mol. Vis , vol.12 , pp. 649-654
    • Yao, W.1    Jiao, X.2    Hejtmancik, J.F.3    Leske, M.C.4    Hennis, A.5    Nemesure, B.6
  • 45
    • 2442589922 scopus 로고    scopus 로고
    • Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A
    • Zuchner, S. et al. (2004). Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A. Nat. Genet. 36, 449-451.
    • (2004) Nat. Genet , vol.36 , pp. 449-451
    • Zuchner, S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.