메뉴 건너뛰기




Volumn 12, Issue 2, 2013, Pages 233-243

A uvs-5 strain is deficient for a mitofusin gene homologue, fzo1, involved in maintenance of long life span in Neurospora crassa

Author keywords

[No Author keywords available]

Indexed keywords

DROSOPHILA PROTEIN; FUNGAL PROTEIN; GUANOSINE TRIPHOSPHATASE; MEMBRANE PROTEIN; MFN2 PROTEIN, DROSOPHILA; MITOCHONDRIAL PROTEIN;

EID: 84873129773     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00226-12     Document Type: Article
Times cited : (12)

References (74)
  • 1
    • 0036596451 scopus 로고    scopus 로고
    • Genes, mitochondria and aging in filamentous fungi
    • Osiewacz HD. 2002. Genes, mitochondria and aging in filamentous fungi. Ageing Res. Rev. 1:425-442.
    • (2002) Ageing Res. Rev. , vol.1 , pp. 425-442
    • Osiewacz, H.D.1
  • 3
    • 0035723838 scopus 로고    scopus 로고
    • Overexpression of the alternative oxidase restores senescence and fertility in a long-lived respiration-deficient mutant of Podospora anserina
    • Lorin S, Dufour E, Boulay J, Begel O, Marsy S, Sainsard-Chanet A. 2001. Overexpression of the alternative oxidase restores senescence and fertility in a long-lived respiration-deficient mutant of Podospora anserina. Mol. Microbiol. 42:1259-1267.
    • (2001) Mol. Microbiol. , vol.42 , pp. 1259-1267
    • Lorin, S.1    Dufour, E.2    Boulay, J.3    Begel, O.4    Marsy, S.5    Sainsard-Chanet, A.6
  • 5
    • 39649101662 scopus 로고    scopus 로고
    • Senescence in fungi: The view from Neurospora
    • Maheshwari R, Navaraj A. 2008. Senescence in fungi: the view from Neurospora. FEMS Microbiol. Lett. 280:135-143.
    • (2008) FEMS Microbiol. Lett. , vol.280 , pp. 135-143
    • Maheshwari, R.1    Navaraj, A.2
  • 6
    • 76549237819 scopus 로고
    • A gene that causes natural death in Neurospora crassa
    • Sheng TC. 1951. A gene that causes natural death in Neurospora crassa. Genetics 36:199-212.
    • (1951) Genetics , vol.36 , pp. 199-212
    • Sheng, T.C.1
  • 7
    • 0033861965 scopus 로고    scopus 로고
    • Senescent: A new Neurospora crassa nuclear gene mutant derived from nature exhibits mitochondrial abnormalities and a "death" phenotype
    • Navaraj A, Pandit A, Maheshwari R. 2000. senescent: a new Neurospora crassa nuclear gene mutant derived from nature exhibits mitochondrial abnormalities and a "death" phenotype. Fungal Genet. Biol. 29:165-173.
    • (2000) Fungal Genet. Biol. , vol.29 , pp. 165-173
    • Navaraj, A.1    Pandit, A.2    Maheshwari, R.3
  • 8
    • 0027445385 scopus 로고
    • Hyperactive recombination in the mitochondrial DNA of the natural death nuclear mutant of Neurospora crassa
    • Bertrand H, Wu Q, Seidel-Rogol BL. 1993. Hyperactive recombination in the mitochondrial DNA of the natural death nuclear mutant of Neurospora crassa. Mol. Cell. Biol. 13:6778-6788.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 6778-6788
    • Bertrand, H.1    Wu, Q.2    Seidel-Rogol, B.L.3
  • 9
    • 12744265226 scopus 로고    scopus 로고
    • Intramolecular recombination and deletions in mitochondrial DNA of senescent, a nuclear-gene mutant of Neurospora crassa exhibiting "death" phenotype
    • D'Souza AD, Bertrand H, Maheshwari R. 2005. Intramolecular recombination and deletions in mitochondrial DNA of senescent, a nuclear-gene mutant of Neurospora crassa exhibiting "death" phenotype. Fungal Genet. Biol. 42:178-190.
    • (2005) Fungal Genet. Biol. , vol.42 , pp. 178-190
    • D'Souza, A.D.1    Bertrand, H.2    Maheshwari, R.3
  • 10
    • 0024469816 scopus 로고
    • Unstable mitochondrial DNA in natural-death nuclear mutants of Neurospora crassa
    • Seidel-Rogol BL, King J, Bertrand H. 1989. Unstable mitochondrial DNA in natural-death nuclear mutants of Neurospora crassa. Mol. Cell. Biol. 9:4259-4264.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 4259-4264
    • Seidel-Rogol, B.L.1    King, J.2    Bertrand, H.3
  • 11
    • 32444451021 scopus 로고    scopus 로고
    • Biogenesis and replication of small plasmid-like derivatives of the mitochondrial DNA in Neurospora crassa
    • Hausner G, Nummy KA, Stoltzner S, Hubert SK, Bertrand H. 2006. Biogenesis and replication of small plasmid-like derivatives of the mitochondrial DNA in Neurospora crassa. Fungal Genet. Biol. 43:75-89.
    • (2006) Fungal Genet. Biol. , vol.43 , pp. 75-89
    • Hausner, G.1    Nummy, K.A.2    Stoltzner, S.3    Hubert, S.K.4    Bertrand, H.5
  • 12
    • 78649639020 scopus 로고    scopus 로고
    • Deletion of a novel F-box protein, MUS-10, in Neurospora crassa leads to altered mitochondrial morphology, instability of mtDNA and senescence
    • Kato A, Kurashima K, Chae M, Sawada S, Hatakeyama S, Tanaka S, Inoue H. 2010. Deletion of a novel F-box protein, MUS-10, in Neurospora crassa leads to altered mitochondrial morphology, instability of mtDNA and senescence. Genetics 185:1257-1269.
    • (2010) Genetics , vol.185 , pp. 1257-1269
    • Kato, A.1    Kurashima, K.2    Chae, M.3    Sawada, S.4    Hatakeyama, S.5    Tanaka, S.6    Inoue, H.7
  • 13
    • 32444443444 scopus 로고
    • Use of helper strain in Neurospora crassa to maintain stocks of uvs-4 and uvs-5, which deteriorate unless sheltered in heterokaryons
    • Perkins DD. 1993. Use of helper strain in Neurospora crassa to maintain stocks of uvs-4 and uvs-5, which deteriorate unless sheltered in heterokaryons. Fungal Genet. Newsl. 40:66.
    • (1993) Fungal Genet. Newsl. , vol.40 , pp. 66
    • Perkins, D.D.1
  • 14
    • 0014927520 scopus 로고
    • Ultraviolet-sensitive mutants of Neurospora. I. Genetic basis and effect on recombination
    • Schroeder AL. 1970. Ultraviolet-sensitive mutants of Neurospora. I. Genetic basis and effect on recombination. Mol. Gen. Genet. 107:291-304.
    • (1970) Mol. Gen. Genet. , vol.107 , pp. 291-304
    • Schroeder, A.L.1
  • 15
    • 0019249216 scopus 로고
    • Isolation and genetic analysis of MMSsensitive mus mutants of Neurospora
    • Käfer E, Perlmutter E. 1980. Isolation and genetic analysis of MMSsensitive mus mutants of Neurospora. Can. J. Genet. Cytol. 22:535-552.
    • (1980) Can. J. Genet. Cytol. , vol.22 , pp. 535-552
    • Käfer, E.1    Perlmutter, E.2
  • 16
    • 56349103980 scopus 로고    scopus 로고
    • The molecular mechanism of mitochondrial fusion
    • Hoppins S, Nunnari J. 2009. The molecular mechanism of mitochondrial fusion. Biochim. Biophys. Acta 1793:20-26.
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 20-26
    • Hoppins, S.1    Nunnari, J.2
  • 17
    • 27544466847 scopus 로고    scopus 로고
    • Mitochondrial morphology and dynamics in yeast and multicellular eukaryotes
    • Okamoto K, Shaw JM. 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
  • 18
    • 0142058391 scopus 로고    scopus 로고
    • Two mitofusin proteins, mammalian homologues of FZO, with distinct functions are both required for mitochondrial fusion
    • Eura Y, Ishihara N, Yokota S, Mihara K. 2003. Two mitofusin proteins, mammalian homologues of FZO, with distinct functions are both required for mitochondrial fusion. J. Biochem. 134:333-344.
    • (2003) J. Biochem. , vol.134 , pp. 333-344
    • Eura, Y.1    Ishihara, N.2    Yokota, S.3    Mihara, K.4
  • 20
    • 0032493625 scopus 로고    scopus 로고
    • Fzo1p is a mitochondrial outer membrane protein essential for the biogenesis of functional mitochondria in Saccharomyces cerevisiae
    • Rapaport D, Brunner M, Neupert W, Westermann B. 1998. Fzo1p is a mitochondrial outer membrane protein essential for the biogenesis of functional mitochondria in Saccharomyces cerevisiae. J. Biol. Chem. 273: 20150-20155.
    • (1998) J. Biol. Chem. , vol.273 , pp. 20150-20155
    • Rapaport, D.1    Brunner, M.2    Neupert, W.3    Westermann, B.4
  • 23
    • 0026544936 scopus 로고
    • Mitochondrial DNA maintenance in yeast requires a protein containing a region related to the GTP-binding domain of dynamin
    • Jones BA, Fangman WL. 1992. Mitochondrial DNA maintenance in yeast requires a protein containing a region related to the GTP-binding domain of dynamin. Genes Dev. 6:380-389.
    • (1992) Genes Dev. , vol.6 , pp. 380-389
    • Jones, B.A.1    Fangman, W.L.2
  • 28
    • 0036314996 scopus 로고    scopus 로고
    • Mitochondrial dynamics in filamentous fungi
    • Westermann B, Prokisch H. 2002. Mitochondrial dynamics in filamentous fungi. Fungal Genet. Biol. 36:91-97.
    • (2002) Fungal Genet. Biol. , vol.36 , pp. 91-97
    • Westermann, B.1    Prokisch, H.2
  • 30
    • 48949119275 scopus 로고    scopus 로고
    • Regulation of mitochondrial dynamics-characterization of fusion and fission genes in the ascomycete Podospora anserina
    • Scheckhuber CQ, Rödel E, Wüstehube J. 2008. Regulation of mitochondrial dynamics-characterization of fusion and fission genes in the ascomycete Podospora anserina. Biotechnol. J. 3:781-790.
    • (2008) Biotechnol. J. , vol.3 , pp. 781-790
    • Scheckhuber, C.Q.1    Rödel, E.2    Wüstehube, J.3
  • 32
    • 80052879466 scopus 로고    scopus 로고
    • Unopposed mitochondrial fission leads to severe lifespan shortening
    • Scheckhuber CQ, Wanger RA, Mignat CA, Osiewacz HD. 2011. Unopposed mitochondrial fission leads to severe lifespan shortening. Cell Cycle 10:3105-3110.
    • (2011) Cell Cycle , vol.10 , pp. 3105-3110
    • Scheckhuber, C.Q.1    Wanger, R.A.2    Mignat, C.A.3    Osiewacz, H.D.4
  • 33
    • 79960339919 scopus 로고    scopus 로고
    • The dynamin-related protein DRP-1 and the insulin signaling pathway cooperate to modulate Caenorhabditis elegans longevity
    • Yang CC, Chen D, Lee SS, Walter L. 2011. The dynamin-related protein DRP-1 and the insulin signaling pathway cooperate to modulate Caenorhabditis elegans longevity. Aging Cell 10:724-728.
    • (2011) Aging Cell , vol.10 , pp. 724-728
    • Yang, C.C.1    Chen, D.2    Lee, S.S.3    Walter, L.4
  • 34
    • 0035146891 scopus 로고    scopus 로고
    • Mitochondrial filaments and clusters as intracellular power-transmitting cables
    • Skulachev VP. 2001. Mitochondrial filaments and clusters as intracellular power-transmitting cables. Trends Biochem. Sci. 26:23-29.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 23-29
    • Skulachev, V.P.1
  • 35
    • 0024439298 scopus 로고
    • Isolation and characterization of a laccasederepressed mutant of Neurospora crassa
    • Tamaru H, Inoue H. 1989. Isolation and characterization of a laccasederepressed mutant of Neurospora crassa. J. Bacteriol. 171:6288-6293.
    • (1989) J. Bacteriol. , vol.171 , pp. 6288-6293
    • Tamaru, H.1    Inoue, H.2
  • 36
    • 4344691833 scopus 로고    scopus 로고
    • Highly efficient gene replacements in Neurospora strains deficient for nonhomologous endjoining
    • Ninomiya Y, Suzuki K, Ishii C, Inoue H. 2004. Highly efficient gene replacements in Neurospora strains deficient for nonhomologous endjoining. Proc. Natl. Acad. Sci. U. S. A. 101:12248-12253.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 12248-12253
    • Ninomiya, Y.1    Suzuki, K.2    Ishii, C.3    Inoue, H.4
  • 37
    • 77956995235 scopus 로고
    • Genetic and microbiological research techniques for Neurospora crassa
    • Davis RH, de Serres FJ. 1970. Genetic and microbiological research techniques for Neurospora crassa. Methods Enzymol. 17A:79-143.
    • (1970) Methods Enzymol. , vol.17 A , pp. 79-143
    • Davis, R.H.1    de Serres, F.J.2
  • 38
    • 0002705742 scopus 로고
    • A series of six compact fungal transformation vectors containing polylinkers with multiple unique restriction sites
    • Pall ML, Brunelli JP. 1993. A series of six compact fungal transformation vectors containing polylinkers with multiple unique restriction sites. Fungal Genet. Newsl. 40:58.
    • (1993) Fungal Genet. Newsl. , vol.40 , pp. 58
    • Pall, M.L.1    Brunelli, J.P.2
  • 39
    • 0001427764 scopus 로고
    • The tube method of measuring the growth rate of Neurospora
    • Ryan FJ, Beadle GW, Tatum EL. 1943. The tube method of measuring the growth rate of Neurospora. Am. J. Bot. 30:784-799.
    • (1943) Am. J. Bot. , vol.30 , pp. 784-799
    • Ryan, F.J.1    Beadle, G.W.2    Tatum, E.L.3
  • 41
    • 4444362481 scopus 로고    scopus 로고
    • GFP as a tool to analyze the organization, dynamics and function of nuclei and microtubules in Neurospora crassa
    • Freitag M, Hickey PC, Raju NB, Selker EU, Read ND. 2004. GFP as a tool to analyze the organization, dynamics and function of nuclei and microtubules in Neurospora crassa. Fungal Genet. Biol. 41:897-910.
    • (2004) Fungal Genet. Biol. , vol.41 , pp. 897-910
    • Freitag, M.1    Hickey, P.C.2    Raju, N.B.3    Selker, E.U.4    Read, N.D.5
  • 42
    • 34548350534 scopus 로고    scopus 로고
    • Neurospora crassa RAD5 homologue, mus-41, inactivation results in higher sensitivity to mutagens but has little effect on PCNA-ubiquitylation in response to UVirradiation
    • Kawabata T, Kato A, Suzuki K, Inoue H. 2007. Neurospora crassa RAD5 homologue, mus-41, inactivation results in higher sensitivity to mutagens but has little effect on PCNA-ubiquitylation in response to UVirradiation. Curr. Genet. 52:125-135.
    • (2007) Curr. Genet. , vol.52 , pp. 125-135
    • Kawabata, T.1    Kato, A.2    Suzuki, K.3    Inoue, H.4
  • 43
    • 39749090575 scopus 로고    scopus 로고
    • Genetic and molecular analysis of the temperature-sensitive mutant un-17 carrying a mutation in the gene encoding poly(A)-polymerase in Neurospora crassa
    • Tanaka S, Takayanagi N, Murasawa K, Ishii C, Inoue H. 2007. Genetic and molecular analysis of the temperature-sensitive mutant un-17 carrying a mutation in the gene encoding poly(A)-polymerase in Neurospora crassa. Genes Genet. Syst. 82:447-454.
    • (2007) Genes Genet. Syst. , vol.82 , pp. 447-454
    • Tanaka, S.1    Takayanagi, N.2    Murasawa, K.3    Ishii, C.4    Inoue, H.5
  • 44
    • 0018817764 scopus 로고
    • Mutagenesis at the ad-3A and ad-3B loci in haploid UV-sensitive strains of Neurospora crassa. I. Development of isogenic strains and spontaneous mutability
    • de Serres FJ, Inoue H, Schupbach ME. 1980. Mutagenesis at the ad-3A and ad-3B loci in haploid UV-sensitive strains of Neurospora crassa. I. Development of isogenic strains and spontaneous mutability. Mutat. Res. 71:53-65.
    • (1980) Mutat. Res. , vol.71 , pp. 53-65
    • de Serres, F.J.1    Inoue, H.2    Schupbach, M.E.3
  • 45
    • 0019378149 scopus 로고
    • Mutagenesis at the ad-3A and ad-3B loci haploid UV-sensitive strains of Neurospora crassa. III. Comparison of dose-response curves for inactivation and mutation induced by gammarays
    • Schüpbach ME, de Serres FJ. 1981. Mutagenesis at the ad-3A and ad-3B loci haploid UV-sensitive strains of Neurospora crassa. III. Comparison of dose-response curves for inactivation and mutation induced by gammarays. Mutat. Res. 81:49-58.
    • (1981) Mutat. Res. , vol.81 , pp. 49-58
    • Schüpbach, M.E.1    de Serres, F.J.2
  • 46
    • 0019364537 scopus 로고
    • Mutagen sensitivities and mutator effects of MMS-sensitive mutants in Neurospora
    • Käfer E. 1981. Mutagen sensitivities and mutator effects of MMS-sensitive mutants in Neurospora. Mutat. Res. 80:43-64.
    • (1981) Mutat. Res. , vol.80 , pp. 43-64
    • Käfer, E.1
  • 47
    • 0019526198 scopus 로고
    • The isolation of mms-and histidinesensitive mutants in Neurospora crassa
    • Delange AM, Mishra NC. 1981. The isolation of mms-and histidinesensitive mutants in Neurospora crassa. Genetics 97:247-259.
    • (1981) Genetics , vol.97 , pp. 247-259
    • Delange, A.M.1    Mishra, N.C.2
  • 48
  • 49
    • 84873161157 scopus 로고
    • Linkage data for group III markers in Neurospora
    • Perkins DD, Ishitani C. 1959. Linkage data for group III markers in Neurospora. Genetics 44:1209-1213.
    • (1959) Genetics , vol.44 , pp. 1209-1213
    • Perkins, D.D.1    Ishitani, C.2
  • 50
    • 0014632718 scopus 로고
    • New markers and map sequences in Neurospora crassa, with a description of mapping by duplication coverage, and of multiple translocation stocks for testing linkage
    • Perkins DD, Newmeyer D, Taylor CW, Bennett DC. 1969. New markers and map sequences in Neurospora crassa, with a description of mapping by duplication coverage, and of multiple translocation stocks for testing linkage. Genetica 40:247-278.
    • (1969) Genetica , vol.40 , pp. 247-278
    • Perkins, D.D.1    Newmeyer, D.2    Taylor, C.W.3    Bennett, D.C.4
  • 51
    • 0037455575 scopus 로고    scopus 로고
    • Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development
    • Chen H, Detmer SA, Ewald AJ, Griffin EE, Fraser SE, Chan DC. 2003. Mitofusins Mfn1 and Mfn2 coordinately regulate mitochondrial fusion and are essential for embryonic development. J. Cell Biol. 160:189-200.
    • (2003) J. Cell Biol. , vol.160 , pp. 189-200
    • Chen, H.1    Detmer, S.A.2    Ewald, A.J.3    Griffin, E.E.4    Fraser, S.E.5    Chan, D.C.6
  • 52
    • 55749090654 scopus 로고    scopus 로고
    • The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila
    • Deng H, Dodson MW, Huang H, Guo M. 2008. The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila. Proc. Natl. Acad. Sci. U. S. A. 105:14503-14508.
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 14503-14508
    • Deng, H.1    Dodson, M.W.2    Huang, H.3    Guo, M.4
  • 53
    • 0037089084 scopus 로고    scopus 로고
    • Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo
    • Rojo M, Legros F, Chateau D, Lombes A. 2002. Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo. J. Cell Sci. 115:1663-1674.
    • (2002) J. Cell Sci. , vol.115 , pp. 1663-1674
    • Rojo, M.1    Legros, F.2    Chateau, D.3    Lombes, A.4
  • 54
    • 0035057837 scopus 로고    scopus 로고
    • Control of mitochondrial morphology by a human mitofusin
    • Santel A, Fuller MT. 2001. Control of mitochondrial morphology by a human mitofusin. J. Cell Sci. 114:867-874.
    • (2001) J. Cell Sci. , vol.114 , pp. 867-874
    • Santel, A.1    Fuller, M.T.2
  • 55
  • 56
    • 0035911963 scopus 로고    scopus 로고
    • UGO1 encodes an outer membrane protein required for mitochondrial fusion
    • Sesaki H, Jensen RE. 2001. UGO1 encodes an outer membrane protein required for mitochondrial fusion. J. Cell Biol. 152:1123-1134.
    • (2001) J. Cell Biol. , vol.152 , pp. 1123-1134
    • Sesaki, H.1    Jensen, R.E.2
  • 57
    • 77957358299 scopus 로고    scopus 로고
    • Mitochondrial dynamics in cell death and neurodegeneration
    • Cho DH, 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
  • 58
    • 38549101188 scopus 로고    scopus 로고
    • Quality control of mitochondria: Protection against neurodegeneration and ageing
    • Tatsuta T, Langer T. 2008. Quality control of mitochondria: protection against neurodegeneration and ageing. EMBO J. 27:306-314.
    • (2008) EMBO J. , vol.27 , pp. 306-314
    • Tatsuta, T.1    Langer, T.2
  • 59
    • 78649413837 scopus 로고    scopus 로고
    • Mitochondrial fusion and fission in cell life and death
    • Westermann B. 2010. Mitochondrial fusion and fission in cell life and death. Nat. Rev. Mol. Cell Biol. 11:872-884.
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 872-884
    • Westermann, B.1
  • 60
    • 84862884156 scopus 로고    scopus 로고
    • Mitochondrial quality control: An integrated network of pathways
    • Fischer F, Hamann A, Osiewacz HD. 2012. Mitochondrial quality control: an integrated network of pathways. Trends Biochem. Sci. 37:284-292.
    • (2012) Trends Biochem. Sci. , vol.37 , pp. 284-292
    • Fischer, F.1    Hamann, A.2    Osiewacz, H.D.3
  • 61
    • 79955664111 scopus 로고    scopus 로고
    • Mitochondrial protein quality control during biogenesis and aging
    • Baker BM, Haynes CM. 2011. Mitochondrial protein quality control during biogenesis and aging. Trends Biochem. Sci. 36:254-261.
    • (2011) Trends Biochem. Sci. , vol.36 , pp. 254-261
    • Baker, B.M.1    Haynes, C.M.2
  • 62
    • 0031440879 scopus 로고    scopus 로고
    • Developmentally regulated mitochondrial fusion mediated by a conserved, novel, predicted GTPase
    • Hales KG, Fuller MT. 1997. Developmentally regulated mitochondrial fusion mediated by a conserved, novel, predicted GTPase. Cell 90:121-129.
    • (1997) Cell , vol.90 , pp. 121-129
    • Hales, K.G.1    Fuller, M.T.2
  • 63
    • 48749116067 scopus 로고    scopus 로고
    • Ubiquitin-proteasome-dependent degradation of a mitofusin, a critical regulator of mitochondrial fusion
    • Cohen MM, Leboucher GP, Livnat-Levanon N, Glickman MH, Weissman AM. 2008. Ubiquitin-proteasome-dependent degradation of a mitofusin, a critical regulator of mitochondrial fusion. Mol. Biol. Cell 19:2457-2464.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 2457-2464
    • Cohen, M.M.1    Leboucher, G.P.2    Livnat-Levanon, N.3    Glickman, M.H.4    Weissman, A.M.5
  • 64
    • 0038037754 scopus 로고    scopus 로고
    • Mdm30 is an F-box protein required for maintenance of fusion-competent mitochondria in yeast
    • Fritz S, Weinbach N, Westermann B. 2003. Mdm30 is an F-box protein required for maintenance of fusion-competent mitochondria in yeast. Mol. Biol. Cell 14:2303-2313.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 2303-2313
    • Fritz, S.1    Weinbach, N.2    Westermann, B.3
  • 67
    • 33748327051 scopus 로고    scopus 로고
    • Nonredundant roles of mitochondria-associated F-box proteins Mfb1 and Mdm30 in maintenance of mitochondrial morphology in yeast
    • Durr M, Escobar-Henriques M, Merz S, Geimer S, Langer T, Westermann B. 2006. Nonredundant roles of mitochondria-associated F-box proteins Mfb1 and Mdm30 in maintenance of mitochondrial morphology in yeast. Mol. Biol. Cell 17:3745-3755.
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3745-3755
    • Durr, M.1    Escobar-Henriques, M.2    Merz, S.3    Geimer, S.4    Langer, T.5    Westermann, B.6
  • 69
    • 78649463381 scopus 로고    scopus 로고
    • Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkindependent manner upon induction of mitophagy
    • Gegg ME, Cooper JM, Chau KY, Rojo M, Schapira AH, Taanman JW. 2010. Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkindependent manner upon induction of mitophagy. Hum. Mol. Genet. 19: 4861-4870.
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 4861-4870
    • Gegg, M.E.1    Cooper, J.M.2    Chau, K.Y.3    Rojo, M.4    Schapira, A.H.5    Taanman, J.W.6
  • 70
    • 77955844260 scopus 로고    scopus 로고
    • The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/parkin pathway
    • doi:10.1371/journal.pone.0010054
    • Poole AC, Thomas RE, Yu S, Vincow ES, Pallanck L. 2010. The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/parkin pathway. PLoS One 5:e10054. doi:10.1371/journal.pone.0010054.
    • (2010) PLoS One , vol.5
    • Poole, A.C.1    Thomas, R.E.2    Yu, S.3    Vincow, E.S.4    Pallanck, L.5
  • 72
    • 0035957433 scopus 로고    scopus 로고
    • A large-scale overexpression screen in Saccharomyces cerevisiae identifies previously uncharacterized cell cycle genes
    • Stevenson LF, Kennedy BK, Harlow E. 2001. A large-scale overexpression screen in Saccharomyces cerevisiae identifies previously uncharacterized cell cycle genes. Proc. Natl. Acad. Sci. U. S. A. 98:3946-3951.
    • (2001) Proc. Natl. Acad. Sci. U. S. A. , vol.98 , pp. 3946-3951
    • Stevenson, L.F.1    Kennedy, B.K.2    Harlow, E.3
  • 73
    • 84859760175 scopus 로고    scopus 로고
    • Mitochondrial dynamics: Functional link with apoptosis
    • doi:10.1155/2012/821676
    • Otera H, Mihara K. 2012. Mitochondrial dynamics: functional link with apoptosis. Int. J. Cell Biol. 2012:821676. doi:10.1155/2012/821676.
    • (2012) Int. J. Cell Biol. , vol.2012 , pp. 821676
    • Otera, H.1    Mihara, K.2
  • 74
    • 84856244072 scopus 로고    scopus 로고
    • Mitophagy plays an essential role in reducing mitochondrial production of reactive oxygen species and mutation of mitochondrial DNA by maintaining mitochondrial quantity and quality in yeast
    • Kurihara Y, Kanki T, Aoki Y, Hirota Y, Saigusa T, Uchiumi T, Kang D. 2012. Mitophagy plays an essential role in reducing mitochondrial production of reactive oxygen species and mutation of mitochondrial DNA by maintaining mitochondrial quantity and quality in yeast. J. Biol. Chem. 287:3265-3272.
    • (2012) J. Biol. Chem. , vol.287 , pp. 3265-3272
    • Kurihara, Y.1    Kanki, T.2    Aoki, Y.3    Hirota, Y.4    Saigusa, T.5    Uchiumi, T.6    Kang, D.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.