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Volumn 1797, Issue 8, 2010, Pages 1378-1388

The human mitochondrial replication fork in health and disease

Author keywords

DNA replication; Mitochondria; Mitochondrial disease; MtDNA; POLRMT; Twinkle

Indexed keywords

DNA DIRECTED DNA POLYMERASE GAMMA; DOUBLE STRANDED DNA; GENE PRODUCT; MITOCHONDRIAL DNA; MITOCHONDRIAL RNA; PROTEIN TWINKLE; RNA POLYMERASE; SINGLE STRANDED DNA BINDING PROTEIN; UNCLASSIFIED DRUG;

EID: 77953811054     PISSN: 00052728     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbabio.2010.04.015     Document Type: Review
Times cited : (89)

References (194)
  • 1
    • 78651128209 scopus 로고
    • Intramitochondrial fibers with DNA characteristics. I. Fixation and electron staining reactions
    • Nass M.M., Nass S. Intramitochondrial fibers with DNA characteristics. I. Fixation and electron staining reactions. J. Cell. Biol. 1963, 19:593-611.
    • (1963) J. Cell. Biol. , vol.19 , pp. 593-611
    • Nass, M.M.1    Nass, S.2
  • 2
    • 0019423856 scopus 로고
    • Sequence and organization of the human mitochondrial genome
    • Anderson S., et al. Sequence and organization of the human mitochondrial genome. Nature 1981, 290(5806):457-465.
    • (1981) Nature , vol.290 , Issue.5806 , pp. 457-465
    • Anderson, S.1
  • 3
    • 0014984183 scopus 로고
    • The folded genome of Escherichia coli isolated in a protein-DNA-RNA complex
    • Stonington O.G., Pettijohn D.E. The folded genome of Escherichia coli isolated in a protein-DNA-RNA complex. Proc. Natl Acad. Sci. USA 1971, 68(1):6-9.
    • (1971) Proc. Natl Acad. Sci. USA , vol.68 , Issue.1 , pp. 6-9
    • Stonington, O.G.1    Pettijohn, D.E.2
  • 4
    • 0034938364 scopus 로고    scopus 로고
    • Human mitochondrial DNA deletions associated with mutations in the gene encoding Twinkle, a phage T7 gene 4-like protein localized in mitochondria
    • Spelbrink J.N., et al. Human mitochondrial DNA deletions associated with mutations in the gene encoding Twinkle, a phage T7 gene 4-like protein localized in mitochondria. Nat. Genet. 2001, 28(3):223-231.
    • (2001) Nat. Genet. , vol.28 , Issue.3 , pp. 223-231
    • Spelbrink, J.N.1
  • 5
    • 77950573964 scopus 로고    scopus 로고
    • Functional organization of mammalian mitochondrial DNA in nucleoids: history, recent developments, and future challenges
    • Spelbrink J.N. Functional organization of mammalian mitochondrial DNA in nucleoids: history, recent developments, and future challenges. IUBMB Life 2010, 62(1):19-32.
    • (2010) IUBMB Life , vol.62 , Issue.1 , pp. 19-32
    • Spelbrink, J.N.1
  • 6
    • 3242705680 scopus 로고    scopus 로고
    • The functional organization of mitochondrial genomes in human cells
    • Iborra F.J., Kimura H., Cook P.R. The functional organization of mitochondrial genomes in human cells. BMC Biol. 2004, 2:9.
    • (2004) BMC Biol. , vol.2 , pp. 9
    • Iborra, F.J.1    Kimura, H.2    Cook, P.R.3
  • 7
    • 0026640728 scopus 로고
    • DNA wrapping and bending by a mitochondrial high mobility group-like transcriptional activator protein
    • Fisher R.P., et al. DNA wrapping and bending by a mitochondrial high mobility group-like transcriptional activator protein. J. Biol. Chem. 1992, 267(5):3358-3367.
    • (1992) J. Biol. Chem. , vol.267 , Issue.5 , pp. 3358-3367
    • Fisher, R.P.1
  • 8
    • 0038709292 scopus 로고    scopus 로고
    • Composition and dynamics of human mitochondrial nucleoids
    • Garrido N., et al. Composition and dynamics of human mitochondrial nucleoids. Mol. Biol. Cell 2003, 14(4):1583-1596.
    • (2003) Mol. Biol. Cell , vol.14 , Issue.4 , pp. 1583-1596
    • Garrido, N.1
  • 9
    • 34548495323 scopus 로고    scopus 로고
    • The mitochondrial transcription factor TFAM coordinates the assembly of multiple DNA molecules into nucleoid-like structures
    • Kaufman B.A., et al. The mitochondrial transcription factor TFAM coordinates the assembly of multiple DNA molecules into nucleoid-like structures. Mol. Biol. Cell 2007, 18(9):3225-3236.
    • (2007) Mol. Biol. Cell , vol.18 , Issue.9 , pp. 3225-3236
    • Kaufman, B.A.1
  • 10
    • 1542375269 scopus 로고    scopus 로고
    • Mechanism of DNA compaction by yeast mitochondrial protein Abf2p
    • Friddle R.W., et al. Mechanism of DNA compaction by yeast mitochondrial protein Abf2p. Biophys. J. 2004, 86(3):1632-1639.
    • (2004) Biophys. J. , vol.86 , Issue.3 , pp. 1632-1639
    • Friddle, R.W.1
  • 11
    • 0141642111 scopus 로고    scopus 로고
    • Packaging of single DNA molecules by the yeast mitochondrial protein Abf2p
    • Brewer L.R., et al. Packaging of single DNA molecules by the yeast mitochondrial protein Abf2p. Biophys. J. 2003, 85(4):2519-2524.
    • (2003) Biophys. J. , vol.85 , Issue.4 , pp. 2519-2524
    • Brewer, L.R.1
  • 12
    • 2442431673 scopus 로고    scopus 로고
    • Mitochondrial transcription factor A regulates mtDNA copy number in mammals
    • Ekstrand M.I., et al. Mitochondrial transcription factor A regulates mtDNA copy number in mammals. Hum. Mol. Genet. 2004, 13(9):935-944.
    • (2004) Hum. Mol. Genet. , vol.13 , Issue.9 , pp. 935-944
    • Ekstrand, M.I.1
  • 13
    • 33845629364 scopus 로고    scopus 로고
    • Alterations to the expression level of mitochondrial transcription factor A, TFAM, modify the mode of mitochondrial DNA replication in cultured human cells
    • Pohjoismaki J.L., et al. Alterations to the expression level of mitochondrial transcription factor A, TFAM, modify the mode of mitochondrial DNA replication in cultured human cells. Nucleic Acids Res. 2006, 34(20):5815-5828.
    • (2006) Nucleic Acids Res. , vol.34 , Issue.20 , pp. 5815-5828
    • Pohjoismaki, J.L.1
  • 14
    • 33748746678 scopus 로고    scopus 로고
    • Human mitochondrial DNA nucleoids are linked to protein folding machinery and metabolic enzymes at the mitochondrial inner membrane
    • Wang Y., Bogenhagen D.F. Human mitochondrial DNA nucleoids are linked to protein folding machinery and metabolic enzymes at the mitochondrial inner membrane. J. Biol. Chem. 2006, 281(35):25791-25802.
    • (2006) J. Biol. Chem. , vol.281 , Issue.35 , pp. 25791-25802
    • Wang, Y.1    Bogenhagen, D.F.2
  • 15
    • 41249098355 scopus 로고    scopus 로고
    • The layered structure of human mitochondrial DNA nucleoids
    • Bogenhagen D.F., Rousseau D., Burke S. The layered structure of human mitochondrial DNA nucleoids. J. Biol. Chem. 2008, 283(6):3665-3675.
    • (2008) J. Biol. Chem. , vol.283 , Issue.6 , pp. 3665-3675
    • Bogenhagen, D.F.1    Rousseau, D.2    Burke, S.3
  • 16
    • 0029587469 scopus 로고
    • Molecular genetic aspects of human mitochondrial disorders
    • Larsson N.G., Clayton D.A. Molecular genetic aspects of human mitochondrial disorders. Annu. Rev. Genet. 1995, 29:151-178.
    • (1995) Annu. Rev. Genet. , vol.29 , pp. 151-178
    • Larsson, N.G.1    Clayton, D.A.2
  • 17
    • 31444454598 scopus 로고    scopus 로고
    • Bacteriophage origins of mitochondrial replication and transcription proteins
    • Shutt T.E., Gray M.W. Bacteriophage origins of mitochondrial replication and transcription proteins. Trends Genet. 2006, 22(2):90-95.
    • (2006) Trends Genet. , vol.22 , Issue.2 , pp. 90-95
    • Shutt, T.E.1    Gray, M.W.2
  • 18
    • 67650741773 scopus 로고    scopus 로고
    • Motors, switches, and contacts in the replisome
    • Hamdan S.M., Richardson C.C. Motors, switches, and contacts in the replisome. Annu. Rev. Biochem. 2009, 78:205-243.
    • (2009) Annu. Rev. Biochem. , vol.78 , pp. 205-243
    • Hamdan, S.M.1    Richardson, C.C.2
  • 20
    • 3242739284 scopus 로고    scopus 로고
    • Reconstitution of a minimal mtDNA replisome in vitro
    • Korhonen J.A., et al. Reconstitution of a minimal mtDNA replisome in vitro. EMBO J. 2004, 23(12):2423-2429.
    • (2004) EMBO J. , vol.23 , Issue.12 , pp. 2423-2429
    • Korhonen, J.A.1
  • 21
    • 49649107261 scopus 로고    scopus 로고
    • Human mitochondrial RNA polymerase primes lagging-strand DNA synthesis in vitro
    • Wanrooij S., et al. Human mitochondrial RNA polymerase primes lagging-strand DNA synthesis in vitro. Proc. Natl Acad. Sci. USA 2008, 105(32):11122-11127.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , Issue.32 , pp. 11122-11127
    • Wanrooij, S.1
  • 22
    • 0030587492 scopus 로고    scopus 로고
    • Cloning and characterization of the human mitochondrial DNA polymerase, DNA polymerase gamma
    • Ropp P.A., Copeland W.C. Cloning and characterization of the human mitochondrial DNA polymerase, DNA polymerase gamma. Genomics 1996, 36(3):449-458.
    • (1996) Genomics , vol.36 , Issue.3 , pp. 449-458
    • Ropp, P.A.1    Copeland, W.C.2
  • 23
    • 0026672705 scopus 로고
    • Purification and identification of subunit structure of the human mitochondrial DNA polymerase
    • Gray H., Wong T.W. Purification and identification of subunit structure of the human mitochondrial DNA polymerase. J. Biol. Chem. 1992, 267(9):5835-5841.
    • (1992) J. Biol. Chem. , vol.267 , Issue.9 , pp. 5835-5841
    • Gray, H.1    Wong, T.W.2
  • 24
    • 0027308839 scopus 로고
    • Cloning of human and rat cDNAs encoding the mitochondrial single-stranded DNA-binding protein (SSB)
    • Tiranti V., et al. Cloning of human and rat cDNAs encoding the mitochondrial single-stranded DNA-binding protein (SSB). Gene 1993, 126(2):219-225.
    • (1993) Gene , vol.126 , Issue.2 , pp. 219-225
    • Tiranti, V.1
  • 25
    • 0030943170 scopus 로고    scopus 로고
    • Identification of the gene encoding the human mitochondrial RNA polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence Tags database
    • Tiranti V., et al. Identification of the gene encoding the human mitochondrial RNA polymerase (h-mtRPOL) by cyberscreening of the Expressed Sequence Tags database. Hum. Mol. Genet. 1997, 6(4):615-625.
    • (1997) Hum. Mol. Genet. , vol.6 , Issue.4 , pp. 615-625
    • Tiranti, V.1
  • 26
    • 0023035980 scopus 로고
    • A nuclear mutant of Saccharomyces cerevisiae deficient in mitochondrial DNA replication and polymerase activity
    • Genga A., Bianchi L., Foury F. A nuclear mutant of Saccharomyces cerevisiae deficient in mitochondrial DNA replication and polymerase activity. J. Biol. Chem. 1986, 261(20):9328-9332.
    • (1986) J. Biol. Chem. , vol.261 , Issue.20 , pp. 9328-9332
    • Genga, A.1    Bianchi, L.2    Foury, F.3
  • 27
    • 0024306516 scopus 로고
    • Cloning and sequencing of the nuclear gene MIP1 encoding the catalytic subunit of the yeast mitochondrial DNA polymerase
    • Foury F. Cloning and sequencing of the nuclear gene MIP1 encoding the catalytic subunit of the yeast mitochondrial DNA polymerase. J. Biol. Chem. 1989, 264(34):20552-20560.
    • (1989) J. Biol. Chem. , vol.264 , Issue.34 , pp. 20552-20560
    • Foury, F.1
  • 28
    • 0031032128 scopus 로고    scopus 로고
    • Mitochondrial DNA polymerases from yeast to man: a new family of polymerases
    • Lecrenier N., Van Der Bruggen P., Foury F. Mitochondrial DNA polymerases from yeast to man: a new family of polymerases. Gene 1997, 185(1):147-152.
    • (1997) Gene , vol.185 , Issue.1 , pp. 147-152
    • Lecrenier, N.1    Van Der Bruggen, P.2    Foury, F.3
  • 29
    • 67349191588 scopus 로고    scopus 로고
    • DNA polymerase gamma and mitochondrial disease: understanding the consequence of POLG mutations
    • Chan S.S., Copeland W.C. DNA polymerase gamma and mitochondrial disease: understanding the consequence of POLG mutations. Biochim. Biophys. Acta 2009, 1787(5):312-319.
    • (2009) Biochim. Biophys. Acta , vol.1787 , Issue.5 , pp. 312-319
    • Chan, S.S.1    Copeland, W.C.2
  • 30
    • 33646859687 scopus 로고    scopus 로고
    • Mutant POLG2 disrupts DNA polymerase gamma subunits and causes progressive external ophthalmoplegia
    • Longley M.J., et al. Mutant POLG2 disrupts DNA polymerase gamma subunits and causes progressive external ophthalmoplegia. Am. J. Hum. Genet. 2006, 78(6):1026-1034.
    • (2006) Am. J. Hum. Genet. , vol.78 , Issue.6 , pp. 1026-1034
    • Longley, M.J.1
  • 31
    • 33644635644 scopus 로고    scopus 로고
    • DNA polymerase gamma in mitochondrial DNA replication and repair
    • Graziewicz M.A., Longley M.J., Copeland W.C. DNA polymerase gamma in mitochondrial DNA replication and repair. Chem. Rev. 2006, 106(2):383-405.
    • (2006) Chem. Rev. , vol.106 , Issue.2 , pp. 383-405
    • Graziewicz, M.A.1    Longley, M.J.2    Copeland, W.C.3
  • 32
    • 2342429459 scopus 로고    scopus 로고
    • DNA polymerase gamma, the mitochondrial replicase
    • Kaguni L.S. DNA polymerase gamma, the mitochondrial replicase. Annu. Rev. Biochem. 2004, 73:293-320.
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 293-320
    • Kaguni, L.S.1
  • 33
    • 70349807756 scopus 로고    scopus 로고
    • Structural insight into processive human mitochondrial DNA synthesis and disease-related polymerase mutations
    • Lee Y.S., Kennedy W.D., Yin Y.W. Structural insight into processive human mitochondrial DNA synthesis and disease-related polymerase mutations. Cell 2009, 139(2):312-324.
    • (2009) Cell , vol.139 , Issue.2 , pp. 312-324
    • Lee, Y.S.1    Kennedy, W.D.2    Yin, Y.W.3
  • 34
    • 33644855097 scopus 로고    scopus 로고
    • Functional human mitochondrial DNA polymerase gamma forms a heterotrimer
    • Yakubovskaya E., et al. Functional human mitochondrial DNA polymerase gamma forms a heterotrimer. J. Biol. Chem. 2006, 281(1):374-382.
    • (2006) J. Biol. Chem. , vol.281 , Issue.1 , pp. 374-382
    • Yakubovskaya, E.1
  • 35
    • 0035101674 scopus 로고    scopus 로고
    • Crystal structure and deletion analysis show that the accessory subunit of mammalian DNA polymerase gamma, Pol gamma B, functions as a homodimer
    • Carrodeguas J.A., et al. Crystal structure and deletion analysis show that the accessory subunit of mammalian DNA polymerase gamma, Pol gamma B, functions as a homodimer. Mol. Cell. 2001, 7(1):43-54.
    • (2001) Mol. Cell. , vol.7 , Issue.1 , pp. 43-54
    • Carrodeguas, J.A.1
  • 36
    • 0033621374 scopus 로고    scopus 로고
    • The mitochondrial p55 accessory subunit of human DNA polymerase gamma enhances DNA binding, promotes processive DNA synthesis, and confers N-ethylmaleimide resistance
    • Lim S.E., Longley M.J., Copeland W.C. The mitochondrial p55 accessory subunit of human DNA polymerase gamma enhances DNA binding, promotes processive DNA synthesis, and confers N-ethylmaleimide resistance. J. Biol. Chem. 1999, 274(53):38197-38203.
    • (1999) J. Biol. Chem. , vol.274 , Issue.53 , pp. 38197-38203
    • Lim, S.E.1    Longley, M.J.2    Copeland, W.C.3
  • 37
    • 74049134918 scopus 로고    scopus 로고
    • Each monomer of the dimeric accessory protein for human mitochondrial DNA polymerase has a distinct role in conferring processivity
    • Lee Y.S., et al. Each monomer of the dimeric accessory protein for human mitochondrial DNA polymerase has a distinct role in conferring processivity. J. Biol. Chem. 2010, 285(2):1490-1499.
    • (2010) J. Biol. Chem. , vol.285 , Issue.2 , pp. 1490-1499
    • Lee, Y.S.1
  • 38
    • 34948819776 scopus 로고    scopus 로고
    • The EM structure of human DNA polymerase gamma reveals a localized contact between the catalytic and accessory subunits
    • Yakubovskaya E., et al. The EM structure of human DNA polymerase gamma reveals a localized contact between the catalytic and accessory subunits. EMBO J. 2007, 26(19):4283-4291.
    • (2007) EMBO J. , vol.26 , Issue.19 , pp. 4283-4291
    • Yakubovskaya, E.1
  • 39
    • 0037147342 scopus 로고    scopus 로고
    • DNA binding properties of human pol gammaB
    • Carrodeguas J.A., Pinz K.G., Bogenhagen D.F. DNA binding properties of human pol gammaB. J. Biol. Chem. 2002, 277(51):50008-50014.
    • (2002) J. Biol. Chem. , vol.277 , Issue.51 , pp. 50008-50014
    • Carrodeguas, J.A.1    Pinz, K.G.2    Bogenhagen, D.F.3
  • 40
    • 33847349331 scopus 로고    scopus 로고
    • The accessory subunit B of DNA polymerase gamma is required for mitochondrial replisome function
    • Farge G., et al. The accessory subunit B of DNA polymerase gamma is required for mitochondrial replisome function. Nucleic Acids Res. 2007, 35(3):902-911.
    • (2007) Nucleic Acids Res. , vol.35 , Issue.3 , pp. 902-911
    • Farge, G.1
  • 41
    • 0031023811 scopus 로고    scopus 로고
    • Crystal structure of human mitochondrial single-stranded DNA binding protein at 2.4 A resolution
    • Yang C., et al. Crystal structure of human mitochondrial single-stranded DNA binding protein at 2.4 A resolution. Nat. Struct. Biol. 1997, 4(2):153-157.
    • (1997) Nat. Struct. Biol. , vol.4 , Issue.2 , pp. 153-157
    • Yang, C.1
  • 42
    • 0025866274 scopus 로고
    • A full-length cDNA encoding a mitochondrial DNA-specific single-stranded DNA binding protein from Xenopus laevis
    • Tiranti V., et al. A full-length cDNA encoding a mitochondrial DNA-specific single-stranded DNA binding protein from Xenopus laevis. Nucleic Acids Res. 1991, 19(15):4291.
    • (1991) Nucleic Acids Res. , vol.19 , Issue.15 , pp. 4291
    • Tiranti, V.1
  • 43
    • 0026784158 scopus 로고
    • A single-stranded DNA binding protein required for mitochondrial DNA replication in S. cerevisiae is homologous to E. coli SSB
    • Van Dyck E., et al. A single-stranded DNA binding protein required for mitochondrial DNA replication in S. cerevisiae is homologous to E. coli SSB. EMBO J. 1992, 11(9):3421-3430.
    • (1992) EMBO J. , vol.11 , Issue.9 , pp. 3421-3430
    • Van Dyck, E.1
  • 44
    • 0029154579 scopus 로고
    • Mitochondrial single-stranded DNA-binding protein from Drosophila embryos. Physical and biochemical characterization
    • Thommes P., et al. Mitochondrial single-stranded DNA-binding protein from Drosophila embryos. Physical and biochemical characterization. J. Biol. Chem. 1995, 270(36):21137-21143.
    • (1995) J. Biol. Chem. , vol.270 , Issue.36 , pp. 21137-21143
    • Thommes, P.1
  • 45
    • 0030961451 scopus 로고    scopus 로고
    • Tetramerization and single-stranded DNA binding properties of native and mutated forms of murine mitochondrial single-stranded DNA-binding proteins
    • Li K., Williams R.S. Tetramerization and single-stranded DNA binding properties of native and mutated forms of murine mitochondrial single-stranded DNA-binding proteins. J. Biol. Chem. 1997, 272(13):8686-8694.
    • (1997) J. Biol. Chem. , vol.272 , Issue.13 , pp. 8686-8694
    • Li, K.1    Williams, R.S.2
  • 46
    • 2342423632 scopus 로고    scopus 로고
    • Physiological and biochemical defects in functional interactions of mitochondrial DNA polymerase and DNA-binding mutants of single-stranded DNA-binding protein
    • Farr C.L., et al. Physiological and biochemical defects in functional interactions of mitochondrial DNA polymerase and DNA-binding mutants of single-stranded DNA-binding protein. J. Biol. Chem. 2004, 279(17):17047-17053.
    • (2004) J. Biol. Chem. , vol.279 , Issue.17 , pp. 17047-17053
    • Farr, C.L.1
  • 47
    • 0022374832 scopus 로고
    • Characterization of DNA-protein complexes from the mitochondria of Xenopus laevis oocytes
    • Barat M., et al. Characterization of DNA-protein complexes from the mitochondria of Xenopus laevis oocytes. Exp. Cell Res. 1985, 157(1):207-217.
    • (1985) Exp. Cell Res. , vol.157 , Issue.1 , pp. 207-217
    • Barat, M.1
  • 48
    • 0035984909 scopus 로고    scopus 로고
    • Regulation of mitochondrial D-loops by transcription factor A and single-stranded DNA-binding protein
    • Takamatsu C., et al. Regulation of mitochondrial D-loops by transcription factor A and single-stranded DNA-binding protein. EMBO Rep. 2002, 3(5):451-456.
    • (2002) EMBO Rep. , vol.3 , Issue.5 , pp. 451-456
    • Takamatsu, C.1
  • 49
    • 0033591435 scopus 로고    scopus 로고
    • Functional interactions of mitochondrial DNA polymerase and single-stranded DNA-binding protein. Template-primer DNA binding and initiation and elongation of DNA strand synthesis
    • Farr C.L., Wang Y., Kaguni L.S. Functional interactions of mitochondrial DNA polymerase and single-stranded DNA-binding protein. Template-primer DNA binding and initiation and elongation of DNA strand synthesis. J. Biol. Chem. 1999, 274(21):14779-14785.
    • (1999) J. Biol. Chem. , vol.274 , Issue.21 , pp. 14779-14785
    • Farr, C.L.1    Wang, Y.2    Kaguni, L.S.3
  • 50
    • 0024287993 scopus 로고
    • Effects of the Xenopus laevis mitochondrial single-stranded DNA-binding protein on the activity of DNA polymerase gamma
    • Mignotte B., Marsault J., Barat-Gueride M. Effects of the Xenopus laevis mitochondrial single-stranded DNA-binding protein on the activity of DNA polymerase gamma. Eur. J. Biochem. 1988, 174(3):479-484.
    • (1988) Eur. J. Biochem. , vol.174 , Issue.3 , pp. 479-484
    • Mignotte, B.1    Marsault, J.2    Barat-Gueride, M.3
  • 51
    • 0027874419 scopus 로고
    • Stimulation of DNA polymerase gamma by a mitochondrial single-strand DNA binding protein
    • Genuario R., Wong T.W. Stimulation of DNA polymerase gamma by a mitochondrial single-strand DNA binding protein. Cell. Mol. Biol. Res. 1993, 39(7):625-634.
    • (1993) Cell. Mol. Biol. Res. , vol.39 , Issue.7 , pp. 625-634
    • Genuario, R.1    Wong, T.W.2
  • 52
    • 1542677230 scopus 로고    scopus 로고
    • TWINKLE Has 5'->3' DNA helicase activity and is specifically stimulated by mitochondrial single-stranded DNA-binding protein
    • Korhonen J.A., Gaspari M., Falkenberg M. TWINKLE Has 5'->3' DNA helicase activity and is specifically stimulated by mitochondrial single-stranded DNA-binding protein. J. Biol. Chem. 2003, 278(49):48627-48632.
    • (2003) J. Biol. Chem. , vol.278 , Issue.49 , pp. 48627-48632
    • Korhonen, J.A.1    Gaspari, M.2    Falkenberg, M.3
  • 53
    • 2942672611 scopus 로고    scopus 로고
    • Twinkle and POLG defects enhance age-dependent accumulation of mutations in the control region of mtDNA
    • Wanrooij S., et al. Twinkle and POLG defects enhance age-dependent accumulation of mutations in the control region of mtDNA. Nucleic Acids Res. 2004, 32(10):3053-3064.
    • (2004) Nucleic Acids Res. , vol.32 , Issue.10 , pp. 3053-3064
    • Wanrooij, S.1
  • 54
    • 0029806951 scopus 로고    scopus 로고
    • Termination within oligo(dT) tracts in template DNA by DNA polymerase gamma occurs with formation of a DNA triplex structure and is relieved by mitochondrial single-stranded DNA-binding protein
    • Mikhailov V.S., Bogenhagen D.F. Termination within oligo(dT) tracts in template DNA by DNA polymerase gamma occurs with formation of a DNA triplex structure and is relieved by mitochondrial single-stranded DNA-binding protein. J. Biol. Chem. 1996, 271(48):30774-30780.
    • (1996) J. Biol. Chem. , vol.271 , Issue.48 , pp. 30774-30780
    • Mikhailov, V.S.1    Bogenhagen, D.F.2
  • 55
    • 0022497229 scopus 로고
    • Yeast RPO41 gene product is required for transcription and maintenance of the mitochondrial genome
    • Greenleaf A.L., Kelly J.L., Lehman I.R. Yeast RPO41 gene product is required for transcription and maintenance of the mitochondrial genome. Proc. Natl Acad. Sci. USA 1986, 83(10):3391-3394.
    • (1986) Proc. Natl Acad. Sci. USA , vol.83 , Issue.10 , pp. 3391-3394
    • Greenleaf, A.L.1    Kelly, J.L.2    Lehman, I.R.3
  • 56
    • 0022828772 scopus 로고
    • Isolation of the nuclear gene encoding a subunit of the yeast mitochondrial RNA polymerase
    • Kelly J.L., Greenleaf A.L., Lehman I.R. Isolation of the nuclear gene encoding a subunit of the yeast mitochondrial RNA polymerase. J. Biol. Chem. 1986, 261(22):10348-10351.
    • (1986) J. Biol. Chem. , vol.261 , Issue.22 , pp. 10348-10351
    • Kelly, J.L.1    Greenleaf, A.L.2    Lehman, I.R.3
  • 57
    • 49649152640 scopus 로고
    • In vitro synthesis of T3 AND T7 RNA polymerase at low magnesium concentration
    • Fuchs E., Fuchs C.M. In vitro synthesis of T3 AND T7 RNA polymerase at low magnesium concentration. FEBS Lett. 1971, 19(2):159-162.
    • (1971) FEBS Lett. , vol.19 , Issue.2 , pp. 159-162
    • Fuchs, E.1    Fuchs, C.M.2
  • 58
    • 33847792061 scopus 로고    scopus 로고
    • Mitochondrial transcription and its regulation in mammalian cells
    • Asin-Cayuela J., Gustafsson C.M. Mitochondrial transcription and its regulation in mammalian cells. Trends Biochem. Sci. 2007, 32(3):111-117.
    • (2007) Trends Biochem. Sci. , vol.32 , Issue.3 , pp. 111-117
    • Asin-Cayuela, J.1    Gustafsson, C.M.2
  • 59
    • 0036648997 scopus 로고    scopus 로고
    • Mitochondrial transcription factors B1 and B2 activate transcription of human mtDNA
    • Falkenberg M., et al. Mitochondrial transcription factors B1 and B2 activate transcription of human mtDNA. Nat. Genet. 2002, 31(3):289-294.
    • (2002) Nat. Genet. , vol.31 , Issue.3 , pp. 289-294
    • Falkenberg, M.1
  • 60
    • 20444458289 scopus 로고    scopus 로고
    • Drosophila mitochondrial transcription factor B1 modulates mitochondrial translation but not transcription or DNA copy number in Schneider cells
    • Matsushima Y., et al. Drosophila mitochondrial transcription factor B1 modulates mitochondrial translation but not transcription or DNA copy number in Schneider cells. J. Biol. Chem. 2005, 280(17):16815-16820.
    • (2005) J. Biol. Chem. , vol.280 , Issue.17 , pp. 16815-16820
    • Matsushima, Y.1
  • 61
    • 63449105579 scopus 로고    scopus 로고
    • Methylation of 12S rRNA is necessary for in vivo stability of the small subunit of the mammalian mitochondrial ribosome
    • Metodiev M.D., et al. Methylation of 12S rRNA is necessary for in vivo stability of the small subunit of the mammalian mitochondrial ribosome. Cell Metab. 2009, 9(4):386-397.
    • (2009) Cell Metab. , vol.9 , Issue.4 , pp. 386-397
    • Metodiev, M.D.1
  • 62
    • 0022081437 scopus 로고
    • Replication priming and transcription initiate from precisely the same site in mouse mitochondrial DNA
    • Chang D.D., Hauswirth W.W., Clayton D.A. Replication priming and transcription initiate from precisely the same site in mouse mitochondrial DNA. EMBO J. 1985, 4(6):1559-1567.
    • (1985) EMBO J. , vol.4 , Issue.6 , pp. 1559-1567
    • Chang, D.D.1    Hauswirth, W.W.2    Clayton, D.A.3
  • 63
    • 0007662353 scopus 로고
    • Priming of human mitochondrial DNA replication occurs at the light-strand promoter
    • Chang D.D., Clayton D.A. Priming of human mitochondrial DNA replication occurs at the light-strand promoter. Proc. Natl Acad. Sci. USA 1985, 82(2):351-355.
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , Issue.2 , pp. 351-355
    • Chang, D.D.1    Clayton, D.A.2
  • 64
    • 0015241303 scopus 로고
    • The presence of DNA molecules with a displacement loop in standard mitochondrial DNA preparations
    • Arnberg A., van Bruggen E.F., Borst P. The presence of DNA molecules with a displacement loop in standard mitochondrial DNA preparations. Biochim. Biophys. Acta 1971, 246(2):353-357.
    • (1971) Biochim. Biophys. Acta , vol.246 , Issue.2 , pp. 353-357
    • Arnberg, A.1    van Bruggen, E.F.2    Borst, P.3
  • 65
    • 49649158958 scopus 로고
    • DNA synthesis by isolated mitochondria. 3. Characterization of D-loop DNA, a novel intermediate in mtDNA synthesis
    • ter Schegget J., Flavell R.A., Borst P. DNA synthesis by isolated mitochondria. 3. Characterization of D-loop DNA, a novel intermediate in mtDNA synthesis. Biochim. Biophys. Acta 1971, 254(1):1-14.
    • (1971) Biochim. Biophys. Acta , vol.254 , Issue.1 , pp. 1-14
    • ter Schegget, J.1    Flavell, R.A.2    Borst, P.3
  • 66
    • 0012353175 scopus 로고
    • Elongation of displacement-loop strands in human and mouse mitochondrial DNA is arrested near specific template sequences
    • Doda J.N., Wright C.T., Clayton D.A. Elongation of displacement-loop strands in human and mouse mitochondrial DNA is arrested near specific template sequences. Proc. Natl Acad. Sci. USA 1981, 78(10):6116-6120.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , Issue.10 , pp. 6116-6120
    • Doda, J.N.1    Wright, C.T.2    Clayton, D.A.3
  • 67
    • 33846407653 scopus 로고    scopus 로고
    • The AAA+protein ATAD3 has displacement loop binding properties and is involved in mitochondrial nucleoid organization
    • He J., et al. The AAA+protein ATAD3 has displacement loop binding properties and is involved in mitochondrial nucleoid organization. J. Cell. Biol. 2007, 176(2):141-146.
    • (2007) J. Cell. Biol. , vol.176 , Issue.2 , pp. 141-146
    • He, J.1
  • 68
    • 73049113711 scopus 로고    scopus 로고
    • The accessory subunit of mitochondrial DNA polymerase gamma determines the DNA content of mitochondrial nucleoids in human cultured cells
    • Di Re M., et al. The accessory subunit of mitochondrial DNA polymerase gamma determines the DNA content of mitochondrial nucleoids in human cultured cells. Nucleic Acids Res. 2009, 37(17):5701-5713.
    • (2009) Nucleic Acids Res. , vol.37 , Issue.17 , pp. 5701-5713
    • Di Re, M.1
  • 69
    • 0029938513 scopus 로고    scopus 로고
    • RNA-DNA hybrid formation at the human mitochondrial heavy-strand origin ceases at replication start sites: an implication for RNA-DNA hybrids serving as primers
    • Xu B., Clayton D.A. RNA-DNA hybrid formation at the human mitochondrial heavy-strand origin ceases at replication start sites: an implication for RNA-DNA hybrids serving as primers. EMBO J. 1996, 15(12):3135-3143.
    • (1996) EMBO J. , vol.15 , Issue.12 , pp. 3135-3143
    • Xu, B.1    Clayton, D.A.2
  • 70
    • 0032836135 scopus 로고    scopus 로고
    • Transcription elongation and human disease
    • Conaway J.W., Conaway R.C. Transcription elongation and human disease. Annu. Rev. Biochem. 1999, 68:301-319.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 301-319
    • Conaway, J.W.1    Conaway, R.C.2
  • 71
    • 0030995020 scopus 로고    scopus 로고
    • In vivo determination of replication origins of human mitochondrial DNA by ligation-mediated polymerase chain reaction
    • Kang D., et al. In vivo determination of replication origins of human mitochondrial DNA by ligation-mediated polymerase chain reaction. J. Biol. Chem. 1997, 272(24):15275-15279.
    • (1997) J. Biol. Chem. , vol.272 , Issue.24 , pp. 15275-15279
    • Kang, D.1
  • 72
    • 33747639275 scopus 로고    scopus 로고
    • Conserved sequence box II directs transcription termination and primer formation in mitochondria
    • Pham X.H., et al. Conserved sequence box II directs transcription termination and primer formation in mitochondria. J. Biol. Chem. 2006, 281(34):24647-24652.
    • (2006) J. Biol. Chem. , vol.281 , Issue.34 , pp. 24647-24652
    • Pham, X.H.1
  • 73
    • 0018137213 scopus 로고
    • Displacement-loop replication initiation sequence in animal mitochondrial DNA exists as a family of discrete lengths
    • Gillum A.M., Clayton D.A. Displacement-loop replication initiation sequence in animal mitochondrial DNA exists as a family of discrete lengths. Proc. Natl Acad. Sci. USA 1978, 75(2):677-681.
    • (1978) Proc. Natl Acad. Sci. USA , vol.75 , Issue.2 , pp. 677-681
    • Gillum, A.M.1    Clayton, D.A.2
  • 74
    • 0018410075 scopus 로고
    • Nucleotide sequence of a region of human mitochondrial DNA containing the precisely identified origin of replication
    • Crews S., et al. Nucleotide sequence of a region of human mitochondrial DNA containing the precisely identified origin of replication. Nature 1979, 277(5693):192-198.
    • (1979) Nature , vol.277 , Issue.5693 , pp. 192-198
    • Crews, S.1
  • 75
    • 10844295852 scopus 로고    scopus 로고
    • Discovery of a major D-loop replication origin reveals two modes of human mtDNA synthesis
    • Fish J., Raule N., Attardi G. Discovery of a major D-loop replication origin reveals two modes of human mtDNA synthesis. Science 2004, 306(5704):2098-2101.
    • (2004) Science , vol.306 , Issue.5704 , pp. 2098-2101
    • Fish, J.1    Raule, N.2    Attardi, G.3
  • 76
    • 0027284549 scopus 로고
    • Primers for mitochondrial DNA replication generated by endonuclease G
    • Cote J., Ruiz-Carrillo A. Primers for mitochondrial DNA replication generated by endonuclease G. Science 1993, 261(5122):765-769.
    • (1993) Science , vol.261 , Issue.5122 , pp. 765-769
    • Cote, J.1    Ruiz-Carrillo, A.2
  • 77
    • 0030952327 scopus 로고    scopus 로고
    • RNase mitochondrial RNA processing correctly cleaves a novel R loop at the mitochondrial DNA leading-strand origin of replication
    • Lee D.Y., Clayton D.A. RNase mitochondrial RNA processing correctly cleaves a novel R loop at the mitochondrial DNA leading-strand origin of replication. Genes Dev. 1997, 11(5):582-592.
    • (1997) Genes Dev. , vol.11 , Issue.5 , pp. 582-592
    • Lee, D.Y.1    Clayton, D.A.2
  • 78
    • 0018577688 scopus 로고
    • Mechanism of mitochondrial DNA replication in mouse L-cells: localization and sequence of the light-strand origin of replication
    • Martens P.A., Clayton D.A. Mechanism of mitochondrial DNA replication in mouse L-cells: localization and sequence of the light-strand origin of replication. J. Mol. Biol. 1979, 135(2):327-351.
    • (1979) J. Mol. Biol. , vol.135 , Issue.2 , pp. 327-351
    • Martens, P.A.1    Clayton, D.A.2
  • 79
    • 0022230199 scopus 로고
    • In vitro replication of human mitochondrial DNA: accurate initiation at the origin of light-strand synthesis
    • Wong T.W., Clayton D.A. In vitro replication of human mitochondrial DNA: accurate initiation at the origin of light-strand synthesis. Cell 1985, 42(3):951-958.
    • (1985) Cell , vol.42 , Issue.3 , pp. 951-958
    • Wong, T.W.1    Clayton, D.A.2
  • 80
    • 0022202524 scopus 로고
    • Isolation and characterization of a DNA primase from human mitochondria
    • Wong T.W., Clayton D.A. Isolation and characterization of a DNA primase from human mitochondria. J. Biol. Chem. 1985, 260(21):11530-11535.
    • (1985) J. Biol. Chem. , vol.260 , Issue.21 , pp. 11530-11535
    • Wong, T.W.1    Clayton, D.A.2
  • 81
    • 0022517876 scopus 로고
    • DNA primase of human mitochondria is associated with structural RNA that is essential for enzymatic activity
    • Wong T.W., Clayton D.A. DNA primase of human mitochondria is associated with structural RNA that is essential for enzymatic activity. Cell 1986, 45(6):817-825.
    • (1986) Cell , vol.45 , Issue.6 , pp. 817-825
    • Wong, T.W.1    Clayton, D.A.2
  • 82
    • 74049123624 scopus 로고    scopus 로고
    • Mitochondrial RNA polymerase is needed for activation of the origin of light-strand DNA replication
    • Fuste J.M., et al. Mitochondrial RNA polymerase is needed for activation of the origin of light-strand DNA replication. Mol. Cell. 2010, 37(1):67-78.
    • (2010) Mol. Cell. , vol.37 , Issue.1 , pp. 67-78
    • Fuste, J.M.1
  • 83
    • 0025017820 scopus 로고
    • Release of RNA polymerase from vero cell mitochondria after herpes simplex virus type 1 infection
    • Tsurumi T., Lehman I.R. Release of RNA polymerase from vero cell mitochondria after herpes simplex virus type 1 infection. J. Virol. 1990, 64(1):450-452.
    • (1990) J. Virol. , vol.64 , Issue.1 , pp. 450-452
    • Tsurumi, T.1    Lehman, I.R.2
  • 84
    • 0033529190 scopus 로고    scopus 로고
    • Stability of the mitochondrial genome requires an amino-terminal domain of yeast mitochondrial RNA polymerase
    • Wang Y., Shadel G.S. Stability of the mitochondrial genome requires an amino-terminal domain of yeast mitochondrial RNA polymerase. Proc. Natl Acad. Sci. USA 1999, 96(14):8046-8051.
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , Issue.14 , pp. 8046-8051
    • Wang, Y.1    Shadel, G.S.2
  • 85
    • 34250868951 scopus 로고    scopus 로고
    • Expression of catalytic mutants of the mtDNA helicase Twinkle and polymerase POLG causes distinct replication stalling phenotypes
    • Wanrooij S., et al. Expression of catalytic mutants of the mtDNA helicase Twinkle and polymerase POLG causes distinct replication stalling phenotypes. Nucleic Acids Res. 2007, 35(10):3238-3251.
    • (2007) Nucleic Acids Res. , vol.35 , Issue.10 , pp. 3238-3251
    • Wanrooij, S.1
  • 86
    • 53049089197 scopus 로고    scopus 로고
    • Physiological and biochemical defects in carboxyl-terminal mutants of mitochondrial DNA helicase
    • Matsushima Y., et al. Physiological and biochemical defects in carboxyl-terminal mutants of mitochondrial DNA helicase. J. Biol. Chem. 2008, 283(35):23964-23971.
    • (2008) J. Biol. Chem. , vol.283 , Issue.35 , pp. 23964-23971
    • Matsushima, Y.1
  • 87
    • 33745637944 scopus 로고    scopus 로고
    • Twinkle, the mitochondrial replicative DNA helicase, is widespread in the eukaryotic radiation and may also be the mitochondrial DNA primase in most eukaryotes
    • Shutt T.E., Gray M.W. Twinkle, the mitochondrial replicative DNA helicase, is widespread in the eukaryotic radiation and may also be the mitochondrial DNA primase in most eukaryotes. J. Mol. Evol. 2006, 62(5):588-599.
    • (2006) J. Mol. Evol. , vol.62 , Issue.5 , pp. 588-599
    • Shutt, T.E.1    Gray, M.W.2
  • 88
    • 39149116732 scopus 로고    scopus 로고
    • The N-terminal domain of TWINKLE contributes to single-stranded DNA binding and DNA helicase activities
    • Farge G., et al. The N-terminal domain of TWINKLE contributes to single-stranded DNA binding and DNA helicase activities. Nucleic Acids Res. 2008, 36(2):393-403.
    • (2008) Nucleic Acids Res. , vol.36 , Issue.2 , pp. 393-403
    • Farge, G.1
  • 89
    • 0027373139 scopus 로고
    • Interactions of bacteriophage T7 DNA primase/helicase protein with single-stranded and double-stranded DNAs
    • Hingorani M.M., Patel S.S. Interactions of bacteriophage T7 DNA primase/helicase protein with single-stranded and double-stranded DNAs. Biochemistry 1993, 32(46):12478-12487.
    • (1993) Biochemistry , vol.32 , Issue.46 , pp. 12478-12487
    • Hingorani, M.M.1    Patel, S.S.2
  • 90
    • 0033786801 scopus 로고    scopus 로고
    • Structure and function of hexameric helicases
    • Patel S.S., Picha K.M. Structure and function of hexameric helicases. Annu. Rev. Biochem. 2000, 69:651-697.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 651-697
    • Patel, S.S.1    Picha, K.M.2
  • 91
    • 0036753338 scopus 로고    scopus 로고
    • DnaB drives DNA branch migration and dislodges proteins while encircling two DNA strands
    • Kaplan D.L., O'Donnell M. DnaB drives DNA branch migration and dislodges proteins while encircling two DNA strands. Mol. Cell. 2002, 10(3):647-657.
    • (2002) Mol. Cell. , vol.10 , Issue.3 , pp. 647-657
    • Kaplan, D.L.1    O'Donnell, M.2
  • 92
    • 69249158083 scopus 로고    scopus 로고
    • Human heart mitochondrial DNA is organized in complex catenated networks containing abundant four-way junctions and replication forks
    • Pohjoismaki J.L., et al. Human heart mitochondrial DNA is organized in complex catenated networks containing abundant four-way junctions and replication forks. J. Biol. Chem. 2009, 284(32):21446-21457.
    • (2009) J. Biol. Chem. , vol.284 , Issue.32 , pp. 21446-21457
    • Pohjoismaki, J.L.1
  • 93
    • 0035195043 scopus 로고    scopus 로고
    • Prominent mitochondrial DNA recombination intermediates in human heart muscle
    • Kajander O.A., et al. Prominent mitochondrial DNA recombination intermediates in human heart muscle. EMBO Rep. 2001, 2(11):1007-1012.
    • (2001) EMBO Rep. , vol.2 , Issue.11 , pp. 1007-1012
    • Kajander, O.A.1
  • 94
    • 0000880652 scopus 로고
    • Isolation and characterization of recombination-deficient mutants of Escherichia coli K12
    • Clark A.J., Margulies A.D. Isolation and characterization of recombination-deficient mutants of Escherichia coli K12. Proc. Natl Acad. Sci. USA 1965, 53:451-459.
    • (1965) Proc. Natl Acad. Sci. USA , vol.53 , pp. 451-459
    • Clark, A.J.1    Margulies, A.D.2
  • 95
    • 67649317029 scopus 로고    scopus 로고
    • Can indirect tests detect a known recombination event in human mtDNA?
    • White D.J., Gemmell N.J. Can indirect tests detect a known recombination event in human mtDNA?. Mol. Biol. Evol. 2009, 26(7):1435-1439.
    • (2009) Mol. Biol. Evol. , vol.26 , Issue.7 , pp. 1435-1439
    • White, D.J.1    Gemmell, N.J.2
  • 96
    • 2442609784 scopus 로고    scopus 로고
    • Recombination of human mitochondrial DNA
    • Kraytsberg Y., et al. Recombination of human mitochondrial DNA. Science 2004, 304(5673):981.
    • (2004) Science , vol.304 , Issue.5673 , pp. 981
    • Kraytsberg, Y.1
  • 97
    • 23044500257 scopus 로고    scopus 로고
    • Recombination of mitochondrial DNA in skeletal muscle of individuals with multiple mitochondrial DNA heteroplasmy
    • Zsurka G., et al. Recombination of mitochondrial DNA in skeletal muscle of individuals with multiple mitochondrial DNA heteroplasmy. Nat. Genet. 2005, 37(8):873-877.
    • (2005) Nat. Genet. , vol.37 , Issue.8 , pp. 873-877
    • Zsurka, G.1
  • 98
    • 19944383101 scopus 로고    scopus 로고
    • Twinkle helicase is essential for mtDNA maintenance and regulates mtDNA copy number
    • Tyynismaa H., et al. Twinkle helicase is essential for mtDNA maintenance and regulates mtDNA copy number. Hum. Mol. Genet. 2004, 13(24):3219-3227.
    • (2004) Hum. Mol. Genet. , vol.13 , Issue.24 , pp. 3219-3227
    • Tyynismaa, H.1
  • 99
    • 34248170868 scopus 로고    scopus 로고
    • Differential phenotypes of active site and human autosomal dominant progressive external ophthalmoplegia mutations in Drosophila mitochondrial DNA helicase expressed in Schneider cells
    • Matsushima Y., Kaguni L.S. Differential phenotypes of active site and human autosomal dominant progressive external ophthalmoplegia mutations in Drosophila mitochondrial DNA helicase expressed in Schneider cells. J. Biol. Chem. 2007, 282(13):9436-9444.
    • (2007) J. Biol. Chem. , vol.282 , Issue.13 , pp. 9436-9444
    • Matsushima, Y.1    Kaguni, L.S.2
  • 100
    • 33947101328 scopus 로고    scopus 로고
    • Modular architecture of the hexameric human mitochondrial DNA helicase
    • Ziebarth T.D., Farr C.L., Kaguni L.S. Modular architecture of the hexameric human mitochondrial DNA helicase. J. Mol. Biol. 2007, 367(5):1382-1391.
    • (2007) J. Mol. Biol. , vol.367 , Issue.5 , pp. 1382-1391
    • Ziebarth, T.D.1    Farr, C.L.2    Kaguni, L.S.3
  • 101
    • 58149163606 scopus 로고    scopus 로고
    • Twinkle mutations associated with autosomal dominant progressive external ophthalmoplegia lead to impaired helicase function and in vivo mtDNA replication stalling
    • Goffart S., et al. Twinkle mutations associated with autosomal dominant progressive external ophthalmoplegia lead to impaired helicase function and in vivo mtDNA replication stalling. Hum. Mol. Genet. 2009, 18(2):328-340.
    • (2009) Hum. Mol. Genet. , vol.18 , Issue.2 , pp. 328-340
    • Goffart, S.1
  • 102
    • 40849097478 scopus 로고    scopus 로고
    • Structure-function defects of the TWINKLE linker region in progressive external ophthalmoplegia
    • Korhonen J.A., et al. Structure-function defects of the TWINKLE linker region in progressive external ophthalmoplegia. J. Mol. Biol. 2008, 377(3):691-705.
    • (2008) J. Mol. Biol. , vol.377 , Issue.3 , pp. 691-705
    • Korhonen, J.A.1
  • 103
    • 0033570097 scopus 로고    scopus 로고
    • The linker region between the helicase and primase domains of the bacteriophage T7 gene 4 protein is critical for hexamer formation
    • Guo S., Tabor S., Richardson C.C. The linker region between the helicase and primase domains of the bacteriophage T7 gene 4 protein is critical for hexamer formation. J. Biol. Chem. 1999, 274(42):30303-30309.
    • (1999) J. Biol. Chem. , vol.274 , Issue.42 , pp. 30303-30309
    • Guo, S.1    Tabor, S.2    Richardson, C.C.3
  • 104
    • 27544440060 scopus 로고    scopus 로고
    • Infantile onset spinocerebellar ataxia is caused by recessive mutations in mitochondrial proteins Twinkle and Twinky
    • Nikali K., et al. Infantile onset spinocerebellar ataxia is caused by recessive mutations in mitochondrial proteins Twinkle and Twinky. Hum. Mol. Genet. 2005, 14(20):2981-2990.
    • (2005) Hum. Mol. Genet. , vol.14 , Issue.20 , pp. 2981-2990
    • Nikali, K.1
  • 105
    • 0028833524 scopus 로고
    • An autosomal locus predisposing to deletions of mitochondrial DNA
    • Suomalainen A., et al. An autosomal locus predisposing to deletions of mitochondrial DNA. Nat. Genet. 1995, 9(2):146-151.
    • (1995) Nat. Genet. , vol.9 , Issue.2 , pp. 146-151
    • Suomalainen, A.1
  • 106
    • 0030898772 scopus 로고    scopus 로고
    • Autosomal dominant progressive external ophthalmoplegia with multiple deletions of mtDNA: clinical, biochemical, and molecular genetic features of the 10q-linked disease
    • Suomalainen A., et al. Autosomal dominant progressive external ophthalmoplegia with multiple deletions of mtDNA: clinical, biochemical, and molecular genetic features of the 10q-linked disease. Neurology 1997, 48(5):1244-1253.
    • (1997) Neurology , vol.48 , Issue.5 , pp. 1244-1253
    • Suomalainen, A.1
  • 107
    • 0026463567 scopus 로고
    • Inherited idiopathic dilated cardiomyopathy with multiple deletions of mitochondrial DNA
    • Suomalainen A., et al. Inherited idiopathic dilated cardiomyopathy with multiple deletions of mitochondrial DNA. Lancet 1992, 340(8831):1319-1320.
    • (1992) Lancet , vol.340 , Issue.8831 , pp. 1319-1320
    • Suomalainen, A.1
  • 108
    • 0026637067 scopus 로고
    • Multiple deletions of mitochondrial DNA in several tissues of a patient with severe retarded depression and familial progressive external ophthalmoplegia
    • Suomalainen A., et al. Multiple deletions of mitochondrial DNA in several tissues of a patient with severe retarded depression and familial progressive external ophthalmoplegia. J. Clin. Invest. 1992, 90(1):61-66.
    • (1992) J. Clin. Invest. , vol.90 , Issue.1 , pp. 61-66
    • Suomalainen, A.1
  • 109
    • 66849097994 scopus 로고    scopus 로고
    • Finding twinkle in the eyes of a 71-year-old lady: a case report and review of the genotypic and phenotypic spectrum of TWINKLE-related dominant disease
    • A
    • Van Hove J.L., et al. Finding twinkle in the eyes of a 71-year-old lady: a case report and review of the genotypic and phenotypic spectrum of TWINKLE-related dominant disease. Am. J. Med. Genet. 2009, 149A(5):861-867.
    • (2009) Am. J. Med. Genet. , vol.149 , Issue.5 , pp. 861-867
    • Van Hove, J.L.1
  • 110
    • 2542440775 scopus 로고    scopus 로고
    • The linker region between the helicase and primase domains of the gene 4 protein of bacteriophage T7. Role in helicase conformation and activity
    • Lee S.J., Richardson C.C. The linker region between the helicase and primase domains of the gene 4 protein of bacteriophage T7. Role in helicase conformation and activity. J. Biol. Chem. 2004, 279(22):23384-23393.
    • (2004) J. Biol. Chem. , vol.279 , Issue.22 , pp. 23384-23393
    • Lee, S.J.1    Richardson, C.C.2
  • 111
    • 29144486726 scopus 로고    scopus 로고
    • Mutant mitochondrial helicase Twinkle causes multiple mtDNA deletions and a late-onset mitochondrial disease in mice
    • Tyynismaa H., et al. Mutant mitochondrial helicase Twinkle causes multiple mtDNA deletions and a late-onset mitochondrial disease in mice. Proc. Natl Acad. Sci. USA 2005, 102(49):17687-17692.
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , Issue.49 , pp. 17687-17692
    • Tyynismaa, H.1
  • 112
    • 0345276497 scopus 로고    scopus 로고
    • The crystal structure of the bifunctional primase-helicase of bacteriophage T7
    • Toth E.A., et al. The crystal structure of the bifunctional primase-helicase of bacteriophage T7. Mol. Cell. 2003, 12(5):1113-1123.
    • (2003) Mol. Cell. , vol.12 , Issue.5 , pp. 1113-1123
    • Toth, E.A.1
  • 113
    • 58749095989 scopus 로고    scopus 로고
    • Structure-function defects of the twinkle amino-terminal region in progressive external ophthalmoplegia
    • Holmlund T., et al. Structure-function defects of the twinkle amino-terminal region in progressive external ophthalmoplegia. Biochim. Biophys. Acta 2009, 1792(2):132-139.
    • (2009) Biochim. Biophys. Acta , vol.1792 , Issue.2 , pp. 132-139
    • Holmlund, T.1
  • 114
    • 77952485613 scopus 로고    scopus 로고
    • Ketogenic diet slows down mitochondrial myopathy progression in mice
    • Ahola-Erkkila S., et al. Ketogenic diet slows down mitochondrial myopathy progression in mice. Hum. Mol. Genet. 2010.
    • (2010) Hum. Mol. Genet.
    • Ahola-Erkkila, S.1
  • 115
    • 35649024143 scopus 로고    scopus 로고
    • Recessive Twinkle mutations in early onset encephalopathy with mtDNA depletion
    • Hakonen A.H., et al. Recessive Twinkle mutations in early onset encephalopathy with mtDNA depletion. Brain 2007, 130(Pt 11):3032-3040.
    • (2007) Brain , vol.130 , Issue.PART 11 , pp. 3032-3040
    • Hakonen, A.H.1
  • 116
    • 37849003416 scopus 로고    scopus 로고
    • Twinkle helicase (PEO1) gene mutation causes mitochondrial DNA depletion
    • Sarzi E., et al. Twinkle helicase (PEO1) gene mutation causes mitochondrial DNA depletion. Ann. Neurol. 2007, 62(6):579-587.
    • (2007) Ann. Neurol. , vol.62 , Issue.6 , pp. 579-587
    • Sarzi, E.1
  • 117
    • 0028089305 scopus 로고
    • Infantile onset spinocerebellar ataxia with sensory neuropathy: a new inherited disease
    • Koskinen T., et al. Infantile onset spinocerebellar ataxia with sensory neuropathy: a new inherited disease. J. Neurol. Sci. 1994, 121(1):50-56.
    • (1994) J. Neurol. Sci. , vol.121 , Issue.1 , pp. 50-56
    • Koskinen, T.1
  • 118
    • 56049111329 scopus 로고    scopus 로고
    • Infantile-onset spinocerebellar ataxia and mitochondrial recessive ataxia syndrome are associated with neuronal complex I defect and mtDNA depletion
    • Hakonen A.H., et al. Infantile-onset spinocerebellar ataxia and mitochondrial recessive ataxia syndrome are associated with neuronal complex I defect and mtDNA depletion. Hum. Mol. Genet. 2008, 17(23):3822-3835.
    • (2008) Hum. Mol. Genet. , vol.17 , Issue.23 , pp. 3822-3835
    • Hakonen, A.H.1
  • 119
    • 2142705756 scopus 로고    scopus 로고
    • POLG mutations associated with Alpers' syndrome and mitochondrial DNA depletion
    • Naviaux R.K., Nguyen K.V. POLG mutations associated with Alpers' syndrome and mitochondrial DNA depletion. Ann. Neurol. 2004, 55(5):706-712.
    • (2004) Ann. Neurol. , vol.55 , Issue.5 , pp. 706-712
    • Naviaux, R.K.1    Nguyen, K.V.2
  • 120
    • 20844442462 scopus 로고    scopus 로고
    • POLG mutations in neurodegenerative disorders with ataxia but no muscle involvement
    • Van Goethem G., et al. POLG mutations in neurodegenerative disorders with ataxia but no muscle involvement. Neurology 2004, 63(7):1251-1257.
    • (2004) Neurology , vol.63 , Issue.7 , pp. 1251-1257
    • Van Goethem, G.1
  • 121
    • 23944508509 scopus 로고    scopus 로고
    • Mitochondrial DNA polymerase W748S mutation: a common cause of autosomal recessive ataxia with ancient European origin
    • Hakonen A.H., et al. Mitochondrial DNA polymerase W748S mutation: a common cause of autosomal recessive ataxia with ancient European origin. Am. J. Hum. Genet. 2005, 77(3):430-441.
    • (2005) Am. J. Hum. Genet. , vol.77 , Issue.3 , pp. 430-441
    • Hakonen, A.H.1
  • 122
    • 39649120348 scopus 로고    scopus 로고
    • Inherited mitochondrial diseases of DNA replication
    • Copeland W.C. Inherited mitochondrial diseases of DNA replication. Annu. Rev. Med. 2008, 59:131-146.
    • (2008) Annu. Rev. Med. , vol.59 , pp. 131-146
    • Copeland, W.C.1
  • 123
    • 0023883150 scopus 로고
    • Deletions of muscle mitochondrial DNA in patients with mitochondrial myopathies
    • Holt I.J., Harding A.E., Morgan-Hughes J.A. Deletions of muscle mitochondrial DNA in patients with mitochondrial myopathies. Nature 1988, 331(6158):717-719.
    • (1988) Nature , vol.331 , Issue.6158 , pp. 717-719
    • Holt, I.J.1    Harding, A.E.2    Morgan-Hughes, J.A.3
  • 124
    • 0034943967 scopus 로고    scopus 로고
    • Mutation of POLG is associated with progressive external ophthalmoplegia characterized by mtDNA deletions
    • Van Goethem G., et al. Mutation of POLG is associated with progressive external ophthalmoplegia characterized by mtDNA deletions. Nat. Genet. 2001, 28(3):211-212.
    • (2001) Nat. Genet. , vol.28 , Issue.3 , pp. 211-212
    • Van Goethem, G.1
  • 125
    • 34447315023 scopus 로고    scopus 로고
    • Defects in maintenance of mitochondrial DNA are associated with intramitochondrial nucleotide imbalances
    • Ashley N., et al. Defects in maintenance of mitochondrial DNA are associated with intramitochondrial nucleotide imbalances. Hum. Mol. Genet. 2007, 16(12):1400-1411.
    • (2007) Hum. Mol. Genet. , vol.16 , Issue.12 , pp. 1400-1411
    • Ashley, N.1
  • 126
    • 0021133987 scopus 로고
    • Cell cycle-dependent regulation of mammalian ribonucleotide reductase. The S phase-correlated increase in subunit M2 is regulated by de novo protein synthesis
    • Eriksson S., et al. Cell cycle-dependent regulation of mammalian ribonucleotide reductase. The S phase-correlated increase in subunit M2 is regulated by de novo protein synthesis. J. Biol. Chem. 1984, 259(19):11695-11700.
    • (1984) J. Biol. Chem. , vol.259 , Issue.19 , pp. 11695-11700
    • Eriksson, S.1
  • 127
    • 0028322120 scopus 로고
    • International commission for protection against environmental mutagens and carcinogens. Deoxyribonucleoside triphosphate levels: a critical factor in the maintenance of genetic stability
    • Kunz B.A., et al. International commission for protection against environmental mutagens and carcinogens. Deoxyribonucleoside triphosphate levels: a critical factor in the maintenance of genetic stability. Mutat. Res. 1994, 318(1):1-64.
    • (1994) Mutat. Res. , vol.318 , Issue.1 , pp. 1-64
    • Kunz, B.A.1
  • 128
    • 33749004245 scopus 로고    scopus 로고
    • Genetic and chemical rescue of the Saccharomyces cerevisiae phenotype induced by mitochondrial DNA polymerase mutations associated with progressive external ophthalmoplegia in humans
    • Baruffini E., et al. Genetic and chemical rescue of the Saccharomyces cerevisiae phenotype induced by mitochondrial DNA polymerase mutations associated with progressive external ophthalmoplegia in humans. Hum. Mol. Genet. 2006, 15(19):2846-2855.
    • (2006) Hum. Mol. Genet. , vol.15 , Issue.19 , pp. 2846-2855
    • Baruffini, E.1
  • 129
    • 77953499335 scopus 로고    scopus 로고
    • Mip1 Containing mutations associated with mitochondrial disease causes mutagenesis and depletion of mtDNA in Saccharomyces cerevisiae
    • Stumpf J.D., et al. mip1 Containing mutations associated with mitochondrial disease causes mutagenesis and depletion of mtDNA in Saccharomyces cerevisiae. Hum. Mol. Genet. 2010.
    • (2010) Hum. Mol. Genet.
    • Stumpf, J.D.1
  • 130
    • 0030725454 scopus 로고    scopus 로고
    • Trinucleotide repeats affect DNA replication in vivo
    • Samadashwily G.M., Raca G., Mirkin S.M. Trinucleotide repeats affect DNA replication in vivo. Nat. Genet. 1997, 17(3):298-304.
    • (1997) Nat. Genet. , vol.17 , Issue.3 , pp. 298-304
    • Samadashwily, G.M.1    Raca, G.2    Mirkin, S.M.3
  • 131
    • 0030844557 scopus 로고    scopus 로고
    • Mechanisms of triplex-caused polymerization arrest
    • Krasilnikov A.S., et al. Mechanisms of triplex-caused polymerization arrest. Nucleic Acids Res. 1997, 25(7):1339-1346.
    • (1997) Nucleic Acids Res. , vol.25 , Issue.7 , pp. 1339-1346
    • Krasilnikov, A.S.1
  • 132
    • 0035902573 scopus 로고    scopus 로고
    • Formation of Holliday junctions by regression of nascent DNA in intermediates containing stalled replication forks: RecG stimulates regression even when the DNA is negatively supercoiled
    • McGlynn P., Lloyd R.G., Marians K.J. Formation of Holliday junctions by regression of nascent DNA in intermediates containing stalled replication forks: RecG stimulates regression even when the DNA is negatively supercoiled. Proc. Natl Acad. Sci. USA 2001, 98(15):8235-8240.
    • (2001) Proc. Natl Acad. Sci. USA , vol.98 , Issue.15 , pp. 8235-8240
    • McGlynn, P.1    Lloyd, R.G.2    Marians, K.J.3
  • 133
    • 0037178723 scopus 로고    scopus 로고
    • ATR homolog Mec1 promotes fork progression, thus averting breaks in replication slow zones
    • Cha R.S., Kleckner N. ATR homolog Mec1 promotes fork progression, thus averting breaks in replication slow zones. Science 2002, 297(5581):602-606.
    • (2002) Science , vol.297 , Issue.5581 , pp. 602-606
    • Cha, R.S.1    Kleckner, N.2
  • 134
    • 0031025093 scopus 로고    scopus 로고
    • DNA double-strand breaks caused by replication arrest
    • Michel B., Ehrlich S.D., Uzest M. DNA double-strand breaks caused by replication arrest. EMBO J. 1997, 16(2):430-438.
    • (1997) EMBO J. , vol.16 , Issue.2 , pp. 430-438
    • Michel, B.1    Ehrlich, S.D.2    Uzest, M.3
  • 135
    • 17344372911 scopus 로고    scopus 로고
    • Double-strand breaks of mouse muscle mtDNA promote large deletions similar to multiple mtDNA deletions in humans
    • Srivastava S., Moraes C.T. Double-strand breaks of mouse muscle mtDNA promote large deletions similar to multiple mtDNA deletions in humans. Hum. Mol. Genet. 2005, 14(7):893-902.
    • (2005) Hum. Mol. Genet. , vol.14 , Issue.7 , pp. 893-902
    • Srivastava, S.1    Moraes, C.T.2
  • 136
    • 39749124232 scopus 로고    scopus 로고
    • What causes mitochondrial DNA deletions in human cells?
    • Krishnan K.J., et al. What causes mitochondrial DNA deletions in human cells?. Nat. Genet. 2008, 40(3):275-279.
    • (2008) Nat. Genet. , vol.40 , Issue.3 , pp. 275-279
    • Krishnan, K.J.1
  • 137
    • 0038604455 scopus 로고    scopus 로고
    • Dna2 helicase/nuclease causes replicative fork stalling and double-strand breaks in the ribosomal DNA of Saccharomyces cerevisiae
    • Weitao T., et al. Dna2 helicase/nuclease causes replicative fork stalling and double-strand breaks in the ribosomal DNA of Saccharomyces cerevisiae. J. Biol. Chem. 2003, 278(25):22513-22522.
    • (2003) J. Biol. Chem. , vol.278 , Issue.25 , pp. 22513-22522
    • Weitao, T.1
  • 138
    • 0029911367 scopus 로고    scopus 로고
    • Mammalian mitochondria possess homologous DNA recombination activity
    • Thyagarajan B., Padua R.A., Campbell C. Mammalian mitochondria possess homologous DNA recombination activity. J. Biol. Chem. 1996, 271(44):27536-27543.
    • (1996) J. Biol. Chem. , vol.271 , Issue.44 , pp. 27536-27543
    • Thyagarajan, B.1    Padua, R.A.2    Campbell, C.3
  • 139
    • 0033557234 scopus 로고    scopus 로고
    • Double strand break rejoining by mammalian mitochondrial extracts
    • Lakshmipathy U., Campbell C. Double strand break rejoining by mammalian mitochondrial extracts. Nucleic Acids Res. 1999, 27(4):1198-1204.
    • (1999) Nucleic Acids Res. , vol.27 , Issue.4 , pp. 1198-1204
    • Lakshmipathy, U.1    Campbell, C.2
  • 140
    • 0034604506 scopus 로고    scopus 로고
    • Role of adenine nucleotide translocator 1 in mtDNA maintenance
    • Kaukonen J., et al. Role of adenine nucleotide translocator 1 in mtDNA maintenance. Science 2000, 289(5480):782-785.
    • (2000) Science , vol.289 , Issue.5480 , pp. 782-785
    • Kaukonen, J.1
  • 141
    • 68249118218 scopus 로고    scopus 로고
    • A heterozygous truncating mutation in RRM2B causes autosomal-dominant progressive external ophthalmoplegia with multiple mtDNA deletions
    • Tyynismaa H., et al. A heterozygous truncating mutation in RRM2B causes autosomal-dominant progressive external ophthalmoplegia with multiple mtDNA deletions. Am. J. Hum. Genet. 2009, 85(2):290-295.
    • (2009) Am. J. Hum. Genet. , vol.85 , Issue.2 , pp. 290-295
    • Tyynismaa, H.1
  • 142
    • 38849151612 scopus 로고    scopus 로고
    • Mutation of OPA1 causes dominant optic atrophy with external ophthalmoplegia, ataxia, deafness and multiple mitochondrial DNA deletions: a novel disorder of mtDNA maintenance
    • Hudson G., et al. Mutation of OPA1 causes dominant optic atrophy with external ophthalmoplegia, ataxia, deafness and multiple mitochondrial DNA deletions: a novel disorder of mtDNA maintenance. Brain 2008, 131(Pt 2):329-337.
    • (2008) Brain , vol.131 , Issue.PART 2 , pp. 329-337
    • Hudson, G.1
  • 144
    • 67349118193 scopus 로고    scopus 로고
    • Mitochondrial disorder with OPA1 mutation lacking optic atrophy
    • Milone M., et al. Mitochondrial disorder with OPA1 mutation lacking optic atrophy. Mitochondrion 2009, 9(4):279-281.
    • (2009) Mitochondrion , vol.9 , Issue.4 , pp. 279-281
    • Milone, M.1
  • 145
    • 38849192448 scopus 로고    scopus 로고
    • OPA1 mutations induce mitochondrial DNA instability and optic atrophy 'plus' phenotypes
    • Amati-Bonneau P., et al. OPA1 mutations induce mitochondrial DNA instability and optic atrophy 'plus' phenotypes. Brain 2008, 131(Pt 2):338-351.
    • (2008) Brain , vol.131 , Issue.PART 2 , pp. 338-351
    • Amati-Bonneau, P.1
  • 146
    • 0042157173 scopus 로고    scopus 로고
    • Concluding remarks: the mitochondrial DNA replication bubble has not burst
    • Bogenhagen D.F., Clayton D.A. Concluding remarks: the mitochondrial DNA replication bubble has not burst. Trends Biochem. Sci. 2003, 28(8):404-405.
    • (2003) Trends Biochem. Sci. , vol.28 , Issue.8 , pp. 404-405
    • Bogenhagen, D.F.1    Clayton, D.A.2
  • 147
    • 0038109027 scopus 로고    scopus 로고
    • The mitochondrial DNA replication bubble has not burst
    • Bogenhagen D.F., Clayton D.A. The mitochondrial DNA replication bubble has not burst. Trends Biochem. Sci. 2003, 28(7):357-360.
    • (2003) Trends Biochem. Sci. , vol.28 , Issue.7 , pp. 357-360
    • Bogenhagen, D.F.1    Clayton, D.A.2
  • 148
    • 0038825342 scopus 로고    scopus 로고
    • Response: the mitochondrial DNA replication bubble has not burst
    • Holt I.J., Jacobs H.T. Response: the mitochondrial DNA replication bubble has not burst. Trends Biochem. Sci. 2003, 28(7):355-356.
    • (2003) Trends Biochem. Sci. , vol.28 , Issue.7 , pp. 355-356
    • Holt, I.J.1    Jacobs, H.T.2
  • 149
    • 0015457563 scopus 로고
    • Replication of mitochondrial DNA in mouse L cells and their thymidine kinase-derivatives: displacement replication on a covalently-closed circular template
    • Robberson D.L., Clayton D.A. Replication of mitochondrial DNA in mouse L cells and their thymidine kinase-derivatives: displacement replication on a covalently-closed circular template. Proc. Natl Acad. Sci. USA 1972, 69(12):3810-3814.
    • (1972) Proc. Natl Acad. Sci. USA , vol.69 , Issue.12 , pp. 3810-3814
    • Robberson, D.L.1    Clayton, D.A.2
  • 150
    • 0015302555 scopus 로고
    • Replication of mitochondrial DNA. Circular replicative intermediates in mouse L cells
    • Robberson D.L., Kasamatsu H., Vinograd J. Replication of mitochondrial DNA. Circular replicative intermediates in mouse L cells. Proc. Natl Acad. Sci. USA 1972, 69(3):737-741.
    • (1972) Proc. Natl Acad. Sci. USA , vol.69 , Issue.3 , pp. 737-741
    • Robberson, D.L.1    Kasamatsu, H.2    Vinograd, J.3
  • 151
    • 0019978703 scopus 로고
    • Replication of animal mitochondrial DNA
    • Clayton D.A. Replication of animal mitochondrial DNA. Cell 1982, 28(4):693-705.
    • (1982) Cell , vol.28 , Issue.4 , pp. 693-705
    • Clayton, D.A.1
  • 152
    • 0025341582 scopus 로고
    • A mechanism of formation of a persistent hybrid between elongating RNA and template DNA
    • Masukata H., Tomizawa J. A mechanism of formation of a persistent hybrid between elongating RNA and template DNA. Cell 1990, 62(2):331-338.
    • (1990) Cell , vol.62 , Issue.2 , pp. 331-338
    • Masukata, H.1    Tomizawa, J.2
  • 153
    • 0027513658 scopus 로고
    • Protein binding to a single termination-associated sequence in the mitochondrial DNA D-loop region
    • Madsen C.S., Ghivizzani S.C., Hauswirth W.W. Protein binding to a single termination-associated sequence in the mitochondrial DNA D-loop region. Mol. Cell. Biol. 1993, 13(4):2162-2171.
    • (1993) Mol. Cell. Biol. , vol.13 , Issue.4 , pp. 2162-2171
    • Madsen, C.S.1    Ghivizzani, S.C.2    Hauswirth, W.W.3
  • 154
    • 0019888066 scopus 로고
    • Mechanism of replication of human mitochondrial DNA. Localization of the 5' ends of nascent daughter strands
    • Tapper D.P., Clayton D.A. Mechanism of replication of human mitochondrial DNA. Localization of the 5' ends of nascent daughter strands. J. Biol. Chem. 1981, 256(10):5109-5115.
    • (1981) J. Biol. Chem. , vol.256 , Issue.10 , pp. 5109-5115
    • Tapper, D.P.1    Clayton, D.A.2
  • 155
    • 42749087154 scopus 로고    scopus 로고
    • Hybridization between mitochondrial heavy strand tDNA and expressed light strand tRNA modulates the function of heavy strand tDNA as light strand replication origin
    • Seligmann H. Hybridization between mitochondrial heavy strand tDNA and expressed light strand tRNA modulates the function of heavy strand tDNA as light strand replication origin. J. Mol. Biol. 2008, 379(1):188-199.
    • (2008) J. Mol. Biol. , vol.379 , Issue.1 , pp. 188-199
    • Seligmann, H.1
  • 156
    • 73649098461 scopus 로고    scopus 로고
    • Mitochondrial tRNAs as light strand replication origins: similarity between anticodon loops and the loop of the light strand replication origin predicts initiation of DNA replication
    • Seligmann H. Mitochondrial tRNAs as light strand replication origins: similarity between anticodon loops and the loop of the light strand replication origin predicts initiation of DNA replication. Biosystems 2010, 99(2):85-93.
    • (2010) Biosystems , vol.99 , Issue.2 , pp. 85-93
    • Seligmann, H.1
  • 157
    • 33745746528 scopus 로고    scopus 로고
    • Possible multiple origins of replication in primate mitochondria: alternative role of tRNA sequences
    • Seligmann H., Krishnan N.M., Rao B.J. Possible multiple origins of replication in primate mitochondria: alternative role of tRNA sequences. J. Theor. Biol. 2006, 241(2):321-332.
    • (2006) J. Theor. Biol. , vol.241 , Issue.2 , pp. 321-332
    • Seligmann, H.1    Krishnan, N.M.2    Rao, B.J.3
  • 158
    • 26944500840 scopus 로고    scopus 로고
    • Replication of mitochondrial DNA occurs by strand displacement with alternative light-strand origins, not via a strand-coupled mechanism
    • Brown T.A., et al. Replication of mitochondrial DNA occurs by strand displacement with alternative light-strand origins, not via a strand-coupled mechanism. Genes Dev. 2005, 19(20):2466-2476.
    • (2005) Genes Dev. , vol.19 , Issue.20 , pp. 2466-2476
    • Brown, T.A.1
  • 159
    • 0034598918 scopus 로고    scopus 로고
    • Coupled leading- and lagging-strand synthesis of mammalian mitochondrial DNA
    • Holt I.J., Lorimer H.E., Jacobs H.T. Coupled leading- and lagging-strand synthesis of mammalian mitochondrial DNA. Cell 2000, 100(5):515-524.
    • (2000) Cell , vol.100 , Issue.5 , pp. 515-524
    • Holt, I.J.1    Lorimer, H.E.2    Jacobs, H.T.3
  • 160
    • 33751088000 scopus 로고    scopus 로고
    • Replication of vertebrate mitochondrial DNA entails transient ribonucleotide incorporation throughout the lagging strand
    • Yasukawa T., et al. Replication of vertebrate mitochondrial DNA entails transient ribonucleotide incorporation throughout the lagging strand. EMBO J. 2006, 25(22):5358-5371.
    • (2006) EMBO J. , vol.25 , Issue.22 , pp. 5358-5371
    • Yasukawa, T.1
  • 161
    • 0347695996 scopus 로고    scopus 로고
    • Mammalian mitochondrial DNA replicates bidirectionally from an initiation zone
    • Bowmaker M., et al. Mammalian mitochondrial DNA replicates bidirectionally from an initiation zone. J. Biol. Chem. 2003, 278(51):50961-50969.
    • (2003) J. Biol. Chem. , vol.278 , Issue.51 , pp. 50961-50969
    • Bowmaker, M.1
  • 162
    • 20444428352 scopus 로고    scopus 로고
    • A bidirectional origin of replication maps to the major noncoding region of human mitochondrial DNA
    • Yasukawa T., et al. A bidirectional origin of replication maps to the major noncoding region of human mitochondrial DNA. Mol. Cell. 2005, 18(6):651-662.
    • (2005) Mol. Cell. , vol.18 , Issue.6 , pp. 651-662
    • Yasukawa, T.1
  • 163
    • 0037112343 scopus 로고    scopus 로고
    • Biased incorporation of ribonucleotides on the mitochondrial L-strand accounts for apparent strand-asymmetric DNA replication
    • Yang M.Y., et al. Biased incorporation of ribonucleotides on the mitochondrial L-strand accounts for apparent strand-asymmetric DNA replication. Cell 2002, 111(4):495-505.
    • (2002) Cell , vol.111 , Issue.4 , pp. 495-505
    • Yang, M.Y.1
  • 164
    • 67649948823 scopus 로고    scopus 로고
    • Mitochondrial DNA replication and repair: all a flap
    • Holt I.J. Mitochondrial DNA replication and repair: all a flap. Trends Biochem. Sci. 2009, 34(7):358-365.
    • (2009) Trends Biochem. Sci. , vol.34 , Issue.7 , pp. 358-365
    • Holt, I.J.1
  • 165
    • 55049112210 scopus 로고    scopus 로고
    • Human DNA2 is a mitochondrial nuclease/helicase for efficient processing of DNA replication and repair intermediates
    • Zheng L., et al. Human DNA2 is a mitochondrial nuclease/helicase for efficient processing of DNA replication and repair intermediates. Mol. Cell. 2008, 32(3):325-336.
    • (2008) Mol. Cell. , vol.32 , Issue.3 , pp. 325-336
    • Zheng, L.1
  • 166
    • 49449102611 scopus 로고    scopus 로고
    • Removal of oxidative DNA damage via FEN1-dependent long-patch base excision repair in human cell mitochondria
    • Liu P., et al. Removal of oxidative DNA damage via FEN1-dependent long-patch base excision repair in human cell mitochondria. Mol. Cell. Biol. 2008, 28(16):4975-4987.
    • (2008) Mol. Cell. Biol. , vol.28 , Issue.16 , pp. 4975-4987
    • Liu, P.1
  • 167
    • 34548635045 scopus 로고    scopus 로고
    • Mitochondrial and nuclear localization of human Pif1 helicase
    • Futami K., Shimamoto A., Furuichi Y. Mitochondrial and nuclear localization of human Pif1 helicase. Biol. Pharm. Bull. 2007, 30(9):1685-1692.
    • (2007) Biol. Pharm. Bull. , vol.30 , Issue.9 , pp. 1685-1692
    • Futami, K.1    Shimamoto, A.2    Furuichi, Y.3
  • 168
    • 61349175928 scopus 로고    scopus 로고
    • Native R-loops persist throughout the mouse mitochondrial DNA genome
    • Brown T.A., Tkachuk A.N., Clayton D.A. Native R-loops persist throughout the mouse mitochondrial DNA genome. J. Biol. Chem. 2008, 283(52):36743-36751.
    • (2008) J. Biol. Chem. , vol.283 , Issue.52 , pp. 36743-36751
    • Brown, T.A.1    Tkachuk, A.N.2    Clayton, D.A.3
  • 169
    • 0011467525 scopus 로고
    • The presence of ribonucleotides in mature closed-circular mitochondrial DNA
    • Grossman L.I., Watson R., Vinograd J. The presence of ribonucleotides in mature closed-circular mitochondrial DNA. Proc. Natl Acad. Sci. USA 1973, 70(12):3339-3343.
    • (1973) Proc. Natl Acad. Sci. USA , vol.70 , Issue.12 , pp. 3339-3343
    • Grossman, L.I.1    Watson, R.2    Vinograd, J.3
  • 170
    • 33646406327 scopus 로고    scopus 로고
    • Genesis and wanderings: origins and migrations in asymmetrically replicating mitochondrial DNA
    • Brown T.A., Clayton D.A. Genesis and wanderings: origins and migrations in asymmetrically replicating mitochondrial DNA. Cell Cycle 2006, 5(9):917-921.
    • (2006) Cell Cycle , vol.5 , Issue.9 , pp. 917-921
    • Brown, T.A.1    Clayton, D.A.2
  • 171
    • 0034712321 scopus 로고    scopus 로고
    • Vertebrate mitochondrial DNA-a circle of surprises
    • Clayton D.A. Vertebrate mitochondrial DNA-a circle of surprises. Exp. Cell Res. 2000, 255(1):4-9.
    • (2000) Exp. Cell Res. , vol.255 , Issue.1 , pp. 4-9
    • Clayton, D.A.1
  • 172
    • 70349776569 scopus 로고    scopus 로고
    • Analysis of mitochondrial DNA by two-dimensional agarose gel electrophoresis
    • Reyes A., et al. Analysis of mitochondrial DNA by two-dimensional agarose gel electrophoresis. Methods Mol. Biol. 2009, 554:15-35.
    • (2009) Methods Mol. Biol. , vol.554 , pp. 15-35
    • Reyes, A.1
  • 173
    • 0023646792 scopus 로고
    • The localization of replication origins on ARS plasmids in S. cerevisiae
    • Brewer B.J., Fangman W.L. The localization of replication origins on ARS plasmids in S. cerevisiae. Cell 1987, 51(3):463-471.
    • (1987) Cell , vol.51 , Issue.3 , pp. 463-471
    • Brewer, B.J.1    Fangman, W.L.2
  • 174
    • 0024291357 scopus 로고
    • A replication fork barrier at the 3' end of yeast ribosomal RNA genes
    • Brewer B.J., Fangman W.L. A replication fork barrier at the 3' end of yeast ribosomal RNA genes. Cell 1988, 55(4):637-643.
    • (1988) Cell , vol.55 , Issue.4 , pp. 637-643
    • Brewer, B.J.1    Fangman, W.L.2
  • 175
    • 36348937182 scopus 로고    scopus 로고
    • The phage T4 protein UvsW drives Holliday junction branch migration
    • Webb M.R., et al. The phage T4 protein UvsW drives Holliday junction branch migration. J. Biol. Chem. 2007, 282(47):34401-34411.
    • (2007) J. Biol. Chem. , vol.282 , Issue.47 , pp. 34401-34411
    • Webb, M.R.1
  • 176
    • 33745219840 scopus 로고    scopus 로고
    • Methods to study replication fork collapse in budding yeast
    • Liberi G., et al. Methods to study replication fork collapse in budding yeast. Methods Enzymol. 2006, 409:442-462.
    • (2006) Methods Enzymol. , vol.409 , pp. 442-462
    • Liberi, G.1
  • 177
    • 62049085766 scopus 로고    scopus 로고
    • Termination structures in the Escherichia coli chromosome replication fork trap
    • Duggin I.G., Bell S.D. Termination structures in the Escherichia coli chromosome replication fork trap. J. Mol. Biol. 2009, 387(3):532-539.
    • (2009) J. Mol. Biol. , vol.387 , Issue.3 , pp. 532-539
    • Duggin, I.G.1    Bell, S.D.2
  • 178
    • 72649095200 scopus 로고    scopus 로고
    • Plasmid DNA replication and topology as visualized by two-dimensional agarose gel electrophoresis
    • Schvartzman J.B., et al. Plasmid DNA replication and topology as visualized by two-dimensional agarose gel electrophoresis. Plasmid 2010, 63(1):1-10.
    • (2010) Plasmid , vol.63 , Issue.1 , pp. 1-10
    • Schvartzman, J.B.1
  • 179
    • 48249141027 scopus 로고    scopus 로고
    • Replication stalling at unstable inverted repeats: interplay between DNA hairpins and fork stabilizing proteins
    • Voineagu I., et al. Replication stalling at unstable inverted repeats: interplay between DNA hairpins and fork stabilizing proteins. Proc. Natl Acad. Sci. USA 2008, 105(29):9936-9941.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , Issue.29 , pp. 9936-9941
    • Voineagu, I.1
  • 180
    • 0027486027 scopus 로고
    • Initiation and termination of DNA replication in human rRNA genes
    • Little R.D., Platt T.H., Schildkraut C.L. Initiation and termination of DNA replication in human rRNA genes. Mol. Cell. Biol. 1993, 13(10):6600-6613.
    • (1993) Mol. Cell. Biol. , vol.13 , Issue.10 , pp. 6600-6613
    • Little, R.D.1    Platt, T.H.2    Schildkraut, C.L.3
  • 181
    • 0035812808 scopus 로고    scopus 로고
    • Replication dynamics of the yeast genome
    • Raghuraman M.K., et al. Replication dynamics of the yeast genome. Science 2001, 294(5540):115-121.
    • (2001) Science , vol.294 , Issue.5540 , pp. 115-121
    • Raghuraman, M.K.1
  • 182
    • 0034176951 scopus 로고    scopus 로고
    • Recombination-dependent DNA replication in phage T4
    • Kreuzer K.N. Recombination-dependent DNA replication in phage T4. Trends Biochem. Sci. 2000, 25(4):165-173.
    • (2000) Trends Biochem. Sci. , vol.25 , Issue.4 , pp. 165-173
    • Kreuzer, K.N.1
  • 183
    • 0037256890 scopus 로고    scopus 로고
    • Herpes virus replication
    • Boehmer P.E., Nimonkar A.V. Herpes virus replication. IUBMB Life 2003, 55(1):13-22.
    • (2003) IUBMB Life , vol.55 , Issue.1 , pp. 13-22
    • Boehmer, P.E.1    Nimonkar, A.V.2
  • 184
    • 0035102131 scopus 로고    scopus 로고
    • Bacteriophage T4 proteins replicate plasmids with a preformed R loop at the T4 ori(uvsY) replication origin in vitro
    • Nossal N.G., Dudas K.C., Kreuzer K.N. Bacteriophage T4 proteins replicate plasmids with a preformed R loop at the T4 ori(uvsY) replication origin in vitro. Mol. Cell. 2001, 7(1):31-41.
    • (2001) Mol. Cell. , vol.7 , Issue.1 , pp. 31-41
    • Nossal, N.G.1    Dudas, K.C.2    Kreuzer, K.N.3
  • 185
    • 3442880816 scopus 로고    scopus 로고
    • Two families with autosomal dominant progressive external ophthalmoplegia
    • Kiechl S., et al. Two families with autosomal dominant progressive external ophthalmoplegia. J. Neurol. Neurosurg. Psychiatry 2004, 75(8):1125-1128.
    • (2004) J. Neurol. Neurosurg. Psychiatry , vol.75 , Issue.8 , pp. 1125-1128
    • Kiechl, S.1
  • 186
    • 12544249406 scopus 로고    scopus 로고
    • Sensory ataxic neuropathy due to a novel C10Orf2 mutation with probable germline mosaicism
    • Hudson G., et al. Sensory ataxic neuropathy due to a novel C10Orf2 mutation with probable germline mosaicism. Neurology 2005, 64(2):371-373.
    • (2005) Neurology , vol.64 , Issue.2 , pp. 371-373
    • Hudson, G.1
  • 187
    • 0037461342 scopus 로고    scopus 로고
    • Mutations of ANT1, Twinkle, and POLG1 in sporadic progressive external ophthalmoplegia (PEO)
    • Agostino A., et al. Mutations of ANT1, Twinkle, and POLG1 in sporadic progressive external ophthalmoplegia (PEO). Neurology 2003, 60(8):1354-1356.
    • (2003) Neurology , vol.60 , Issue.8 , pp. 1354-1356
    • Agostino, A.1
  • 188
    • 55149119156 scopus 로고    scopus 로고
    • Novel Twinkle (PEO1) gene mutations in mendelian progressive external ophthalmoplegia
    • Virgilio R., et al. Novel Twinkle (PEO1) gene mutations in mendelian progressive external ophthalmoplegia. J. Neurol. 2008, 255(9):1384-1391.
    • (2008) J. Neurol. , vol.255 , Issue.9 , pp. 1384-1391
    • Virgilio, R.1
  • 189
    • 0043073110 scopus 로고    scopus 로고
    • A novel Twinkle gene mutation in autosomal dominant progressive external ophthalmoplegia
    • Deschauer M., et al. A novel Twinkle gene mutation in autosomal dominant progressive external ophthalmoplegia. Neuromuscul. Disord. 2003, 13(7-8):568-572.
    • (2003) Neuromuscul. Disord. , vol.13 , Issue.7-8 , pp. 568-572
    • Deschauer, M.1
  • 190
    • 0037105957 scopus 로고    scopus 로고
    • Clinical and molecular features of adPEO due to mutations in the Twinkle gene
    • Lewis S., et al. Clinical and molecular features of adPEO due to mutations in the Twinkle gene. J. Neurol. Sci. 2002, 201(1-2):39-44.
    • (2002) J. Neurol. Sci. , vol.201 , Issue.1-2 , pp. 39-44
    • Lewis, S.1
  • 191
    • 34548471803 scopus 로고    scopus 로고
    • Mild ocular myopathy associated with a novel mutation in mitochondrial twinkle helicase
    • Rivera H., et al. Mild ocular myopathy associated with a novel mutation in mitochondrial twinkle helicase. Neuromuscul. Disord. 2007, 17(9-10):677-680.
    • (2007) Neuromuscul. Disord. , vol.17 , Issue.9-10 , pp. 677-680
    • Rivera, H.1
  • 192
    • 70449518025 scopus 로고    scopus 로고
    • Novel Twinkle gene mutation in autosomal dominant progressive external ophthalmoplegia and multisystem failure
    • Bohlega S., et al. Novel Twinkle gene mutation in autosomal dominant progressive external ophthalmoplegia and multisystem failure. Neuromuscul. Disord. 2009, 19(12):845-848.
    • (2009) Neuromuscul. Disord. , vol.19 , Issue.12 , pp. 845-848
    • Bohlega, S.1
  • 193
    • 43049121302 scopus 로고    scopus 로고
    • Phenotype and clinical course in a family with a new de novo Twinkle gene mutation
    • Jeppesen T.D., et al. Phenotype and clinical course in a family with a new de novo Twinkle gene mutation. Neuromuscul. Disord. 2008, 18(4):306-309.
    • (2008) Neuromuscul. Disord. , vol.18 , Issue.4 , pp. 306-309
    • Jeppesen, T.D.1
  • 194
    • 76549093888 scopus 로고    scopus 로고
    • A novel variation in the Twinkle linker region causing late-onset dementia
    • Echaniz-Laguna A., et al. A novel variation in the Twinkle linker region causing late-onset dementia. Neurogenetics 2010, 11(1):21-25.
    • (2010) Neurogenetics , vol.11 , Issue.1 , pp. 21-25
    • Echaniz-Laguna, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.