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Volumn 353, Issue 6296, 2016, Pages

ER-mitochondria contacts couple mtDNA synthesis with Mitochondrial division in human cells

Author keywords

[No Author keywords available]

Indexed keywords

DNA POLYMERASE; MITOCHONDRIAL DNA; DNA DIRECTED DNA POLYMERASE; GREEN FLUORESCENT PROTEIN; POLGBETA PROTEIN, HUMAN; RECOMBINANT PROTEIN;

EID: 84978394425     PISSN: 00368075     EISSN: 10959203     Source Type: Journal    
DOI: 10.1126/science.aaf5549     Document Type: Article
Times cited : (476)

References (48)
  • 1
    • 84927714536 scopus 로고    scopus 로고
    • Defects of mitochondrial DNA replication
    • pmid: 24985751
    • W. C. Copeland, Defects of mitochondrial DNA replication. J. Child Neurol. 29, 1216-1224 (2014). doi: 10.1177/0883073814537380; pmid: 24985751
    • (2014) J. Child Neurol. , vol.29 , pp. 1216-1224
    • Copeland, W.C.1
  • 2
    • 84858376953 scopus 로고    scopus 로고
    • Mitochondria: In sickness and in health
    • pmid: 22424226
    • J. Nunnari, A. Suomalainen, Mitochondria: In sickness and in health. Cell 148, 1145-1159 (2012). doi: 10.1016/j.cell.2012.02.035; pmid: 22424226
    • (2012) Cell , vol.148 , pp. 1145-1159
    • Nunnari, J.1    Suomalainen, A.2
  • 3
    • 2642580016 scopus 로고    scopus 로고
    • Premature ageing in mice expressing defective mitochondrial DNA polymerase
    • pmid: 15164064
    • A. Trifunovic et al., Premature ageing in mice expressing defective mitochondrial DNA polymerase. Nature 429, 417-423 (2004). doi: 10.1038/nature02517; pmid: 15164064
    • (2004) Nature , vol.429 , pp. 417-423
    • Trifunovic, A.1
  • 4
    • 22344456832 scopus 로고    scopus 로고
    • Mitochondrial DNA mutations, oxidative stress, and apoptosis in mammalian aging
    • pmid: 16020738
    • G. C. Kujoth et al., Mitochondrial DNA mutations, oxidative stress, and apoptosis in mammalian aging. Science 309, 481-484 (2005). doi: 10.1126/science.1112125; pmid: 16020738
    • (2005) Science , vol.309 , pp. 481-484
    • Kujoth, G.C.1
  • 5
    • 0038709292 scopus 로고    scopus 로고
    • Composition and dynamics of human mitochondrial nucleoids
    • pmid: 12686611
    • N. Garrido et al., Composition and dynamics of human mitochondrial nucleoids. Mol. Biol. Cell 14, 1583-1596 (2003). doi: 10.1091/mbc. E02-07-0399; pmid: 12686611
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1583-1596
    • Garrido, N.1
  • 6
    • 0030587492 scopus 로고    scopus 로고
    • Cloning and characterization of the human mitochondrial DNA polymerase, DNA polymerase gamma
    • pmid: 8884268
    • P. A. Ropp, W. C. Copeland, Cloning and characterization of the human mitochondrial DNA polymerase, DNA polymerase gamma. Genomics 36, 449-458 (1996). doi: 10.1006/geno. 1996.0490; pmid: 8884268
    • (1996) Genomics , vol.36 , pp. 449-458
    • Ropp, P.A.1    Copeland, W.C.2
  • 7
    • 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
    • pmid: 10608893
    • S. E. Lim, M. J. Longley, W. C. Copeland, 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. 274, 38197-38203 (1999). doi: 10.1074/jbc.274.53.38197; pmid: 10608893
    • (1999) J. Biol. Chem. , vol.274 , pp. 38197-38203
    • Lim, S.E.1    Longley, M.J.2    Copeland, W.C.3
  • 8
    • 2342429459 scopus 로고    scopus 로고
    • DNA polymerase g, the mitochondrial replicase
    • pmid: 15189144
    • L. S. Kaguni, DNA polymerase g, the mitochondrial replicase. Annu. Rev. Biochem. 73, 293-320 (2004). doi: 10.1146/annurev. biochem.72.121801.161455; pmid: 15189144
    • (2004) Annu. Rev. Biochem. , vol.73 , pp. 293-320
    • Kaguni, L.S.1
  • 9
    • 34250868951 scopus 로고    scopus 로고
    • Expression of catalytic mutants of the mtDNA helicase Twinkle and polymerase POLG causes distinct replication stalling phenotypes
    • pmid: 17452351
    • S. Wanrooij, S. Goffart, J. L. O. Pohjoismäki, T. Yasukawa, J. N. Spelbrink, Expression of catalytic mutants of the mtDNA helicase Twinkle and polymerase POLG causes distinct replication stalling phenotypes. Nucleic Acids Res. 35, 3238-3251 (2007). doi: 10.1093/nar/gkm215; pmid: 17452351
    • (2007) Nucleic Acids Res. , vol.35 , pp. 3238-3251
    • Wanrooij, S.1    Goffart, S.2    Pohjoismäki, J.L.O.3    Yasukawa, T.4    Spelbrink, J.N.5
  • 10
    • 77953811054 scopus 로고    scopus 로고
    • The human mitochondrial replication fork in health and disease
    • pmid: 20417176
    • S. Wanrooij, M. Falkenberg, The human mitochondrial replication fork in health and disease. Biochim. Biophys. Acta 1797, 1378-1388 (2010). doi: 10.1016/j.bbabio.2010.04.015; pmid: 20417176
    • (2010) Biochim. Biophys. Acta , vol.1797 , pp. 1378-1388
    • Wanrooij, S.1    Falkenberg, M.2
  • 11
    • 19944383101 scopus 로고    scopus 로고
    • Twinkle helicase is essential for mtDNA maintenance and regulates mtDNA copy number
    • pmid: 15509589
    • H. Tyynismaa et al., Twinkle helicase is essential for mtDNA maintenance and regulates mtDNA copy number. Hum. Mol. Genet. 13, 3219-3227 (2004). doi: 10.1093/hmg/ddh342; pmid: 15509589
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 3219-3227
    • Tyynismaa, H.1
  • 12
    • 3242739284 scopus 로고    scopus 로고
    • Reconstitution of a minimal mtDNA replisome in vitro
    • pmid: 15167897
    • J. A. Korhonen, X. H. Pham, M. Pellegrini, M. Falkenberg, Reconstitution of a minimal mtDNA replisome in vitro. EMBO J. 23, 2423-2429 (2004). doi: 10.1038/sj.emboj.7600257; pmid: 15167897
    • (2004) EMBO J. , vol.23 , pp. 2423-2429
    • Korhonen, J.A.1    Pham, X.H.2    Pellegrini, M.3    Falkenberg, M.4
  • 13
    • 0037443884 scopus 로고    scopus 로고
    • Human mitochondrial DNA is packaged with TFAM
    • pmid: 12626705
    • T. I. Alam et al., Human mitochondrial DNA is packaged with TFAM. Nucleic Acids Res. 31, 1640-1645 (2003). doi: 10.1093/nar/gkg251; pmid: 12626705
    • (2003) Nucleic Acids Res. , vol.31 , pp. 1640-1645
    • Alam, T.I.1
  • 14
    • 34548495323 scopus 로고    scopus 로고
    • The mitochondrial transcription factor TFAM coordinates the assembly of multiple DNA molecules into nucleoid-like structures
    • pmid: 17581862
    • B. A. Kaufman et al., The mitochondrial transcription factor TFAM coordinates the assembly of multiple DNA molecules into nucleoid-like structures. Mol. Biol. Cell 18, 3225-3236 (2007). doi: 10.1091/mbc. E07-05-0404; pmid: 17581862
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3225-3236
    • Kaufman, B.A.1
  • 15
    • 80555128721 scopus 로고    scopus 로고
    • The mitochondrial transcription and packaging factor Tfam imposes a U-turn on mitochondrial DNA
    • pmid: 22037171
    • H. B. Ngo, J. T. Kaiser, D. C. Chan, The mitochondrial transcription and packaging factor Tfam imposes a U-turn on mitochondrial DNA. Nat. Struct. Mol. Biol. 18, 1290-1296 (2011). doi: 10.1038/nsmb.2159; pmid: 22037171
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 1290-1296
    • Ngo, H.B.1    Kaiser, J.T.2    Chan, D.C.3
  • 16
    • 80051972817 scopus 로고    scopus 로고
    • Super-resolution microscopy reveals that mammalian mitochondrial nucleoids have a uniform size and frequently contain a single copy of mtDNA
    • pmid: 21808029
    • C. Kukat et al., Super-resolution microscopy reveals that mammalian mitochondrial nucleoids have a uniform size and frequently contain a single copy of mtDNA. Proc. Natl. Acad. Sci. U. S. A. 108, 13534-13539 (2011). doi: 10.1073/pnas.1109263108; pmid: 21808029
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 13534-13539
    • Kukat, C.1
  • 17
    • 84941074817 scopus 로고    scopus 로고
    • Cross-strand binding of TFAM to a single mtDNA molecule forms the mitochondrial nucleoid
    • pmid: 26305956
    • C. Kukat et al., Cross-strand binding of TFAM to a single mtDNA molecule forms the mitochondrial nucleoid. Proc. Natl. Acad. Sci. U. S. A. 112, 11288-11293 (2015). doi: 10.1073/pnas.1512131112; pmid: 26305956
    • (2015) Proc. Natl. Acad. Sci. U. S. A. , vol.112 , pp. 11288-11293
    • Kukat, C.1
  • 18
    • 83255188980 scopus 로고    scopus 로고
    • Superresolution fluorescence imaging of mitochondrial nucleoids reveals their spatial range, limits, and membrane interaction
    • pmid: 22006021
    • T. A. Brown et al., Superresolution fluorescence imaging of mitochondrial nucleoids reveals their spatial range, limits, and membrane interaction. Mol. Cell. Biol. 31, 4994-5010 (2011). doi: 10.1128/MCB.05694-11; pmid: 22006021
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 4994-5010
    • Brown, T.A.1
  • 19
    • 0035671887 scopus 로고    scopus 로고
    • The inheritance of genes in mitochondria and chloroplasts: Laws, mechanisms, and models
    • pmid: 11700280
    • C. W. Birky Jr., The inheritance of genes in mitochondria and chloroplasts: Laws, mechanisms, and models. Annu. Rev. Genet. 35, 125-148 (2001). doi: 10.1146/annurev. genet.35.102401.090231; pmid: 11700280
    • (2001) Annu. Rev. Genet. , vol.35 , pp. 125-148
    • Birky, C.W.1
  • 20
    • 69249158083 scopus 로고    scopus 로고
    • Human heart mitochondrial DNA is organized in complex catenated networks containing abundant four-way junctions and replication forks
    • pmid: 19525233
    • J. L. O. Pohjoismäki et al., Human heart mitochondrial DNA is organized in complex catenated networks containing abundant four-way junctions and replication forks. J. Biol. Chem. 284, 21446-21457 (2009). doi: 10.1074/jbc. M109.016600; pmid: 19525233
    • (2009) J. Biol. Chem. , vol.284 , pp. 21446-21457
    • Pohjoismäki, J.L.O.1
  • 21
    • 0041661881 scopus 로고    scopus 로고
    • Replication of mitochondrial DNA occurs throughout the mitochondria of cultured human cells
    • pmid: 12941611
    • J. Magnusson, M. Orth, P. Lestienne, J.-W. Taanman, Replication of mitochondrial DNA occurs throughout the mitochondria of cultured human cells. Exp. Cell Res. 289, 133-142 (2003). doi: 10.1016/S0014-4827 (03) 00249-0; pmid: 12941611
    • (2003) Exp. Cell Res. , vol.289 , pp. 133-142
    • Magnusson, J.1    Orth, M.2    Lestienne, P.3    Taanman, J.-W.4
  • 22
    • 0030841103 scopus 로고    scopus 로고
    • Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA
    • pmid: 9243504
    • J. Nunnari et al., Mitochondrial transmission during mating in Saccharomyces cerevisiae is determined by mitochondrial fusion and fission and the intramitochondrial segregation of mitochondrial DNA. Mol. Biol. Cell 8, 1233-1242 (1997). doi: 10.1091/mbc.8.7.1233; pmid: 9243504
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1233-1242
    • Nunnari, J.1
  • 23
    • 84908250304 scopus 로고    scopus 로고
    • Determinants and functions of mitochondrial behavior
    • pmid: 25288115
    • K. Labbé, A. Murley, J. Nunnari, Determinants and functions of mitochondrial behavior. Annu. Rev. Cell Dev. Biol. 30, 357-391 (2014). doi: 10.1146/annurev-cellbio-101011-155756; pmid: 25288115
    • (2014) Annu. Rev. Cell Dev. Biol. , vol.30 , pp. 357-391
    • Labbé, K.1    Murley, A.2    Nunnari, J.3
  • 24
    • 0035166814 scopus 로고    scopus 로고
    • Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells
    • pmid: 11514614
    • E. Smirnova, L. Griparic, D. L. Shurland, A. M. Van Der Bliek, Dynamin-related protein Drp1 is required for mitochondrial division in mammalian cells. Mol. Biol. Cell 12, 2245-2256 (2001). doi: 10.1091/mbc.12.8.2245; pmid: 11514614
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2245-2256
    • Smirnova, E.1    Griparic, L.2    Shurland, D.L.3    Van Der Bliek, A.M.4
  • 25
    • 0032547754 scopus 로고    scopus 로고
    • A human dynamin-related protein controls the distribution of mitochondria
    • pmid: 9786947
    • E. Smirnova, D. L. Shurland, S. N. Ryazantsev, A. M. Van Der Bliek, A human dynamin-related protein controls the distribution of mitochondria. J. Cell Biol. 143, 351-358 (1998). doi: 10.1083/jcb.143.2.351; pmid: 9786947
    • (1998) J. Cell Biol. , vol.143 , pp. 351-358
    • Smirnova, E.1    Shurland, D.L.2    Ryazantsev, S.N.3    Van Der Bliek, A.M.4
  • 26
    • 80054844842 scopus 로고    scopus 로고
    • ER tubules mark sites of mitochondrial division
    • pmid: 21885730
    • J. R. Friedman et al., ER tubules mark sites of mitochondrial division. Science 334, 358-362 (2011). doi: 10.1126/science.1207385; pmid: 21885730
    • (2011) Science , vol.334 , pp. 358-362
    • Friedman, J.R.1
  • 27
    • 84880384547 scopus 로고    scopus 로고
    • Dynamics of nucleoid structure regulated by mitochondrial fission contributes to cristae reformation and release of cytochrome c
    • pmid: 23821750
    • R. Ban-Ishihara, T. Ishihara, N. Sasaki, K. Mihara, N. Ishihara, Dynamics of nucleoid structure regulated by mitochondrial fission contributes to cristae reformation and release of cytochrome c. Proc. Natl. Acad. Sci. U. S. A. 110, 11863-11868 (2013). doi: 10.1073/pnas.1301951110; pmid: 23821750
    • (2013) Proc. Natl. Acad. Sci. U. S. A. , vol.110 , pp. 11863-11868
    • Ban-Ishihara, R.1    Ishihara, T.2    Sasaki, N.3    Mihara, K.4    Ishihara, N.5
  • 28
    • 84920060443 scopus 로고    scopus 로고
    • Dynamics of mitochondrial DNA nucleoids regulated by mitochondrial fission is essential for maintenance of homogeneously active mitochondria during neonatal heart development
    • pmid: 25348719
    • T. Ishihara et al., Dynamics of mitochondrial DNA nucleoids regulated by mitochondrial fission is essential for maintenance of homogeneously active mitochondria during neonatal heart development. Mol. Cell. Biol. 35, 211-223 (2015). doi: 10.1128/MCB.01054-14; pmid: 25348719
    • (2015) Mol. Cell. Biol. , vol.35 , pp. 211-223
    • Ishihara, T.1
  • 29
    • 84879590455 scopus 로고    scopus 로고
    • Effects of Fcj1-Mos1 and mitochondrial division on aggregation of mitochondrial DNA nucleoids and organelle morphology
    • pmid: 23615445
    • K. Itoh, Y. Tamura, M. Iijima, H. Sesaki, Effects of Fcj1-Mos1 and mitochondrial division on aggregation of mitochondrial DNA nucleoids and organelle morphology. Mol. Biol. Cell 24, 1842-1851 (2013). doi: 10.1091/mbc. E13-03-0125; pmid: 23615445
    • (2013) Mol. Biol. Cell , vol.24 , pp. 1842-1851
    • Itoh, K.1    Tamura, Y.2    Iijima, M.3    Sesaki, H.4
  • 30
    • 84879059164 scopus 로고    scopus 로고
    • ER-associated mitochondrial division links the distribution of mitochondria and mitochondrial DNA in yeast
    • pmid: 23682313
    • A. Murley et al., ER-associated mitochondrial division links the distribution of mitochondria and mitochondrial DNA in yeast. eLife 2, e00422 (2013). pmid: 23682313
    • (2013) ELife , vol.2 , pp. e00422
    • Murley, A.1
  • 31
    • 3242705680 scopus 로고    scopus 로고
    • The functional organization of mitochondrial genomes in human cells
    • pmid: 15157274
    • F. J. Iborra, H. Kimura, P. R. Cook, The functional organization of mitochondrial genomes in human cells. BMC Biol. 2, 9 (2004). doi: 10.1186/1741-7007-2-9; pmid: 15157274
    • (2004) BMC Biol. , vol.2 , pp. 9
    • Iborra, F.J.1    Kimura, H.2    Cook, P.R.3
  • 32
    • 84893317772 scopus 로고    scopus 로고
    • Replication factors transiently associate with mtDNA at the mitochondrial inner membrane to facilitate replication
    • pmid: 24163258
    • N. Rajala, J. M. Gerhold, P. Martinsson, A. Klymov, J. N. Spelbrink, Replication factors transiently associate with mtDNA at the mitochondrial inner membrane to facilitate replication. Nucleic Acids Res. 42, 952-967 (2014). doi: 10.1093/nar/gkt988; pmid: 24163258
    • (2014) Nucleic Acids Res. , vol.42 , pp. 952-967
    • Rajala, N.1    Gerhold, J.M.2    Martinsson, P.3    Klymov, A.4    Spelbrink, J.N.5
  • 33
    • 0242593934 scopus 로고    scopus 로고
    • Evidence for a two membranespanning autonomous mitochondrial DNA replisome
    • pmid: 14597773
    • S. Meeusen, J. Nunnari, Evidence for a two membranespanning autonomous mitochondrial DNA replisome. J. Cell Biol. 163, 503-510 (2003). doi: 10.1083/jcb.200304040; pmid: 14597773
    • (2003) J. Cell Biol. , vol.163 , pp. 503-510
    • Meeusen, S.1    Nunnari, J.2
  • 34
    • 84940641863 scopus 로고    scopus 로고
    • POLG2 disease variants: Analyses reveal a dominant negative heterodimer, altered mitochondrial localization and impaired respiratory capacity
    • pmid: 26123486
    • M. J. Young, M. M. Humble, K. L. DeBalsi, K. Y. Sun, W. C. Copeland, POLG2 disease variants: Analyses reveal a dominant negative heterodimer, altered mitochondrial localization and impaired respiratory capacity. Hum. Mol. Genet. 24, 5184-5197 (2015). doi: 10.1093/hmg/ddv240; pmid: 26123486
    • (2015) Hum. Mol. Genet. , vol.24 , pp. 5184-5197
    • Young, M.J.1    Humble, M.M.2    De Balsi, K.L.3    Sun, K.Y.4    Copeland, W.C.5
  • 35
    • 40649111377 scopus 로고    scopus 로고
    • A chemical method for fast and sensitive detection of DNA synthesis in vivo
    • pmid: 18272492
    • A. Salic, T. J. Mitchison, A chemical method for fast and sensitive detection of DNA synthesis in vivo. Proc. Natl. Acad. Sci. U. S. A. 105, 2415-2420 (2008). doi: 10.1073/pnas.0712168105; pmid: 18272492
    • (2008) Proc. Natl. Acad. Sci. U. S. A. , vol.105 , pp. 2415-2420
    • Salic, A.1    Mitchison, T.J.2
  • 36
    • 7644237446 scopus 로고    scopus 로고
    • Architectural role of mitochondrial transcription factor A in maintenance of human mitochondrial DNA
    • pmid: 15509786
    • T. Kanki et al., Architectural role of mitochondrial transcription factor A in maintenance of human mitochondrial DNA. Mol. Cell. Biol. 24, 9823-9834 (2004). doi: 10.1128/MCB.24.22.9823-9834.2004; pmid: 15509786
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 9823-9834
    • Kanki, T.1
  • 37
    • 83255162641 scopus 로고    scopus 로고
    • Weaving the web of ER tubules
    • pmid: 22153070
    • J. Hu, W. A. Prinz, T. A. Rapoport, Weaving the web of ER tubules. Cell 147, 1226-1231 (2011). doi: 10.1016/j.cell.2011.11.022; pmid: 22153070
    • (2011) Cell , vol.147 , pp. 1226-1231
    • Hu, J.1    Prinz, W.A.2    Rapoport, T.A.3
  • 38
    • 0036776098 scopus 로고    scopus 로고
    • Structural organization of the endoplasmic reticulum
    • pmid: 12370207
    • G. K. Voeltz, M. M. Rolls, T. A. Rapoport, Structural organization of the endoplasmic reticulum. EMBO Rep. 3, 944-950 (2002). doi: 10.1093/embo-reports/kvf202; pmid: 12370207
    • (2002) EMBO Rep. , vol.3 , pp. 944-950
    • Voeltz, G.K.1    Rolls, M.M.2    Rapoport, T.A.3
  • 39
    • 79955488489 scopus 로고    scopus 로고
    • A 3D analysis of yeast ER structure reveals how ER domains are organized by membrane curvature
    • pmid: 21502358
    • M. West, N. Zurek, A. Hoenger, G. K. Voeltz, A 3D analysis of yeast ER structure reveals how ER domains are organized by membrane curvature. J. Cell Biol. 193, 333-346 (2011). doi: 10.1083/jcb.201011039; pmid: 21502358
    • (2011) J. Cell Biol. , vol.193 , pp. 333-346
    • West, M.1    Zurek, N.2    Hoenger, A.3    Voeltz, G.K.4
  • 40
    • 32044445021 scopus 로고    scopus 로고
    • A class of membrane proteins shaping the tubular endoplasmic reticulum
    • pmid: 16469703
    • G. K. Voeltz, W. A. Prinz, Y. Shibata, J. M. Rist, T. A. Rapoport, A class of membrane proteins shaping the tubular endoplasmic reticulum. Cell 124, 573-586 (2006). doi: 10.1016/j.cell.2005.11.047; pmid: 16469703
    • (2006) Cell , vol.124 , pp. 573-586
    • Voeltz, G.K.1    Prinz, W.A.2    Shibata, Y.3    Rist, J.M.4    Rapoport, T.A.5
  • 41
    • 79251471434 scopus 로고    scopus 로고
    • Mechanisms determining the morphology of the peripheral ER
    • pmid: 21111237
    • Y. Shibata et al., Mechanisms determining the morphology of the peripheral ER. Cell 143, 774-788 (2010). doi: 10.1016/j.cell.2010.11.007; pmid: 21111237
    • (2010) Cell , vol.143 , pp. 774-788
    • Shibata, Y.1
  • 42
    • 0035844877 scopus 로고    scopus 로고
    • Subdomain-specific localization of CLIMP-63 (p63) in the endoplasmic reticulum is mediated by its luminal alpha-helical segment
    • pmid: 11402071
    • D. R. Klopfenstein et al., Subdomain-specific localization of CLIMP-63 (p63) in the endoplasmic reticulum is mediated by its luminal alpha-helical segment. J. Cell Biol. 153, 1287-1300 (2001). pmid: 11402071
    • (2001) J. Cell Biol. , vol.153 , pp. 1287-1300
    • Klopfenstein, D.R.1
  • 43
    • 84856099972 scopus 로고    scopus 로고
    • Local zones of endoplasmic reticulum complexity confine cargo in neuronal dendrites
    • pmid: 22265418
    • T. Cui-Wang et al., Local zones of endoplasmic reticulum complexity confine cargo in neuronal dendrites. Cell 148, 309-321 (2012). doi: 10.1016/j.cell.2011.11.056; pmid: 22265418
    • (2012) Cell , vol.148 , pp. 309-321
    • Cui-Wang, T.1
  • 44
    • 49649084487 scopus 로고    scopus 로고
    • The reticulon and DP1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum
    • pmid: 18442980
    • Y. Shibata et al., The reticulon and DP1/Yop1p proteins form immobile oligomers in the tubular endoplasmic reticulum. J. Biol. Chem. 283, 18892-18904 (2008). doi: 10.1074/jbc. M800986200; pmid: 18442980
    • (2008) J. Biol. Chem. , vol.283 , pp. 18892-18904
    • Shibata, Y.1
  • 45
    • 84959512966 scopus 로고    scopus 로고
    • The emerging network of mitochondriaorganelle contacts
    • pmid: 26942669
    • A. Murley, J. Nunnari, The emerging network of mitochondriaorganelle contacts. Mol. Cell 61, 648-653 (2016). doi: 10.1016/j.molcel.2016.01.031; pmid: 26942669
    • (2016) Mol. Cell , vol.61 , pp. 648-653
    • Murley, A.1    Nunnari, J.2
  • 46
    • 84945182351 scopus 로고    scopus 로고
    • Human mitochondrial DNA-protein complexes attach to a cholesterol-rich membrane structure
    • pmid: 26478270
    • J. M. Gerhold et al., Human mitochondrial DNA-protein complexes attach to a cholesterol-rich membrane structure. Sci. Rep. 5, 15292 (2015). doi: 10.1038/srep15292; pmid: 26478270
    • (2015) Sci. Rep. , vol.5 , pp. 15292
    • Gerhold, J.M.1
  • 47
    • 84862701627 scopus 로고    scopus 로고
    • Cellular pathways of hereditary spastic paraplegia
    • pmid: 22540978
    • C. Blackstone, Cellular pathways of hereditary spastic paraplegia. Annu. Rev. Neurosci. 35, 25-47 (2012). doi: 10.1146/annurev-neuro-062111-150400; pmid: 22540978
    • (2012) Annu. Rev. Neurosci. , vol.35 , pp. 25-47
    • Blackstone, C.1
  • 48
    • 33744970020 scopus 로고    scopus 로고
    • Translating m-AAA protease function in mitochondria to hereditary spastic paraplegia
    • pmid: 16647881
    • E. I. Rugarli, T. Langer, Translating m-AAA protease function in mitochondria to hereditary spastic paraplegia. Trends Mol. Med. 12, 262-269 (2006). doi: 10.1016/j.molmed.2006.04.002; pmid: 16647881
    • (2006) Trends Mol. Med. , vol.12 , pp. 262-269
    • Rugarli, E.I.1    Langer, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.