메뉴 건너뛰기




Volumn 17, Issue 3, 2013, Pages 386-398

The mitochondrial RNA-binding protein GRSF1 localizes to RNA granules and is required for posttranscriptional mitochondrial gene expression

Author keywords

[No Author keywords available]

Indexed keywords

GRSF1 PROTEIN; MITOCHONDRIAL DNA; MITOCHONDRIAL RNA; RNA BINDING PROTEIN; UNCLASSIFIED DRUG; UNTRANSLATED RNA;

EID: 84875309966     PISSN: 15504131     EISSN: 19327420     Source Type: Journal    
DOI: 10.1016/j.cmet.2013.02.006     Document Type: Article
Times cited : (177)

References (62)
  • 1
    • 66249103703 scopus 로고    scopus 로고
    • RNA granules: Post-transcriptional and epigenetic modulators of gene expression
    • P. Anderson, and N. Kedersha RNA granules: post-transcriptional and epigenetic modulators of gene expression Nat. Rev. Mol. Cell Biol. 10 2009 430 436
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 430-436
    • Anderson, P.1    Kedersha, N.2
  • 3
    • 0242353332 scopus 로고    scopus 로고
    • Identification and characterization of a common set of complex i assembly intermediates in mitochondria from patients with complex i deficiency
    • H. Antonicka, I. Ogilvie, T. Taivassalo, R.P. Anitori, R.G. Haller, J. Vissing, N.G. Kennaway, and E.A. Shoubridge Identification and characterization of a common set of complex I assembly intermediates in mitochondria from patients with complex I deficiency J. Biol. Chem. 278 2003 43081 43088
    • (2003) J. Biol. Chem. , vol.278 , pp. 43081-43088
    • Antonicka, H.1    Ogilvie, I.2    Taivassalo, T.3    Anitori, R.P.4    Haller, R.G.5    Vissing, J.6    Kennaway, N.G.7    Shoubridge, E.A.8
  • 4
    • 33744752749 scopus 로고    scopus 로고
    • The molecular basis for tissue specificity of the oxidative phosphorylation deficiencies in patients with mutations in the mitochondrial translation factor EFG1
    • H. Antonicka, F. Sasarman, N.G. Kennaway, and E.A. Shoubridge The molecular basis for tissue specificity of the oxidative phosphorylation deficiencies in patients with mutations in the mitochondrial translation factor EFG1 Hum. Mol. Genet. 15 2006 1835 1846
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 1835-1846
    • Antonicka, H.1    Sasarman, F.2    Kennaway, N.G.3    Shoubridge, E.A.4
  • 6
    • 67849130819 scopus 로고    scopus 로고
    • A computational screen for regulators of oxidative phosphorylation implicates SLIRP in mitochondrial RNA homeostasis
    • 10.1371/journal.pgen.1000590
    • J.M. Baughman, R. Nilsson, V.M. Gohil, D.H. Arlow, Z. Gauhar, and V.K. Mootha A computational screen for regulators of oxidative phosphorylation implicates SLIRP in mitochondrial RNA homeostasis PLoS Genet. 5 2009 e1000590 10.1371/journal.pgen.1000590
    • (2009) PLoS Genet. , vol.5 , pp. 1000590
    • Baughman, J.M.1    Nilsson, R.2    Gohil, V.M.3    Arlow, D.H.4    Gauhar, Z.5    Mootha, V.K.6
  • 7
    • 41249098355 scopus 로고    scopus 로고
    • The layered structure of human mitochondrial DNA nucleoids
    • D.F. Bogenhagen, D. Rousseau, and S. Burke The layered structure of human mitochondrial DNA nucleoids J. Biol. Chem. 283 2008 3665 3675
    • (2008) J. Biol. Chem. , vol.283 , pp. 3665-3675
    • Bogenhagen, D.F.1    Rousseau, D.2    Burke, S.3
  • 9
    • 83255188980 scopus 로고    scopus 로고
    • Superresolution fluorescence imaging of mitochondrial nucleoids reveals their spatial range, limits, and membrane interaction
    • T.A. Brown, A.N. Tkachuk, G. Shtengel, B.G. Kopek, D.F. Bogenhagen, H.F. Hess, and D.A. Clayton Superresolution fluorescence imaging of mitochondrial nucleoids reveals their spatial range, limits, and membrane interaction Mol. Cell. Biol. 31 2011 4994 5010
    • (2011) Mol. Cell. Biol. , vol.31 , pp. 4994-5010
    • Brown, T.A.1    Tkachuk, A.N.2    Shtengel, G.3    Kopek, B.G.4    Bogenhagen, D.F.5    Hess, H.F.6    Clayton, D.A.7
  • 10
    • 85046980054 scopus 로고    scopus 로고
    • Involvement of human ELAC2 gene product in 3′ end processing of mitochondrial tRNAs
    • L.K. Brzezniak, M. Bijata, R.J. Szczesny, and P.P. Stepien Involvement of human ELAC2 gene product in 3′ end processing of mitochondrial tRNAs RNA Biol. 8 2011 616 626
    • (2011) RNA Biol. , vol.8 , pp. 616-626
    • Brzezniak, L.K.1    Bijata, M.2    Szczesny, R.J.3    Stepien, P.P.4
  • 11
    • 72149095755 scopus 로고    scopus 로고
    • Eukaryotic stress granules: The ins and outs of translation
    • J.R. Buchan, and R. Parker Eukaryotic stress granules: the ins and outs of translation Mol. Cell 36 2009 932 941
    • (2009) Mol. Cell , vol.36 , pp. 932-941
    • Buchan, J.R.1    Parker, R.2
  • 12
    • 84862229118 scopus 로고    scopus 로고
    • 5′-UTR RNA G-quadruplexes: Translation regulation and targeting
    • A. Bugaut, and S. Balasubramanian 5′-UTR RNA G-quadruplexes: translation regulation and targeting Nucleic Acids Res. 40 2012 4727 4741
    • (2012) Nucleic Acids Res. , vol.40 , pp. 4727-4741
    • Bugaut, A.1    Balasubramanian, S.2
  • 13
    • 85052429967 scopus 로고    scopus 로고
    • Combined immunofluorescence, RNA fluorescent in situ hybridization, and DNA fluorescent in situ hybridization to study chromatin changes, transcriptional activity, nuclear organization, and X-chromosome inactivation
    • J. Chaumeil, S. Augui, J.C. Chow, and E. Heard Combined immunofluorescence, RNA fluorescent in situ hybridization, and DNA fluorescent in situ hybridization to study chromatin changes, transcriptional activity, nuclear organization, and X-chromosome inactivation Methods Mol. Biol. 463 2008 297 308
    • (2008) Methods Mol. Biol. , vol.463 , pp. 297-308
    • Chaumeil, J.1    Augui, S.2    Chow, J.C.3    Heard, E.4
  • 15
    • 84869822219 scopus 로고    scopus 로고
    • LRPPRC/SLIRP suppresses PNPase-mediated mRNA decay and promotes polyadenylation in human mitochondria
    • T. Chujo, T. Ohira, Y. Sakaguchi, N. Goshima, N. Nomura, A. Nagao, and T. Suzuki LRPPRC/SLIRP suppresses PNPase-mediated mRNA decay and promotes polyadenylation in human mitochondria Nucleic Acids Res. 40 2012 8033 8047
    • (2012) Nucleic Acids Res. , vol.40 , pp. 8033-8047
    • Chujo, T.1    Ohira, T.2    Sakaguchi, Y.3    Goshima, N.4    Nomura, N.5    Nagao, A.6    Suzuki, T.7
  • 16
    • 0035900649 scopus 로고    scopus 로고
    • Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function
    • J.C. Darnell, K.B. Jensen, P. Jin, V. Brown, S.T. Warren, and R.B. Darnell Fragile X mental retardation protein targets G quartet mRNAs important for neuronal function Cell 107 2001 489 499
    • (2001) Cell , vol.107 , pp. 489-499
    • Darnell, J.C.1    Jensen, K.B.2    Jin, P.3    Brown, V.4    Warren, S.T.5    Darnell, R.B.6
  • 17
    • 67349234111 scopus 로고    scopus 로고
    • Pentatricopeptide repeat domain protein 3 associates with the mitochondrial small ribosomal subunit and regulates translation
    • S.M. Davies, O. Rackham, A.M. Shearwood, K.L. Hamilton, R. Narsai, J. Whelan, and A. Filipovska Pentatricopeptide repeat domain protein 3 associates with the mitochondrial small ribosomal subunit and regulates translation FEBS Lett. 583 2009 1853 1858
    • (2009) FEBS Lett. , vol.583 , pp. 1853-1858
    • Davies, S.M.1    Rackham, O.2    Shearwood, A.M.3    Hamilton, K.L.4    Narsai, R.5    Whelan, J.6    Filipovska, A.7
  • 19
    • 44449166478 scopus 로고    scopus 로고
    • RNA-binding proteins and post-transcriptional gene regulation
    • T. Glisovic, J.L. Bachorik, J. Yong, and G. Dreyfuss RNA-binding proteins and post-transcriptional gene regulation FEBS Lett. 582 2008 1977 1986
    • (2008) FEBS Lett. , vol.582 , pp. 1977-1986
    • Glisovic, T.1    Bachorik, J.L.2    Yong, J.3    Dreyfuss, G.4
  • 20
    • 0031682732 scopus 로고    scopus 로고
    • The deafness-associated mitochondrial DNA mutation at position 7445, which affects tRNASer(UCN) precursor processing, has long-range effects on NADH dehydrogenase subunit ND6 gene expression
    • M.X. Guan, J.A. Enriquez, N. Fischel-Ghodsian, R.S. Puranam, C.P. Lin, M.A. Maw, and G. Attardi The deafness-associated mitochondrial DNA mutation at position 7445, which affects tRNASer(UCN) precursor processing, has long-range effects on NADH dehydrogenase subunit ND6 gene expression Mol. Cell. Biol. 18 1998 5868 5879
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 5868-5879
    • Guan, M.X.1    Enriquez, J.A.2    Fischel-Ghodsian, N.3    Puranam, R.S.4    Lin, C.P.5    Maw, M.A.6    Attardi, G.7
  • 21
    • 80054966979 scopus 로고    scopus 로고
    • Contacts between mammalian mitochondrial translational initiation factor 3 and ribosomal proteins in the small subunit
    • M.E. Haque, H. Koc, H. Cimen, E.C. Koc, and L.L. Spremulli Contacts between mammalian mitochondrial translational initiation factor 3 and ribosomal proteins in the small subunit Biochim. Biophys. Acta 1814 2011 1779 1784
    • (2011) Biochim. Biophys. Acta , vol.1814 , pp. 1779-1784
    • Haque, M.E.1    Koc, H.2    Cimen, H.3    Koc, E.C.4    Spremulli, L.L.5
  • 23
    • 0016153699 scopus 로고
    • Assembly mapping of 30 S ribosomal proteins from Escherichia coli. Further studies
    • W.A. Held, B. Ballou, S. Mizushima, and M. Nomura Assembly mapping of 30 S ribosomal proteins from Escherichia coli. Further studies J. Biol. Chem. 249 1974 3103 3111
    • (1974) J. Biol. Chem. , vol.249 , pp. 3103-3111
    • Held, W.A.1    Ballou, B.2    Mizushima, S.3    Nomura, M.4
  • 24
    • 54549088876 scopus 로고    scopus 로고
    • RNase P without RNA: Identification and functional reconstitution of the human mitochondrial tRNA processing enzyme
    • J. Holzmann, P. Frank, E. Löffler, K.L. Bennett, C. Gerner, and W. Rossmanith RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme Cell 135 2008 462 474
    • (2008) Cell , vol.135 , pp. 462-474
    • Holzmann, J.1    Frank, P.2    Löffler, E.3    Bennett, K.L.4    Gerner, C.5    Rossmanith, W.6
  • 25
    • 3242705680 scopus 로고    scopus 로고
    • The functional organization of mitochondrial genomes in human cells
    • 10.1186/1741-7007-2-9
    • F.J. Iborra, H. Kimura, and P.R. Cook The functional organization of mitochondrial genomes in human cells BMC Biol. 2 2004 9 10.1186/1741-7007-2-9
    • (2004) BMC Biol. , vol.2 , pp. 9
    • Iborra, F.J.1    Kimura, H.2    Cook, P.R.3
  • 26
    • 58149502545 scopus 로고    scopus 로고
    • Role of cellular RNA processing factors in human immunodeficiency virus type 1 mRNA metabolism, replication, and infectivity
    • J.A. Jablonski, and M. Caputi Role of cellular RNA processing factors in human immunodeficiency virus type 1 mRNA metabolism, replication, and infectivity J. Virol. 83 2009 981 992
    • (2009) J. Virol. , vol.83 , pp. 981-992
    • Jablonski, J.A.1    Caputi, M.2
  • 27
    • 0033616764 scopus 로고    scopus 로고
    • Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein
    • J. Jiang, Y. Zhang, A.R. Krainer, and R.M. Xu Crystal structure of human p32, a doughnut-shaped acidic mitochondrial matrix protein Proc. Natl. Acad. Sci. USA 96 1999 3572 3577
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 3572-3577
    • Jiang, J.1    Zhang, Y.2    Krainer, A.R.3    Xu, R.M.4
  • 28
    • 0036784592 scopus 로고    scopus 로고
    • Selective translation of eukaryotic mRNAs: Functional molecular analysis of GRSF-1, a positive regulator of influenza virus protein synthesis
    • J.C. Kash, D.M. Cunningham, M.W. Smit, Y. Park, D. Fritz, J. Wilusz, and M.G. Katze Selective translation of eukaryotic mRNAs: functional molecular analysis of GRSF-1, a positive regulator of influenza virus protein synthesis J. Virol. 76 2002 10417 10426
    • (2002) J. Virol. , vol.76 , pp. 10417-10426
    • Kash, J.C.1    Cunningham, D.M.2    Smit, M.W.3    Park, Y.4    Fritz, D.5    Wilusz, J.6    Katze, M.G.7
  • 29
    • 34548495323 scopus 로고    scopus 로고
    • The mitochondrial transcription factor TFAM coordinates the assembly of multiple DNA molecules into nucleoid-like structures
    • B.A. Kaufman, N. Durisic, J.M. Mativetsky, S. Costantino, M.A. Hancock, P. Grutter, and E.A. Shoubridge The mitochondrial transcription factor TFAM coordinates the assembly of multiple DNA molecules into nucleoid-like structures Mol. Biol. Cell 18 2007 3225 3236
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3225-3236
    • Kaufman, B.A.1    Durisic, N.2    Mativetsky, J.M.3    Costantino, S.4    Hancock, M.A.5    Grutter, P.6    Shoubridge, E.A.7
  • 30
    • 34250735674 scopus 로고    scopus 로고
    • RNA regulons: Coordination of post-transcriptional events
    • J.D. Keene RNA regulons: coordination of post-transcriptional events Nat. Rev. Genet. 8 2007 533 543
    • (2007) Nat. Rev. Genet. , vol.8 , pp. 533-543
    • Keene, J.D.1
  • 31
    • 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
    • C. Kukat, C.A. Wurm, H. Spåhr, M. Falkenberg, N.G. Larsson, and S. Jakobs Super-resolution microscopy reveals that mammalian mitochondrial nucleoids have a uniform size and frequently contain a single copy of mtDNA Proc. Natl. Acad. Sci. USA 108 2011 13534 13539
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 13534-13539
    • Kukat, C.1    Wurm, C.A.2    Spåhr, H.3    Falkenberg, M.4    Larsson, N.G.5    Jakobs, S.6
  • 32
    • 70349777791 scopus 로고    scopus 로고
    • Oxidative phosphorylation: Synthesis of mitochondrially encoded proteins and assembly of individual structural subunits into functional holoenzyme complexes
    • S.C. Leary, and F. Sasarman Oxidative phosphorylation: synthesis of mitochondrially encoded proteins and assembly of individual structural subunits into functional holoenzyme complexes Methods Mol. Biol. 554 2009 143 162
    • (2009) Methods Mol. Biol. , vol.554 , pp. 143-162
    • Leary, S.C.1    Sasarman, F.2
  • 33
    • 21244490466 scopus 로고    scopus 로고
    • Dissecting Wnt/beta-catenin signaling during gastrulation using RNA interference in mouse embryos
    • H. Lickert, B. Cox, C. Wehrle, M.M. Taketo, R. Kemler, and J. Rossant Dissecting Wnt/beta-catenin signaling during gastrulation using RNA interference in mouse embryos Development 132 2005 2599 2609
    • (2005) Development , vol.132 , pp. 2599-2609
    • Lickert, H.1    Cox, B.2    Wehrle, C.3    Taketo, M.M.4    Kemler, R.5    Rossant, J.6
  • 35
    • 34249316905 scopus 로고    scopus 로고
    • RNA-binding proteins: Modular design for efficient function
    • B.M. Lunde, C. Moore, and G. Varani RNA-binding proteins: modular design for efficient function Nat. Rev. Mol. Cell Biol. 8 2007 479 490
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 479-490
    • Lunde, B.M.1    Moore, C.2    Varani, G.3
  • 36
    • 84864485953 scopus 로고    scopus 로고
    • QGRS-H Predictor: A web server for predicting homologous quadruplex forming G-rich sequence motifs in nucleotide sequences
    • C. Menendez, S. Frees, and P.S. Bagga QGRS-H Predictor: a web server for predicting homologous quadruplex forming G-rich sequence motifs in nucleotide sequences Nucleic Acids Res. 40 Web Server issue 2012 W96 W103
    • (2012) Nucleic Acids Res. , vol.40 , Issue.WEB SERVER ISSUE
    • Menendez, C.1    Frees, S.2    Bagga, P.S.3
  • 39
    • 0037029122 scopus 로고    scopus 로고
    • Evolution of a protein-rich mitochondrial ribosome: Implications for human genetic disease
    • T.W. O'Brien Evolution of a protein-rich mitochondrial ribosome: implications for human genetic disease Gene 286 2002 73 79
    • (2002) Gene , vol.286 , pp. 73-79
    • O'Brien, T.W.1
  • 41
    • 0000075974 scopus 로고    scopus 로고
    • Regulation of eukaryotic protein synthesis: Selective influenza viral mRNA translation is mediated by the cellular RNA-binding protein GRSF-1
    • Y.W. Park, J. Wilusz, and M.G. Katze Regulation of eukaryotic protein synthesis: selective influenza viral mRNA translation is mediated by the cellular RNA-binding protein GRSF-1 Proc. Natl. Acad. Sci. USA 96 1999 6694 6699
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6694-6699
    • Park, Y.W.1    Wilusz, J.2    Katze, M.G.3
  • 42
    • 0028246701 scopus 로고
    • GRSF-1: A poly(A)+ mRNA binding protein which interacts with a conserved G-rich element
    • Z. Qian, and J. Wilusz GRSF-1: a poly(A)+ mRNA binding protein which interacts with a conserved G-rich element Nucleic Acids Res. 22 1994 2334 2343
    • (1994) Nucleic Acids Res. , vol.22 , pp. 2334-2343
    • Qian, Z.1    Wilusz, J.2
  • 43
    • 81755161589 scopus 로고    scopus 로고
    • Long noncoding RNAs are generated from the mitochondrial genome and regulated by nuclear-encoded proteins
    • O. Rackham, A.M. Shearwood, T.R. Mercer, S.M. Davies, J.S. Mattick, and A. Filipovska Long noncoding RNAs are generated from the mitochondrial genome and regulated by nuclear-encoded proteins RNA 17 2011 2085 2093
    • (2011) RNA , vol.17 , pp. 2085-2093
    • Rackham, O.1    Shearwood, A.M.2    Mercer, T.R.3    Davies, S.M.4    Mattick, J.S.5    Filipovska, A.6
  • 44
    • 84862227617 scopus 로고    scopus 로고
    • The post-transcriptional life of mammalian mitochondrial RNA
    • J. Rorbach, and M. Minczuk The post-transcriptional life of mammalian mitochondrial RNA Biochem. J. 444 2012 357 373
    • (2012) Biochem. J. , vol.444 , pp. 357-373
    • Rorbach, J.1    Minczuk, M.2
  • 47
    • 84856325285 scopus 로고    scopus 로고
    • Radioactive labeling of mitochondrial translation products in cultured cells
    • F. Sasarman, and E.A. Shoubridge Radioactive labeling of mitochondrial translation products in cultured cells Methods Mol. Biol. 837 2012 207 217
    • (2012) Methods Mol. Biol. , vol.837 , pp. 207-217
    • Sasarman, F.1    Shoubridge, E.A.2
  • 48
    • 77950901962 scopus 로고    scopus 로고
    • LRPPRC and SLIRP interact in a ribonucleoprotein complex that regulates posttranscriptional gene expression in mitochondria
    • LSFC Consortium
    • F. Sasarman, C. Brunel-Guitton, H. Antonicka, T. Wai, E.A. Shoubridge LSFC Consortium LRPPRC and SLIRP interact in a ribonucleoprotein complex that regulates posttranscriptional gene expression in mitochondria Mol. Biol. Cell 21 2010 1315 1323
    • (2010) Mol. Biol. Cell , vol.21 , pp. 1315-1323
    • Sasarman, F.1    Brunel-Guitton, C.2    Antonicka, H.3    Wai, T.4    Shoubridge, E.A.5
  • 49
    • 34250313662 scopus 로고    scopus 로고
    • Members of the heterogeneous nuclear ribonucleoprotein H family activate splicing of an HIV-1 splicing substrate by promoting formation of ATP-dependent spliceosomal complexes
    • M.C. Schaub, S.R. Lopez, and M. Caputi Members of the heterogeneous nuclear ribonucleoprotein H family activate splicing of an HIV-1 splicing substrate by promoting formation of ATP-dependent spliceosomal complexes J. Biol. Chem. 282 2007 13617 13626
    • (2007) J. Biol. Chem. , vol.282 , pp. 13617-13626
    • Schaub, M.C.1    Lopez, S.R.2    Caputi, M.3
  • 50
    • 56549095978 scopus 로고    scopus 로고
    • Pentatricopeptide repeat proteins: A socket set for organelle gene expression
    • C. Schmitz-Linneweber, and I. Small Pentatricopeptide repeat proteins: a socket set for organelle gene expression Trends Plant Sci. 13 2008 663 670
    • (2008) Trends Plant Sci. , vol.13 , pp. 663-670
    • Schmitz-Linneweber, C.1    Small, I.2
  • 52
    • 22544448652 scopus 로고    scopus 로고
    • Polyadenylation and degradation of human mitochondrial RNA: The prokaryotic past leaves its mark
    • S. Slomovic, D. Laufer, D. Geiger, and G. Schuster Polyadenylation and degradation of human mitochondrial RNA: the prokaryotic past leaves its mark Mol. Cell. Biol. 25 2005 6427 6435
    • (2005) Mol. Cell. Biol. , vol.25 , pp. 6427-6435
    • Slomovic, S.1    Laufer, D.2    Geiger, D.3    Schuster, G.4
  • 54
    • 28444479853 scopus 로고    scopus 로고
    • An assembly landscape for the 30S ribosomal subunit
    • M.W. Talkington, G. Siuzdak, and J.R. Williamson An assembly landscape for the 30S ribosomal subunit Nature 438 2005 628 632
    • (2005) Nature , vol.438 , pp. 628-632
    • Talkington, M.W.1    Siuzdak, G.2    Williamson, J.R.3
  • 56
    • 46249086161 scopus 로고    scopus 로고
    • Translational regulation of glutathione peroxidase 4 expression through guanine-rich sequence-binding factor 1 is essential for embryonic brain development
    • C. Ufer, C.C. Wang, M. Fähling, H. Schiebel, B.J. Thiele, E.E. Billett, H. Kuhn, and A. Borchert Translational regulation of glutathione peroxidase 4 expression through guanine-rich sequence-binding factor 1 is essential for embryonic brain development Genes Dev. 22 2008 1838 1850
    • (2008) Genes Dev. , vol.22 , pp. 1838-1850
    • Ufer, C.1    Wang, C.C.2    Fähling, M.3    Schiebel, H.4    Thiele, B.J.5    Billett, E.E.6    Kuhn, H.7    Borchert, A.8
  • 57
    • 80053045739 scopus 로고    scopus 로고
    • Molecular mechanisms of long noncoding RNAs
    • K.C. Wang, and H.Y. Chang Molecular mechanisms of long noncoding RNAs Mol. Cell 43 2011 904 914
    • (2011) Mol. Cell , vol.43 , pp. 904-914
    • Wang, K.C.1    Chang, H.Y.2
  • 59
    • 70350012303 scopus 로고    scopus 로고
    • Isolation of mitochondria-associated membranes and mitochondria from animal tissues and cells
    • M.R. Wieckowski, C. Giorgi, M. Lebiedzinska, J. Duszynski, and P. Pinton Isolation of mitochondria-associated membranes and mitochondria from animal tissues and cells Nat. Protoc. 4 2009 1582 1590
    • (2009) Nat. Protoc. , vol.4 , pp. 1582-1590
    • Wieckowski, M.R.1    Giorgi, C.2    Lebiedzinska, M.3    Duszynski, J.4    Pinton, P.5
  • 60
    • 56049093869 scopus 로고    scopus 로고
    • Disruption of a mitochondrial RNA-binding protein gene results in decreased cytochrome b expression and a marked reduction in ubiquinol-cytochrome c reductase activity in mouse heart mitochondria
    • F. Xu, C. Ackerley, M.C. Maj, J.B. Addis, V. Levandovskiy, J. Lee, N. Mackay, J.M. Cameron, and B.H. Robinson Disruption of a mitochondrial RNA-binding protein gene results in decreased cytochrome b expression and a marked reduction in ubiquinol-cytochrome c reductase activity in mouse heart mitochondria Biochem. J. 416 2008 15 26
    • (2008) Biochem. J. , vol.416 , pp. 15-26
    • Xu, F.1    Ackerley, C.2    Maj, M.C.3    Addis, J.B.4    Levandovskiy, V.5    Lee, J.6    Mackay, N.7    Cameron, J.M.8    Robinson, B.H.9
  • 61
    • 84868109828 scopus 로고    scopus 로고
    • P32/gC1qR is indispensable for fetal development and mitochondrial translation: Importance of its RNA-binding ability
    • M. Yagi, T. Uchiumi, S. Takazaki, B. Okuno, M. Nomura, S. Yoshida, T. Kanki, and D. Kang p32/gC1qR is indispensable for fetal development and mitochondrial translation: importance of its RNA-binding ability Nucleic Acids Res. 40 2012 9717 9737
    • (2012) Nucleic Acids Res. , vol.40 , pp. 9717-9737
    • Yagi, M.1    Uchiumi, T.2    Takazaki, S.3    Okuno, B.4    Nomura, M.5    Yoshida, S.6    Kanki, T.7    Kang, D.8
  • 62
    • 0032760675 scopus 로고    scopus 로고
    • Expression and functional analysis of SURF1 in Leigh syndrome patients with cytochrome c oxidase deficiency
    • J. Yao, and E.A. Shoubridge Expression and functional analysis of SURF1 in Leigh syndrome patients with cytochrome c oxidase deficiency Hum. Mol. Genet. 8 1999 2541 2549
    • (1999) Hum. Mol. Genet. , vol.8 , pp. 2541-2549
    • Yao, J.1    Shoubridge, E.A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.