메뉴 건너뛰기




Volumn 367, Issue 1, 2017, Pages 5-20

The process of mammalian mitochondrial protein synthesis

Author keywords

Mitochondria; Mitochondrial diseases; Mitochondrial translation; Mitoribosome; Protein synthesis

Indexed keywords

GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE; MEMBRANE PROTEIN; METHYLTRANSFERASE; MITOCHONDRIAL PROTEIN; MITOCHONDRIAL PROTEIN L37; MITOCHONDRIAL PROTEIN L65; MITOCHONDRIAL PROTEIN S29; PROTEIN PTCD3; REACTIVE OXYGEN METABOLITE; UNCLASSIFIED DRUG;

EID: 84978062509     PISSN: 0302766X     EISSN: 14320878     Source Type: Journal    
DOI: 10.1007/s00441-016-2456-0     Document Type: Review
Times cited : (101)

References (142)
  • 1
    • 84907587253 scopus 로고    scopus 로고
    • Ribosome rescue and translation termination at non-standard stop codons by ICT1 in mammalian mitochondria
    • PID: 25233460
    • Akabane S, Ueda T, Nierhaus KH, Takeuchi N (2014) Ribosome rescue and translation termination at non-standard stop codons by ICT1 in mammalian mitochondria. PLoS Genet 10:e1004616
    • (2014) PLoS Genet , vol.10
    • Akabane, S.1    Ueda, T.2    Nierhaus, K.H.3    Takeuchi, N.4
  • 3
    • 84927930436 scopus 로고    scopus 로고
    • Ribosome. The structure of the human mitochondrial mitoribosome
    • COI: 1:CAS:528:DC%2BC2MXls1Wmurs%3D, PID: 25838379
    • Amunts A, Brown A, Toots J, Scheres SH, Ramakrishnan V (2015) Ribosome. The structure of the human mitochondrial mitoribosome. Science 348:95–98
    • (2015) Science , vol.348 , pp. 95-98
    • Amunts, A.1    Brown, A.2    Toots, J.3    Scheres, S.H.4    Ramakrishnan, V.5
  • 5
    • 84923069270 scopus 로고    scopus 로고
    • Mitochondrial RNA granules are centers for posttranscriptional RNA processing and ribosome biogenesis
    • COI: 1:CAS:528:DC%2BC2MXivVSjur8%3D
    • Antonicka H, Shoubridge EA (2015) Mitochondrial RNA granules are centers for posttranscriptional RNA processing and ribosome biogenesis. Cell Rep 10:920–932. doi:10.1016/j.celrep.2015.01.030
    • (2015) Cell Rep , vol.10 , pp. 920-932
    • Antonicka, H.1    Shoubridge, E.A.2
  • 6
    • 84875309966 scopus 로고    scopus 로고
    • The mitochondrial RNA-binding protein GRSF1 localizes to RNA granules and is required for posttranscriptional mitochondrial gene expression
    • COI: 1:CAS:528:DC%2BC3sXktFWru70%3D, PID: 23473033
    • Antonicka H, Sasarman F, Nishimura T, Paupe V, Shoubridge EA (2013) The mitochondrial RNA-binding protein GRSF1 localizes to RNA granules and is required for posttranscriptional mitochondrial gene expression. Cell Metab 17:386–398
    • (2013) Cell Metab , vol.17 , pp. 386-398
    • Antonicka, H.1    Sasarman, F.2    Nishimura, T.3    Paupe, V.4    Shoubridge, E.A.5
  • 7
    • 0034637111 scopus 로고    scopus 로고
    • The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution
    • COI: 1:STN:280:DC%2BD3cvgslCgsA%3D%3D, PID: 10937989
    • Ban N, Nissen P, Hansen J, Moore PB, Steitz TA (2000) The complete atomic structure of the large ribosomal subunit at 2.4 Å resolution. Science 289:905–920
    • (2000) Science , vol.289 , pp. 905-920
    • Ban, N.1    Nissen, P.2    Hansen, J.3    Moore, P.B.4    Steitz, T.A.5
  • 9
    • 84897527933 scopus 로고    scopus 로고
    • Initial steps in RNA processing and ribosome assembly occur at mitochondrial DNA nucleoids
    • COI: 1:CAS:528:DC%2BC2cXlvFeqtrk%3D, PID: 24703694
    • Bogenhagen DF, Martin DW, Koller A (2014) Initial steps in RNA processing and ribosome assembly occur at mitochondrial DNA nucleoids. Cell Metab 19:618–629
    • (2014) Cell Metab , vol.19 , pp. 618-629
    • Bogenhagen, D.F.1    Martin, D.W.2    Koller, A.3
  • 10
    • 77953790077 scopus 로고    scopus 로고
    • RNA turnover in human mitochondria: more questions than answers?
    • COI: 1:CAS:528:DC%2BC3cXnvV2rtb4%3D, PID: 20117077
    • Borowski LS, Szczesny RJ, Brzezniak LK, Stepien PP (2010) RNA turnover in human mitochondria: more questions than answers? Biochim Biophys Acta 1797:1066–1070
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 1066-1070
    • Borowski, L.S.1    Szczesny, R.J.2    Brzezniak, L.K.3    Stepien, P.P.4
  • 11
    • 84875307449 scopus 로고    scopus 로고
    • Human mitochondrial RNA decay mediated by PNPase-hSuv3 complex takes place in distinct foci
    • COI: 1:CAS:528:DC%2BC3sXhtFyjtbs%3D, PID: 23221631
    • Borowski LS, Dziembowski A, Hejnowicz MS, Stepien PP, Szczesny RJ (2013) Human mitochondrial RNA decay mediated by PNPase-hSuv3 complex takes place in distinct foci. Nucleic Acids Res 41:1223–1240
    • (2013) Nucleic Acids Res , vol.41 , pp. 1223-1240
    • Borowski, L.S.1    Dziembowski, A.2    Hejnowicz, M.S.3    Stepien, P.P.4    Szczesny, R.J.5
  • 15
    • 0034617088 scopus 로고    scopus 로고
    • Interaction of mitochondrial elongation factor Tu with aminoacyl-tRNA and elongation factor Ts
    • COI: 1:CAS:528:DC%2BD3cXkvVyiurc%3D, PID: 10801827
    • Cai YC, Bullard JM, Thompson NL, Spremulli LL (2000) Interaction of mitochondrial elongation factor Tu with aminoacyl-tRNA and elongation factor Ts. J Biol Chem 275:20308–20314
    • (2000) J Biol Chem , vol.275 , pp. 20308-20314
    • Cai, Y.C.1    Bullard, J.M.2    Thompson, N.L.3    Spremulli, L.L.4
  • 18
    • 77956249282 scopus 로고    scopus 로고
    • Preferential selection of the 5'-terminal start codon on leaderless mRNAs by mammalian mitochondrial ribosomes
    • COI: 1:CAS:528:DC%2BC3cXhtVOnsLbI, PID: 20610392
    • Christian BE, Spremulli LL (2010) Preferential selection of the 5'-terminal start codon on leaderless mRNAs by mammalian mitochondrial ribosomes. J Biol Chem 285:28379–28386
    • (2010) J Biol Chem , vol.285 , pp. 28379-28386
    • Christian, B.E.1    Spremulli, L.L.2
  • 19
    • 84864319440 scopus 로고    scopus 로고
    • Mechanism of protein biosynthesis in mammalian mitochondria
    • COI: 1:CAS:528:DC%2BC38XhtVyksbnP, PID: 22172991
    • Christian BE, Spremulli LL (2012) Mechanism of protein biosynthesis in mammalian mitochondria. Biochim Biophys Acta 1819:1035–1054
    • (2012) Biochim Biophys Acta , vol.1819 , pp. 1035-1054
    • Christian, B.E.1    Spremulli, L.L.2
  • 20
    • 84937777305 scopus 로고    scopus 로고
    • Response to "Ribosome rescue and translation termination at non-standard stop codons by ICT1 in mammalian mitochondria"
    • PID: 26087262
    • Chrzanowska-Lightowlers ZM, Lightowlers RN (2015) Response to "Ribosome rescue and translation termination at non-standard stop codons by ICT1 in mammalian mitochondria". PLoS Genet 11:e1005227
    • (2015) PLoS Genet , vol.11
    • Chrzanowska-Lightowlers, Z.M.1    Lightowlers, R.N.2
  • 21
    • 80053402383 scopus 로고    scopus 로고
    • Termination of protein synthesis in mammalian mitochondria
    • COI: 1:CAS:528:DC%2BC3MXht1Cqt7rL, PID: 21873426
    • Chrzanowska-Lightowlers ZM, Pajak A, Lightowlers RN (2011) Termination of protein synthesis in mammalian mitochondria. J Biol Chem 286:34479–34485
    • (2011) J Biol Chem , vol.286 , pp. 34479-34485
    • Chrzanowska-Lightowlers, Z.M.1    Pajak, A.2    Lightowlers, R.N.3
  • 22
    • 84869822219 scopus 로고    scopus 로고
    • LRPPRC/SLIRP suppresses PNPase-mediated mRNA decay and promotes polyadenylation in human mitochondria
    • COI: 1:CAS:528:DC%2BC38XhtlKltrvJ, PID: 22661577
    • Chujo T, Ohira T, Sakaguchi Y, Goshima N, Nomura N, Nagao A, Suzuki T (2012) LRPPRC/SLIRP suppresses PNPase-mediated mRNA decay and promotes polyadenylation in human mitochondria. Nucleic Acids Res 40:8033–8047
    • (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
  • 23
    • 78650306521 scopus 로고    scopus 로고
    • Small RNA sorting: matchmaking for argonautes
    • COI: 1:CAS:528:DC%2BC3cXhsFOiu7rE, PID: 21116305
    • Czech B, Hannon GJ (2011) Small RNA sorting: matchmaking for argonautes. Nat Rev Genet 12:19–31
    • (2011) Nat Rev Genet , vol.12 , pp. 19-31
    • Czech, B.1    Hannon, G.J.2
  • 26
    • 77956658496 scopus 로고    scopus 로고
    • Human ERAL1 is a mitochondrial RNA chaperone involved in the assembly of the 28S small mitochondrial ribosomal subunit
    • COI: 1:CAS:528:DC%2BC3cXhtVyrtbrM, PID: 20604745
    • Dennerlein S, Rozanska A, Wydro M, Chrzanowska-Lightowlers ZM, Lightowlers RN (2010) Human ERAL1 is a mitochondrial RNA chaperone involved in the assembly of the 28S small mitochondrial ribosomal subunit. Biochem J 430:551–558
    • (2010) Biochem J , vol.430 , pp. 551-558
    • Dennerlein, S.1    Rozanska, A.2    Wydro, M.3    Chrzanowska-Lightowlers, Z.M.4    Lightowlers, R.N.5
  • 27
    • 0025786898 scopus 로고
    • Bovine mitochondrial ribosomes possess a high affinity binding site for guanine nucleotide
    • COI: 1:CAS:528:DyaK3MXksVClsb0%3D, PID: 2033053
    • Denslow ND, Andersg JC, O’Brien TW (1991) Bovine mitochondrial ribosomes possess a high affinity binding site for guanine nucleotide. J Biol Chem 266:9586–9590
    • (1991) J Biol Chem , vol.266 , pp. 9586-9590
    • Denslow, N.D.1    Andersg, J.C.2    O’Brien, T.W.3
  • 28
    • 84896862486 scopus 로고    scopus 로고
    • The mitochondrial aminoacyl tRNA synthetases: genes and syndromes
    • PID: 24639874
    • Diodato D, Ghezzi D, Tiranti V (2014) The mitochondrial aminoacyl tRNA synthetases: genes and syndromes. Int J Cell Biol 2014:787956
    • (2014) Int J Cell Biol , vol.2014 , pp. 787956-789590
    • Diodato, D.1    Ghezzi, D.2    Tiranti, V.3
  • 29
    • 0017881089 scopus 로고
    • Modification of mitochondrial ribosomal RNA from hamster cells: the presence of GmG and late-methylated UmGmU in the large subunit (17S) RNA
    • COI: 1:CAS:528:DyaE1cXkvVGqtbg%3D, PID: 671547
    • Dubin DT, Taylor RH (1978) Modification of mitochondrial ribosomal RNA from hamster cells: the presence of GmG and late-methylated UmGmU in the large subunit (17S) RNA. J Mol Biol 121:523–540
    • (1978) J Mol Biol , vol.121 , pp. 523-540
    • Dubin, D.T.1    Taylor, R.H.2
  • 30
    • 34548627532 scopus 로고    scopus 로고
    • DNA replication and transcription in mammalian mitochondria
    • COI: 1:CAS:528:DC%2BD2sXhtVehtbzK, PID: 17408359
    • Falkenberg M, Larsson NG, Gustafsson CM (2007) DNA replication and transcription in mammalian mitochondria. Annu Rev Biochem 76:679–699
    • (2007) Annu Rev Biochem , vol.76 , pp. 679-699
    • Falkenberg, M.1    Larsson, N.G.2    Gustafsson, C.M.3
  • 31
    • 84962382611 scopus 로고    scopus 로고
    • Human cells require non-stop ribosome rescue activity in mitochondria
    • PID: 27029019
    • Feaga HA, Quickel MD, Hankey-Giblin PA, Keiler KC (2016) Human cells require non-stop ribosome rescue activity in mitochondria. PLoS Genet 12:e1005964
    • (2016) PLoS Genet , vol.12
    • Feaga, H.A.1    Quickel, M.D.2    Hankey-Giblin, P.A.3    Keiler, K.C.4
  • 32
    • 84885087930 scopus 로고    scopus 로고
    • Modular blocks for building RNA-binding proteins
    • COI: 1:CAS:528:DC%2BC2cXmsVyqtL0%3D, PID: 23635770
    • Filipovska A, Rackham O (2013) Modular blocks for building RNA-binding proteins. RNA Biol 10:1426–1432
    • (2013) RNA Biol , vol.10 , pp. 1426-1432
    • Filipovska, A.1    Rackham, O.2
  • 33
    • 0032840382 scopus 로고    scopus 로고
    • Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis
    • COI: 1:CAS:528:DyaK1MXltFCmsrs%3D, PID: 10445876
    • Frolova LY, Tsivkovskii RY, Sivolobova GF, Oparina NY, Serpinsky OI, Blinov VM, Tatkov SI, Kisselev LL (1999) Mutations in the highly conserved GGQ motif of class 1 polypeptide release factors abolish ability of human eRF1 to trigger peptidyl-tRNA hydrolysis. RNA 5:1014–1020
    • (1999) RNA , vol.5 , pp. 1014-1020
    • Frolova, L.Y.1    Tsivkovskii, R.Y.2    Sivolobova, G.F.3    Oparina, N.Y.4    Serpinsky, O.I.5    Blinov, V.M.6    Tatkov, S.I.7    Kisselev, L.L.8
  • 34
    • 84873332767 scopus 로고    scopus 로고
    • The conserved interaction of C7orf30 with MRPL14 promotes biogenesis of the mitochondrial large ribosomal subunit and mitochondrial translation
    • COI: 1:CAS:528:DC%2BC3sXitlGjs7s%3D, PID: 23171548
    • Fung S, Nishimura T, Sasarman F, Shoubridge EA (2013) The conserved interaction of C7orf30 with MRPL14 promotes biogenesis of the mitochondrial large ribosomal subunit and mitochondrial translation. Mol Biol Cell 24:184–193
    • (2013) Mol Biol Cell , vol.24 , pp. 184-193
    • Fung, S.1    Nishimura, T.2    Sasarman, F.3    Shoubridge, E.A.4
  • 36
    • 0033525788 scopus 로고    scopus 로고
    • Mitochondrial evolution
    • COI: 1:CAS:528:DyaK1MXhs1ygt70%3D, PID: 10066161
    • Gray MW (1999) Mitochondrial evolution. Science 283:1476–1481
    • (1999) Science , vol.283 , pp. 1476-1481
    • Gray, M.W.1
  • 37
    • 84974701548 scopus 로고    scopus 로고
    • Structure and function of the mitochondrial ribosome
    • COI: 1:CAS:528:DC%2BC28XltFGrsL8%3D, PID: 27023846
    • Greber BJ, Ban N (2016) Structure and function of the mitochondrial ribosome. Annu Rev Biochem 85:103–132
    • (2016) Annu Rev Biochem , vol.85 , pp. 103-132
    • Greber, B.J.1    Ban, N.2
  • 38
    • 84922065877 scopus 로고    scopus 로고
    • The complete structure of the large subunit of the mammalian mitochondrial ribosome
    • COI: 1:CAS:528:DC%2BC2cXitVykurfJ, PID: 25271403
    • Greber BJ, Boehringer D, Leibundgut M, Bieri P, Leitner A, Schmitz N, Aebersold R, Ban N (2014a) The complete structure of the large subunit of the mammalian mitochondrial ribosome. Nature 515:283–286
    • (2014) Nature , vol.515 , pp. 283-286
    • Greber, B.J.1    Boehringer, D.2    Leibundgut, M.3    Bieri, P.4    Leitner, A.5    Schmitz, N.6    Aebersold, R.7    Ban, N.8
  • 41
    • 84974661182 scopus 로고    scopus 로고
    • Maintenance and expression of mammalian mitochondrial DNA
    • COI: 1:CAS:528:DC%2BC28XltFGrs78%3D, PID: 27023847
    • Gustafsson CM, Falkenberg M, Larsson NG (2016) Maintenance and expression of mammalian mitochondrial DNA. Annu Rev Biochem 85:133–160. doi:10.1146/annurev-biochem-060815-014402
    • (2016) Annu Rev Biochem , vol.85 , pp. 133-160
    • Gustafsson, C.M.1    Falkenberg, M.2    Larsson, N.G.3
  • 42
    • 10944267609 scopus 로고    scopus 로고
    • A surfeit of factors: why is ribosome assembly so much more complicated in eukaryotes than bacteria?
    • PID: 17194932
    • Hage AE, Tollervey D (2004) A surfeit of factors: why is ribosome assembly so much more complicated in eukaryotes than bacteria? RNA Biol 1:10–15
    • (2004) RNA Biol , vol.1 , pp. 10-15
    • Hage, A.E.1    Tollervey, D.2
  • 44
    • 77956250214 scopus 로고    scopus 로고
    • Properties of the C-terminal tail of human mitochondrial inner membrane protein Oxa1L and its interactions with mammalian mitochondrial ribosomes
    • COI: 1:CAS:528:DC%2BC3cXhtVOnsLbN, PID: 20601428
    • Haque ME, Elmore KB, Tripathy A, Koc H, Koc EC, Spremulli LL (2010) Properties of the C-terminal tail of human mitochondrial inner membrane protein Oxa1L and its interactions with mammalian mitochondrial ribosomes. J Biol Chem 285:28353–28362
    • (2010) J Biol Chem , vol.285 , pp. 28353-28362
    • Haque, M.E.1    Elmore, K.B.2    Tripathy, A.3    Koc, H.4    Koc, E.C.5    Spremulli, L.L.6
  • 45
    • 84864454280 scopus 로고    scopus 로고
    • Human C4orf14 interacts with the mitochondrial nucleoid and is involved in the biogenesis of the small mitochondrial ribosomal subunit
    • COI: 1:CAS:528:DC%2BC38XhtFSls7fJ, PID: 22447445
    • He J, Cooper HM, Reyes A, Di Re M, Kazak L, Wood SR, Mao CC, Fearnley IM, Walker JE, Holt IJ (2012) Human C4orf14 interacts with the mitochondrial nucleoid and is involved in the biogenesis of the small mitochondrial ribosomal subunit. Nucleic Acids Res 40:6097–6108
    • (2012) Nucleic Acids Res , vol.40 , pp. 6097-6108
    • He, J.1    Cooper, H.M.2    Reyes, A.3    Di Re, M.4    Kazak, L.5    Wood, S.R.6    Mao, C.C.7    Fearnley, I.M.8    Walker, J.E.9    Holt, I.J.10
  • 46
    • 84931281857 scopus 로고    scopus 로고
    • YidC/Alb3/Oxa1 family of insertases
    • COI: 1:CAS:528:DC%2BC2MXpvV2nsbY%3D, PID: 25947384
    • Hennon SW, Soman R, Zhu L, Dalbey RE (2015) YidC/Alb3/Oxa1 family of insertases. J Biol Chem 290:14866–14874
    • (2015) J Biol Chem , vol.290 , pp. 14866-14874
    • Hennon, S.W.1    Soman, R.2    Zhu, L.3    Dalbey, R.E.4
  • 47
    • 84871819218 scopus 로고    scopus 로고
    • Control of protein synthesis in yeast mitochondria: the concept of translational activators
    • COI: 1:CAS:528:DC%2BC38XltVyjtb8%3D, PID: 22450032
    • Herrmann JM, Woellhaf MW, Bonnefoy N (2013) Control of protein synthesis in yeast mitochondria: the concept of translational activators. Biochim Biophys Acta 1833:286–294
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 286-294
    • Herrmann, J.M.1    Woellhaf, M.W.2    Bonnefoy, N.3
  • 48
    • 0023883150 scopus 로고
    • Deletions of muscle mitochondrial DNA in patients with mitochondrial myopathies
    • COI: 1:STN:280:DyaL1c7ktlWmtQ%3D%3D, PID: 2830540
    • Holt IJ, Harding AE, Morgan-Hughes JA (1988) Deletions of muscle mitochondrial DNA in patients with mitochondrial myopathies. Nature 331:717–719
    • (1988) Nature , vol.331 , pp. 717-719
    • Holt, I.J.1    Harding, A.E.2    Morgan-Hughes, J.A.3
  • 49
    • 54549088876 scopus 로고    scopus 로고
    • RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme
    • COI: 1:CAS:528:DC%2BD1cXhtlyqtrzL, PID: 18984158
    • Holzmann J, Frank P, Löffler E, Bennett KL, Gerner C, Rossmanith W (2008) RNase P without RNA: identification and functional reconstitution of the human mitochondrial tRNA processing enzyme. Cell 135:462–474
    • (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
  • 51
    • 0348136787 scopus 로고    scopus 로고
    • Yeast Oxa1 interacts with mitochondrial ribosomes: the importance of the C-terminal region of Oxa1
    • COI: 1:CAS:528:DC%2BD3sXpvVemt7s%3D, PID: 14657017
    • Jia L, Dienhart M, Schramp M, McCauley M, Hell K, Stuart RA (2003) Yeast Oxa1 interacts with mitochondrial ribosomes: the importance of the C-terminal region of Oxa1. EMBO J 22:6438–6447
    • (2003) EMBO J , vol.22 , pp. 6438-6447
    • Jia, L.1    Dienhart, M.2    Schramp, M.3    McCauley, M.4    Hell, K.5    Stuart, R.A.6
  • 54
    • 0033556151 scopus 로고    scopus 로고
    • Structure-function analysis of an evolutionary conserved protein, DAP3, which mediates TNF-alpha- and Fas-induced cell death
    • COI: 1:CAS:528:DyaK1MXotlentQ%3D%3D, PID: 9889192
    • Kissil JL, Cohen O, Raveh T, Kimchi A (1999) Structure-function analysis of an evolutionary conserved protein, DAP3, which mediates TNF-alpha- and Fas-induced cell death. EMBO J 18:353–362
    • (1999) EMBO J , vol.18 , pp. 353-362
    • Kissil, J.L.1    Cohen, O.2    Raveh, T.3    Kimchi, A.4
  • 55
    • 0035380711 scopus 로고    scopus 로고
    • The small subunit of the mammalian mitochondrial ribosome. Identification of the full complement of ribosomal proteins present
    • COI: 1:CAS:528:DC%2BD3MXkt12rsbc%3D
    • Koc EC, Burkhart W, Blackburn K, Moseley A, Spremulli LL (2001a) The small subunit of the mammalian mitochondrial ribosome. Identification of the full complement of ribosomal proteins present. J Biol Chem 276:19363–19374
    • (2001) J Biol Chem , vol.276 , pp. 19363-19374
    • Koc, E.C.1    Burkhart, W.2    Blackburn, K.3    Moseley, A.4    Spremulli, L.L.5
  • 56
    • 0035941287 scopus 로고    scopus 로고
    • The large subunit of the mammalian mitochondrial ribosome. Analysis of the complement of ribosomal proteins present
    • COI: 1:STN:280:DC%2BD3MnmslKgug%3D%3D, PID: 11551941
    • Koc EC, Burkhart W, Blackburn K, Moyer MB, Schlatzer DM, Moseley A, Spremulli LL (2001b) The large subunit of the mammalian mitochondrial ribosome. Analysis of the complement of ribosomal proteins present. J Biol Chem 276:43958–43969
    • (2001) J Biol Chem , vol.276 , pp. 43958-43969
    • Koc, E.C.1    Burkhart, W.2    Blackburn, K.3    Moyer, M.B.4    Schlatzer, D.M.5    Moseley, A.6    Spremulli, L.L.7
  • 57
    • 84876035699 scopus 로고    scopus 로고
    • Human G-proteins, ObgH1 and Mtg1, associate with the large mitochondrial ribosome subunit and are involved in translation and assembly of respiratory complexes
    • COI: 1:CAS:528:DC%2BC3sXlsVCnu7o%3D, PID: 23396448
    • Kotani T, Akabane S, Takeyasu K, Ueda T, Takeuchi N (2013) Human G-proteins, ObgH1 and Mtg1, associate with the large mitochondrial ribosome subunit and are involved in translation and assembly of respiratory complexes. Nucleic Acids Res 41:3713–3722
    • (2013) Nucleic Acids Res , vol.41 , pp. 3713-3722
    • Kotani, T.1    Akabane, S.2    Takeyasu, K.3    Ueda, T.4    Takeuchi, N.5
  • 58
    • 84906968851 scopus 로고    scopus 로고
    • Assignment of 2'-O-methyltransferases to modification sites on the mammalian mitochondrial large subunit 16 S ribosomal RNA (rRNA)
    • COI: 1:CAS:528:DC%2BC2cXhsVyrtb3E, PID: 25074936
    • Lee KW, Bogenhagen DF (2014) Assignment of 2'-O-methyltransferases to modification sites on the mammalian mitochondrial large subunit 16 S ribosomal RNA (rRNA). J Biol Chem 289:24936–24942
    • (2014) J Biol Chem , vol.289 , pp. 24936-24942
    • Lee, K.W.1    Bogenhagen, D.F.2
  • 60
    • 84960510179 scopus 로고    scopus 로고
    • Identification of LACTB2, a metallo-β-lactamase protein, as a human mitochondrial endoribonuclease
    • PID: 26826708
    • Levy S, Allerston CK, Liveanu V, Habib MR, Gileadi O, Schuster G (2016) Identification of LACTB2, a metallo-β-lactamase protein, as a human mitochondrial endoribonuclease. Nucleic Acids Res 44:1813–1832
    • (2016) Nucleic Acids Res , vol.44 , pp. 1813-1832
    • Levy, S.1    Allerston, C.K.2    Liveanu, V.3    Habib, M.R.4    Gileadi, O.5    Schuster, G.6
  • 61
    • 0034703062 scopus 로고    scopus 로고
    • Interaction of mammalian mitochondrial ribosomes with the inner membrane
    • Li M, Spremulli LL (2000) Interaction of mammalian mitochondrial ribosomes with the inner membrane. J Biol Chem 275:29400–29406
    • (2000) J Biol Chem , vol.275 , pp. 29400-29406
    • Li, M.1    Spremulli, L.L.2
  • 62
    • 84885135073 scopus 로고    scopus 로고
    • Human pentatricopeptide proteins: only a few and what do they do?
    • COI: 1:CAS:528:DC%2BC2cXmsVyqtLo%3D, PID: 23635806
    • Lightowlers RN, Chrzanowska-Lightowlers ZM (2013) Human pentatricopeptide proteins: only a few and what do they do? RNA Biol 10:1433–1438
    • (2013) RNA Biol , vol.10 , pp. 1433-1438
    • Lightowlers, R.N.1    Chrzanowska-Lightowlers, Z.M.2
  • 63
    • 84904265044 scopus 로고    scopus 로고
    • Mitochondrial protein synthesis: figuring the fundamentals, complexities and complications, of mammalian mitochondrial translation
    • COI: 1:CAS:528:DC%2BC2cXhtVCjtLfN, PID: 24911204
    • Lightowlers RN, Rozanska A, Chrzanowska-Lightowlers ZM (2014) Mitochondrial protein synthesis: figuring the fundamentals, complexities and complications, of mammalian mitochondrial translation. FEBS Lett 588:2496–2503
    • (2014) FEBS Lett , vol.588 , pp. 2496-2503
    • Lightowlers, R.N.1    Rozanska, A.2    Chrzanowska-Lightowlers, Z.M.3
  • 64
    • 84942287874 scopus 로고    scopus 로고
    • Mutations causing mitochondrial disease: What is new and what challenges remain?
    • COI: 1:CAS:528:DC%2BC2MXhsFCrtbnO, PID: 26404827
    • Lightowlers RN, Taylor RW, Turnbull DM (2015) Mutations causing mitochondrial disease: What is new and what challenges remain? Science 349:1494–1499
    • (2015) Science , vol.349 , pp. 1494-1499
    • Lightowlers, R.N.1    Taylor, R.W.2    Turnbull, D.M.3
  • 65
    • 79960724199 scopus 로고    scopus 로고
    • From unwinding to clamping—the DEAD box RNA helicase family
    • COI: 1:CAS:528:DC%2BC3MXpt1aqtL4%3D, PID: 21779027
    • Linder P, Jankowsky E (2011) From unwinding to clamping—the DEAD box RNA helicase family. Nat Rev Mol Cell Biol 12:505–516
    • (2011) Nat Rev Mol Cell Biol , vol.12 , pp. 505-516
    • Linder, P.1    Jankowsky, E.2
  • 66
    • 84962198319 scopus 로고    scopus 로고
    • Intersubunit bridges of the bacterial ribosome
    • COI: 1:CAS:528:DC%2BC28XktVeiu7w%3D, PID: 26880335
    • Liu Q, Fredrick K (2016) Intersubunit bridges of the bacterial ribosome. J Mol Biol 428:2146–2164. doi:10.1016/j.jmb.2016.02.009
    • (2016) J Mol Biol , vol.428 , pp. 2146-2164
    • Liu, Q.1    Fredrick, K.2
  • 67
    • 80052631022 scopus 로고    scopus 로고
    • Mdm38 is a 14-3-3-like receptor and associates with the protein synthesis machinery at the inner mitochondrial membrane
    • COI: 1:CAS:528:DC%2BC3MXht1Cgs7fN, PID: 21718401
    • Lupo D, Vollmer C, Deckers M, Mick DU, Tews I, Sinning I, Rehling P (2011) Mdm38 is a 14-3-3-like receptor and associates with the protein synthesis machinery at the inner mitochondrial membrane. Traffic 12:1457–1466
    • (2011) Traffic , vol.12 , pp. 1457-1466
    • Lupo, D.1    Vollmer, C.2    Deckers, M.3    Mick, D.U.4    Tews, I.5    Sinning, I.6    Rehling, P.7
  • 69
    • 0001515799 scopus 로고
    • Incorporation of labeled amino acids into the protein of muscle and liver mitochondria
    • COI: 1:CAS:528:DyaG1MXht1KktA%3D%3D, PID: 13575431
    • McLean J, Cohn GL, Brandt IK, Simpson MV (1958) Incorporation of labeled amino acids into the protein of muscle and liver mitochondria. J Biol Chem 233:657–663
    • (1958) J Biol Chem , vol.233 , pp. 657-663
    • McLean, J.1    Cohn, G.L.2    Brandt, I.K.3    Simpson, M.V.4
  • 72
    • 63449105579 scopus 로고    scopus 로고
    • Methylation of 12S rRNA is necessary for in vivo stability of the small subunit of the mammalian mitochondrial ribosome
    • COI: 1:CAS:528:DC%2BD1MXlsFyru7k%3D, PID: 19356719
    • Metodiev MD, Lesko N, Park CB, Cámara Y, Shi Y, Wibom R, Hultenby K, Gustafsson CM, Larsson NG (2009) Methylation of 12S rRNA is necessary for in vivo stability of the small subunit of the mammalian mitochondrial ribosome. Cell Metab 9:386–397
    • (2009) Cell Metab , vol.9 , pp. 386-397
    • Metodiev, M.D.1    Lesko, N.2    Park, C.B.3    Cámara, Y.4    Shi, Y.5    Wibom, R.6    Hultenby, K.7    Gustafsson, C.M.8    Larsson, N.G.9
  • 76
    • 38649090322 scopus 로고    scopus 로고
    • Identification of phosphorylation sites in mammalian mitochondrial ribosomal protein DAP3
    • COI: 1:CAS:528:DC%2BD1cXhvVOntLg%3D, PID: 18227431
    • Miller JL, Koc H, Koc EC (2008) Identification of phosphorylation sites in mammalian mitochondrial ribosomal protein DAP3. Protein Sci 17:251–260
    • (2008) Protein Sci , vol.17 , pp. 251-260
    • Miller, J.L.1    Koc, H.2    Koc, E.C.3
  • 77
    • 70349970268 scopus 로고    scopus 로고
    • Phosphorylated proteins of the mammalian mitochondrial ribosome: implications in protein synthesis
    • COI: 1:CAS:528:DC%2BD1MXhtFehurfF, PID: 19702336
    • Miller JL, Cimen H, Koc EC (2009) Phosphorylated proteins of the mammalian mitochondrial ribosome: implications in protein synthesis. J Proteome Res 8:4789–4798
    • (2009) J Proteome Res , vol.8 , pp. 4789-4798
    • Miller, J.L.1    Cimen, H.2    Koc, E.C.3
  • 79
    • 0019423857 scopus 로고
    • Distinctive features of the 5'-terminal sequences of the human mitochondrial mRNAs
    • COI: 1:CAS:528:DyaL3MXksFKmtL0%3D, PID: 7219535
    • Montoya J, Ojala D, Attardi G (1981) Distinctive features of the 5'-terminal sequences of the human mitochondrial mRNAs. Nature 290:465–470
    • (1981) Nature , vol.290 , pp. 465-470
    • Montoya, J.1    Ojala, D.2    Attardi, G.3
  • 80
    • 0035955658 scopus 로고    scopus 로고
    • Identification and characterization of mammalian mitochondrial tRNA nucleotidyltransferases
    • COI: 1:CAS:528:DC%2BD3MXotFGhsb4%3D, PID: 11504732
    • Nagaike T, Suzuki T, Tomari Y, Takemoto-Hori C, Negayama F, Watanabe K, Ueda T (2001) Identification and characterization of mammalian mitochondrial tRNA nucleotidyltransferases. J Biol Chem 276:40041–40049
    • (2001) J Biol Chem , vol.276 , pp. 40041-40049
    • Nagaike, T.1    Suzuki, T.2    Tomari, Y.3    Takemoto-Hori, C.4    Negayama, F.5    Watanabe, K.6    Ueda, T.7
  • 81
    • 21244454028 scopus 로고    scopus 로고
    • Human mitochondrial mRNAs are stabilized with polyadenylation regulated by mitochondria-specific poly(A) polymerase and polynucleotide phosphorylase
    • COI: 1:CAS:528:DC%2BD2MXktFymu74%3D, PID: 15769737
    • Nagaike T, Suzuki T, Katoh T, Ueda T (2005) Human mitochondrial mRNAs are stabilized with polyadenylation regulated by mitochondria-specific poly(A) polymerase and polynucleotide phosphorylase. J Biol Chem 280:19721–19727
    • (2005) J Biol Chem , vol.280 , pp. 19721-19727
    • Nagaike, T.1    Suzuki, T.2    Katoh, T.3    Ueda, T.4
  • 82
    • 84924232481 scopus 로고    scopus 로고
    • A perspective on transport of proteins into mitochondria: a myriad of open questions
    • COI: 1:CAS:528:DC%2BC2MXivVShtLk%3D, PID: 25676309
    • Neupert W (2015) A perspective on transport of proteins into mitochondria: a myriad of open questions. J Mol Biol 427:1135–1158
    • (2015) J Mol Biol , vol.427 , pp. 1135-1158
    • Neupert, W.1
  • 83
    • 26844484821 scopus 로고    scopus 로고
    • The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria
    • COI: 1:CAS:528:DC%2BD2MXhtFOqsbbE, PID: 16239145
    • Nolden M, Ehses S, Koppen M, Bernacchia A, Rugarli EI, Langer T (2005) The m-AAA protease defective in hereditary spastic paraplegia controls ribosome assembly in mitochondria. Cell 123:277–289
    • (2005) Cell , vol.123 , pp. 277-289
    • Nolden, M.1    Ehses, S.2    Koppen, M.3    Bernacchia, A.4    Rugarli, E.I.5    Langer, T.6
  • 84
    • 84954165040 scopus 로고    scopus 로고
    • Mitochondrial ribosomal protein L12 is required for POLRMT stability and exists as two forms generated by alternative proteolysis during import
    • COI: 1:CAS:528:DC%2BC28Xltlynsw%3D%3D, PID: 26586915
    • Nouws J, Goswami AV, Bestwick M, McCann BJ, Surovtseva YV, Shadel GS (2016) Mitochondrial ribosomal protein L12 is required for POLRMT stability and exists as two forms generated by alternative proteolysis during import. J Biol Chem 291:989–997
    • (2016) J Biol Chem , vol.291 , pp. 989-997
    • Nouws, J.1    Goswami, A.V.2    Bestwick, M.3    McCann, B.J.4    Surovtseva, Y.V.5    Shadel, G.S.6
  • 85
    • 0015239528 scopus 로고
    • The general occurrence of 55 S ribosomes in mammalian liver mitochondria
    • PID: 4930061
    • O'Brien TW (1971) The general occurrence of 55 S ribosomes in mammalian liver mitochondria. J Biol Chem 246:3409–3417
    • (1971) J Biol Chem , vol.246 , pp. 3409-3417
    • O'Brien, T.W.1
  • 86
    • 0014198305 scopus 로고
    • Ribosomes from rat liver mitochondria
    • PID: 6022863
    • O'Brien TW, Kalf GF (1967) Ribosomes from rat liver mitochondria. J Biol Chem 242:2172–2179
    • (1967) J Biol Chem , vol.242 , pp. 2172-2179
    • O'Brien, T.W.1    Kalf, G.F.2
  • 88
    • 0031581856 scopus 로고    scopus 로고
    • Mapping to nucleotide resolution of pseudouridine residues in large subunit ribosomal RNAs from representative eukaryotes, prokaryotes, archaebacteria, mitochondria and chloroplasts
    • COI: 1:CAS:528:DyaK2sXhs1GmsLw%3D, PID: 9047361
    • Ofengand J, Bakin A (1997) Mapping to nucleotide resolution of pseudouridine residues in large subunit ribosomal RNAs from representative eukaryotes, prokaryotes, archaebacteria, mitochondria and chloroplasts. J Mol Biol 266:246–268
    • (1997) J Mol Biol , vol.266 , pp. 246-268
    • Ofengand, J.1    Bakin, A.2
  • 89
    • 0019444843 scopus 로고
    • tRNA punctuation model of RNA processing in human mitochondria
    • COI: 1:CAS:528:DyaL3MXksFKmtLo%3D, PID: 7219536
    • Ojala D, Montoya J, Attardi G (1981) tRNA punctuation model of RNA processing in human mitochondria. Nature 290:470–474
    • (1981) Nature , vol.290 , pp. 470-474
    • Ojala, D.1    Montoya, J.2    Attardi, G.3
  • 91
    • 84962371949 scopus 로고    scopus 로고
    • Organization and regulation of mitochondrial protein synthesis
    • COI: 1:CAS:528:DC%2BC28Xht1Kqs70%3D, PID: 26789594
    • Ott M, Amunts A, Brown A (2016) Organization and regulation of mitochondrial protein synthesis. Annu Rev Biochem 85:77–101. doi:10.1146/annurev-biochem-060815-014334
    • (2016) Annu Rev Biochem , vol.85 , pp. 77-101
    • Ott, M.1    Amunts, A.2    Brown, A.3
  • 92
    • 84931561092 scopus 로고    scopus 로고
    • Organization of the mitochondrial translation machinery studied in situ by cryoelectron tomography
    • COI: 1:CAS:528:DC%2BC2MXhtF2lurfK, PID: 25609543
    • Pfeffer S, Woellhaf MW, Herrmann JM, Forster F (2015) Organization of the mitochondrial translation machinery studied in situ by cryoelectron tomography. Nat Commun 6:6019
    • (2015) Nat Commun , vol.6 , pp. 6019
    • Pfeffer, S.1    Woellhaf, M.W.2    Herrmann, J.M.3    Forster, F.4
  • 94
    • 84944721159 scopus 로고    scopus 로고
    • FASTKD2 is an RNA-binding protein required for mitochondrial RNA processing and translation
    • COI: 1:CAS:528:DC%2BC28XjvFSkt78%3D, PID: 26370583
    • Popow J, Alleaume AM, Curk T, Schwarzl T, Sauer S, Hentze MW (2015) FASTKD2 is an RNA-binding protein required for mitochondrial RNA processing and translation. RNA 21:1873–1884
    • (2015) RNA , vol.21 , pp. 1873-1884
    • Popow, J.1    Alleaume, A.M.2    Curk, T.3    Schwarzl, T.4    Sauer, S.5    Hentze, M.W.6
  • 95
    • 0032102374 scopus 로고    scopus 로고
    • Ribosomal protein structures: insights into the architecture, machinery and evolution of the ribosome
    • COI: 1:CAS:528:DyaK1cXktVSlsLY%3D, PID: 9644974
    • Ramakrishnan V, White SW (1998) Ribosomal protein structures: insights into the architecture, machinery and evolution of the ribosome. Trends Biochem Sci 23:208–212
    • (1998) Trends Biochem Sci , vol.23 , pp. 208-212
    • Ramakrishnan, V.1    White, S.W.2
  • 98
    • 84861392482 scopus 로고    scopus 로고
    • C7orf30 is necessary for biogenesis of the large subunit of the mitochondrial ribosome
    • COI: 1:CAS:528:DC%2BC38XmvF2msLs%3D, PID: 22238376
    • Rorbach J, Gammage PA, Minczuk M (2012) C7orf30 is necessary for biogenesis of the large subunit of the mitochondrial ribosome. Nucleic Acids Res 40:4097–4109
    • (2012) Nucleic Acids Res , vol.40 , pp. 4097-4109
    • Rorbach, J.1    Gammage, P.A.2    Minczuk, M.3
  • 100
    • 79955716664 scopus 로고    scopus 로고
    • Localization of human RNase Z isoforms: dual nuclear/mitochondrial targeting of the ELAC2 gene product by alternative translation initiation
    • COI: 1:CAS:528:DC%2BC3MXlslGgt74%3D, PID: 21559454
    • Rossmanith W (2011) Localization of human RNase Z isoforms: dual nuclear/mitochondrial targeting of the ELAC2 gene product by alternative translation initiation. PLoS ONE 6: e19152
    • (2011) PLoS ONE , vol.6
    • Rossmanith, W.1
  • 101
    • 37249071299 scopus 로고    scopus 로고
    • Antenatal mitochondrial disease caused by mitochondrial ribosomal protein (MRPS22) mutation
    • COI: 1:CAS:528:DC%2BD1cXnvVertg%3D%3D, PID: 17873122
    • Saada A, Shaag A, Arnon S, Dolfin T, Miller C, Fuchs-Telem D, Lombes A, Elpeleg O (2007) Antenatal mitochondrial disease caused by mitochondrial ribosomal protein (MRPS22) mutation. J Med Genet 44:784–786
    • (2007) J Med Genet , vol.44 , pp. 784-786
    • Saada, A.1    Shaag, A.2    Arnon, S.3    Dolfin, T.4    Miller, C.5    Fuchs-Telem, D.6    Lombes, A.7    Elpeleg, O.8
  • 102
    • 84925874857 scopus 로고    scopus 로고
    • tRNA biology in mitochondria
    • COI: 1:CAS:528:DC%2BC2MXlvVKqtLs%3D, PID: 25734984
    • Salinas-Giege T, Giege R, Giege P (2015) tRNA biology in mitochondria. Int J Mol Sci 16:4518–4559
    • (2015) Int J Mol Sci , vol.16 , pp. 4518-4559
    • Salinas-Giege, T.1    Giege, R.2    Giege, P.3
  • 103
    • 77950901962 scopus 로고    scopus 로고
    • LRPPRC and SLIRP interact in a ribonucleoprotein complex that regulates posttranscriptional gene expression in mitochondria
    • COI: 1:CAS:528:DC%2BC3cXlvFCjsb8%3D, PID: 20200222
    • Sasarman F, Brunel-Guitton C, Antonicka H, Wai T, Shoubridge EA (2010) LRPPRC and SLIRP interact in a ribonucleoprotein complex that regulates posttranscriptional gene expression in mitochondria. Mol Biol Cell 21:1315–1323
    • (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
  • 104
    • 28544452248 scopus 로고    scopus 로고
    • An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA
    • COI: 1:CAS:528:DC%2BD2MXht1Gis7jK, PID: 16306996
    • Schmeing TM, Huang KS, Strobel SA, Steit TA (2005) An induced-fit mechanism to promote peptide bond formation and exclude hydrolysis of peptidyl-tRNA. Nature 438:520–524
    • (2005) Nature , vol.438 , pp. 520-524
    • Schmeing, T.M.1    Huang, K.S.2    Strobel, S.A.3    Steit, T.A.4
  • 106
    • 0037228525 scopus 로고    scopus 로고
    • Human mitochondrial transcription factor B1 methylates ribosomal RNA at a conserved stem-loop
    • PID: 12496758
    • Seidel-Rogol BL, McCulloch V, Shadel GS (2002) Human mitochondrial transcription factor B1 methylates ribosomal RNA at a conserved stem-loop. Nat Genet 33:23–24
    • (2002) Nat Genet , vol.33 , pp. 23-24
    • Seidel-Rogol, B.L.1    McCulloch, V.2    Shadel, G.S.3
  • 107
    • 84877320879 scopus 로고    scopus 로고
    • Mutations in mitochondrial ribosomal protein MRPL12 leads to growth retardation, neurological deterioration and mitochondrial translation deficiency
    • COI: 1:CAS:528:DC%2BC3sXptV2nsbs%3D, PID: 23603806
    • Serre V, Rozanska A, Beinat M, Chretien D, Boddaert N, Munnich A, Rotiq A, Chrzanowska-Lightowlers ZM (2013) Mutations in mitochondrial ribosomal protein MRPL12 leads to growth retardation, neurological deterioration and mitochondrial translation deficiency. Biochim Biophys Acta 1832:1304–1312
    • (2013) Biochim Biophys Acta , vol.1832 , pp. 1304-1312
    • Serre, V.1    Rozanska, A.2    Beinat, M.3    Chretien, D.4    Boddaert, N.5    Munnich, A.6    Rotiq, A.7    Chrzanowska-Lightowlers, Z.M.8
  • 108
    • 0141953259 scopus 로고    scopus 로고
    • Structure of the mammalian mitochondrial ribosome reveals an expanded functional role for its component proteins
    • COI: 1:CAS:528:DC%2BD3sXotFSltb8%3D, PID: 14532006
    • Sharma MR, Koc EC, Datta PP, Booth TM, Spremulli LL, Agrawal RK (2003) Structure of the mammalian mitochondrial ribosome reveals an expanded functional role for its component proteins. Cell 115:97–108
    • (2003) Cell , vol.115 , pp. 97-108
    • Sharma, M.R.1    Koc, E.C.2    Datta, P.P.3    Booth, T.M.4    Spremulli, L.L.5    Agrawal, R.K.6
  • 110
    • 22544448652 scopus 로고    scopus 로고
    • Polyadenylation and degradation of human mitochondrial RNA: the prokaryotic past leaves its mark
    • COI: 1:CAS:528:DC%2BD2MXntVShur8%3D, PID: 16024781
    • Slomovic S, Laufer D, Geiger D, Schuster G (2005) Polyadenylation and degradation of human mitochondrial RNA: the prokaryotic past leaves its mark. Mol Cell Biol 25:6427–6435
    • (2005) Mol Cell Biol , vol.25 , pp. 6427-6435
    • Slomovic, S.1    Laufer, D.2    Geiger, D.3    Schuster, G.4
  • 111
    • 79959673883 scopus 로고    scopus 로고
    • Biological significance of 5S rRNA import into human mitochondria: role of ribosomal protein MRP-L18
    • COI: 1:CAS:528:DC%2BC3MXosFWms7g%3D, PID: 21685364
    • Smirnov A, Entelis N, Martin RP, Tarassov I (2011) Biological significance of 5S rRNA import into human mitochondria: role of ribosomal protein MRP-L18. Genes Dev 25:1289–1305
    • (2011) Genes Dev , vol.25 , pp. 1289-1305
    • Smirnov, A.1    Entelis, N.2    Martin, R.P.3    Tarassov, I.4
  • 114
    • 35548996344 scopus 로고    scopus 로고
    • Knockdown of human Oxa1l impairs the biogenesis of F1Fo-ATP synthase and NADH:ubiquinone oxidoreductase
    • COI: 1:CAS:528:DC%2BD2sXht1KjtrnN, PID: 17936786
    • Stiburek L, Fornuskova D, Wenchich L, Pejznochova M, Hansikova H, Zeman J (2007) Knockdown of human Oxa1l impairs the biogenesis of F1Fo-ATP synthase and NADH:ubiquinone oxidoreductase. J Mol Biol 374:506–516
    • (2007) J Mol Biol , vol.374 , pp. 506-516
    • Stiburek, L.1    Fornuskova, D.2    Wenchich, L.3    Pejznochova, M.4    Hansikova, H.5    Zeman, J.6
  • 116
    • 0032570607 scopus 로고    scopus 로고
    • A novel 52 kDa protein induces apoptosis and concurrently activates c-Jun N-terminal kinase 1 (JNK1) in mouse C3H10T1/2 fibroblasts
    • COI: 1:CAS:528:DyaK1cXitVenu7w%3D, PID: 9524256
    • Sun L, Liu Y, Frémont M, Schwarz S, Siegmann M, Matthies R, Jost JP (1998) A novel 52 kDa protein induces apoptosis and concurrently activates c-Jun N-terminal kinase 1 (JNK1) in mouse C3H10T1/2 fibroblasts. Gene 208:157–166
    • (1998) Gene , vol.208 , pp. 157-166
    • Sun, L.1    Liu, Y.2    Frémont, M.3    Schwarz, S.4    Siegmann, M.5    Matthies, R.6    Jost, J.P.7
  • 117
    • 81055126308 scopus 로고    scopus 로고
    • Mitochondrial ribosomal protein L12 selectively associates with human mitochondrial RNA polymerase to activate transcription
    • COI: 1:CAS:528:DC%2BC3MXhsVOktLjO, PID: 22003127
    • Surovtseva YV, Shutta TE, Cotneya J, Cimenb H, Chena SY, Koc EC, Shadela GS (2011) Mitochondrial ribosomal protein L12 selectively associates with human mitochondrial RNA polymerase to activate transcription. Proc Natl Acad Sci U S A 108:17921–17926
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 17921-17926
    • Surovtseva, Y.V.1    Shutta, T.E.2    Cotneya, J.3    Cimenb, H.4    Chena, S.Y.5    Koc, E.C.6    Shadela, G.S.7
  • 118
    • 84903151976 scopus 로고    scopus 로고
    • A complete landscape of post-transcriptional modifications in mammalian mitochondrial tRNAs
    • COI: 1:CAS:528:DC%2BC2cXhtVCjs7rM, PID: 24831542
    • Suzuki T (2014) A complete landscape of post-transcriptional modifications in mammalian mitochondrial tRNAs. Nucleic Acids Res 42:7346–7357
    • (2014) Nucleic Acids Res , vol.42 , pp. 7346-7357
    • Suzuki, T.1
  • 119
    • 80755169463 scopus 로고    scopus 로고
    • Human mitochondrial tRNAs: biogenesis, function, structural aspects, and diseases
    • COI: 1:CAS:528:DC%2BC3MXhs1ahtrrP, PID: 21910628
    • Suzuki T, Nagao A, Suzuki T (2011) Human mitochondrial tRNAs: biogenesis, function, structural aspects, and diseases. Annu Rev Genet 45:299–329
    • (2011) Annu Rev Genet , vol.45 , pp. 299-329
    • Suzuki, T.1    Nagao, A.2    Suzuki, T.3
  • 121
    • 63249103619 scopus 로고    scopus 로고
    • Unconventional decoding of the AUA codon as methionine by mitochondrial tRNAMet with the anticodon f5CAU as revealed with a mitochondrial in vitro translation system
    • COI: 1:CAS:528:DC%2BD1MXjsV2kt7o%3D, PID: 19151083
    • Takemoto C, Spremulli LL, Benkowski LA, Ueda T, Yokogawa T, Watanabe K (2009) Unconventional decoding of the AUA codon as methionine by mitochondrial tRNAMet with the anticodon f5CAU as revealed with a mitochondrial in vitro translation system. Nucleic Acids Res 37:1616–1627
    • (2009) Nucleic Acids Res , vol.37 , pp. 1616-1627
    • Takemoto, C.1    Spremulli, L.L.2    Benkowski, L.A.3    Ueda, T.4    Yokogawa, T.5    Watanabe, K.6
  • 123
    • 77953871736 scopus 로고    scopus 로고
    • Human mitochondrial mRNAs—like members of all families, similar but different
    • COI: 1:CAS:528:DC%2BC3cXnvV2rtb0%3D, PID: 20211597
    • Temperley RJ, Wydro M, Lightowlers RN, Chrzanowska-Lightowlers ZM (2010b) Human mitochondrial mRNAs—like members of all families, similar but different. Biochim Biophys Acta 1797:1081–1085
    • (2010) Biochim Biophys Acta , vol.1797 , pp. 1081-1085
    • Temperley, R.J.1    Wydro, M.2    Lightowlers, R.N.3    Chrzanowska-Lightowlers, Z.M.4
  • 124
    • 11344287222 scopus 로고    scopus 로고
    • Identification of a novel human nuclear-encoded mitochondrial poly(A) polymerase
    • COI: 1:CAS:528:DC%2BD2cXhtVanurrF, PID: 15547249
    • Tomecki R, Dmochowska A, Gewartowski K, Dziembowski A, Stepien PP (2004) Identification of a novel human nuclear-encoded mitochondrial poly(A) polymerase. Nucleic Acids Res 32:6001–6014
    • (2004) Nucleic Acids Res , vol.32 , pp. 6001-6014
    • Tomecki, R.1    Dmochowska, A.2    Gewartowski, K.3    Dziembowski, A.4    Stepien, P.P.5
  • 125
    • 68949204220 scopus 로고    scopus 로고
    • EF-G2mt is an exclusive recycling factor in mammalian mitochondrial protein synthesis
    • COI: 1:CAS:528:DC%2BD1MXhsVChsrvE, PID: 19716793
    • Tsuboi M, Morita H, Nozaki Y, Akama K, Ueda T, Ito K, Nierhaus KH, Takeuchi N (2009) EF-G2mt is an exclusive recycling factor in mammalian mitochondrial protein synthesis. Mol Cell 35:502–510
    • (2009) Mol Cell , vol.35 , pp. 502-510
    • Tsuboi, M.1    Morita, H.2    Nozaki, Y.3    Akama, K.4    Ueda, T.5    Ito, K.6    Nierhaus, K.H.7    Takeuchi, N.8
  • 126
    • 84923084754 scopus 로고    scopus 로고
    • The human mitochondrial DEAD-box protein DDX28 resides in RNA granules and functions in mitoribosome assembly
    • COI: 1:CAS:528:DC%2BC2MXivVSjur4%3D
    • Tu YT, Barrientos A (2015) The human mitochondrial DEAD-box protein DDX28 resides in RNA granules and functions in mitoribosome assembly. Cell Rep 10:854–864
    • (2015) Cell Rep , vol.10 , pp. 854-864
    • Tu, Y.T.1    Barrientos, A.2
  • 129
    • 77956539977 scopus 로고    scopus 로고
    • ERAL1 is associated with mitochondrial ribosome and elimination of ERAL1 leads to mitochondrial dysfunction and growth retardation
    • COI: 1:CAS:528:DC%2BC3cXhtFGgsLfP, PID: 20430825
    • Uchiumi T, Ohgaki K, Yagi M, Aoki Y, Sakai A, Matsumoto S, Kang D (2010) ERAL1 is associated with mitochondrial ribosome and elimination of ERAL1 leads to mitochondrial dysfunction and growth retardation. Nucleic Acids Res 38:5554–5568
    • (2010) Nucleic Acids Res , vol.38 , pp. 5554-5568
    • Uchiumi, T.1    Ohgaki, K.2    Yagi, M.3    Aoki, Y.4    Sakai, A.5    Matsumoto, S.6    Kang, D.7
  • 133
    • 84855835044 scopus 로고    scopus 로고
    • Mutations in C12orf62, a factor that couples COX I synthesis with cytochrome c oxidase assembly, cause fatal neonatal lactic acidosis
    • COI: 1:CAS:528:DC%2BC38XovFGhtA%3D%3D, PID: 22243966
    • Weraarpachai W, Sasarman F, Nishimura T, Antonicka H, Auré K, Rötig A, Lombès A, Shoubridge EA (2012) Mutations in C12orf62, a factor that couples COX I synthesis with cytochrome c oxidase assembly, cause fatal neonatal lactic acidosis. Am J Hum Genet 90:142–151
    • (2012) Am J Hum Genet , vol.90 , pp. 142-151
    • Weraarpachai, W.1    Sasarman, F.2    Nishimura, T.3    Antonicka, H.4    Auré, K.5    Rötig, A.6    Lombès, A.7    Shoubridge, E.A.8
  • 134
    • 0001906930 scopus 로고
    • Binding of transfer ribonucleic acid to ribosomes engaged in protein synthesis: number and properties of ribosomal binding sites
    • COI: 1:CAS:528:DyaF2MXmslGltA%3D%3D, PID: 14255759
    • Wettstein FO, Noll H (1965) Binding of transfer ribonucleic acid to ribosomes engaged in protein synthesis: number and properties of ribosomal binding sites. J Mol Biol 11:35–53
    • (1965) J Mol Biol , vol.11 , pp. 35-53
    • Wettstein, F.O.1    Noll, H.2
  • 136
    • 0020408539 scopus 로고
    • Structure and evolution of ribosomes
    • COI: 1:CAS:528:DyaL38XlslOisr4%3D, PID: 6129626
    • Wittmann HG (1982) Structure and evolution of ribosomes. Proc R Soc Lond B Biol Sci 216:117–135
    • (1982) Proc R Soc Lond B Biol Sci , vol.216 , pp. 117-135
    • Wittmann, H.G.1
  • 137
    • 84899852363 scopus 로고    scopus 로고
    • Functional genomic analysis of human mitochondrial RNA processing
    • COI: 1:CAS:528:DC%2BC2cXmsVeqsbs%3D, PID: 24746820
    • Wolf AR, Mootha VK (2014) Functional genomic analysis of human mitochondrial RNA processing. Cell Rep 7:918–931
    • (2014) Cell Rep , vol.7 , pp. 918-931
    • Wolf, A.R.1    Mootha, V.K.2
  • 139
    • 22544448366 scopus 로고    scopus 로고
    • Mitochondrial ribosomal protein L41 suppresses cell growth in association with p53 and p27Kip1
    • COI: 1:CAS:528:DC%2BD2MXntVShu7g%3D, PID: 16024796
    • Yoo YA, Kim MJ, Park JK, Chung YM, Lee JH, Chi SG, Kim JS, Yoo YD (2005) Mitochondrial ribosomal protein L41 suppresses cell growth in association with p53 and p27Kip1. Mol Cell Biol 25:6603–6616
    • (2005) Mol Cell Biol , vol.25 , pp. 6603-6616
    • Yoo, Y.A.1    Kim, M.J.2    Park, J.K.3    Chung, Y.M.4    Lee, J.H.5    Chi, S.G.6    Kim, J.S.7    Yoo, Y.D.8
  • 140
    • 77952729843 scopus 로고    scopus 로고
    • Bioinformatic, structural, and functional analyses support release factor-like MTRF1 as a protein able to decode nonstandard stop codons beginning with adenine in vertebrate mitochondria
    • COI: 1:CAS:528:DC%2BC3cXntV2iu7k%3D, PID: 20421313
    • Young DJ, Edgar CD, Murphy J, Fredebohm J, Poole ES, Tate WP (2010) Bioinformatic, structural, and functional analyses support release factor-like MTRF1 as a protein able to decode nonstandard stop codons beginning with adenine in vertebrate mitochondria. RNA 16:1146–1155
    • (2010) RNA , vol.16 , pp. 1146-1155
    • Young, D.J.1    Edgar, C.D.2    Murphy, J.3    Fredebohm, J.4    Poole, E.S.5    Tate, W.P.6
  • 141
    • 84929153389 scopus 로고    scopus 로고
    • Translational control of the cytosolic stress response by mitochondrial ribosomal protein L18
    • COI: 1:CAS:528:DC%2BC2MXmtlKlt7w%3D, PID: 25866880
    • Zhang X, Gao X, Coots RA, Conn CS, Liu B, Qian SB (2015) Translational control of the cytosolic stress response by mitochondrial ribosomal protein L18. Nat Struct Mol Biol 22:404–410
    • (2015) Nat Struct Mol Biol , vol.22 , pp. 404-410
    • Zhang, X.1    Gao, X.2    Coots, R.A.3    Conn, C.S.4    Liu, B.5    Qian, S.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.