메뉴 건너뛰기




Volumn 1857, Issue 7, 2016, Pages 980-990

Unraveling the complexity of mitochondrial complex i assembly: A dynamic process

Author keywords

Assembly factors; Complex I assembly; Human complex I; Mitochondria; Mitochondrial disorders

Indexed keywords

CELL NUCLEUS DNA; MITOCHONDRIAL DNA; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE DEHYDROGENASE (UBIQUINONE); MITOCHONDRIAL PROTEIN; PROTEIN BINDING;

EID: 84969756531     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2016.03.031     Document Type: Article
Times cited : (98)

References (119)
  • 1
    • 33746329868 scopus 로고    scopus 로고
    • Energy converting NADH:quinone oxidoreductase (complex I)
    • U. Brandt Energy converting NADH:quinone oxidoreductase (complex I) Annu. Rev. Biochem. 75 2006 69 92
    • (2006) Annu. Rev. Biochem. , vol.75 , pp. 69-92
    • Brandt, U.1
  • 2
    • 84878905186 scopus 로고    scopus 로고
    • Mitochondrial complex i
    • J. Hirst Mitochondrial complex I Annu. Rev. Biochem. 82 2013 551 575
    • (2013) Annu. Rev. Biochem. , vol.82 , pp. 551-575
    • Hirst, J.1
  • 3
    • 84863738048 scopus 로고    scopus 로고
    • Molecular mechanisms of superoxide production by the mitochondrial respiratory chain
    • S. Drose, and U. Brandt Molecular mechanisms of superoxide production by the mitochondrial respiratory chain Adv. Exp. Med. Biol. 748 2012 145 169
    • (2012) Adv. Exp. Med. Biol. , vol.748 , pp. 145-169
    • Drose, S.1    Brandt, U.2
  • 7
    • 84915761829 scopus 로고    scopus 로고
    • Architecture of mammalian respiratory complex i
    • K.R. Vinothkumar, J. Zhu, and J. Hirst Architecture of mammalian respiratory complex I Nature 515 2014 80 84
    • (2014) Nature , vol.515 , pp. 80-84
    • Vinothkumar, K.R.1    Zhu, J.2    Hirst, J.3
  • 8
    • 84922479528 scopus 로고    scopus 로고
    • Structural biology. Mechanistic insight from the crystal structure of mitochondrial complex i
    • V. Zickermann, C. Wirth, H. Nasiri, K. Siegmund, H. Schwalbe, C. Hunte, and U. Brandt Structural biology. Mechanistic insight from the crystal structure of mitochondrial complex I Science 347 2015 44 49
    • (2015) Science , vol.347 , pp. 44-49
    • Zickermann, V.1    Wirth, C.2    Nasiri, H.3    Siegmund, K.4    Schwalbe, H.5    Hunte, C.6    Brandt, U.7
  • 9
    • 84905820302 scopus 로고    scopus 로고
    • Making proteins in the powerhouse
    • B.M. Hallberg, and N.G. Larsson Making proteins in the powerhouse Cell Metab. 20 2014 226 240
    • (2014) Cell Metab. , vol.20 , pp. 226-240
    • Hallberg, B.M.1    Larsson, N.G.2
  • 10
    • 84863741781 scopus 로고    scopus 로고
    • Assembly factors of human mitochondrial respiratory chain complexes: Physiology and pathophysiology
    • D. Ghezzi, and M. Zeviani Assembly factors of human mitochondrial respiratory chain complexes: physiology and pathophysiology Adv. Exp. Med. Biol. 748 2012 65 106
    • (2012) Adv. Exp. Med. Biol. , vol.748 , pp. 65-106
    • Ghezzi, D.1    Zeviani, M.2
  • 11
    • 84856734831 scopus 로고    scopus 로고
    • Assembly factors as a new class of disease genes for mitochondrial complex i deficiency: Cause, pathology and treatment options
    • J. Nouws, L.G. Nijtmans, J.A. Smeitink, and R.O. Vogel Assembly factors as a new class of disease genes for mitochondrial complex I deficiency: cause, pathology and treatment options Brain 135 2012 12 22
    • (2012) Brain , vol.135 , pp. 12-22
    • Nouws, J.1    Nijtmans, L.G.2    Smeitink, J.A.3    Vogel, R.O.4
  • 14
    • 0029915525 scopus 로고    scopus 로고
    • Computational method to predict mitochondrially imported proteins and their targeting sequences
    • M.G. Claros, and P. Vincens Computational method to predict mitochondrially imported proteins and their targeting sequences Eur. J. Biochem. 241 1996 779 786
    • (1996) Eur. J. Biochem. , vol.241 , pp. 779-786
    • Claros, M.G.1    Vincens, P.2
  • 15
    • 0026611680 scopus 로고
    • Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism
    • B.S. Glick, A. Brandt, K. Cunningham, S. Muller, R.L. Hallberg, and G. Schatz Cytochromes c1 and b2 are sorted to the intermembrane space of yeast mitochondria by a stop-transfer mechanism Cell 69 1992 809 822
    • (1992) Cell , vol.69 , pp. 809-822
    • Glick, B.S.1    Brandt, A.2    Cunningham, K.3    Muller, S.4    Hallberg, R.L.5    Schatz, G.6
  • 18
    • 84875417594 scopus 로고    scopus 로고
    • Signal recognition initiates reorganization of the presequence translocase during protein import
    • O. Lytovchenko, J. Melin, C. Schulz, M. Kilisch, D.P. Hutu, and P. Rehling Signal recognition initiates reorganization of the presequence translocase during protein import EMBO J. 32 2013 886 898
    • (2013) EMBO J. , vol.32 , pp. 886-898
    • Lytovchenko, O.1    Melin, J.2    Schulz, C.3    Kilisch, M.4    Hutu, D.P.5    Rehling, P.6
  • 19
    • 84908193702 scopus 로고    scopus 로고
    • Molecular basis of the dynamic structure of the TIM23 complex in the mitochondrial intermembrane space
    • R. Bajaj, L. Jaremko, M. Jaremko, S. Becker, and M. Zweckstetter Molecular basis of the dynamic structure of the TIM23 complex in the mitochondrial intermembrane space Structure 22 2014 1501 1511
    • (2014) Structure , vol.22 , pp. 1501-1511
    • Bajaj, R.1    Jaremko, L.2    Jaremko, M.3    Becker, S.4    Zweckstetter, M.5
  • 20
    • 84923074902 scopus 로고    scopus 로고
    • Cooperation of TOM and TIM23 complexes during translocation of proteins into mitochondria
    • K. Waegemann, D. Popov-Celeketic, W. Neupert, A. Azem, and D. Mokranjac Cooperation of TOM and TIM23 complexes during translocation of proteins into mitochondria J. Mol. Biol. 427 2015 1075 1084
    • (2015) J. Mol. Biol. , vol.427 , pp. 1075-1084
    • Waegemann, K.1    Popov-Celeketic, D.2    Neupert, W.3    Azem, A.4    Mokranjac, D.5
  • 22
    • 84875738395 scopus 로고    scopus 로고
    • The mitochondrial protein import machinery has multiple connections to the respiratory chain
    • B. Kulawiak, J. Hopker, M. Gebert, B. Guiard, N. Wiedemann, and N. Gebert The mitochondrial protein import machinery has multiple connections to the respiratory chain Biochim. Biophys. Acta 1827 2013 612 626
    • (2013) Biochim. Biophys. Acta , vol.1827 , pp. 612-626
    • Kulawiak, B.1    Hopker, J.2    Gebert, M.3    Guiard, B.4    Wiedemann, N.5    Gebert, N.6
  • 24
    • 44349105790 scopus 로고    scopus 로고
    • Active remodelling of the TIM23 complex during translocation of preproteins into mitochondria
    • D. Popov-Celeketic, K. Mapa, W. Neupert, and D. Mokranjac Active remodelling of the TIM23 complex during translocation of preproteins into mitochondria EMBO J. 27 2008 1469 1480
    • (2008) EMBO J. , vol.27 , pp. 1469-1480
    • Popov-Celeketic, D.1    Mapa, K.2    Neupert, W.3    Mokranjac, D.4
  • 26
    • 84904191032 scopus 로고    scopus 로고
    • Remodelling of the active presequence translocase drives motor-dependent mitochondrial protein translocation
    • C. Schulz, and P. Rehling Remodelling of the active presequence translocase drives motor-dependent mitochondrial protein translocation Nat. Commun. 5 2014 4349
    • (2014) Nat. Commun. , vol.5 , pp. 4349
    • Schulz, C.1    Rehling, P.2
  • 27
    • 84871792997 scopus 로고    scopus 로고
    • Mitochondrial protein import: Common principles and physiological networks
    • J. Dudek, P. Rehling, and M. van der Laan Mitochondrial protein import: common principles and physiological networks Biochim. Biophys. Acta 1833 2013 274 285
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 274-285
    • Dudek, J.1    Rehling, P.2    Van Der Laan, M.3
  • 28
  • 29
    • 37249039150 scopus 로고    scopus 로고
    • Sorting switch of mitochondrial presequence translocase involves coupling of motor module to respiratory chain
    • N. Wiedemann, M. van der Laan, D.P. Hutu, P. Rehling, and N. Pfanner Sorting switch of mitochondrial presequence translocase involves coupling of motor module to respiratory chain J. Cell Biol. 179 2007 1115 1122
    • (2007) J. Cell Biol. , vol.179 , pp. 1115-1122
    • Wiedemann, N.1    Van Der Laan, M.2    Hutu, D.P.3    Rehling, P.4    Pfanner, N.5
  • 30
    • 55549119296 scopus 로고    scopus 로고
    • The yeast Aac2 protein exists in physical association with the cytochrome bc1-COX supercomplex and the TIM23 machinery
    • M.K. Dienhart, and R.A. Stuart The yeast Aac2 protein exists in physical association with the cytochrome bc1-COX supercomplex and the TIM23 machinery Mol. Biol. Cell 19 2008 3934 3943
    • (2008) Mol. Biol. Cell , vol.19 , pp. 3934-3943
    • Dienhart, M.K.1    Stuart, R.A.2
  • 31
    • 84864447566 scopus 로고    scopus 로고
    • Dual location of the mitochondrial preprotein transporters B14.7 and Tim23-2 in complex i and the TIM17:23 complex in Arabidopsis links mitochondrial activity and biogenesis
    • Y. Wang, C. Carrie, E. Giraud, D. Elhafez, R. Narsai, O. Duncan, J. Whelan, and M.W. Murcha Dual location of the mitochondrial preprotein transporters B14.7 and Tim23-2 in complex I and the TIM17:23 complex in Arabidopsis links mitochondrial activity and biogenesis Plant Cell 24 2012 2675 2695
    • (2012) Plant Cell , vol.24 , pp. 2675-2695
    • Wang, Y.1    Carrie, C.2    Giraud, E.3    Elhafez, D.4    Narsai, R.5    Duncan, O.6    Whelan, J.7    Murcha, M.W.8
  • 33
    • 84942879598 scopus 로고    scopus 로고
    • Structure of subcomplex Ibeta of mammalian respiratory complex i leads to new supernumerary subunit assignments
    • J. Zhu, M.S. King, M. Yu, L. Klipcan, A.G. Leslie, and J. Hirst Structure of subcomplex Ibeta of mammalian respiratory complex I leads to new supernumerary subunit assignments Proc. Natl. Acad. Sci. U. S. A. 112 2015 12087 12092
    • (2015) Proc. Natl. Acad. Sci. U. S. A. , vol.112 , pp. 12087-12092
    • Zhu, J.1    King, M.S.2    Yu, M.3    Klipcan, L.4    Leslie, A.G.5    Hirst, J.6
  • 34
    • 21244497717 scopus 로고    scopus 로고
    • A disulfide relay system in mitochondria
    • K. Tokatlidis A disulfide relay system in mitochondria Cell 121 2005 965 967
    • (2005) Cell , vol.121 , pp. 965-967
    • Tokatlidis, K.1
  • 35
    • 0346687594 scopus 로고    scopus 로고
    • The small Tim proteins and the twin Cx3C motif
    • C.M. Koehler The small Tim proteins and the twin Cx3C motif Trends Biochem. Sci. 29 2004 1 4
    • (2004) Trends Biochem. Sci. , vol.29 , pp. 1-4
    • Koehler, C.M.1
  • 38
    • 84931561092 scopus 로고    scopus 로고
    • Organization of the mitochondrial translation machinery studied in situ by cryoelectron tomography
    • S. Pfeffer, M.W. Woellhaf, J.M. Herrmann, and F. Forster Organization of the mitochondrial translation machinery studied in situ by cryoelectron tomography Nat. Commun. 6 2015 6019
    • (2015) Nat. Commun. , vol.6 , pp. 6019
    • Pfeffer, S.1    Woellhaf, M.W.2    Herrmann, J.M.3    Forster, F.4
  • 39
    • 56349118008 scopus 로고    scopus 로고
    • Roles of Oxa1-related inner-membrane translocases in assembly of respiratory chain complexes
    • N. Bonnefoy, H.L. Fiumera, G. Dujardin, and T.D. Fox Roles of Oxa1-related inner-membrane translocases in assembly of respiratory chain complexes Biochim. Biophys. Acta 1793 2009 60 70
    • (2009) Biochim. Biophys. Acta , vol.1793 , pp. 60-70
    • Bonnefoy, N.1    Fiumera, H.L.2    Dujardin, G.3    Fox, T.D.4
  • 40
    • 0028245283 scopus 로고
    • OXA1, a Saccharomyces cerevisiae nuclear gene whose sequence is conserved from prokaryotes to eukaryotes controls cytochrome oxidase biogenesis
    • N. Bonnefoy, F. Chalvet, P. Hamel, P.P. Slonimski, and G. Dujardin OXA1, a Saccharomyces cerevisiae nuclear gene whose sequence is conserved from prokaryotes to eukaryotes controls cytochrome oxidase biogenesis J. Mol. Biol. 239 1994 201 212
    • (1994) J. Mol. Biol. , vol.239 , pp. 201-212
    • Bonnefoy, N.1    Chalvet, F.2    Hamel, P.3    Slonimski, P.P.4    Dujardin, G.5
  • 42
    • 0345732691 scopus 로고    scopus 로고
    • Ribosome binding to the Oxa1 complex facilitates co-translational protein insertion in mitochondria
    • G. Szyrach, M. Ott, N. Bonnefoy, W. Neupert, and J.M. Herrmann Ribosome binding to the Oxa1 complex facilitates co-translational protein insertion in mitochondria EMBO J. 22 2003 6448 6457
    • (2003) EMBO J. , vol.22 , pp. 6448-6457
    • Szyrach, G.1    Ott, M.2    Bonnefoy, N.3    Neupert, W.4    Herrmann, J.M.5
  • 43
    • 0348136787 scopus 로고    scopus 로고
    • Yeast Oxa1 interacts with mitochondrial ribosomes: The importance of the C-terminal region of Oxa1
    • L. Jia, M. Dienhart, M. Schramp, M. McCauley, K. Hell, and R.A. Stuart Yeast Oxa1 interacts with mitochondrial ribosomes: the importance of the C-terminal region of Oxa1 EMBO J. 22 2003 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
  • 44
    • 35548996344 scopus 로고    scopus 로고
    • Knockdown of human Oxa1l impairs the biogenesis of F1Fo-ATP synthase and NADH:ubiquinone oxidoreductase
    • L. Stiburek, D. Fornuskova, L. Wenchich, M. Pejznochova, H. Hansikova, and J. Zeman Knockdown of human Oxa1l impairs the biogenesis of F1Fo-ATP synthase and NADH:ubiquinone oxidoreductase J. Mol. Biol. 374 2007 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
  • 45
    • 84929194905 scopus 로고    scopus 로고
    • The complex crosstalk between mitochondria and the nucleus: What goes in between?
    • U. Cagin, and J.A. Enriquez The complex crosstalk between mitochondria and the nucleus: What goes in between? Int. J. Biochem. Cell Biol. 63 2015 10 15
    • (2015) Int. J. Biochem. Cell Biol. , vol.63 , pp. 10-15
    • Cagin, U.1    Enriquez, J.A.2
  • 47
    • 77955400948 scopus 로고    scopus 로고
    • Cooperation of stop-transfer and conservative sorting mechanisms in mitochondrial protein transport
    • M. Bohnert, P. Rehling, B. Guiard, J.M. Herrmann, N. Pfanner, and M. van der Laan Cooperation of stop-transfer and conservative sorting mechanisms in mitochondrial protein transport Curr. Biol. 20 2010 1227 1232
    • (2010) Curr. Biol. , vol.20 , pp. 1227-1232
    • Bohnert, M.1    Rehling, P.2    Guiard, B.3    Herrmann, J.M.4    Pfanner, N.5    Van Der Laan, M.6
  • 48
    • 84862527999 scopus 로고    scopus 로고
    • The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates
    • S. Stoldt, D. Wenzel, M. Hildenbeutel, C.A. Wurm, J.M. Herrmann, and S. Jakobs The inner-mitochondrial distribution of Oxa1 depends on the growth conditions and on the availability of substrates Mol. Biol. Cell 23 2012 2292 2301
    • (2012) Mol. Biol. Cell , vol.23 , pp. 2292-2301
    • Stoldt, S.1    Wenzel, D.2    Hildenbeutel, M.3    Wurm, C.A.4    Herrmann, J.M.5    Jakobs, S.6
  • 49
    • 84908680736 scopus 로고    scopus 로고
    • Mode of membrane insertion of individual transmembrane segments in Mdl1 and Mdl2, multi-spanning mitochondrial ABC transporters
    • K. Park, S.J. Jung, H. Kim, and H. Kim Mode of membrane insertion of individual transmembrane segments in Mdl1 and Mdl2, multi-spanning mitochondrial ABC transporters FEBS Lett. 588 2014 3445 3453
    • (2014) FEBS Lett. , vol.588 , pp. 3445-3453
    • Park, K.1    Jung, S.J.2    Kim, H.3    Kim, H.4
  • 51
    • 84865073903 scopus 로고    scopus 로고
    • Early complex i assembly defects result in rapid turnover of the ND1 subunit
    • O. Zurita Rendon, and E.A. Shoubridge Early complex I assembly defects result in rapid turnover of the ND1 subunit Hum. Mol. Genet. 21 2012 3815 3824
    • (2012) Hum. Mol. Genet. , vol.21 , pp. 3815-3824
    • Zurita Rendon, O.1    Shoubridge, E.A.2
  • 53
    • 0036523991 scopus 로고    scopus 로고
    • CIA30 complex i assembly factor: A candidate for human complex i deficiency?
    • R. Janssen, J. Smeitink, R. Smeets, and L. van Den Heuvel CIA30 complex I assembly factor: a candidate for human complex I deficiency? Hum. Genet. 110 2002 264 270
    • (2002) Hum. Genet. , vol.110 , pp. 264-270
    • Janssen, R.1    Smeitink, J.2    Smeets, R.3    Van Den Heuvel, L.4
  • 59
    • 26444488636 scopus 로고    scopus 로고
    • A molecular chaperone for mitochondrial complex i assembly is mutated in a progressive encephalopathy
    • I. Ogilvie, N.G. Kennaway, and E.A. Shoubridge A molecular chaperone for mitochondrial complex I assembly is mutated in a progressive encephalopathy J. Clin. Invest. 115 2005 2784 2792
    • (2005) J. Clin. Invest. , vol.115 , pp. 2784-2792
    • Ogilvie, I.1    Kennaway, N.G.2    Shoubridge, E.A.3
  • 68
    • 84893853456 scopus 로고    scopus 로고
    • TIMMDC1/C3orf1 functions as a membrane-embedded mitochondrial complex i assembly factor through association with the MCIA complex
    • V. Guarani, J. Paulo, B. Zhai, E.L. Huttlin, S.P. Gygi, and J.W. Harper TIMMDC1/C3orf1 functions as a membrane-embedded mitochondrial complex I assembly factor through association with the MCIA complex Mol. Cell. Biol. 34 2014 847 861
    • (2014) Mol. Cell. Biol. , vol.34 , pp. 847-861
    • Guarani, V.1    Paulo, J.2    Zhai, B.3    Huttlin, E.L.4    Gygi, S.P.5    Harper, J.W.6
  • 69
    • 84929769475 scopus 로고    scopus 로고
    • The arginine methyltransferase NDUFAF7 is essential for complex i assembly and early vertebrate embryogenesis
    • O. Zurita Rendon, L. Silva Neiva, F. Sasarman, and E.A. Shoubridge The arginine methyltransferase NDUFAF7 is essential for complex I assembly and early vertebrate embryogenesis Hum. Mol. Genet. 23 2014 5159 5170
    • (2014) Hum. Mol. Genet. , vol.23 , pp. 5159-5170
    • Zurita Rendon, O.1    Silva Neiva, L.2    Sasarman, F.3    Shoubridge, E.A.4
  • 75
    • 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
  • 78
    • 77956513916 scopus 로고    scopus 로고
    • Mass estimation of native proteins by blue native electrophoresis: Principles and practical hints
    • I. Wittig, T. Beckhaus, Z. Wumaier, M. Karas, and H. Schagger Mass estimation of native proteins by blue native electrophoresis: principles and practical hints Mol. Cell. Proteomics 9 2010 2149 2161
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 2149-2161
    • Wittig, I.1    Beckhaus, T.2    Wumaier, Z.3    Karas, M.4    Schagger, H.5
  • 82
    • 82555168324 scopus 로고    scopus 로고
    • Mutations in the gene encoding C8orf38 block complex i assembly by inhibiting production of the mitochondria-encoded subunit ND1
    • M. McKenzie, E.J. Tucker, A.G. Compton, M. Lazarou, C. George, D.R. Thorburn, and M.T. Ryan Mutations in the gene encoding C8orf38 block complex I assembly by inhibiting production of the mitochondria-encoded subunit ND1 J. Mol. Biol. 414 2011 413 426
    • (2011) J. Mol. Biol. , vol.414 , pp. 413-426
    • McKenzie, M.1    Tucker, E.J.2    Compton, A.G.3    Lazarou, M.4    George, C.5    Thorburn, D.R.6    Ryan, M.T.7
  • 85
    • 19544369483 scopus 로고    scopus 로고
    • Human mitochondrial complex i assembles through the combination of evolutionary conserved modules: A framework to interpret complex i deficiencies
    • C. Ugalde, R. Vogel, R. Huijbens, B. Van Den Heuvel, J. Smeitink, and L. Nijtmans Human mitochondrial complex I assembles through the combination of evolutionary conserved modules: a framework to interpret complex I deficiencies Hum. Mol. Genet. 13 2004 2461 2472
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 2461-2472
    • Ugalde, C.1    Vogel, R.2    Huijbens, R.3    Van Den Heuvel, B.4    Smeitink, J.5    Nijtmans, L.6
  • 87
    • 58149092094 scopus 로고    scopus 로고
    • The essential cytosolic iron-sulfur protein Nbp35 acts without Cfd1 partner in the green lineage
    • K. Bych, D.J. Netz, G. Vigani, E. Bill, R. Lill, A.J. Pierik, and J. Balk The essential cytosolic iron-sulfur protein Nbp35 acts without Cfd1 partner in the green lineage J. Biol. Chem. 283 2008 35797 35804
    • (2008) J. Biol. Chem. , vol.283 , pp. 35797-35804
    • Bych, K.1    Netz, D.J.2    Vigani, G.3    Bill, E.4    Lill, R.5    Pierik, A.J.6    Balk, J.7
  • 88
    • 68949128587 scopus 로고    scopus 로고
    • Function and biogenesis of iron-sulphur proteins
    • R. Lill Function and biogenesis of iron-sulphur proteins Nature 460 2009 831 838
    • (2009) Nature , vol.460 , pp. 831-838
    • Lill, R.1
  • 89
    • 84883866807 scopus 로고    scopus 로고
    • Insights into the pathogenic character of a common NUBPL branch-site mutation associated with mitochondrial disease and complex i deficiency using a yeast model
    • M.M. Wydro, and J. Balk Insights into the pathogenic character of a common NUBPL branch-site mutation associated with mitochondrial disease and complex I deficiency using a yeast model Dis. Model. Mech. 6 2013 1279 1284
    • (2013) Dis. Model. Mech. , vol.6 , pp. 1279-1284
    • Wydro, M.M.1    Balk, J.2
  • 90
    • 84880650976 scopus 로고    scopus 로고
    • Novel insights into the role of Neurospora crassa NDUFAF2, an evolutionarily conserved mitochondrial complex i assembly factor
    • B. Pereira, A. Videira, and M. Duarte Novel insights into the role of Neurospora crassa NDUFAF2, an evolutionarily conserved mitochondrial complex I assembly factor Mol. Cell. Biol. 33 2013 2623 2634
    • (2013) Mol. Cell. Biol. , vol.33 , pp. 2623-2634
    • Pereira, B.1    Videira, A.2    Duarte, M.3
  • 92
    • 1642382090 scopus 로고    scopus 로고
    • Differences in assembly or stability of complex i and other mitochondrial OXPHOS complexes in inherited complex i deficiency
    • C. Ugalde, R.J. Janssen, L.P. van den Heuvel, J.A. Smeitink, and L.G. Nijtmans Differences in assembly or stability of complex I and other mitochondrial OXPHOS complexes in inherited complex I deficiency Hum. Mol. Genet. 13 2004 659 667
    • (2004) Hum. Mol. Genet. , vol.13 , pp. 659-667
    • Ugalde, C.1    Janssen, R.J.2    Van Den Heuvel, L.P.3    Smeitink, J.A.4    Nijtmans, L.G.5
  • 93
    • 34147109143 scopus 로고    scopus 로고
    • Identification of mitochondrial complex i assembly intermediates by tracing tagged NDUFS3 demonstrates the entry point of mitochondrial subunits
    • R.O. Vogel, C.E. Dieteren, L.P. van den Heuvel, P.H. Willems, J.A. Smeitink, W.J. Koopman, and L.G. Nijtmans Identification of mitochondrial complex I assembly intermediates by tracing tagged NDUFS3 demonstrates the entry point of mitochondrial subunits J. Biol. Chem. 282 2007 7582 7590
    • (2007) J. Biol. Chem. , vol.282 , pp. 7582-7590
    • Vogel, R.O.1    Dieteren, C.E.2    Van Den Heuvel, L.P.3    Willems, P.H.4    Smeitink, J.A.5    Koopman, W.J.6    Nijtmans, L.G.7
  • 94
    • 84872696246 scopus 로고    scopus 로고
    • Gene knockout using transcription activator-like effector nucleases (TALENs) reveals that human NDUFA9 protein is essential for stabilizing the junction between membrane and matrix arms of complex i
    • D.A. Stroud, L.E. Formosa, X.W. Wijeyeratne, T.N. Nguyen, and M.T. Ryan Gene knockout using transcription activator-like effector nucleases (TALENs) reveals that human NDUFA9 protein is essential for stabilizing the junction between membrane and matrix arms of complex I J. Biol. Chem. 288 2013 1685 1690
    • (2013) J. Biol. Chem. , vol.288 , pp. 1685-1690
    • Stroud, D.A.1    Formosa, L.E.2    Wijeyeratne, X.W.3    Nguyen, T.N.4    Ryan, M.T.5
  • 95
    • 33751561773 scopus 로고    scopus 로고
    • Tight binding of NADPH to the 39-kDa subunit of complex i is not required for catalytic activity but stabilizes the multiprotein complex
    • A. Abdrakhmanova, K. Zwicker, S. Kerscher, V. Zickermann, and U. Brandt Tight binding of NADPH to the 39-kDa subunit of complex I is not required for catalytic activity but stabilizes the multiprotein complex Biochim. Biophys. Acta 1757 2006 1676 1682
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 1676-1682
    • Abdrakhmanova, A.1    Zwicker, K.2    Kerscher, S.3    Zickermann, V.4    Brandt, U.5
  • 97
    • 9644268262 scopus 로고    scopus 로고
    • Molecular genetics of complex I-deficient Chinese hamster cell lines
    • I.E. Scheffler, N. Yadava, and P. Potluri Molecular genetics of complex I-deficient Chinese hamster cell lines Biochim. Biophys. Acta 1659 2004 160 171
    • (2004) Biochim. Biophys. Acta , vol.1659 , pp. 160-171
    • Scheffler, I.E.1    Yadava, N.2    Potluri, P.3
  • 100
    • 78049433528 scopus 로고    scopus 로고
    • Coevolution predicts direct interactions between mtDNA-encoded and nDNA-encoded subunits of oxidative phosphorylation complex i
    • M. Gershoni, A. Fuchs, N. Shani, Y. Fridman, M. Corral-Debrinski, A. Aharoni, D. Frishman, and D. Mishmar Coevolution predicts direct interactions between mtDNA-encoded and nDNA-encoded subunits of oxidative phosphorylation complex i J. Mol. Biol. 404 2010 158 171
    • (2010) J. Mol. Biol. , vol.404 , pp. 158-171
    • Gershoni, M.1    Fuchs, A.2    Shani, N.3    Fridman, Y.4    Corral-Debrinski, M.5    Aharoni, A.6    Frishman, D.7    Mishmar, D.8
  • 101
    • 84928610806 scopus 로고    scopus 로고
    • Redefining the roles of mitochondrial DNA-encoded subunits in respiratory Complex i assembly
    • R. Vartak, J. Deng, H. Fang, and Y. Bai Redefining the roles of mitochondrial DNA-encoded subunits in respiratory Complex I assembly Biochim. Biophys. Acta 1852 2015 1531 1539
    • (2015) Biochim. Biophys. Acta , vol.1852 , pp. 1531-1539
    • Vartak, R.1    Deng, J.2    Fang, H.3    Bai, Y.4
  • 102
    • 84923045322 scopus 로고    scopus 로고
    • Eukaryotic LYR proteins interact with mitochondrial protein complexes
    • H. Angerer Eukaryotic LYR proteins interact with mitochondrial protein complexes Biology (Basel) 4 2015 133 150
    • (2015) Biology (Basel) , vol.4 , pp. 133-150
    • Angerer, H.1
  • 104
    • 84879336524 scopus 로고    scopus 로고
    • The mitochondrial disease associated protein Ndufaf2 is dispensable for Complex-1 assembly but critical for the regulation of oxidative stress
    • J.S. Schlehe, M.S. Journel, K.P. Taylor, K.D. Amodeo, and M.J. LaVoie The mitochondrial disease associated protein Ndufaf2 is dispensable for Complex-1 assembly but critical for the regulation of oxidative stress Neurobiol. Dis. 58 2013 57 67
    • (2013) Neurobiol. Dis. , vol.58 , pp. 57-67
    • Schlehe, J.S.1    Journel, M.S.2    Taylor, K.P.3    Amodeo, K.D.4    LaVoie, M.J.5
  • 106
    • 84857794576 scopus 로고    scopus 로고
    • Next-generation sequencing in molecular diagnosis: NUBPL mutations highlight the challenges of variant detection and interpretation
    • E.J. Tucker, M. Mimaki, A.G. Compton, M. McKenzie, M.T. Ryan, and D.R. Thorburn Next-generation sequencing in molecular diagnosis: NUBPL mutations highlight the challenges of variant detection and interpretation Hum. Mutat. 33 2012 411 418
    • (2012) Hum. Mutat. , vol.33 , pp. 411-418
    • Tucker, E.J.1    Mimaki, M.2    Compton, A.G.3    McKenzie, M.4    Ryan, M.T.5    Thorburn, D.R.6
  • 108
    • 84982802748 scopus 로고    scopus 로고
    • Leukodystrophy associated with mitochondrial complex i deficiency due to a novel mutation in the NDUFAF1 gene
    • L. Wu, J. Peng, Y. Ma, F. He, X. Deng, G. Wang, Y. Lifen, and F. Yin Leukodystrophy associated with mitochondrial complex I deficiency due to a novel mutation in the NDUFAF1 gene Mitochondrial DNA 27 2016 1034 1037
    • (2016) Mitochondrial DNA , vol.27 , pp. 1034-1037
    • Wu, L.1    Peng, J.2    Ma, Y.3    He, F.4    Deng, X.5    Wang, G.6    Lifen, Y.7    Yin, F.8
  • 110
    • 80955136595 scopus 로고    scopus 로고
    • Mutations in the mitochondrial complex i assembly factor NDUFAF1 cause fatal infantile hypertrophic cardiomyopathy
    • E. Fassone, J.W. Taanman, I.P. Hargreaves, N.J. Sebire, M.A. Cleary, M. Burch, and S. Rahman Mutations in the mitochondrial complex I assembly factor NDUFAF1 cause fatal infantile hypertrophic cardiomyopathy J. Med. Genet. 48 2011 691 697
    • (2011) J. Med. Genet. , vol.48 , pp. 691-697
    • Fassone, E.1    Taanman, J.W.2    Hargreaves, I.P.3    Sebire, N.J.4    Cleary, M.A.5    Burch, M.6    Rahman, S.7
  • 114
    • 84958241864 scopus 로고    scopus 로고
    • Neonatal multiorgan failure due to ACAD9 mutation and complex i deficiency with mitochondrial hyperplasia in liver, cardiac myocytes, skeletal muscle, and renal tubules
    • N. Leslie, X. Wang, Y. Peng, C.A. Valencia, Z. Khuchua, J. Hata, D. Witte, T. Huang, and K.E. Bove Neonatal multiorgan failure due to ACAD9 mutation and complex I deficiency with mitochondrial hyperplasia in liver, cardiac myocytes, skeletal muscle, and renal tubules Hum. Pathol. 49 2016 27 32
    • (2016) Hum. Pathol. , vol.49 , pp. 27-32
    • Leslie, N.1    Wang, X.2    Peng, Y.3    Valencia, C.A.4    Khuchua, Z.5    Hata, J.6    Witte, D.7    Huang, T.8    Bove, K.E.9


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.