메뉴 건너뛰기




Volumn 4, Issue 1, 2015, Pages 133-150

Eukaryotic LYR proteins interact with mitochondrial protein complexes

Author keywords

ACPM; Insulin resistance; Lipoic acid (6,8 dithio octanoic acid); LYR motif; LYR proteins; LYRM; Mitochondria; Mitochondrial acyl carrier protein; Mitochondrial fatty acid synthesis type II; OXPHOS complexes; Reactive oxygen species; Respiratory complex I

Indexed keywords


EID: 84923045322     PISSN: None     EISSN: 20797737     Source Type: Journal    
DOI: 10.3390/biology4010133     Document Type: Review
Times cited : (68)

References (83)
  • 2
    • 84884600998 scopus 로고    scopus 로고
    • The superfamily of mitochondrial Complex1_LYR motif-containing (LYRM) proteins
    • Angerer, H. The superfamily of mitochondrial Complex1_LYR motif-containing (LYRM) proteins. Biochem. Soc. Trans. 2013, 41, 1335–1341.
    • (2013) Biochem. Soc. Trans , vol.41 , pp. 1335-1341
    • Angerer, H.1
  • 4
    • 0033119486 scopus 로고    scopus 로고
    • ACN9 is a novel protein of gluconeogenesis that is located in the mitochondrial intermembrane space
    • Dennis, R.A.; McCammon, M.T. ACN9 is a novel protein of gluconeogenesis that is located in the mitochondrial intermembrane space. Eur. J. Biochem. 1999, 261, 236–243.
    • (1999) Eur. J. Biochem , vol.261 , pp. 236-243
    • Dennis, R.A.1    McCammon, M.T.2
  • 5
    • 84905860097 scopus 로고    scopus 로고
    • The LYR factors SDHAF1 and SDHAF3 mediate maturation of the iron-sulfur subunit of succinate dehydrogenase
    • Na, U.; Yu, W.; Cox, J.; Bricker, D.K.; Brockmann, K.; Rutter, J.; Thummel, C.S.; Winge, D.R. The LYR factors SDHAF1 and SDHAF3 mediate maturation of the iron-sulfur subunit of succinate dehydrogenase. Cell Metab. 2014, 20, 253–266.
    • (2014) Cell Metab , vol.20 , pp. 253-266
    • Na, U.1    Yu, W.2    Cox, J.3    Bricker, D.K.4    Brockmann, K.5    Rutter, J.6    Thummel, C.S.7    Winge, D.R.8
  • 6
    • 0035794147 scopus 로고    scopus 로고
    • Identification of a nuclear gene (FMC1) required for the assembly/stability of yeast mitochondrial F(1)-ATPase in heat stress conditions
    • Lefebvre-Legendre, L.; Vaillier, J.; Benabdelhak, H.; Velours, J.; Slonimski, P.P.; di Rago, J.P. Identification of a nuclear gene (FMC1) required for the assembly/stability of yeast mitochondrial F(1)-ATPase in heat stress conditions. J. Biol. Chem. 2001, 276, 6789–6796.
    • (2001) J. Biol. Chem , vol.276 , pp. 6789-6796
    • Lefebvre-Legendre, L.1    Vaillier, J.2    Benabdelhak, H.3    Velours, J.4    Slonimski, P.P.5    Di Rago, J.P.6
  • 8
    • 68049086933 scopus 로고    scopus 로고
    • Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis
    • Shi, Y.; Ghosh, M.C.; Tong, W.H.; Rouault, T.A. Human ISD11 is essential for both iron-sulfur cluster assembly and maintenance of normal cellular iron homeostasis. Hum. Mol. Genet. 2009, 18, 3014–3025.
    • (2009) Hum. Mol. Genet , vol.18 , pp. 3014-3025
    • Shi, Y.1    Ghosh, M.C.2    Tong, W.H.3    Rouault, T.A.4
  • 9
    • 84862831266 scopus 로고    scopus 로고
    • Effects of LYRM1 knockdown on mitochondrial function in 3 T3-L1 murine adipocytes
    • Zhu, G.Z.; Zhang, M.; Kou, C.Z.; Ni, Y.H.; Ji, C.B.; Cao, X.G.; Guo, X.R. Effects of LYRM1 knockdown on mitochondrial function in 3 T3-L1 murine adipocytes. J. Bioenerg. Biomembr. 2012, 44, 225–232.
    • (2012) J. Bioenerg. Biomembr , vol.44 , pp. 225-232
    • Zhu, G.Z.1    Zhang, M.2    Kou, C.Z.3    Ni, Y.H.4    Ji, C.B.5    Cao, X.G.6    Guo, X.R.7
  • 12
    • 27344435796 scopus 로고    scopus 로고
    • Mitochondrial complex I activity is impaired during HIV-1-induced T-cell apoptosis
    • Ladha, J.S.; Tripathy, M.K.; Mitra, D. Mitochondrial complex I activity is impaired during HIV-1-induced T-cell apoptosis. Cell Death. Differ. 2005, 12, 1417–1428.
    • (2005) Cell Death. Differ , vol.12 , pp. 1417-1428
    • Ladha, J.S.1    Tripathy, M.K.2    Mitra, D.3
  • 13
    • 84887613215 scopus 로고    scopus 로고
    • A homozygous mutation in LYRM7/MZM1L associated with early onset encephalopathy, lactic acidosis, and severe reduction of mitochondrial complex III activity
    • Invernizzi, F.; Tigano, M.; Dallabona, C.; Donnini, C.; Ferrero, I.; Cremonte, M.; Ghezzi, D.; Lamperti, C.; Zeviani, M. A homozygous mutation in LYRM7/MZM1L associated with early onset encephalopathy, lactic acidosis, and severe reduction of mitochondrial complex III activity. Hum. Mutat. 2013, 34, 1619–1622.
    • (2013) Hum. Mutat , vol.34 , pp. 1619-1622
    • Invernizzi, F.1    Tigano, M.2    Dallabona, C.3    Donnini, C.4    Ferrero, I.5    Cremonte, M.6    Ghezzi, D.7    Lamperti, C.8    Zeviani, M.9
  • 15
    • 43049171797 scopus 로고    scopus 로고
    • A Systematic single nucleotide polymorphism screen to fine-map alcohol dependence genes on chromosome 7 identifies association with a novel susceptibility gene ACN9
    • Dick, D.M.; Aliev, F.; Wang, J.C.; Saccone, S.; Hinrichs, A.; Bertelsen, S.; Budde, J.; Saccone, N.; Foroud, T.; Nurnberger, J.; et al. A Systematic single nucleotide polymorphism screen to fine-map alcohol dependence genes on chromosome 7 identifies association with a novel susceptibility gene ACN9. Biol. Psychiatry2008, 63, 1047–1053.
    • (2008) Biol. Psychiatry , vol.63 , pp. 1047-1053
    • Dick, D.M.1    Aliev, F.2    Wang, J.C.3    Saccone, S.4    Hinrichs, A.5    Bertelsen, S.6    Budde, J.7    Saccone, N.8    Foroud, T.9    Nurnberger, J.10
  • 16
    • 33745618402 scopus 로고    scopus 로고
    • Evolution of the Isd11-IscS complex reveals a single alpha-proteobacterial endosymbiosis for all eukaryotes
    • Richards, T.A.; van der Giezen, M. Evolution of the Isd11-IscS complex reveals a single alpha-proteobacterial endosymbiosis for all eukaryotes. Mol. Biol. Evol. 2006, 23, 1341–1344.
    • (2006) Mol. Biol. Evol , vol.23 , pp. 1341-1344
    • Richards, T.A.1    Van Der Giezen, M.2
  • 17
    • 84897000909 scopus 로고    scopus 로고
    • Mitochondrial iron-sulfur protein biogenesis and human disease
    • Stehling, O.; Wilbrecht, C.; Lill, R. Mitochondrial iron-sulfur protein biogenesis and human disease. Biochimie2014, 100, 61–77.
    • (2014) Biochimie , vol.100 , pp. 61-77
    • Stehling, O.1    Wilbrecht, C.2    Lill, R.3
  • 18
    • 84895735383 scopus 로고    scopus 로고
    • Cochaperone binding to LYR motifs confers specificity of iron sulfur cluster delivery
    • Maio, N.; Singh, A.; Uhrigshardt, H.; Saxena, N.; Tong, W.H.; Rouault, T.A. Cochaperone binding to LYR motifs confers specificity of iron sulfur cluster delivery. Cell Metab. 2014, 19, 445–457.
    • (2014) Cell Metab , vol.19 , pp. 445-457
    • Maio, N.1    Singh, A.2    Uhrigshardt, H.3    Saxena, N.4    Tong, W.H.5    Rouault, T.A.6
  • 19
    • 84885117582 scopus 로고    scopus 로고
    • Human mitochondrial chaperone (MtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU)
    • Cai, K.; Frederick, R.O.; Kim, J.H.; Reinen, N.M.; Tonelli, M.; Markley, J.L. Human mitochondrial chaperone (mtHSP70) and cysteine desulfurase (NFS1) bind preferentially to the disordered conformation, whereas co-chaperone (HSC20) binds to the structured conformation of the iron-sulfur cluster scaffold protein (ISCU). J. Biol. Chem. 2013, 288, 28755–28770.
    • (2013) J. Biol. Chem , vol.288 , pp. 28755-28770
    • Cai, K.1    Frederick, R.O.2    Kim, J.H.3    Reinen, N.M.4    Tonelli, M.5    Markley, J.L.6
  • 20
    • 84930051032 scopus 로고    scopus 로고
    • Iron-sulfur cluster biogenesis in mammalian cells: New insights into the molecular mechanisms of cluster delivery
    • Maio, N.; Rouault, T.A. Iron-sulfur cluster biogenesis in mammalian cells: New insights into the molecular mechanisms of cluster delivery. Biochim. Biophys. Acta2014, doi:10.1016/j.bbamcr.2014.09.009.
    • (2014) Biochim. Biophys. Acta
    • Maio, N.1    Rouault, T.A.2
  • 21
    • 0029915525 scopus 로고    scopus 로고
    • Computational method to predict mitochondrially imported proteins and their targeting sequences
    • Claros, M.G.; Vincens, P. Computational method to predict mitochondrially imported proteins and their targeting sequences. Eur. J. Biochem. 1996, 241, 779–786.
    • (1996) Eur. J. Biochem , vol.241 , pp. 779-786
    • Claros, M.G.1    Vincens, P.2
  • 23
    • 84922479528 scopus 로고    scopus 로고
    • Structural biology. Mechanistic insight from the crystal structure of mitochondrial complex I
    • Zickermann, V.; Wirth, C.; Nasiri, H.; Siegmund, K.; Schwalbe, H.; Hunte, C.; and Brandt, U. Structural biology. Mechanistic insight from the crystal structure of mitochondrial complex I. Science2015, 347, 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
  • 24
    • 84915761829 scopus 로고    scopus 로고
    • Architecture of mammalian respiratory complex I
    • Vinothkumar, K.R.; Zhu, J.; Hirst, J. Architecture of mammalian respiratory complex I. Nature2014, 515, 80–84.
    • (2014) Nature , vol.515 , pp. 80-84
    • Vinothkumar, K.R.1    Zhu, J.2    Hirst, J.3
  • 26
    • 77954848120 scopus 로고    scopus 로고
    • Functional modules and structural basis of conformational coupling in mitochondrial complex I
    • Hunte, C.; Zickermann, V.; Brandt, U. Functional modules and structural basis of conformational coupling in mitochondrial complex I. Science2010, 329, 448–451.
    • (2010) Science , vol.329 , pp. 448-451
    • Hunte, C.1    Zickermann, V.2    Brandt, U.3
  • 27
    • 84878905186 scopus 로고    scopus 로고
    • Mitochondrial complex I
    • Hirst, J. Mitochondrial complex I. Annu. Rev. Biochem. 2013, 82, 551–575.
    • (2013) Annu. Rev. Biochem , vol.82 , pp. 551-575
    • Hirst, J.1
  • 28
    • 0025827137 scopus 로고
    • Presence of an acyl carrier protein in NADH:Ubiquinone oxidoreductase from bovine heart mitochondria
    • Runswick, M.J.; Fearnley, I.M.; Skehel, J.M.; Walker, J.E. Presence of an acyl carrier protein in NADH:Ubiquinone oxidoreductase from bovine heart mitochondria. FEBS Lett. 1991, 286, 121–124.
    • (1991) FEBS Lett , vol.286 , pp. 121-124
    • Runswick, M.J.1    Fearnley, I.M.2    Skehel, J.M.3    Walker, J.E.4
  • 29
    • 24044496587 scopus 로고    scopus 로고
    • Mammalian mitochondria contain a soluble acyl carrier protein
    • Cronan, J.E.; Fearnley, I.M.; Walker, J.E. Mammalian mitochondria contain a soluble acyl carrier protein. FEBS Lett. 2005, 579, 4892–4896.
    • (2005) FEBS Lett , vol.579 , pp. 4892-4896
    • Cronan, J.E.1    Fearnley, I.M.2    Walker, J.E.3
  • 32
    • 66449128208 scopus 로고    scopus 로고
    • Down-regulation of mitochondrial acyl carrier protein in mammalian cells compromises protein lipoylation and respiratory complex I and results in cell death
    • Feng, D.; Witkowski, A.; Smith, S. Down-regulation of mitochondrial acyl carrier protein in mammalian cells compromises protein lipoylation and respiratory complex I and results in cell death. J. Biol. Chem. 2009, 284, 11436–11445.
    • (2009) J. Biol. Chem , vol.284 , pp. 11436-11445
    • Feng, D.1    Witkowski, A.2    Smith, S.3
  • 34
    • 0029556942 scopus 로고
    • Different respiratory-defective phenotypes of
    • Schneider, R.; Massow, M.; Lisowsky, T.; Weiss, H. Different respiratory-defective phenotypes of Neurospora crassa and Saccharomyces cerevisiae after inactivation of the gene encoding the mitochondrial acyl carrier protein. Curr. Genet. 1995, 29, 10–17.
    • (1995) Curr. Genet , vol.29 , pp. 10-17
    • Schneider, R.1    Massow, M.2    Lisowsky, T.3    Weiss, H.4
  • 36
    • 24344504437 scopus 로고    scopus 로고
    • Endogenous production of lipoic acid is essential for mouse development
    • Yi, X.; Maeda, N. Endogenous production of lipoic acid is essential for mouse development. Mol. Cell Biol. 2005, 25, 8387–8392.
    • (2005) Mol. Cell Biol , vol.25 , pp. 8387-8392
    • Yi, X.1    Maeda, N.2
  • 37
  • 38
    • 84884646222 scopus 로고    scopus 로고
    • Accessory subunits of mitochondrial complex I
    • Kmita, K.; Zickermann, V. Accessory subunits of mitochondrial complex I. Biochem. Soc. Trans. 2013, 41, 1272–1279.
    • (2013) Biochem. Soc. Trans , vol.41 , pp. 1272-1279
    • Kmita, K.1    Zickermann, V.2
  • 39
    • 84901841671 scopus 로고    scopus 로고
    • Characterisation of the active/de-active transition of mitochondrial complex I
    • Babot, M.; Birch, A.; Labarbuta, P.; Galkin, A. Characterisation of the active/de-active transition of mitochondrial complex I. Biochim. Biophys. Acta2014, 1837, 1083–1092.
    • (2014) Biochim. Biophys. Acta , vol.1837 , pp. 1083-1092
    • Babot, M.1    Birch, A.2    Labarbuta, P.3    Galkin, A.4
  • 40
    • 0023904887 scopus 로고
    • Neurospora mitochondria contain an acyl-carrier protein
    • Brody, S.; Mikolajczyk, S. Neurospora mitochondria contain an acyl-carrier protein. Eur. J. Biochem. 1988, 173, 353–359.
    • (1988) Eur. J. Biochem , vol.173 , pp. 353-359
    • Brody, S.1    Mikolajczyk, S.2
  • 45
    • 34447316711 scopus 로고    scopus 로고
    • Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex and multiple mitochondrial chaperones
    • Shan, Y.; Napoli, E.; Cortopassi, G. Mitochondrial frataxin interacts with ISD11 of the NFS1/ISCU complex and multiple mitochondrial chaperones. Hum. Mol. Genet. 2007, 16, 929–941.
    • (2007) Hum. Mol. Genet , vol.16 , pp. 929-941
    • Shan, Y.1    Napoli, E.2    Cortopassi, G.3
  • 47
    • 84869029429 scopus 로고    scopus 로고
    • Persulfide formation on mitochondrial cysteine desulfurase: Enzyme activation by a eukaryote-specific interacting protein and Fe-S cluster synthesis
    • Pandey, A.; Golla, R.; Yoon, H.; Dancis, A.; Pain, D. Persulfide formation on mitochondrial cysteine desulfurase: Enzyme activation by a eukaryote-specific interacting protein and Fe-S cluster synthesis. Biochem. J. 2012, 448, 171–187.
    • (2012) Biochem. J , vol.448 , pp. 171-187
    • Pandey, A.1    Golla, R.2    Yoon, H.3    Dancis, A.4    Pain, D.5
  • 48
    • 84885867368 scopus 로고    scopus 로고
    • The effect of the adaptor protein Isd11 on the quaternary structure of the eukaryotic cysteine desulphurase Nfs1
    • Terali, K.; Beavil, R.L.; Pickersgill, R.W.; van der Giezen, M. The effect of the adaptor protein Isd11 on the quaternary structure of the eukaryotic cysteine desulphurase Nfs1. Biochem. Biophys. Res. Commun. 2013, 440, 235–240.
    • (2013) Biochem. Biophys. Res. Commun , vol.440 , pp. 235-240
    • Terali, K.1    Beavil, R.L.2    Pickersgill, R.W.3    Van Der Giezen, M.4
  • 50
    • 14844317304 scopus 로고    scopus 로고
    • Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: Both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide
    • Cicchillo, R.M.; Booker, S.J. Mechanistic investigations of lipoic acid biosynthesis in Escherichia coli: Both sulfur atoms in lipoic acid are contributed by the same lipoyl synthase polypeptide. J. Am. Chem. Soc. 2005, 127, 2860–2861.
    • (2005) J. Am. Chem. Soc , vol.127 , pp. 2860-2861
    • Cicchillo, R.M.1    Booker, S.J.2
  • 52
    • 0141623560 scopus 로고    scopus 로고
    • An interaction between frataxin and Isu1/NFS1 that is crucial for Fe/S cluster synthesis on Isu1
    • Gerber, J.; Muhlenhoff, U.; Lill, R. An interaction between frataxin and Isu1/NFS1 that is crucial for Fe/S cluster synthesis on Isu1. EMBO Rep. 2003, 4, 906–911.
    • (2003) EMBO Rep , vol.4 , pp. 906-911
    • Gerber, J.1    Muhlenhoff, U.2    Lill, R.3
  • 53
    • 77952480112 scopus 로고    scopus 로고
    • Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin
    • Condo, I.; Malisan, F.; Guccini, I.; Serio, D.; Rufini, A.; Testi, R. Molecular control of the cytosolic aconitase/IRP1 switch by extramitochondrial frataxin. Hum. Mol. Genet. 2010, 19, 1221–1229.
    • (2010) Hum. Mol. Genet , vol.19 , pp. 1221-1229
    • Condo, I.1    Malisan, F.2    Guccini, I.3    Serio, D.4    Rufini, A.5    Testi, R.6
  • 54
    • 3042763187 scopus 로고    scopus 로고
    • Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity
    • Bulteau, A.L.; O’Neill, H.A.; Kennedy, M.C.; Ikeda-Saito, M.; Isaya, G.; Szweda, L.I. Frataxin acts as an iron chaperone protein to modulate mitochondrial aconitase activity. Science2004, 305, 242–245.
    • (2004) Science , vol.305 , pp. 242-245
    • Bulteau, A.L.1    O’Neill, H.A.2    Kennedy, M.C.3    Ikeda-Saito, M.4    Isaya, G.5    Szweda, L.I.6
  • 56
    • 84860439210 scopus 로고    scopus 로고
    • Interplay between lipids and branched-chain amino acids in development of insulin resistance
    • Newgard, C.B. Interplay between lipids and branched-chain amino acids in development of insulin resistance. Cell Metab. 2012, 15, 606–614.
    • (2012) Cell Metab , vol.15 , pp. 606-614
    • Newgard, C.B.1
  • 57
    • 84927173996 scopus 로고    scopus 로고
    • Branched-chain amino acids in metabolic signalling and insulin resistance
    • Lynch, C.J.; Adams, S.H. Branched-chain amino acids in metabolic signalling and insulin resistance. Nat. Rev. Endocrinol. 2014, 10, 723–736.
    • (2014) Nat. Rev. Endocrinol , vol.10 , pp. 723-736
    • Lynch, C.J.1    Adams, S.H.2
  • 58
    • 48949087618 scopus 로고    scopus 로고
    • A branched-chain fatty acid is involved in post-embryonic growth control in parallel to the insulin receptor pathway and its biosynthesis is feedback-regulated in C. Elegans
    • Kniazeva, M.; Euler, T.; Han, M. A branched-chain fatty acid is involved in post-embryonic growth control in parallel to the insulin receptor pathway and its biosynthesis is feedback-regulated in C. elegans. Genes Dev. 2008, 22, 2102–2110.
    • (2008) Genes Dev , vol.22 , pp. 2102-2110
    • Kniazeva, M.1    Euler, T.2    Han, M.3
  • 59
    • 84863338081 scopus 로고    scopus 로고
    • Regulation of maternal phospholipid composition and IP (3)-dependent embryonic membrane dynamics by a specific fatty acid metabolic event in C. Elegans
    • Kniazeva, M.; Shen, H.; Euler, T.; Wang, C.; Han, M. Regulation of maternal phospholipid composition and IP (3)-dependent embryonic membrane dynamics by a specific fatty acid metabolic event in C. elegans. Genes Dev. 2012, 26, 554–566.
    • (2012) Genes Dev , vol.26 , pp. 554-566
    • Kniazeva, M.1    Shen, H.2    Euler, T.3    Wang, C.4    Han, M.5
  • 61
    • 0026662355 scopus 로고
    • Zensen, R.; Husmann, H.; Schneider, R.; Peine, T.; Weiss, H. De novo synthesis and desaturation of fatty acids at the mitochondrial acyl-carrier protein, a subunit of NADH:Ubiquinone oxidoreductase in Neurospora crassa. FEBS Lett. 1992, 310, 179–181.
    • (1992) FEBS Lett , vol.310 , pp. 179-181
    • Zensen, R.1    Husmann, H.2    Schneider, R.3    Peine, T.4    Weiss, H.5
  • 62
    • 0343168085 scopus 로고    scopus 로고
    • Succinate: Quinone oxidoreductases: New insights from X-ray crystal structures
    • Lancaster, C.R.; Kroger, A. Succinate: Quinone oxidoreductases: New insights from X-ray crystal structures. Biochim. Biophys. Acta2000, 1459, 422–431.
    • (2000) Biochim. Biophys. Acta , vol.1459 , pp. 422-431
    • Lancaster, C.R.1    Kroger, A.2
  • 63
    • 84863738048 scopus 로고    scopus 로고
    • Molecular mechanisms of superoxide production by the mitochondrial respiratory chain
    • Drose, S.; Brandt, U. Molecular mechanisms of superoxide production by the mitochondrial respiratory chain. Adv. Exp. Med. Biol. 2012, 748, 145–169.
    • (2012) Adv. Exp. Med. Biol , vol.748 , pp. 145-169
    • Drose, S.1    Brandt, U.2
  • 64
    • 1942447877 scopus 로고    scopus 로고
    • The cytochrome bc1 complex: Function in the context of structure
    • Crofts, A.R. The cytochrome bc1 complex: Function in the context of structure. Annu. Rev. Physiol. 2004, 66, 689–733.
    • (2004) Annu. Rev. Physiol , vol.66 , pp. 689-733
    • Crofts, A.R.1
  • 65
    • 80053601731 scopus 로고    scopus 로고
    • The LYR protein Mzm1 functions in the insertion of the Rieske Fe/S protein in yeast mitochondria
    • Atkinson, A.; Smith, P.; Fox, J.L.; Cui, T.Z.; Khalimonchuk, O.; Winge, D.R. The LYR protein Mzm1 functions in the insertion of the Rieske Fe/S protein in yeast mitochondria. Mol. Cell Biol. 2011, 31, 3988–3996.
    • (2011) Mol. Cell Biol , vol.31 , pp. 3988-3996
    • Atkinson, A.1    Smith, P.2    Fox, J.L.3    Cui, T.Z.4    Khalimonchuk, O.5    Winge, D.R.6
  • 66
    • 84868691750 scopus 로고    scopus 로고
    • Late-stage maturation of the Rieske Fe/S protein: Mzm1 stabilizes Rip1 but does not facilitate its translocation by the AAA ATPase Bcs1
    • Cui, T.Z.; Smith, P.M.; Fox, J.L.; Khalimonchuk, O.; Winge, D.R. Late-stage maturation of the Rieske Fe/S protein: Mzm1 stabilizes Rip1 but does not facilitate its translocation by the AAA ATPase Bcs1. Mol. Cell Biol. 2012, 32, 4400–4409.
    • (2012) Mol. Cell Biol , vol.32 , pp. 4400-4409
    • Cui, T.Z.1    Smith, P.M.2    Fox, J.L.3    Khalimonchuk, O.4    Winge, D.R.5
  • 67
    • 84872100371 scopus 로고    scopus 로고
    • LYRM7/MZM1L is a UQCRFS1 chaperone involved in the last steps of mitochondrial complex III assembly in human cells
    • Sanchez, E.; Lobo, T.; Fox, J.L.; Zeviani, M.; Winge, D.R.; Fernandez-Vizarra, E. LYRM7/MZM1L is a UQCRFS1 chaperone involved in the last steps of mitochondrial complex III assembly in human cells. Biochim. Biophys. Acta2013, 1827, 285–293.
    • (2013) Biochim. Biophys. Acta , vol.1827 , pp. 285-293
    • Sanchez, E.1    Lobo, T.2    Fox, J.L.3    Zeviani, M.4    Winge, D.R.5    Fernandez-Vizarra, E.6
  • 69
    • 84904111748 scopus 로고    scopus 로고
    • DNA microarray analysis of genes differentially expressed in adipocyte differentiation
    • Yin, C.; Xiao, Y.; Zhang, W.; Xu, E.; Liu, W.; Yi, X.; Chang, M. DNA microarray analysis of genes differentially expressed in adipocyte differentiation. J. Biosci. 2014, 39, 415–423.
    • (2014) J. Biosci , vol.39 , pp. 415-423
    • Yin, C.1    Xiao, Y.2    Zhang, W.3    Xu, E.4    Liu, W.5    Yi, X.6    Chang, M.7
  • 71
  • 72
    • 78651313301 scopus 로고    scopus 로고
    • Over-expression of LYRM1 inhibits glucose transport in rat skeletal muscles via attenuated phosphorylation of PI3K (P85) and Akt
    • Kou, C.; Cao, X.; Qin, D.; Ji, C.; Zhu, J.; Zhang, C.; Zhu, C.; Gao, C.; Chen, R.; Guo, X.; et al. Over-expression of LYRM1 inhibits glucose transport in rat skeletal muscles via attenuated phosphorylation of PI3K (p85) and Akt. Mol. Cell Biochem. 2011, 348, 149–154.
    • (2011) Mol. Cell Biochem , vol.348 , pp. 149-154
    • Kou, C.1    Cao, X.2    Qin, D.3    Ji, C.4    Zhu, J.5    Zhang, C.6    Zhu, C.7    Gao, C.8    Chen, R.9    Guo, X.10
  • 73
    • 84866739022 scopus 로고    scopus 로고
    • Alpha-lipoic acid ameliorates impaired glucose uptake in LYRM1 overexpressing 3T3-L1 adipocytes through the IRS-1/Akt signaling pathway
    • Qin, Z.Y.; Zhang, M.; Guo, X.R.; Wang, Y.M.; Zhu, G.Z.; Ni, Y.H.; Zhao, Y.P.; Qiu, J.; Kou, C.Z.; Qin, R.; et al. Alpha-lipoic acid ameliorates impaired glucose uptake in LYRM1 overexpressing 3T3-L1 adipocytes through the IRS-1/Akt signaling pathway. J. Bioenerg. Biomembr. 2012, 44, 579–586.
    • (2012) J. Bioenerg. Biomembr , vol.44 , pp. 579-586
    • Qin, Z.Y.1    Zhang, M.2    Guo, X.R.3    Wang, Y.M.4    Zhu, G.Z.5    Ni, Y.H.6    Zhao, Y.P.7    Qiu, J.8    Kou, C.Z.9    Qin, R.10
  • 75
    • 84907370814 scopus 로고    scopus 로고
    • Effects of metformin and other biguanides on oxidative phosphorylation in mitochondria
    • Bridges, H.R.; Jones, A.J.; Pollak, M.N.; Hirst, J. Effects of metformin and other biguanides on oxidative phosphorylation in mitochondria. Biochem. J. 2014, 462, 475–487.
    • (2014) Biochem. J , vol.462 , pp. 475-487
    • Bridges, H.R.1    Jones, A.J.2    Pollak, M.N.3    Hirst, J.4
  • 76
    • 73949143923 scopus 로고    scopus 로고
    • Temporal gene expression changes induced by a low concentration of benzo[a]pyrene diol epoxide in a normal human cell line
    • Lu, X.; Shao, J.; Li, H.; Yu, Y. Temporal gene expression changes induced by a low concentration of benzo[a]pyrene diol epoxide in a normal human cell line. Mutat. Res. 2010, 684, 74–80.
    • (2010) Mutat. Res , vol.684 , pp. 74-80
    • Lu, X.1    Shao, J.2    Li, H.3    Yu, Y.4
  • 79
    • 33746267471 scopus 로고    scopus 로고
    • Sequential processing of a mitochondrial tandem protein: Insights into protein import in Schizosaccharomyces pombe
    • Khalimonchuk, O.; Ott, M.; Funes, S.; Ostermann, K.; Rodel, G.; Herrmann, J.M. Sequential processing of a mitochondrial tandem protein: Insights into protein import in Schizosaccharomyces pombe. Eukaryot. Cell2006, 5, 997–1006.
    • (2006) Eukaryot. Cell , vol.5 , pp. 997-1006
    • Khalimonchuk, O.1    Ott, M.2    Funes, S.3    Ostermann, K.4    Rodel, G.5    Herrmann, J.M.6
  • 80
  • 81
    • 84888424052 scopus 로고    scopus 로고
    • The evolutionarily conserved iron-sulfur protein INDH is required for complex I assembly and mitochondrial translation in
    • Wydro, M.M.; Sharma, P.; Foster, J.M.; Bych, K.; Meyer, E.H.; Balk, J. The evolutionarily conserved iron-sulfur protein INDH is required for complex I assembly and mitochondrial translation in Arabidopsis (corrected). Plant Cell2013, 25, 4014–4027.
    • (2013) Plant Cell , vol.25 , pp. 4014-4027
    • Wydro, M.M.1    Sharma, P.2    Foster, J.M.3    Bych, K.4    Meyer, E.H.5    Balk, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.