메뉴 건너뛰기




Volumn 49, Issue 1, 2013, Pages 121-132

Phosphorylation of Human TFAM in Mitochondria Impairs DNA Binding and Promotes Degradation by the AAA+ Lon Protease

Author keywords

[No Author keywords available]

Indexed keywords

BORTEZOMIB; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC AMP DEPENDENT PROTEIN KINASE ANCHORING PROTEIN; CYCLOHEXIMIDE; ENDOPEPTIDASE LA; HIGH MOBILITY GROUP B1 PROTEIN; MITOCHONDRIAL DNA; MITOCHONDRIAL TRANSCRIPTION FACTOR A; SMALL INTERFERING RNA;

EID: 84872271398     PISSN: 10972765     EISSN: 10974164     Source Type: Journal    
DOI: 10.1016/j.molcel.2012.10.023     Document Type: Article
Times cited : (243)

References (65)
  • 2
    • 79958034385 scopus 로고    scopus 로고
    • Protein phosphorylation and prevention of cytochrome oxidase inhibition by ATP: coupled mechanisms of energy metabolism regulation
    • Acin-Perez R., Gatti D.L., Bai Y., Manfredi G. Protein phosphorylation and prevention of cytochrome oxidase inhibition by ATP: coupled mechanisms of energy metabolism regulation. Cell Metab. 2011, 13:712-719.
    • (2011) Cell Metab. , vol.13 , pp. 712-719
    • Acin-Perez, R.1    Gatti, D.L.2    Bai, Y.3    Manfredi, G.4
  • 3
    • 2342613652 scopus 로고    scopus 로고
    • The proteasome: a suitable antineoplastic target
    • Adams J. The proteasome: a suitable antineoplastic target. Nat. Rev. Cancer 2004, 4:349-360.
    • (2004) Nat. Rev. Cancer , vol.4 , pp. 349-360
    • Adams, J.1
  • 4
    • 77951682590 scopus 로고    scopus 로고
    • Suborganelle sensing of mitochondrial cAMP-dependent protein kinase activity
    • Agnes R.S., Jernigan F., Shell J.R., Sharma V., Lawrence D.S. Suborganelle sensing of mitochondrial cAMP-dependent protein kinase activity. J. Am. Chem. Soc. 2010, 132:6075-6080.
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 6075-6080
    • Agnes, R.S.1    Jernigan, F.2    Shell, J.R.3    Sharma, V.4    Lawrence, D.S.5
  • 5
    • 33847792061 scopus 로고    scopus 로고
    • Mitochondrial transcription and its regulation in mammalian cells
    • Asin-Cayuela J., Gustafsson C.M. Mitochondrial transcription and its regulation in mammalian cells. Trends Biochem. Sci. 2007, 32:111-117.
    • (2007) Trends Biochem. Sci. , vol.32 , pp. 111-117
    • Asin-Cayuela, J.1    Gustafsson, C.M.2
  • 6
    • 84859585597 scopus 로고    scopus 로고
    • The mitochondrial ATP-dependent Lon protease: a novel target in lymphoma death mediated by the synthetic triterpenoid CDDO and its derivatives
    • Bernstein S.H., Venkatesh S., Li M., Lee J., Lu B., Hilchey S.P., Morse K.M., Metcalfe H.M., Skalska J., Andreeff M., et al. The mitochondrial ATP-dependent Lon protease: a novel target in lymphoma death mediated by the synthetic triterpenoid CDDO and its derivatives. Blood 2012, 119:3321-3329.
    • (2012) Blood , vol.119 , pp. 3321-3329
    • Bernstein, S.H.1    Venkatesh, S.2    Li, M.3    Lee, J.4    Lu, B.5    Hilchey, S.P.6    Morse, K.M.7    Metcalfe, H.M.8    Skalska, J.9    Andreeff, M.10
  • 7
    • 84864308607 scopus 로고    scopus 로고
    • Mitochondrial DNA nucleoid structure
    • Bogenhagen D.F. Mitochondrial DNA nucleoid structure. Biochim. Biophys. Acta 2012, 1819:914-920.
    • (2012) Biochim. Biophys. Acta , vol.1819 , pp. 914-920
    • Bogenhagen, D.F.1
  • 8
    • 41249098355 scopus 로고    scopus 로고
    • The layered structure of human mitochondrial DNA nucleoids
    • Bogenhagen D.F., Rousseau D., Burke S. The layered structure of human mitochondrial DNA nucleoids. J. Biol. Chem. 2008, 283:3665-3675.
    • (2008) J. Biol. Chem. , vol.283 , pp. 3665-3675
    • Bogenhagen, D.F.1    Rousseau, D.2    Burke, S.3
  • 9
    • 33845744837 scopus 로고    scopus 로고
    • Initiation and beyond: multiple functions of the human mitochondrial transcription machinery
    • Bonawitz N.D., Clayton D.A., Shadel G.S. Initiation and beyond: multiple functions of the human mitochondrial transcription machinery. Mol. Cell 2006, 24:813-825.
    • (2006) Mol. Cell , vol.24 , pp. 813-825
    • Bonawitz, N.D.1    Clayton, D.A.2    Shadel, G.S.3
  • 10
    • 0003097634 scopus 로고    scopus 로고
    • Protein degradation in mitochondria: implications for oxidative stress, aging and disease: a novel etiological classification of mitochondrial proteolytic disorders
    • Bota D.A., Davies K.J. Protein degradation in mitochondria: implications for oxidative stress, aging and disease: a novel etiological classification of mitochondrial proteolytic disorders. Mitochondrion 2001, 1:33-49.
    • (2001) Mitochondrion , vol.1 , pp. 33-49
    • Bota, D.A.1    Davies, K.J.2
  • 11
    • 0036713692 scopus 로고    scopus 로고
    • Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism
    • Bota D.A., Davies K.J.A. Lon protease preferentially degrades oxidized mitochondrial aconitase by an ATP-stimulated mechanism. Nat. Cell Biol. 2002, 4:674-680.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 674-680
    • Bota, D.A.1    Davies, K.J.A.2
  • 12
    • 79955604131 scopus 로고    scopus 로고
    • Genetic insights into OXPHOS defect and its role in cancer
    • Chandra D., Singh K.K. Genetic insights into OXPHOS defect and its role in cancer. Biochim. Biophys. Acta 2011, 1807:620-625.
    • (2011) Biochim. Biophys. Acta , vol.1807 , pp. 620-625
    • Chandra, D.1    Singh, K.K.2
  • 13
    • 40249107680 scopus 로고    scopus 로고
    • Thermodynamic characterization of specific interactions between the human Lon protease and G-quartet DNA
    • Chen S.H., Suzuki C.K., Wu S.H. Thermodynamic characterization of specific interactions between the human Lon protease and G-quartet DNA. Nucleic Acids Res. 2008, 36:1273-1287.
    • (2008) Nucleic Acids Res. , vol.36 , pp. 1273-1287
    • Chen, S.H.1    Suzuki, C.K.2    Wu, S.H.3
  • 14
    • 0035977454 scopus 로고    scopus 로고
    • The modulation of the biological activities of mitochondrial histone Abf2p by yeast PKA and its possible role in the regulation of mitochondrial DNA content during glucose repression
    • Cho J.H., Lee Y.K., Chae C.B. The modulation of the biological activities of mitochondrial histone Abf2p by yeast PKA and its possible role in the regulation of mitochondrial DNA content during glucose repression. Biochim. Biophys. Acta 2001, 1522:175-186.
    • (2001) Biochim. Biophys. Acta , vol.1522 , pp. 175-186
    • Cho, J.H.1    Lee, Y.K.2    Chae, C.B.3
  • 15
    • 34547621748 scopus 로고    scopus 로고
    • Relative abundance of the human mitochondrial transcription system and distinct roles for h-mtTFB1 and h-mtTFB2 in mitochondrial biogenesis and gene expression
    • Cotney J., Wang Z., Shadel G.S. Relative abundance of the human mitochondrial transcription system and distinct roles for h-mtTFB1 and h-mtTFB2 in mitochondrial biogenesis and gene expression. Nucleic Acids Res. 2007, 35:4042-4054.
    • (2007) Nucleic Acids Res. , vol.35 , pp. 4042-4054
    • Cotney, J.1    Wang, Z.2    Shadel, G.S.3
  • 16
    • 0029070402 scopus 로고
    • Addition of a 29 residue carboxyl-terminal tail converts a simple HMG box-containing protein into a transcriptional activator
    • Dairaghi D.J., Shadel G.S., Clayton D.A. Addition of a 29 residue carboxyl-terminal tail converts a simple HMG box-containing protein into a transcriptional activator. J. Mol. Biol. 1995, 249:11-28.
    • (1995) J. Mol. Biol. , vol.249 , pp. 11-28
    • Dairaghi, D.J.1    Shadel, G.S.2    Clayton, D.A.3
  • 19
  • 20
    • 34249894175 scopus 로고    scopus 로고
    • Peptidyl boronates inhibit Salmonella enterica serovar Typhimurium Lon protease by a competitive ATP-dependent mechanism
    • Frase H., Lee I. Peptidyl boronates inhibit Salmonella enterica serovar Typhimurium Lon protease by a competitive ATP-dependent mechanism. Biochemistry 2007, 46:6647-6657.
    • (2007) Biochemistry , vol.46 , pp. 6647-6657
    • Frase, H.1    Lee, I.2
  • 21
    • 33947724515 scopus 로고    scopus 로고
    • HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells
    • Fukuda R., Zhang H., Kim J.W., Shimoda L., Dang C.V., Semenza G.L. HIF-1 regulates cytochrome oxidase subunits to optimize efficiency of respiration in hypoxic cells. Cell 2007, 129:111-122.
    • (2007) Cell , vol.129 , pp. 111-122
    • Fukuda, R.1    Zhang, H.2    Kim, J.W.3    Shimoda, L.4    Dang, C.V.5    Semenza, G.L.6
  • 22
    • 67249159596 scopus 로고    scopus 로고
    • Structural analysis and DNA binding of the HMG domains of the human mitochondrial transcription factor A
    • Gangelhoff T.A., Mungalachetty P.S., Nix J.C., Churchill M.E. Structural analysis and DNA binding of the HMG domains of the human mitochondrial transcription factor A. Nucleic Acids Res. 2009, 37:3153-3164.
    • (2009) Nucleic Acids Res. , vol.37 , pp. 3153-3164
    • Gangelhoff, T.A.1    Mungalachetty, P.S.2    Nix, J.C.3    Churchill, M.E.4
  • 24
    • 79954609874 scopus 로고    scopus 로고
    • Frequent truncating mutation of TFAM induces mitochondrial DNA depletion and apoptotic resistance in microsatellite-unstable colorectal cancer
    • Guo J., Zheng L., Liu W., Wang X., Wang Z., Wang Z., French A.J., Kang D., Chen L., Thibodeau S.N., Liu W. Frequent truncating mutation of TFAM induces mitochondrial DNA depletion and apoptotic resistance in microsatellite-unstable colorectal cancer. Cancer Res 2011, 71:2978-2987.
    • (2011) Cancer Res , vol.71 , pp. 2978-2987
    • Guo, J.1    Zheng, L.2    Liu, W.3    Wang, X.4    Wang, Z.5    Wang, Z.6    French, A.J.7    Kang, D.8    Chen, L.9    Thibodeau, S.N.10    Liu, W.11
  • 25
    • 77954829313 scopus 로고    scopus 로고
    • Overexpression of mitochondrial transcription factor A (TFAM) ameliorates delayed neuronal death due to transient forebrain ischemia in mice
    • Hokari M., Kuroda S., Kinugawa S., Ide T., Tsutsui H., Iwasaki Y. Overexpression of mitochondrial transcription factor A (TFAM) ameliorates delayed neuronal death due to transient forebrain ischemia in mice. Neuropathology 2010, 30:401-407.
    • (2010) Neuropathology , vol.30 , pp. 401-407
    • Hokari, M.1    Kuroda, S.2    Kinugawa, S.3    Ide, T.4    Tsutsui, H.5    Iwasaki, Y.6
  • 29
    • 34548495323 scopus 로고    scopus 로고
    • The mitochondrial transcription factor TFAM coordinates the assembly of multiple DNA molecules into nucleoid-like structures
    • Kaufman B.A., Durisic N., Mativetsky J.M., Costantino S., Hancock M.A., Grutter P., Shoubridge E.A. The mitochondrial transcription factor TFAM coordinates the assembly of multiple DNA molecules into nucleoid-like structures. Mol. Biol. Cell 2007, 18:3225-3236.
    • (2007) Mol. Biol. Cell , vol.18 , pp. 3225-3236
    • Kaufman, B.A.1    Durisic, N.2    Mativetsky, J.M.3    Costantino, S.4    Hancock, M.A.5    Grutter, P.6    Shoubridge, E.A.7
  • 30
    • 0029922167 scopus 로고    scopus 로고
    • Isolation of human cell lines lacking mitochondrial DNA
    • King M.P., Attardi G. Isolation of human cell lines lacking mitochondrial DNA. Methods Enzymol. 1996, 264:304-313.
    • (1996) Methods Enzymol. , vol.264 , pp. 304-313
    • King, M.P.1    Attardi, G.2
  • 31
    • 80051972817 scopus 로고    scopus 로고
    • Super-resolution microscopy reveals that mammalian mitochondrial nucleoids have a uniform size and frequently contain a single copy of mtDNA
    • Kukat C., Wurm C.A., Spåhr H., Falkenberg M., Larsson N.G., Jakobs S. Super-resolution microscopy reveals that mammalian mitochondrial nucleoids have a uniform size and frequently contain a single copy of mtDNA. Proc. Natl. Acad. Sci. USA 2011, 108:13534-13539.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 13534-13539
    • Kukat, C.1    Wurm, C.A.2    Spåhr, H.3    Falkenberg, M.4    Larsson, N.G.5    Jakobs, S.6
  • 32
    • 0028223609 scopus 로고
    • Low levels of mitochondrial transcription factor A in mitochondrial DNA depletion
    • Larsson N.G., Oldfors A., Holme E., Clayton D.A. Low levels of mitochondrial transcription factor A in mitochondrial DNA depletion. Biochem. Biophys. Res. Commun. 1994, 200:1374-1381.
    • (1994) Biochem. Biophys. Res. Commun. , vol.200 , pp. 1374-1381
    • Larsson, N.G.1    Oldfors, A.2    Holme, E.3    Clayton, D.A.4
  • 34
    • 0346725952 scopus 로고    scopus 로고
    • Negative regulation of histone deacetylase 8 activity by cyclic AMP-dependent protein kinase A
    • Lee H., Rezai-Zadeh N., Seto E. Negative regulation of histone deacetylase 8 activity by cyclic AMP-dependent protein kinase A. Mol. Cell. Biol. 2004, 24:765-773.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 765-773
    • Lee, H.1    Rezai-Zadeh, N.2    Seto, E.3
  • 36
    • 77953319998 scopus 로고    scopus 로고
    • Human mitochondrial transcription revisited: only TFAM and TFB2M are required for transcription of the mitochondrial genes in vitro
    • Litonin D., Sologub M., Shi Y., Savkina M., Anikin M., Falkenberg M., Gustafsson C.M., Temiakov D. Human mitochondrial transcription revisited: only TFAM and TFB2M are required for transcription of the mitochondrial genes in vitro. J. Biol. Chem. 2010, 285:18129-18133.
    • (2010) J. Biol. Chem. , vol.285 , pp. 18129-18133
    • Litonin, D.1    Sologub, M.2    Shi, Y.3    Savkina, M.4    Anikin, M.5    Falkenberg, M.6    Gustafsson, C.M.7    Temiakov, D.8
  • 37
    • 1842690145 scopus 로고    scopus 로고
    • DNA and RNA binding by the mitochondrial lon protease is regulated by nucleotide and protein substrate
    • Liu T., Lu B., Lee I., Ondrovicová G., Kutejová E., Suzuki C.K. DNA and RNA binding by the mitochondrial lon protease is regulated by nucleotide and protein substrate. J. Biol. Chem. 2004, 279:13902-13910.
    • (2004) J. Biol. Chem. , vol.279 , pp. 13902-13910
    • Liu, T.1    Lu, B.2    Lee, I.3    Ondrovicová, G.4    Kutejová, E.5    Suzuki, C.K.6
  • 39
    • 0037434941 scopus 로고    scopus 로고
    • The ATP-dependent Lon protease of Mus musculus is a DNA-binding protein that is functionally conserved between yeast and mammals
    • Lu B., Liu T., Crosby J.A., Thomas-Wohlever J., Lee I., Suzuki C.K. The ATP-dependent Lon protease of Mus musculus is a DNA-binding protein that is functionally conserved between yeast and mammals. Gene 2003, 306:45-55.
    • (2003) Gene , vol.306 , pp. 45-55
    • Lu, B.1    Liu, T.2    Crosby, J.A.3    Thomas-Wohlever, J.4    Lee, I.5    Suzuki, C.K.6
  • 41
    • 11344277076 scopus 로고    scopus 로고
    • Transient overexpression of mitochondrial transcription factor A (TFAM) is sufficient to stimulate mitochondrial DNA transcription, but not sufficient to increase mtDNA copy number in cultured cells
    • Maniura-Weber K., Goffart S., Garstka H.L., Montoya J., Wiesner R.J. Transient overexpression of mitochondrial transcription factor A (TFAM) is sufficient to stimulate mitochondrial DNA transcription, but not sufficient to increase mtDNA copy number in cultured cells. Nucleic Acids Res. 2004, 32:6015-6027.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 6015-6027
    • Maniura-Weber, K.1    Goffart, S.2    Garstka, H.L.3    Montoya, J.4    Wiesner, R.J.5
  • 42
    • 78649842154 scopus 로고    scopus 로고
    • Mitochondrial Lon protease regulates mitochondrial DNA copy number and transcription by selective degradation of mitochondrial transcription factor A (TFAM)
    • Matsushima Y., Goto Y., Kaguni L.S. Mitochondrial Lon protease regulates mitochondrial DNA copy number and transcription by selective degradation of mitochondrial transcription factor A (TFAM). Proc. Natl. Acad. Sci. USA 2010, 107:18410-18415.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 18410-18415
    • Matsushima, Y.1    Goto, Y.2    Kaguni, L.S.3
  • 43
    • 80555128721 scopus 로고    scopus 로고
    • The mitochondrial transcription and packaging factor Tfam imposes a U-turn on mitochondrial DNA
    • Ngo H.B., Kaiser J.T., Chan D.C. The mitochondrial transcription and packaging factor Tfam imposes a U-turn on mitochondrial DNA. Nat. Struct. Mol. Biol. 2011, 18:1290-1296.
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 1290-1296
    • Ngo, H.B.1    Kaiser, J.T.2    Chan, D.C.3
  • 46
    • 0027447290 scopus 로고
    • A human mitochondrial transcriptional activator can functionally replace a yeast mitochondrial HMG-box protein both in vivo and in vitro
    • Parisi M.A., Xu B., Clayton D.A. A human mitochondrial transcriptional activator can functionally replace a yeast mitochondrial HMG-box protein both in vivo and in vitro. Mol. Cell. Biol. 1993, 13:1951-1961.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1951-1961
    • Parisi, M.A.1    Xu, B.2    Clayton, D.A.3
  • 47
    • 34250768073 scopus 로고    scopus 로고
    • A cut short to death: Parl and Opa1 in the regulation of mitochondrial morphology and apoptosis
    • Pellegrini L., Scorrano L. A cut short to death: Parl and Opa1 in the regulation of mitochondrial morphology and apoptosis. Cell Death Differ. 2007, 14:1275-1284.
    • (2007) Cell Death Differ. , vol.14 , pp. 1275-1284
    • Pellegrini, L.1    Scorrano, L.2
  • 48
    • 33644867986 scopus 로고    scopus 로고
    • Protein kinase A-mediated phosphorylation modulates cytochrome c oxidase function and augments hypoxia and myocardial ischemia-related injury
    • Prabu S.K., Anandatheerthavarada H.K., Raza H., Srinivasan S., Spear J.F., Avadhani N.G. Protein kinase A-mediated phosphorylation modulates cytochrome c oxidase function and augments hypoxia and myocardial ischemia-related injury. J. Biol. Chem. 2006, 281:2061-2070.
    • (2006) J. Biol. Chem. , vol.281 , pp. 2061-2070
    • Prabu, S.K.1    Anandatheerthavarada, H.K.2    Raza, H.3    Srinivasan, S.4    Spear, J.F.5    Avadhani, N.G.6
  • 49
    • 0038482043 scopus 로고    scopus 로고
    • Phosphorylation enhances mitochondrial targeting of GSTA4-4 through increased affinity for binding to cytoplasmic Hsp70
    • Robin M.A., Prabu S.K., Raza H., Anandatheerthavarada H.K., Avadhani N.G. Phosphorylation enhances mitochondrial targeting of GSTA4-4 through increased affinity for binding to cytoplasmic Hsp70. J. Biol. Chem. 2003, 278:18960-18970.
    • (2003) J. Biol. Chem. , vol.278 , pp. 18960-18970
    • Robin, M.A.1    Prabu, S.K.2    Raza, H.3    Anandatheerthavarada, H.K.4    Avadhani, N.G.5
  • 52
    • 0025639158 scopus 로고
    • The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53
    • Scheffner M., Werness B.A., Huibregtse J.M., Levine A.J., Howley P.M. The E6 oncoprotein encoded by human papillomavirus types 16 and 18 promotes the degradation of p53. Cell 1990, 63:1129-1136.
    • (1990) Cell , vol.63 , pp. 1129-1136
    • Scheffner, M.1    Werness, B.A.2    Huibregtse, J.M.3    Levine, A.J.4    Howley, P.M.5
  • 54
    • 0036566855 scopus 로고    scopus 로고
    • Modulation of mitochondrial transcription in response to mtDNA depletion and repletion in HeLa cells
    • Seidel-Rogol B.L., Shadel G.S. Modulation of mitochondrial transcription in response to mtDNA depletion and repletion in HeLa cells. Nucleic Acids Res. 2002, 30:1929-1934.
    • (2002) Nucleic Acids Res. , vol.30 , pp. 1929-1934
    • Seidel-Rogol, B.L.1    Shadel, G.S.2
  • 56
    • 77955456575 scopus 로고    scopus 로고
    • Core human mitochondrial transcription apparatus is a regulated two-component system in vitro
    • Shutt T.E., Lodeiro M.F., Cotney J., Cameron C.E., Shadel G.S. Core human mitochondrial transcription apparatus is a regulated two-component system in vitro. Proc. Natl. Acad. Sci. USA 2010, 107:12133-12138.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 12133-12138
    • Shutt, T.E.1    Lodeiro, M.F.2    Cotney, J.3    Cameron, C.E.4    Shadel, G.S.5
  • 57
    • 34548785473 scopus 로고    scopus 로고
    • Non-oncogene addiction and the stress phenotype of cancer cells
    • Solimini N.L., Luo J., Elledge S.J. Non-oncogene addiction and the stress phenotype of cancer cells. Cell 2007, 130:986-988.
    • (2007) Cell , vol.130 , pp. 986-988
    • Solimini, N.L.1    Luo, J.2    Elledge, S.J.3
  • 58
    • 70449807055 scopus 로고    scopus 로고
    • TFB2 is a transient component of the catalytic site of the human mitochondrial RNA polymerase
    • Sologub M., Litonin D., Anikin M., Mustaev A., Temiakov D. TFB2 is a transient component of the catalytic site of the human mitochondrial RNA polymerase. Cell 2009, 139:934-944.
    • (2009) Cell , vol.139 , pp. 934-944
    • Sologub, M.1    Litonin, D.2    Anikin, M.3    Mustaev, A.4    Temiakov, D.5
  • 60
    • 79960659551 scopus 로고    scopus 로고
    • Lon peptidase 1 (LONP1)-dependent breakdown of mitochondrial 5-aminolevulinic acid synthase protein by heme in human liver cells
    • Tian Q., Li T., Hou W., Zheng J., Schrum L.W., Bonkovsky H.L. Lon peptidase 1 (LONP1)-dependent breakdown of mitochondrial 5-aminolevulinic acid synthase protein by heme in human liver cells. J. Biol. Chem. 2011, 286:26424-26430.
    • (2011) J. Biol. Chem. , vol.286 , pp. 26424-26430
    • Tian, Q.1    Li, T.2    Hou, W.3    Zheng, J.4    Schrum, L.W.5    Bonkovsky, H.L.6
  • 63
    • 79959947007 scopus 로고    scopus 로고
    • Generation, function and diagnostic value of mitochondrial DNA copy number alterations in human cancers
    • Yu M. Generation, function and diagnostic value of mitochondrial DNA copy number alterations in human cancers. Life Sci. 2011, 89:65-71.
    • (2011) Life Sci. , vol.89 , pp. 65-71
    • Yu, M.1
  • 64
    • 0031943922 scopus 로고    scopus 로고
    • Functions of the high mobility group protein, Abf2p, in mitochondrial DNA segregation, recombination and copy number in Saccharomyces cerevisiae
    • Zelenaya-Troitskaya O., Newman S.M., Okamoto K., Perlman P.S., Butow R.A. Functions of the high mobility group protein, Abf2p, in mitochondrial DNA segregation, recombination and copy number in Saccharomyces cerevisiae. Genetics 1998, 148:1763-1776.
    • (1998) Genetics , vol.148 , pp. 1763-1776
    • Zelenaya-Troitskaya, O.1    Newman, S.M.2    Okamoto, K.3    Perlman, P.S.4    Butow, R.A.5
  • 65
    • 84860211886 scopus 로고    scopus 로고
    • Transcriptional requirements of the distal heavy-strand promoter of mtDNA
    • Zollo O., Tiranti V., Sondheimer N. Transcriptional requirements of the distal heavy-strand promoter of mtDNA. Proc. Natl. Acad. Sci. USA 2012, 109:6508-6512.
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 6508-6512
    • Zollo, O.1    Tiranti, V.2    Sondheimer, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.