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Volumn 311, Issue 3, 2003, Pages 774-779

Direct evidence for expression of Type II flavoprotein subunit in human complex II (succinate-ubiquinone reductase)

Author keywords

Complex II; Flavoprotein subunit; Human mitochondria; Isoforms; Succinate ubiquinone reductase

Indexed keywords

FLAVOPROTEIN; ISOENZYME; MITOCHONDRIAL ENZYME; PROTEIN SUBUNIT; SUCCINATE DEHYDROGENASE (UBIQUINONE); SUCROSE LAURATE;

EID: 0242493177     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbrc.2003.10.065     Document Type: Article
Times cited : (19)

References (26)
  • 2
    • 0034651685 scopus 로고    scopus 로고
    • Simple redox-linked proton-transfer design: New insights from structures of quinol-fumarate reductase
    • Ohnishi T., Christopher C.M., Christopher C.P., Dutton P.L., Yano Y. Simple redox-linked proton-transfer design: new insights from structures of quinol-fumarate reductase. Struct. Fold. Des. 8:2000;R23-R32.
    • (2000) Struct. Fold. Des. , vol.8
    • Ohnishi, T.1    Christopher, C.M.2    Christopher, C.P.3    Dutton, P.L.4    Yano, Y.5
  • 3
    • 0037122942 scopus 로고    scopus 로고
    • Role of complex II in anaerobic respiration of the parasite mitochondria from Ascaris suum and Plasmodium falciparum
    • Kita K., Hirawake H., Miyadera H., Amino H., Takeo S. Role of complex II in anaerobic respiration of the parasite mitochondria from Ascaris suum and Plasmodium falciparum. Biochim. Biophys. Acta. 1553:2002;123-139.
    • (2002) Biochim. Biophys. Acta , vol.1553 , pp. 123-139
    • Kita, K.1    Hirawake, H.2    Miyadera, H.3    Amino, H.4    Takeo, S.5
  • 4
    • 0034646270 scopus 로고    scopus 로고
    • Mitochondrial dysfunction during hypoxia/reoxygenation and its correction by anaerobic metabolism of citric acid cycle intermediate
    • Weinberg J.M., Venkatachalam M.A., Roeser N.F., Nissim I. Mitochondrial dysfunction during hypoxia/reoxygenation and its correction by anaerobic metabolism of citric acid cycle intermediate. Proc. Natl. Acad. Sci. USA. 97:2000;2826-2831.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 2826-2831
    • Weinberg, J.M.1    Venkatachalam, M.A.2    Roeser, N.F.3    Nissim, I.4
  • 9
    • 0027954897 scopus 로고
    • Single muscle fibre analyses in 2 brothers with succinate dehydrogenase deficiency
    • Reichmann H., Angelini C. Single muscle fibre analyses in 2 brothers with succinate dehydrogenase deficiency. Eur. Neurol. 34:1994;95-98.
    • (1994) Eur. Neurol. , vol.34 , pp. 95-98
    • Reichmann, H.1    Angelini, C.2
  • 10
    • 0034709403 scopus 로고    scopus 로고
    • A patient with mitochondrial myopathy associated with isolated succinate dehydrogenase deficiency
    • Sugimoto J., Shimohira M., Osawa Y., Matsubara M., Yamamoto H., Goto Y., Nonaka I. A patient with mitochondrial myopathy associated with isolated succinate dehydrogenase deficiency. Brain Dev. 22:2000;158-162.
    • (2000) Brain Dev. , vol.22 , pp. 158-162
    • Sugimoto, J.1    Shimohira, M.2    Osawa, Y.3    Matsubara, M.4    Yamamoto, H.5    Goto, Y.6    Nonaka, I.7
  • 13
    • 0034059135 scopus 로고    scopus 로고
    • Compound heterozygous mutations in the flavoprotein gene of the respiratory chain complex II in a patient with Leigh syndrome
    • Parfait B., Chretien D., Rotig A., Marsac C., Muunich A., Rustin P. Compound heterozygous mutations in the flavoprotein gene of the respiratory chain complex II in a patient with Leigh syndrome. Hum. Genet. 106:2000;236-243.
    • (2000) Hum. Genet. , vol.106 , pp. 236-243
    • Parfait, B.1    Chretien, D.2    Rotig, A.3    Marsac, C.4    Muunich, A.5    Rustin, P.6
  • 14
    • 0037364314 scopus 로고    scopus 로고
    • A role for mitochondrial enzymes in inherited neoplasia and beyond
    • Eng C., Kiuru M., Fernandez M.J., Aaltonen L.A. A role for mitochondrial enzymes in inherited neoplasia and beyond. Nat. Rev. 3:2003;193-202.
    • (2003) Nat. Rev. , vol.3 , pp. 193-202
    • Eng, C.1    Kiuru, M.2    Fernandez, M.J.3    Aaltonen, L.A.4
  • 15
    • 0036712593 scopus 로고    scopus 로고
    • Hereditary paraganglioma targets diverse palaganglia
    • Baysal B.E. Hereditary paraganglioma targets diverse palaganglia. J. Med. Genet. 39:2002;617-622.
    • (2002) J. Med. Genet. , vol.39 , pp. 617-622
    • Baysal, B.E.1
  • 16
    • 0036798174 scopus 로고    scopus 로고
    • The pressure rises: Update on the genetics of phaeochromocytoma
    • Maher E.R., Eng C. The pressure rises: update on the genetics of phaeochromocytoma. Hum. Mol. Genet. 11:2002;2347-2354.
    • (2002) Hum. Mol. Genet. , vol.11 , pp. 2347-2354
    • Maher, E.R.1    Eng, C.2
  • 17
    • 0141814715 scopus 로고    scopus 로고
    • Direct evidence for two distinct forms of the flavoprotein subunit of human mitochondrial complex II (succinate-ubiquinone reductase)
    • Tomitsuka E., Hirawake H., Goto Y., Taniwaki M., Harada S., Kita K. Direct evidence for two distinct forms of the flavoprotein subunit of human mitochondrial complex II (succinate-ubiquinone reductase). J. Biochem. 134:2003;191-195.
    • (2003) J. Biochem. , vol.134 , pp. 191-195
    • Tomitsuka, E.1    Hirawake, H.2    Goto, Y.3    Taniwaki, M.4    Harada, S.5    Kita, K.6
  • 20
    • 0038034950 scopus 로고    scopus 로고
    • Analysis of steady-state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye
    • Schulenberg B., Aggeler R., Beechem J.M., Capaldi R.A., Patton W.F. Analysis of steady-state protein phosphorylation in mitochondria using a novel fluorescent phosphosensor dye. J. Biol. Chem. 278:2003;27251-27255.
    • (2003) J. Biol. Chem. , vol.278 , pp. 27251-27255
    • Schulenberg, B.1    Aggeler, R.2    Beechem, J.M.3    Capaldi, R.A.4    Patton, W.F.5
  • 21
    • 0242434921 scopus 로고    scopus 로고
    • Direct and indirect inhibitor of mitochondrial ATP synthesis
    • Johnson N.O-. Direct and indirect inhibitor of mitochondrial ATP synthesis. Methods Cell. Biol. 65:2001;483-493.
    • (2001) Methods Cell. Biol. , vol.65 , pp. 483-493
    • Johnson, N.O.1
  • 23
    • 0033983147 scopus 로고    scopus 로고
    • Progress in understanding structure-function relationships in respiratory chain complex II
    • Ackrell B.A.C. Progress in understanding structure-function relationships in respiratory chain complex II. FEBS Lett. 466:2000;1-5.
    • (2000) FEBS Lett. , vol.466 , pp. 1-5
    • Ackrell, B.A.C.1
  • 24
    • 0242687126 scopus 로고    scopus 로고
    • Parasite mitochondria as drug target: Diversity and dynamic changes during the life cycle
    • Kita K., Nihei C., Tomitsuka E. Parasite mitochondria as drug target: diversity and dynamic changes during the life cycle. Curr. Med. Chem. 10:2003;1241-1253.
    • (2003) Curr. Med. Chem. , vol.10 , pp. 1241-1253
    • Kita, K.1    Nihei, C.2    Tomitsuka, E.3
  • 25
    • 0032764173 scopus 로고    scopus 로고
    • Characterization of the human SDHD gene encoding the small subunit of cytochrome b (cybS) in mitochondrial succinate-ubiquinone oxidoreductase
    • Hirawake H., Taniwaki M., Tamura A., Amino H., Tomitsuka E., Kita K. Characterization of the human SDHD gene encoding the small subunit of cytochrome. b (cybS) in mitochondrial succinate-ubiquinone oxidoreductase Biochem. Bioophys. Acta. 1412:1999;295-300.
    • (1999) Biochem. Bioophys. Acta , vol.1412 , pp. 295-300
    • Hirawake, H.1    Taniwaki, M.2    Tamura, A.3    Amino, H.4    Tomitsuka, E.5    Kita, K.6
  • 26
    • 0029931901 scopus 로고    scopus 로고
    • Biochemical investigations and immunoblot analysis of two unrelated patients with an isolated deficiency in complex II of the mitochondrial respiratory chain
    • Birch-Machin M.A., Marsac C., Ponsot G., Parfait B., Taylor R.W., Rustin P., Munnich A. Biochemical investigations and immunoblot analysis of two unrelated patients with an isolated deficiency in complex II of the mitochondrial respiratory chain. Biochem. Biophys. Res. Commun. 220:1996;57-62.
    • (1996) Biochem. Biophys. Res. Commun. , vol.220 , pp. 57-62
    • Birch-Machin, M.A.1    Marsac, C.2    Ponsot, G.3    Parfait, B.4    Taylor, R.W.5    Rustin, P.6    Munnich, A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.