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Volumn 292, Issue 2, 2007, Pages

Tissue heterogeneity of the mammalian mitochondrial proteome

Author keywords

Brain; Electrophoresis; Heart; Histone; Kidney; Liquid chromatography; Liver; Mass spectrometry; Oxidative phosphorylation; Structural proteins

Indexed keywords

PEPTIDE; PROTEOME; STRUCTURAL PROTEIN;

EID: 33847084336     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00108.2006     Document Type: Article
Times cited : (173)

References (36)
  • 3
    • 27144525581 scopus 로고    scopus 로고
    • New mitochondrial carriers: An overview
    • Arco AD, Satrustegui J. New mitochondrial carriers: an overview. Cell Mol Life Sci 62: 2204-2227, 2005.
    • (2005) Cell Mol Life Sci , vol.62 , pp. 2204-2227
    • Arco, A.D.1    Satrustegui, J.2
  • 4
    • 0017704388 scopus 로고
    • Induction of mitochondrial contraction and concomitant inhibition of succinate oxidation by magnesium ions
    • Blair PV. Induction of mitochondrial contraction and concomitant inhibition of succinate oxidation by magnesium ions. Arch Biochem Biophys 181: 550-568, 1977.
    • (1977) Arch Biochem Biophys , vol.181 , pp. 550-568
    • Blair, P.V.1
  • 5
    • 0014211643 scopus 로고
    • Contraction of hypotonically swollen mitochondria by oxidizable substrates
    • Blair PV, Sollars FA. Contraction of hypotonically swollen mitochondria by oxidizable substrates. Biochem Biophys Res Commun 27: 202-208, 1967.
    • (1967) Biochem Biophys Res Commun , vol.27 , pp. 202-208
    • Blair, P.V.1    Sollars, F.A.2
  • 6
    • 0037316303 scopus 로고    scopus 로고
    • A comparison of normalization methods for high density oligonucleotide array data based on variance and bias
    • Bolstad BM, Irizarry RA, Astrand M, Speed TP. A comparison of normalization methods for high density oligonucleotide array data based on variance and bias. Bioinformatics 19: 185-193, 2003.
    • (2003) Bioinformatics , vol.19 , pp. 185-193
    • Bolstad, B.M.1    Irizarry, R.A.2    Astrand, M.3    Speed, T.P.4
  • 7
    • 0018307726 scopus 로고
    • Characterization of a histone-like protein extracted from yeast mitochondria
    • Caron F, Jacq C, Rouviere-Yaniv J. Characterization of a histone-like protein extracted from yeast mitochondria. Proc Natl Acad Sci USA 76: 4265-4269, 1979.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4265-4269
    • Caron, F.1    Jacq, C.2    Rouviere-Yaniv, J.3
  • 8
    • 3042735127 scopus 로고    scopus 로고
    • The need for guidelines in publication of peptide and protein identification data: Working Group on Publication Guidelines for Peptide and Protein Identification Data
    • Carr S, Aebersold R, Baldwin M, Burlingame A, Clauser K, Nesvizhskii A. The need for guidelines in publication of peptide and protein identification data: Working Group on Publication Guidelines for Peptide and Protein Identification Data. Mol Cell Proteomics 3: 531-533, 2004.
    • (2004) Mol Cell Proteomics , vol.3 , pp. 531-533
    • Carr, S.1    Aebersold, R.2    Baldwin, M.3    Burlingame, A.4    Clauser, K.5    Nesvizhskii, A.6
  • 9
    • 0021761290 scopus 로고
    • Yeast may not contain histone H1: The only known "histone H1-like" protein in Saccharomyces cerevisiae is a mitochondrial protein
    • Certa U, Colavito-Shepanski M, Grunstein M. Yeast may not contain histone H1: the only known "histone H1-like" protein in Saccharomyces cerevisiae is a mitochondrial protein. Nucleic Acids Res 12: 7975-7985, 1984.
    • (1984) Nucleic Acids Res , vol.12 , pp. 7975-7985
    • Certa, U.1    Colavito-Shepanski, M.2    Grunstein, M.3
  • 11
    • 0000950174 scopus 로고    scopus 로고
    • A novel DNA-binding protein bound to the mitochondrial inner membrane restores the null mutation of mitochondrial histone Abf2p in Saccharomyces cerevisiae
    • Cho JH, Ha SJ, Kao LR, Megraw TL, Chae CB. A novel DNA-binding protein bound to the mitochondrial inner membrane restores the null mutation of mitochondrial histone Abf2p in Saccharomyces cerevisiae. Mol Cell Biol 18: 5712-5723, 1998.
    • (1998) Mol Cell Biol , vol.18 , pp. 5712-5723
    • Cho, J.H.1    Ha, S.J.2    Kao, L.R.3    Megraw, T.L.4    Chae, C.B.5
  • 12
    • 0029915525 scopus 로고    scopus 로고
    • Computational method to predict mitochondrially imported proteins and their targeting sequences
    • Claros MG, Vincens P. Computational method to predict mitochondrially imported proteins and their targeting sequences. Eur J Biochem 241: 779-786, 1996.
    • (1996) Eur J Biochem , vol.241 , pp. 779-786
    • Claros, M.G.1    Vincens, P.2
  • 14
    • 0018355912 scopus 로고    scopus 로고
    • Danner DJ, Lemmon SK, Besharse JC, Elsas LJ 2nd. Purification and characterization of branched chain α-ketoacid dehydrogenase from bovine liver mitochondria. J Biol Chem 254: 5522-5526, 1979.
    • Danner DJ, Lemmon SK, Besharse JC, Elsas LJ 2nd. Purification and characterization of branched chain α-ketoacid dehydrogenase from bovine liver mitochondria. J Biol Chem 254: 5522-5526, 1979.
  • 16
    • 0026040110 scopus 로고
    • Maple syrup urine disease in Mennonites. Evidence that the Y393N mutation in E1-α impedes assembly of the E1 component of branched-chain α-keto acid dehydrogenase complex
    • Fisher CR, Chuang JL, Cox RP, Fisher CW, Star RA, Chuang DT. Maple syrup urine disease in Mennonites. Evidence that the Y393N mutation in E1-α impedes assembly of the E1 component of branched-chain α-keto acid dehydrogenase complex. J Clin Invest 88: 1034-1037, 1991.
    • (1991) J Clin Invest , vol.88 , pp. 1034-1037
    • Fisher, C.R.1    Chuang, J.L.2    Cox, R.P.3    Fisher, C.W.4    Star, R.A.5    Chuang, D.T.6
  • 17
    • 33645704767 scopus 로고    scopus 로고
    • Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver
    • Forner F, Foster LJ, Campanaro S, Valle G, Mann M. Quantitative proteomic comparison of rat mitochondria from muscle, heart, and liver. Mol Cell Proteomics 5: 608-619, 2006.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 608-619
    • Forner, F.1    Foster, L.J.2    Campanaro, S.3    Valle, G.4    Mann, M.5
  • 18
    • 23944472666 scopus 로고    scopus 로고
    • Comprehensive label-free method for the relative quantification of proteins from biological samples
    • Higgs RE, Knierman MD, Gelfanova V, Butler JP, Hale JE. Comprehensive label-free method for the relative quantification of proteins from biological samples. J Proteome Res 4: 1442-1450, 2005.
    • (2005) J Proteome Res , vol.4 , pp. 1442-1450
    • Higgs, R.E.1    Knierman, M.D.2    Gelfanova, V.3    Butler, J.P.4    Hale, J.E.5
  • 22
    • 18844421618 scopus 로고    scopus 로고
    • Protein import into mitochondria: Origins and functions today
    • Lister R, Hulett JM, Lithgow T, Whelan J. Protein import into mitochondria: origins and functions today. Mol Membr Biol 22: 87-100, 2005.
    • (2005) Mol Membr Biol , vol.22 , pp. 87-100
    • Lister, R.1    Hulett, J.M.2    Lithgow, T.3    Whelan, J.4
  • 23
    • 0027242020 scopus 로고
    • Functional complementarity between the HMG1-like yeast mitochondrial histone HM and the bacterial histone-like protein HU
    • Megraw TL, Chae CB. Functional complementarity between the HMG1-like yeast mitochondrial histone HM and the bacterial histone-like protein HU. J Biol Chem 268: 12758-12763, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 12758-12763
    • Megraw, T.L.1    Chae, C.B.2
  • 24
    • 27844535385 scopus 로고    scopus 로고
    • Protein import into mitochondria
    • Mokranjac D, Neupert W. Protein import into mitochondria. Biochem Soc Trans 33: 1019-1023, 2005.
    • (2005) Biochem Soc Trans , vol.33 , pp. 1019-1023
    • Mokranjac, D.1    Neupert, W.2
  • 26
    • 0032736989 scopus 로고    scopus 로고
    • Developmentally regulated expression of the transcriptional cofactors/histone acetyltransferases CBP and p300 during mouse embryogenesis
    • Partanen A, Motoyama J, Hui CC. Developmentally regulated expression of the transcriptional cofactors/histone acetyltransferases CBP and p300 during mouse embryogenesis. Int J Dev Biol 43: 487-494, 1999.
    • (1999) Int J Dev Biol , vol.43 , pp. 487-494
    • Partanen, A.1    Motoyama, J.2    Hui, C.C.3
  • 27
    • 0037277179 scopus 로고    scopus 로고
    • Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: The yeast proteome
    • Peng J, Elias JE, Thoreen CC, Licklider LJ, Gygi SP. Evaluation of multidimensional chromatography coupled with tandem mass spectrometry (LC/LC-MS/MS) for large-scale protein analysis: the yeast proteome. J Proteome Res 2: 43-50, 2003.
    • (2003) J Proteome Res , vol.2 , pp. 43-50
    • Peng, J.1    Elias, J.E.2    Thoreen, C.C.3    Licklider, L.J.4    Gygi, S.P.5
  • 28
    • 2442728373 scopus 로고
    • Purification and characterization of branched chain α-keto acid dehydrogenase complex of bovine kidney
    • Pettit FH, Yeaman SJ, Reed LJ. Purification and characterization of branched chain α-keto acid dehydrogenase complex of bovine kidney. Proc Natl Acad Sci USA 75: 4881-4885, 1978.
    • (1978) Proc Natl Acad Sci USA , vol.75 , pp. 4881-4885
    • Pettit, F.H.1    Yeaman, S.J.2    Reed, L.J.3
  • 29
    • 0038015611 scopus 로고    scopus 로고
    • Evolutionary diversification of mitochondrial proteomes: Implications for human disease
    • Richly E, Chinnery PF, Leister D. Evolutionary diversification of mitochondrial proteomes: implications for human disease. Trends Genet 19: 356-362, 2003.
    • (2003) Trends Genet , vol.19 , pp. 356-362
    • Richly, E.1    Chinnery, P.F.2    Leister, D.3
  • 33
  • 35
    • 0025933357 scopus 로고
    • Isolation of histone-like proteins from mitochondria of bovine heart
    • Yamada EW, Dotzlaw H, Huzel NJ. Isolation of histone-like proteins from mitochondria of bovine heart. Prep Biochem 21: 11-23, 1991.
    • (1991) Prep Biochem , vol.21 , pp. 11-23
    • Yamada, E.W.1    Dotzlaw, H.2    Huzel, N.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.