메뉴 건너뛰기




Volumn 292, Issue 2, 2007, Pages

Functional consequences of mitochondrial proteome heterogeneity

Author keywords

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

Indexed keywords

4 AMINOBUTYRIC ACID; COENZYME A TRANSFERASE; MITOCHONDRIAL PROTEIN; NUCLEAR PROTEIN; PROTEOME;

EID: 33847083940     PISSN: 03636143     EISSN: 15221563     Source Type: Journal    
DOI: 10.1152/ajpcell.00109.2006     Document Type: Article
Times cited : (100)

References (51)
  • 1
    • 0025294601 scopus 로고
    • Purification and characterization of formylcoenzyme A transferase from Oxalobacter formigenes
    • Baetz AL, Allison MJ. Purification and characterization of formylcoenzyme A transferase from Oxalobacter formigenes. J Bacteriol 172: 3537-3540, 1990.
    • (1990) J Bacteriol , vol.172 , pp. 3537-3540
    • Baetz, A.L.1    Allison, M.J.2
  • 2
    • 0033507201 scopus 로고    scopus 로고
    • Fatty acid utilization in the hypertrophied and failing heart: Molecular regulatory mechanisms
    • Barger PM, Kelly DP. Fatty acid utilization in the hypertrophied and failing heart: molecular regulatory mechanisms. Am J Med Sci 318: 36-42, 1999.
    • (1999) Am J Med Sci , vol.318 , pp. 36-42
    • Barger, P.M.1    Kelly, D.P.2
  • 4
    • 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
  • 6
    • 3843147327 scopus 로고    scopus 로고
    • Mitochondrial ATP synthasome: Three-dimensional structure by electron microscopy of the ATP synthase in complex formation with carriers for Pi and ADP/ATP
    • Chen C, Ko Y, Delannoy M, Ludtke SJ, Chiu W, Pedersen PL. Mitochondrial ATP synthasome: three-dimensional structure by electron microscopy of the ATP synthase in complex formation with carriers for Pi and ADP/ATP. J Biol Chem 279: 31761-31768, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 31761-31768
    • Chen, C.1    Ko, Y.2    Delannoy, M.3    Ludtke, S.J.4    Chiu, W.5    Pedersen, P.L.6
  • 7
    • 0017229768 scopus 로고
    • A major polypeptide component of rat liver mitochondria: Carbamyl phosphate synthetase
    • Clarke S. A major polypeptide component of rat liver mitochondria: carbamyl phosphate synthetase. J Biol Chem 251: 950-961, 1976.
    • (1976) J Biol Chem , vol.251 , pp. 950-961
    • Clarke, S.1
  • 8
    • 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
  • 9
    • 0016308635 scopus 로고
    • Changes of nuclear structure in cells of the developing Xenopus embryo
    • Csaba G, Do NK. Changes of nuclear structure in cells of the developing Xenopus embryo. Acta Morphol Acad Sci Hung 22: 203-211, 1974.
    • (1974) Acta Morphol Acad Sci Hung , vol.22 , pp. 203-211
    • Csaba, G.1    Do, N.K.2
  • 10
    • 0037119946 scopus 로고    scopus 로고
    • The role of the Tim8p-Tim13p complex in a conserved import pathway for mitochondrial polytopic inner membrane proteins
    • Curran SP, Leuenberger D, Schmidt E, Koehler CM. The role of the Tim8p-Tim13p complex in a conserved import pathway for mitochondrial polytopic inner membrane proteins. J Cell Biol 158: 1017-1027, 2002.
    • (2002) J Cell Biol , vol.158 , pp. 1017-1027
    • Curran, S.P.1    Leuenberger, D.2    Schmidt, E.3    Koehler, C.M.4
  • 11
    • 0028156973 scopus 로고
    • Can arginine and ornithine support gut functions?
    • Cynober L. Can arginine and ornithine support gut functions? Gut 35: S42-S45, 1994.
    • (1994) Gut , vol.35
    • Cynober, L.1
  • 12
    • 7544224771 scopus 로고    scopus 로고
    • Regulated interactions of mtHsp70 with Tim44 at the translocon in the mitochondrial inner membrane
    • D'Silva P, Liu Q, Walter W, Craig EA. Regulated interactions of mtHsp70 with Tim44 at the translocon in the mitochondrial inner membrane. Nat Struct Mol Biol 11: 1084-1091, 2004.
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 1084-1091
    • D'Silva, P.1    Liu, Q.2    Walter, W.3    Craig, E.A.4
  • 13
    • 0037313051 scopus 로고    scopus 로고
    • Gene expression and activity of enzymes in the arginine biosynthetic pathway in porcine fetal small intestine
    • Dekaney CM, Wu G, Jaeger LA. Gene expression and activity of enzymes in the arginine biosynthetic pathway in porcine fetal small intestine. Pediatr Res 53: 274-280, 2003.
    • (2003) Pediatr Res , vol.53 , pp. 274-280
    • Dekaney, C.M.1    Wu, G.2    Jaeger, L.A.3
  • 14
    • 0036227857 scopus 로고    scopus 로고
    • Molecular characterization of phenyllactate dehydratase and its initiator from Clostridium sporogenes
    • Dickert S, Pierik AJ, Buckel W. Molecular characterization of phenyllactate dehydratase and its initiator from Clostridium sporogenes. Mol Microbiol 44: 49-60, 2002.
    • (2002) Mol Microbiol , vol.44 , pp. 49-60
    • Dickert, S.1    Pierik, A.J.2    Buckel, W.3
  • 15
    • 0018256010 scopus 로고
    • Homeostatic regulation of cellular energy metabolism: Experimental characterization in vivo and fit to a model
    • Erecinska M, Wilson DF, Nishiki K. Homeostatic regulation of cellular energy metabolism: experimental characterization in vivo and fit to a model. Am J Physiol Cell Physiol 234: C82-C89, 1978.
    • (1978) Am J Physiol Cell Physiol , vol.234
    • Erecinska, M.1    Wilson, D.F.2    Nishiki, K.3
  • 16
    • 0021112372 scopus 로고
    • Dependence of mitochondrial oxidative phosphorylation on activity of the adenine nucleotide translocase
    • Forman NG, Wilson DF. Dependence of mitochondrial oxidative phosphorylation on activity of the adenine nucleotide translocase. J Biol Chem 258: 8649-8655, 1983.
    • (1983) J Biol Chem , vol.258 , pp. 8649-8655
    • Forman, N.G.1    Wilson, D.F.2
  • 17
    • 0035861886 scopus 로고    scopus 로고
    • A new family of CoA-transferases
    • Heider J. A new family of CoA-transferases. FEBS Lett 509: 345-349, 2001.
    • (2001) FEBS Lett , vol.509 , pp. 345-349
    • Heider, J.1
  • 18
    • 0027934742 scopus 로고
    • Plasma proline and leucine kinetics: Response to 4 wk with proline-free diets in young adults
    • Hiramatsu T, Cortiella J, Marchini JS, Chapman TE, Young VR. Plasma proline and leucine kinetics: response to 4 wk with proline-free diets in young adults. Am J Clin Nutr 60: 207-215, 1994.
    • (1994) Am J Clin Nutr , vol.60 , pp. 207-215
    • Hiramatsu, T.1    Cortiella, J.2    Marchini, J.S.3    Chapman, T.E.4    Young, V.R.5
  • 20
    • 1842478040 scopus 로고    scopus 로고
    • The Tim8-Tim13 complex of Neurospora crassa functions in the assembly of proteins into both mitochondrial membranes
    • Hoppins SC, Nargang FE. The Tim8-Tim13 complex of Neurospora crassa functions in the assembly of proteins into both mitochondrial membranes. J Biol Chem 279: 12396-12405, 2004.
    • (2004) J Biol Chem , vol.279 , pp. 12396-12405
    • Hoppins, S.C.1    Nargang, F.E.2
  • 21
    • 0033525863 scopus 로고    scopus 로고
    • Molecular enzymology of mammalian Δ1-pyrroline-5-carboxylate synthase. Alternative splice donor utilization generates isoforms with different sensitivity to ornithine inhibition
    • Hu CA, Lin WW, Obie C, Valle D. Molecular enzymology of mammalian Δ1-pyrroline-5-carboxylate synthase. Alternative splice donor utilization generates isoforms with different sensitivity to ornithine inhibition. J Biol Chem 274: 6754-6762, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 6754-6762
    • Hu, C.A.1    Lin, W.W.2    Obie, C.3    Valle, D.4
  • 23
    • 0038053908 scopus 로고    scopus 로고
    • Proton translocation by transhydrogenase
    • Jackson JB. Proton translocation by transhydrogenase. FEBS Lett 545: 18-24, 2003.
    • (2003) FEBS Lett , vol.545 , pp. 18-24
    • Jackson, J.B.1
  • 24
    • 25844520458 scopus 로고    scopus 로고
    • Mitochondria in homeostasis of reactive oxygen species in cell, tissues, and organism
    • Jezek P, Hlavata L. Mitochondria in homeostasis of reactive oxygen species in cell, tissues, and organism. Int J Biochem Cell Biol 37: 2478-2503, 2005.
    • (2005) Int J Biochem Cell Biol , vol.37 , pp. 2478-2503
    • Jezek, P.1    Hlavata, L.2
  • 28
    • 0034971989 scopus 로고    scopus 로고
    • Succinyl-CoA:(R)-benzylsuccinate CoA-transferase: An enzyme of the anaerobic toluene catabolic pathway in denitrifying bacteria
    • Leutwein C, Heider J. Succinyl-CoA:(R)-benzylsuccinate CoA-transferase: an enzyme of the anaerobic toluene catabolic pathway in denitrifying bacteria. J Bacteriol 183: 4288-4295, 2001.
    • (2001) J Bacteriol , vol.183 , pp. 4288-4295
    • Leutwein, C.1    Heider, J.2
  • 29
    • 13744252283 scopus 로고    scopus 로고
    • Localization and differential expression of arginase II in the kidney of male and female mice
    • Levillain O, Balvay S, Peyrol S. Localization and differential expression of arginase II in the kidney of male and female mice. Pflügers Arch 449: 491-503, 2005.
    • (2005) Pflügers Arch , vol.449 , pp. 491-503
    • Levillain, O.1    Balvay, S.2    Peyrol, S.3
  • 30
    • 0029164213 scopus 로고
    • Decreased cysteine and proline synthesis in parenterally fed, premature infants
    • Miller RG, Jahoor F, Jaksic T. Decreased cysteine and proline synthesis in parenterally fed, premature infants. J Pediatr Surg 30: 953-958, 1995.
    • (1995) J Pediatr Surg , vol.30 , pp. 953-958
    • Miller, R.G.1    Jahoor, F.2    Jaksic, T.3
  • 31
    • 0029611723 scopus 로고
    • A new stable isotope tracer technique to assess human neonatal amino acid synthesis
    • Miller RG, Jahoor F, Reeds PJ, Heird WC, Jaksic T. A new stable isotope tracer technique to assess human neonatal amino acid synthesis. J Pediatr Surg 30: 1325-1329, 1995.
    • (1995) J Pediatr Surg , vol.30 , pp. 1325-1329
    • Miller, R.G.1    Jahoor, F.2    Reeds, P.J.3    Heird, W.C.4    Jaksic, T.5
  • 32
    • 0029977679 scopus 로고    scopus 로고
    • Compartmentation of endogenously synthesized amino acids in neonates
    • Miller RG, Keshen TH, Jahoor F, Shew SB, Jaksic T. Compartmentation of endogenously synthesized amino acids in neonates. J Surg Res 63: 199-203, 1996.
    • (1996) J Surg Res , vol.63 , pp. 199-203
    • Miller, R.G.1    Keshen, T.H.2    Jahoor, F.3    Shew, S.B.4    Jaksic, T.5
  • 33
    • 0024272372 scopus 로고
    • Yeast adenylate kinase is transcribed constitutively from a promoter in the short intergenic region to the histone H2A-1 gene
    • Oechsner U, Magdolen V, Zoglowek C, Hacker U, Bandlow W. Yeast adenylate kinase is transcribed constitutively from a promoter in the short intergenic region to the histone H2A-1 gene. FEBS Lett 242: 187-193, 1988.
    • (1988) FEBS Lett , vol.242 , pp. 187-193
    • Oechsner, U.1    Magdolen, V.2    Zoglowek, C.3    Hacker, U.4    Bandlow, W.5
  • 36
    • 0037433040 scopus 로고    scopus 로고
    • Identifying differentially expressed genes using false discovery rate controlling procedures
    • Reiner A, Yekutieli D, Benjamini Y. Identifying differentially expressed genes using false discovery rate controlling procedures. Bioinformatics 19: 368-375, 2003.
    • (2003) Bioinformatics , vol.19 , pp. 368-375
    • Reiner, A.1    Yekutieli, D.2    Benjamini, Y.3
  • 37
    • 0037588575 scopus 로고    scopus 로고
    • Formyl-CoA transferase encloses the CoA binding site at the interface of an interlocked dimer
    • Ricagno S, Jonsson S, Richards N, Lindqvist Y. Formyl-CoA transferase encloses the CoA binding site at the interface of an interlocked dimer. EMBO J 22: 3210-3219, 2003.
    • (2003) EMBO J , vol.22 , pp. 3210-3219
    • Ricagno, S.1    Jonsson, S.2    Richards, N.3    Lindqvist, Y.4
  • 38
    • 21844445823 scopus 로고    scopus 로고
    • Nuclear localization and mitogen-activated protein kinase phosphorylation of the multifunctional protein CAD
    • Sigoillot FD, Kotsis DH, Serre V, Sigoillot SM, Evans DR, Guy HI. Nuclear localization and mitogen-activated protein kinase phosphorylation of the multifunctional protein CAD. J Biol Chem 280: 25611-25620, 2005.
    • (2005) J Biol Chem , vol.280 , pp. 25611-25620
    • Sigoillot, F.D.1    Kotsis, D.H.2    Serre, V.3    Sigoillot, S.M.4    Evans, D.R.5    Guy, H.I.6
  • 39
    • 0018629861 scopus 로고
    • Studies of renal urea cycle enzymes. II. Human renal arginase activity and location of the adaptive changes of renal arginase in the protein deprived rat
    • Snellman K, Aperia A, Broberger O. Studies of renal urea cycle enzymes. II. Human renal arginase activity and location of the adaptive changes of renal arginase in the protein deprived rat. Scand J Clin Lab Invest 39: 337-342, 1979.
    • (1979) Scand J Clin Lab Invest , vol.39 , pp. 337-342
    • Snellman, K.1    Aperia, A.2    Broberger, O.3
  • 40
    • 0021063883 scopus 로고
    • Activities of arginase, transamidinase, and ornithine aminotransferase in glia, neurons, and synaptosomes
    • Swamy M, Shrivastaw KP, Prasad MS, Sadasivudu B. Activities of arginase, transamidinase, and ornithine aminotransferase in glia, neurons, and synaptosomes. J Neurosci Res 10: 363-368, 1983.
    • (1983) J Neurosci Res , vol.10 , pp. 363-368
    • Swamy, M.1    Shrivastaw, K.P.2    Prasad, M.S.3    Sadasivudu, B.4
  • 42
    • 0032106406 scopus 로고    scopus 로고
    • Tissue-selective expression of enzymes of arginine synthesis
    • Wakabayashi Y. Tissue-selective expression of enzymes of arginine synthesis. Curr Opin Clin Nutr Metab Care 1: 335-339, 1998.
    • (1998) Curr Opin Clin Nutr Metab Care , vol.1 , pp. 335-339
    • Wakabayashi, Y.1
  • 43
    • 0017115996 scopus 로고
    • The elementary reactions of the pig heart pyruvate dehydrogenase complex. A study of the inhibition by phosphorylation
    • Walsh DA, Cooper RH, Denton RM, Bridges BJ, Randle PJ. The elementary reactions of the pig heart pyruvate dehydrogenase complex. A study of the inhibition by phosphorylation. Biochem J 157: 41-67, 1976.
    • (1976) Biochem J , vol.157 , pp. 41-67
    • Walsh, D.A.1    Cooper, R.H.2    Denton, R.M.3    Bridges, B.J.4    Randle, P.J.5
  • 44
    • 0025787971 scopus 로고
    • The concept of symmorphosis: A testable hypothesis of structure-function relationship
    • Weibel ER, Taylor CR, Hoppeler H. The concept of symmorphosis: a testable hypothesis of structure-function relationship. Proc Natl Acad Sci USA 88: 10357-10361, 1991.
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 10357-10361
    • Weibel, E.R.1    Taylor, C.R.2    Hoppeler, H.3
  • 45
    • 0031691175 scopus 로고    scopus 로고
    • Urea: Diverse functions of a 'waste' product
    • Withers PC. Urea: diverse functions of a 'waste' product. Clin Exp Pharmacol Physiol 25: 722-727, 1998.
    • (1998) Clin Exp Pharmacol Physiol , vol.25 , pp. 722-727
    • Withers, P.C.1
  • 46
    • 0029560828 scopus 로고
    • Urea synthesis in enterocytes of developing pigs
    • Wu G. Urea synthesis in enterocytes of developing pigs. Biochem J 312: 717-723, 1995.
    • (1995) Biochem J , vol.312 , pp. 717-723
    • Wu, G.1
  • 47
    • 4344584138 scopus 로고    scopus 로고
    • Arginine deficiency in preterm infants: Biochemical mechanisms and nutritional implications
    • Wu G, Jaeger LA, Bazer FW, Rhoads JM. Arginine deficiency in preterm infants: biochemical mechanisms and nutritional implications. J Nutr Biochem 15: 442-451, 2004.
    • (2004) J Nutr Biochem , vol.15 , pp. 442-451
    • Wu, G.1    Jaeger, L.A.2    Bazer, F.W.3    Rhoads, J.M.4
  • 49
    • 0028230017 scopus 로고
    • Synthesis of citrulline from glutamine in pig enterocytes
    • Wu G, Knabe DA, Flynn NE. Synthesis of citrulline from glutamine in pig enterocytes. Biochem J 299: 115-121, 1994.
    • (1994) Biochem J , vol.299 , pp. 115-121
    • Wu, G.1    Knabe, D.A.2    Flynn, N.E.3
  • 50
    • 0032533159 scopus 로고    scopus 로고
    • Arginine metabolism: Nitric oxide and beyond
    • Wu G, Morris SM Jr. Arginine metabolism: nitric oxide and beyond. Biochem J 336: 1-17, 1998.
    • (1998) Biochem J , vol.336 , pp. 1-17
    • Wu, G.1    Morris Jr., S.M.2
  • 51
    • 0032792498 scopus 로고    scopus 로고
    • Mechanism responsible for inactivation of skeletal muscle pyruvate dehydrogenase complex in starvation and diabetes
    • Wu P, Inskeep K, Bowker-Kinley MM, Popov KM, Harris RA. Mechanism responsible for inactivation of skeletal muscle pyruvate dehydrogenase complex in starvation and diabetes. Diabetes 48: 1593-1599, 1999.
    • (1999) Diabetes , vol.48 , pp. 1593-1599
    • Wu, P.1    Inskeep, K.2    Bowker-Kinley, M.M.3    Popov, K.M.4    Harris, R.A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.