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Volumn 893, Issue , 1999, Pages 61-78

The α-ketoglutarate dehydrogenase complex

Author keywords

[No Author keywords available]

Indexed keywords

4 HYDROXYNONENAL; 6 PHOSPHOFRUCTOKINASE; ACONITATE HYDRATASE; GLUTAMIC ACID; MULTIENZYME COMPLEX; NEUROTRANSMITTER; OXOGLUTARATE DEHYDROGENASE; REACTIVE OXYGEN METABOLITE;

EID: 0033387202     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.1999.tb07818.x     Document Type: Conference Paper
Times cited : (103)

References (97)
  • 1
    • 0031605517 scopus 로고
    • From lipoic acid to multi-enzyme complexes
    • 1. Reed, L.J. 1988. From lipoic acid to multi-enzyme complexes. Protein Sci. 7: 220-224.
    • (1988) Protein Sci. , vol.7 , pp. 220-224
    • Reed, L.J.1
  • 2
    • 0020021375 scopus 로고
    • Structure-function relationships in pyruvate and α-ketoglutarate dehydrogenase complexes
    • 2. Reed, L.J. & R.M. Oliver. 1982. Structure-function relationships in pyruvate and α-ketoglutarate dehydrogenase complexes. Adv. Exp. Med. Biol. 148: 231-241.
    • (1982) Adv. Exp. Med. Biol. , vol.148 , pp. 231-241
    • Reed, L.J.1    Oliver, R.M.2
  • 3
    • 2442728373 scopus 로고
    • Purification and characterization of branched chain α-keto acid dehydrogenase complex of bovine kidney
    • 3. Pettit, F.H., S.J. Yeaman & L.J. Reed. 1978. Purification and characterization of branched chain α-keto acid dehydrogenase complex of bovine kidney. Proc. Natl. Acad. Sci. USA 75: 4881-4885.
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 4881-4885
    • Pettit, F.H.1    Yeaman, S.J.2    Reed, L.J.3
  • 4
    • 0020021375 scopus 로고
    • Structure-function relationships in pyruvate and α-ketoglutarate dehydrogenase complexes
    • 4. Reed, L.J. & R.M. Oliver. 1982. Structure-function relationships in pyruvate and α-ketoglutarate dehydrogenase complexes. Adv. Exp. Med. Biol. 148: 231-241.
    • (1982) Adv. Exp. Med. Biol. , vol.148 , pp. 231-241
    • Reed, L.J.1    Oliver, R.M.2
  • 6
    • 0032537555 scopus 로고    scopus 로고
    • Cloning, structure, chromosomal location and promoter analysis of human 2-oxoglutarate dehydrogenase gene
    • 6. Koike, K. 1998. Cloning, structure, chromosomal location and promoter analysis of human 2-oxoglutarate dehydrogenase gene. Biochim. Biophys. Acta1385: 373-384.
    • (1998) Biochim. Biophys. Acta , vol.1385 , pp. 373-384
    • Koike, K.1
  • 7
    • 0031579441 scopus 로고    scopus 로고
    • Functional characterization of the 5'-flanking region of the gene encoding human 2-oxoglutarate dehydrogenase
    • 7. Koike, K. & S. Matsuo. 1997. Functional characterization of the 5'-flanking region of the gene encoding human 2-oxoglutarate dehydrogenase. Gene 186: 45-53.
    • (1997) Gene , vol.186 , pp. 45-53
    • Koike, K.1    Matsuo, S.2
  • 8
    • 0026595273 scopus 로고
    • Cloning and nucleotide sequence of the cDNA encoding human 2oxoglutarate dehydrogenase (lipoamide)
    • 8. Koike, K. et al. 1992. Cloning and nucleotide sequence of the cDNA encoding human 2oxoglutarate dehydrogenase (lipoamide). Proc. Natl. Acad. Sci. USA 89(5): 1963-1967.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , Issue.5 , pp. 1963-1967
    • Koike, K.1
  • 9
    • 0031896743 scopus 로고    scopus 로고
    • Thiamine deficiency decreases steady-state transketolase and pyruvate dehydrogenase but not α-ketoglutarate dehydrogenase levels in three human cell types
    • 9. Pekovich, S.R., P.R. Martin & C.K. Singleton. 1998. Thiamine deficiency decreases steady-state transketolase and pyruvate dehydrogenase but not α-ketoglutarate dehydrogenase levels in three human cell types. J. Nutrition 128: 683-687.
    • (1998) J. Nutrition , vol.128 , pp. 683-687
    • Pekovich, S.R.1    Martin, P.R.2    Singleton, C.K.3
  • 10
    • 0027935643 scopus 로고
    • Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex
    • 10. Nakano, K., C. Takase, T. Sakomoto, S. Nakagawa, J. Inazawa, S. Ohta & S. Matuda. 1994. Isolation, characterization and structural organization of the gene and pseudogene for the dihydrolipoamide succinyltransferase component of the human 2-oxoglutarate dehydrogenase complex. Eur. J. Biochem. 224: 179-189.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 179-189
    • Nakano, K.1    Takase, C.2    Sakomoto, T.3    Nakagawa, S.4    Inazawa, J.5    Ohta, S.6    Matuda, S.7
  • 18
    • 0000476175 scopus 로고    scopus 로고
    • Association of DLST polymorphisms with familial Alzheimer's Disease
    • 18. Lilius, L., K-F.R. Sheu, L. Lannfelt & J.P. Blass. 1998. Association of DLST polymorphisms with familial Alzheimer's Disease. Neurosci. Abstr. 24: 255.
    • (1998) Neurosci. Abstr. , vol.24 , pp. 255
    • Lilius, L.1    Sheu, K.-F.R.2    Lannfelt, L.3    Blass, J.P.4
  • 19
    • 0028080953 scopus 로고
    • A pseudogene of dihydrolipoyl succinyltransferase (E2k) found by PCR amplification and direct sequencing of rodent-human cell hybrid DNAs
    • 19. Cai, X., P. Szabo, G. Ali, R.F. Tanzi & J.P. Blass. 1994. A pseudogene of dihydrolipoyl succinyltransferase (E2k) found by PCR amplification and direct sequencing of rodent-human cell hybrid DNAs. Somatic Cell Mol. Genet. 20: 339-343.
    • (1994) Somatic Cell Mol. Genet. , vol.20 , pp. 339-343
    • Cai, X.1    Szabo, P.2    Ali, G.3    Tanzi, R.F.4    Blass, J.P.5
  • 20
    • 0028387219 scopus 로고
    • Abnormality of the α-ketoglutarate dehydrogenase complex in fibroblasts from familial Alzheimer's disease
    • 20. Sheu, K-F.R., A.J.L. Cooper, J.G. Lindsay & J.P. Blass. 1994. Abnormality of the α-ketoglutarate dehydrogenase complex in fibroblasts from familial Alzheimer's disease. Ann. Neurol. 35: 312-318.
    • (1994) Ann. Neurol. , vol.35 , pp. 312-318
    • Sheu, K.-F.R.1    Cooper, A.J.L.2    Lindsay, J.G.3    Blass, J.P.4
  • 21
    • 0029809947 scopus 로고    scopus 로고
    • Reconstitution of mammalian pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes: Analysis of protein X involvement and interaction of homologous and heterologous dihydrolipoamide dehydrogenases
    • 21. Sanderson, S.J., S.S. Khan, G. McCartney, C. Miller & J.G. Lindsay. 1996. Reconstitution of mammalian pyruvate dehydrogenase and 2-oxoglutarate dehydrogenase complexes: analysis of protein X involvement and interaction of homologous and heterologous dihydrolipoamide dehydrogenases. Biochem. J. 1319: 109-116.
    • (1996) Biochem. J. , vol.1319 , pp. 109-116
    • Sanderson, S.J.1    Khan, S.S.2    McCartney, G.3    Miller, C.4    Lindsay, J.G.5
  • 22
    • 0027305994 scopus 로고
    • The structure of the human dihydrolipoamide dehydrogenase gene (DLD) and its upstream elements
    • 22. Feigenbaum, A.S. & B.H. Robinson. 1993. The structure of the human dihydrolipoamide dehydrogenase gene (DLD) and its upstream elements. Genomics 17: 376-381.
    • (1993) Genomics , vol.17 , pp. 376-381
    • Feigenbaum, A.S.1    Robinson, B.H.2
  • 23
    • 0024616270 scopus 로고    scopus 로고
    • Dihydrolipoamide dehydrogenase: Functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases
    • 23. Carothers, D.J., G. Pons & M.S. Patel. Dihydrolipoamide dehydrogenase: functional similarities and divergent evolution of the pyridine nucleotide-disulfide oxidoreductases. Arch. Biochem. Biophys. 268: 409-425.
    • Arch. Biochem. Biophys. , vol.268 , pp. 409-425
    • Carothers, D.J.1    Pons, G.2    Patel, M.S.3
  • 24
    • 0023621278 scopus 로고
    • Isolation and sequence determination of cDNA clones for porcine and human lipoamide dehydrogenase
    • 24. Otulakowski, G. & B.H. Robinson. 1987. Isolation and sequence determination of cDNA clones for porcine and human lipoamide dehydrogenase. J. Biol. Chem. 262: 17313-17318.
    • (1987) J. Biol. Chem. , vol.262 , pp. 17313-17318
    • Otulakowski, G.1    Robinson, B.H.2
  • 26
    • 0026469993 scopus 로고
    • Characterization of the transcriptional regulatory region of the human dihydrolipoamide dehydrogenase gene
    • 26. Johanning, G.L., J.L. Morris, K.T. Madhusudhan, D. Samols & M.S. Patel. 1992. Characterization of the transcriptional regulatory region of the human dihydrolipoamide dehydrogenase gene. Proc. Natl. Acad. Sci. USA 89: 10964-10968.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 10964-10968
    • Johanning, G.L.1    Morris, J.L.2    Madhusudhan, K.T.3    Samols, D.4    Patel, M.S.5
  • 27
    • 0026571038 scopus 로고
    • Isolation, characterization, and sequence analysis of a cDNA encoding L-protein, the dihydrolipoamide dehydrogenase component of the glycine cleavage system from pea-leaf mitochondria
    • 27. Bourgignon, J., D. Macharel, M. Neuburger & R. Douce. 1992. Isolation, characterization, and sequence analysis of a cDNA encoding L-protein, the dihydrolipoamide dehydrogenase component of the glycine cleavage system from pea-leaf mitochondria. Eur. J. Biochem. 204: 865-873.
    • (1992) Eur. J. Biochem. , vol.204 , pp. 865-873
    • Bourgignon, J.1    Macharel, D.2    Neuburger, M.3    Douce, R.4
  • 28
    • 0025370816 scopus 로고
    • Structure-function relationships in dihydrolipoamide acyltransferases
    • 28. Reed, L.J. & M.L. Hackert. 1990. Structure-function relationships in dihydrolipoamide acyltransferases. J. Biol. Chem. 265(16): 8971-8974.
    • (1990) J. Biol. Chem. , vol.265 , Issue.16 , pp. 8971-8974
    • Reed, L.J.1    Hackert, M.L.2
  • 29
    • 0020563497 scopus 로고
    • Evidence for a multiple random coupling mechanism in the α-ketoglutarate dehydrogenase multienzyme complex of Escherichia coli: A computer model analysis
    • 29. Hackert, M.L., R.M. Oliver & L.J. Reed. 1983. Evidence for a multiple random coupling mechanism in the α-ketoglutarate dehydrogenase multienzyme complex of Escherichia coli: a computer model analysis. Proc. Natl. Acad. Sci. USA 80: 2226-2230.
    • (1983) Proc. Natl. Acad. Sci. USA , vol.80 , pp. 2226-2230
    • Hackert, M.L.1    Oliver, R.M.2    Reed, L.J.3
  • 30
    • 0032563138 scopus 로고    scopus 로고
    • Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex
    • 30. Knapp, J.E., D.T. Mitchell, M.A. Yazdi, S.R. Ernst, L.J. Reed & M.L. Hackert. 1998. Crystal structure of the truncated cubic core component of the Escherichia coli 2-oxoglutarate dehydrogenase multienzyme complex. J. Mol. Biol. 280: 655-658
    • (1998) J. Mol. Biol. , vol.280 , pp. 655-658
    • Knapp, J.E.1    Mitchell, D.T.2    Yazdi, M.A.3    Ernst, S.R.4    Reed, L.J.5    Hackert, M.L.6
  • 31
    • 0030598366 scopus 로고    scopus 로고
    • Three-dimensional structure of the lipoyl domain from the dihydrolipoyl succinyltransferase component of the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli
    • 31. Ricaud, P.M., M.J. Howard, E.L. Roberts, R.W. Broadhurst & R.N. Perham. 1996. Three-dimensional structure of the lipoyl domain from the dihydrolipoyl succinyltransferase component of the 2-oxoglutarate dehydrogenase multienzyme complex of Escherichia coli. J. Mol. Biol. 264: 179-190.
    • (1996) J. Mol. Biol. , vol.264 , pp. 179-190
    • Ricaud, P.M.1    Howard, M.J.2    Roberts, E.L.3    Broadhurst, R.W.4    Perham, R.N.5
  • 32
    • 0032508722 scopus 로고    scopus 로고
    • Subunit interactions in the mammalian α-ketoglutarate dehydrogenase complex. Evidence for direct association of the α-ketoglutarate dehydrogenase and dihydrolipoamide dehydrogenase components
    • 32. McCartney, R.G., J.E. Rice, S.J. Sanderson, V. Bunik, H. Lindsay & J.G. Lindsay. 1998. Subunit interactions in the mammalian α-ketoglutarate dehydrogenase complex. Evidence for direct association of the α-ketoglutarate dehydrogenase and dihydrolipoamide dehydrogenase components. J. Biol. Chem. 273: 24158-24164.
    • (1998) J. Biol. Chem. , vol.273 , pp. 24158-24164
    • McCartney, R.G.1    Rice, J.E.2    Sanderson, S.J.3    Bunik, V.4    Lindsay, H.5    Lindsay, J.G.6
  • 33
    • 0033153520 scopus 로고    scopus 로고
    • Site-directed mutagenesis of dihydrolipoamide dehydrogenase: Role of lysine-54 and glutamate-192 in stabilizing the thiolate-FAD intermediate
    • 33. Liu, T.C., Y.S. Hong, L.G. Korotchkina, N.N. Vettakkorumankankav & M.S. Patel. 1999. Site-directed mutagenesis of dihydrolipoamide dehydrogenase: role of lysine-54 and glutamate-192 in stabilizing the thiolate-FAD intermediate. Protein Expression Purif. 16: 27-39.
    • (1999) Protein Expression Purif. , vol.16 , pp. 27-39
    • Liu, T.C.1    Hong, Y.S.2    Korotchkina, L.G.3    Vettakkorumankankav, N.N.4    Patel, M.S.5
  • 34
    • 0343417073 scopus 로고    scopus 로고
    • Receptor site and sterospecificity of dihydrolipoamide dehydrogenase for R-and S-lipoamide: A molecular modelling study
    • 34. Raddatz, G. & H. Bisswanger. 1997. Receptor site and sterospecificity of dihydrolipoamide dehydrogenase for R-and S-lipoamide: a molecular modelling study. J. Biotech. 58: 89-100
    • (1997) J. Biotech. , vol.58 , pp. 89-100
    • Raddatz, G.1    Bisswanger, H.2
  • 35
    • 0030087797 scopus 로고    scopus 로고
    • α-Lipoic acid dependent regeneration of ascorbic acid from dehydroascorbic acid in rat liver mitochondria
    • 35. Xu, D.P. & W.W. Wells. 1996. α-Lipoic acid dependent regeneration of ascorbic acid from dehydroascorbic acid in rat liver mitochondria. J. Bioenerg. Biomembr. 28: 77-85.
    • (1996) J. Bioenerg. Biomembr. , vol.28 , pp. 77-85
    • Xu, D.P.1    Wells, W.W.2
  • 36
    • 0032991061 scopus 로고    scopus 로고
    • Ubiquinone is reduced by lipoamide dehydrogenase and this reaction is potently stimulated by zinc
    • 36. Olsson, J.M., L. Xia, L.C. Eriksson & M. Bjornstedt. 1999. Ubiquinone is reduced by lipoamide dehydrogenase and this reaction is potently stimulated by zinc. FEBS Lett. 448: 190-192.
    • (1999) FEBS Lett. , vol.448 , pp. 190-192
    • Olsson, J.M.1    Xia, L.2    Eriksson, L.C.3    Bjornstedt, M.4
  • 37
    • 0001712238 scopus 로고    scopus 로고
    • A tetrahymena thermophila G4-DNA binding protein with dihydrolipoamide dehydrogenase activity
    • 37. Kee, K., L. Niu & E. Henderson. 1998. A tetrahymena thermophila G4-DNA binding protein with dihydrolipoamide dehydrogenase activity. Biochemistry 37: 4224-4334.
    • (1998) Biochemistry , vol.37 , pp. 4224-4334
    • Kee, K.1    Niu, L.2    Henderson, E.3
  • 38
    • 0031958863 scopus 로고    scopus 로고
    • Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast
    • 38. Toyoda, T., K. Suzuki, T. Sekiguchi, L.J. Reed & Takenaka. 1998. Crystal structure of eucaryotic E3, lipoamide dehydrogenase from yeast. J. Biochem. 123: 668-674.
    • (1998) J. Biochem. , vol.123 , pp. 668-674
    • Toyoda, T.1    Suzuki, K.2    Sekiguchi, T.3    Reed, L.J.4    Takenaka5
  • 39
    • 18744432273 scopus 로고
    • Towards the molecular basis for the regulation of mitochondrial dehydrogenases by calcium ions
    • Aug.-Sep.
    • 39. Nichols, B.J. & R.M. Denton. 1995. Towards the molecular basis for the regulation of mitochondrial dehydrogenases by calcium ions. Mol. Cell. Biochem. Aug.-Sep.: 149-150; 203-212.
    • (1995) Mol. Cell. Biochem. , pp. 149-150
    • Nichols, B.J.1    Denton, R.M.2
  • 41
    • 0031680036 scopus 로고    scopus 로고
    • Role of mitochondrial calcium transport in the control of substrate oxidation
    • 41. Hansford, R.G. & D. Zorov. 1998. Role of mitochondrial calcium transport in the control of substrate oxidation. Mol. Cell. Biochem. 184: 359-369.
    • (1998) Mol. Cell. Biochem. , vol.184 , pp. 359-369
    • Hansford, R.G.1    Zorov, D.2
  • 42
    • 0032512411 scopus 로고    scopus 로고
    • Inhibition of NADH-linked mitochondrial respiration by 4-hydroxy-2-nonenal
    • 42. Humphries, K.M., Y. Yoo & L.I. Szewda. 1998. Inhibition of NADH-linked mitochondrial respiration by 4-hydroxy-2-nonenal. Biochemistry 37: 552-557.
    • (1998) Biochemistry , vol.37 , pp. 552-557
    • Humphries, K.M.1    Yoo, Y.2    Szewda, L.I.3
  • 43
    • 0032506040 scopus 로고    scopus 로고
    • Selective inactivation of α-ketoglutarate dehydrogenase and pyruvate dehydrogenase: Reaction of lipoic acid with 4-hydroxy-2-nonenal
    • 43. Humphries, K.M. & L.I. Sweda. 1998. Selective inactivation of α-ketoglutarate dehydrogenase and pyruvate dehydrogenase: reaction of lipoic acid with 4-hydroxy-2-nonenal. Biochemistry 37: 15835-15841.
    • (1998) Biochemistry , vol.37 , pp. 15835-15841
    • Humphries, K.M.1    Sweda, L.I.2
  • 44
    • 0032547309 scopus 로고    scopus 로고
    • Inactivation of aconitase and oxoglutarate dehydrogenase in skeletal muscle in vitro by superoxide anions and/or nitric oxide
    • 44. Andersson, U., B. Leighton, M.E. Young, E. Blomstrand & E.A. Newsholme. 1998. Inactivation of aconitase and oxoglutarate dehydrogenase in skeletal muscle in vitro by superoxide anions and/or nitric oxide. Biochem. Biophys. Res. Commun. 249: 512-516.
    • (1998) Biochem. Biophys. Res. Commun. , vol.249 , pp. 512-516
    • Andersson, U.1    Leighton, B.2    Young, M.E.3    Blomstrand, E.4    Newsholme, E.A.5
  • 45
    • 0033048258 scopus 로고    scopus 로고
    • Metabolic impairment induces oxidative stress, compromises inflammatory responses, and inactivates a key mitochondrial enzyme in microglia
    • 45. Park. L.C., H. Zhang, K.F. Sheu, N.Y. Calingasan, B.S. Kristal, J.G. Lindsay & G.E. Gibson. 1999. Metabolic impairment induces oxidative stress, compromises inflammatory responses, and inactivates a key mitochondrial enzyme in microglia. J. Neurochem. 72: 1948-1958.
    • (1999) J. Neurochem. , vol.72 , pp. 1948-1958
    • Park, L.C.1    Zhang, H.2    Sheu, K.F.3    Calingasan, N.Y.4    Kristal, B.S.5    Lindsay, J.G.6    Gibson, G.E.7
  • 46
    • 0033000269 scopus 로고    scopus 로고
    • Depolarization of in situ mitochondria due to hydrogen peroxide-induced oxidative stress in nerve terminals: Inhibition of α-ketoglutarate dehydrogenase
    • 46. Chinopoulos, C., L. Tretter & V. Adam-Vizi. 1999. Depolarization of in situ mitochondria due to hydrogen peroxide-induced oxidative stress in nerve terminals: inhibition of α-ketoglutarate dehydrogenase. J. Neurochem. 73: 220-228.
    • (1999) J. Neurochem. , vol.73 , pp. 220-228
    • Chinopoulos, C.1    Tretter, L.2    Adam-Vizi, V.3
  • 47
    • 0033535948 scopus 로고    scopus 로고
    • Declines in mitochondrial respiration during cardiac reperfusion: Age-dependent inactivation of α-ketoglutarate dehydrogenase
    • 47. Lucas, D.T. & L.I. Szweda. 1999. Declines in mitochondrial respiration during cardiac reperfusion: age-dependent inactivation of α-ketoglutarate dehydrogenase. Proc. Natl. Acad. Sci. USA 96: 6689-6693.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 6689-6693
    • Lucas, D.T.1    Szweda, L.I.2
  • 48
    • 0008923430 scopus 로고    scopus 로고
    • Inhibition of select mitochondrial enzymes in PC12 cells exposed to S-(1,1,2,2-tetrafluoroethyl)-L-Cysteine
    • In press
    • 48. Park, L.C.H., G.E. Gibson, V. Bunik & A.J.L. Cooper. 1999. Inhibition of select mitochondrial enzymes in PC12 cells exposed to S-(1,1,2,2-tetrafluoroethyl)-L-Cysteine. J. Neurochem. In press.
    • (1999) J. Neurochem.
    • Park, L.C.H.1    Gibson, G.E.2    Bunik, V.3    Cooper, A.J.L.4
  • 49
    • 0032994403 scopus 로고    scopus 로고
    • Inactivation of myocardial dihydrolipoamide dehydrogenase by myeloperoxidase systems: Effects of halides, nitrite and thiol compounds
    • 49. Guttierez-Correa, J. & A.O. Stoppani. 1999. Inactivation of myocardial dihydrolipoamide dehydrogenase by myeloperoxidase systems: effects of halides, nitrite and thiol compounds. Free Radical Res. 30: 105-117.
    • (1999) Free Radical Res. , vol.30 , pp. 105-117
    • Guttierez-Correa, J.1    Stoppani, A.O.2
  • 51
    • 1842296939 scopus 로고    scopus 로고
    • Maximum rate of oxygen uptake by human skeletal muscle in relation to maximal activities of enzymes in the Krebs cycle
    • 51. Blomstrand, E., G. Radegran & B. Saltin. 1997. Maximum rate of oxygen uptake by human skeletal muscle in relation to maximal activities of enzymes in the Krebs cycle. J. Physiol. 501: 455-460.
    • (1997) J. Physiol. , vol.501 , pp. 455-460
    • Blomstrand, E.1    Radegran, G.2    Saltin, B.3
  • 53
    • 0027426832 scopus 로고    scopus 로고
    • Metabolic alterations common to neural and non-neural cells in Alzheimer's disease
    • 53. Blass, J.P. Metabolic alterations common to neural and non-neural cells in Alzheimer's disease. Hippocampus 13: 45-54.
    • Hippocampus , vol.13 , pp. 45-54
    • Blass, J.P.1
  • 54
    • 0023732664 scopus 로고
    • Reduced activities of thiamine-dependent enzymes in the brains and peripheral tissues of patients with Alzheimer's disease
    • 54. Gibson, G.E., K-F.R. Sheu, J.P. Blass, A. Baker, K.C. Carlson, B. Harding & P. Perino. 1988. Reduced activities of thiamine-dependent enzymes in the brains and peripheral tissues of patients with Alzheimer's disease. Arch. Neurol. 45: 841-845.
    • (1988) Arch. Neurol. , vol.45 , pp. 841-845
    • Gibson, G.E.1    Sheu, K.-F.R.2    Blass, J.P.3    Baker, A.4    Carlson, K.C.5    Harding, B.6    Perino, P.7
  • 55
    • 0032569826 scopus 로고    scopus 로고
    • Affected enzyme activities in Alzheimer's disease are sensitive to antemortem hypoxia
    • 55. Terwel, D., J. Bothmer, E. Wolf, F. Meng & J. Jolles. 1998. Affected enzyme activities in Alzheimer's disease are sensitive to antemortem hypoxia. J. Neurol. Sci. 161: 47-56.
    • (1998) J. Neurol. Sci. , vol.161 , pp. 47-56
    • Terwel, D.1    Bothmer, J.2    Wolf, E.3    Meng, F.4    Jolles, J.5
  • 56
    • 0023434105 scopus 로고
    • Light microscopic immunocytochemical localization of pyruvate dehydrogenase in rat brain: Topographical distribution and relation to cholinergic and catecholaminergic nuclei
    • 56. Milner, T.A., C. Aoki, K.F.R. Sheu, J.P. Blass & V.M. Pickel. 1987. Light microscopic immunocytochemical localization of pyruvate dehydrogenase in rat brain: topographical distribution and relation to cholinergic and catecholaminergic nuclei. J. Neurosci. 7: 3171-3190.
    • (1987) J. Neurosci. , vol.7 , pp. 3171-3190
    • Milner, T.A.1    Aoki, C.2    Sheu, K.F.R.3    Blass, J.P.4    Pickel, V.M.5
  • 57
    • 0023372146 scopus 로고
    • Regional distribution of astrocytes with intense immunoreactivity for glutamate dehydrogenase in rat brain: Implications for neuron-glia interactions in glutamate transmission
    • 57. Aoki, C., T.A. Milner, K.F.R. Sheu, J.P. Blass & V.M. Pickel. 1987. Regional distribution of astrocytes with intense immunoreactivity for glutamate dehydrogenase in rat brain: implications for neuron-glia interactions in glutamate transmission. J. Neurosci. 7: 2214-2231.
    • (1987) J. Neurosci. , vol.7 , pp. 2214-2231
    • Aoki, C.1    Milner, T.A.2    Sheu, K.F.R.3    Blass, J.P.4    Pickel, V.M.5
  • 58
    • 0028169899 scopus 로고
    • Distribution of the α-ketoglutarate dehydrogenase complex in rat brain
    • 58. Calingasan. N., H. Baker, K.F. Sheu & G.E. Gibson. 1994. Distribution of the α-ketoglutarate dehydrogenase complex in rat brain. J. Comp. Neurol. 346: 461-479.
    • (1994) J. Comp. Neurol. , vol.346 , pp. 461-479
    • Calingasan, N.1    Baker, H.2    Sheu, K.F.3    Gibson, G.E.4
  • 59
    • 0031748099 scopus 로고    scopus 로고
    • Immunoreactivity of porcine heart lipoamide acetyl-and succinyl-transferases (PDC-E2, OGDC-E2) with primary biliary cirrhosis sera: Characterization of the autoantigenic region and effects of enzymateic delipoylation and relipoylation
    • 59. Koike, K., H. Ishibashi & M. Koike. 1998. Immunoreactivity of porcine heart lipoamide acetyl-and succinyl-transferases (PDC-E2, OGDC-E2) with primary biliary cirrhosis sera: characterization of the autoantigenic region and effects of enzymateic delipoylation and relipoylation. Hepatology 27: 1467-1474.
    • (1998) Hepatology , vol.27 , pp. 1467-1474
    • Koike, K.1    Ishibashi, H.2    Koike, M.3
  • 60
    • 77956852578 scopus 로고    scopus 로고
    • Metabolism of the aging brain
    • M.P. Mattson, J.W. Gedes, P. Tamiras & E.E. Bittar, Eds.: JAI Press. London
    • 60. Blass, J.P., G.E. Gibson & S. Hoyer. 1997. Metabolism of the aging brain. In Advances in Cell Aging and Gerontology, Vol 2: The Aging Brain. M.P. Mattson, J.W. Gedes, P. Tamiras & E.E. Bittar, Eds.: 109-128. JAI Press. London.
    • (1997) Advances in Cell Aging and Gerontology, Vol 2: The Aging Brain , vol.2 , pp. 109-128
    • Blass, J.P.1    Gibson, G.E.2    Hoyer, S.3
  • 61
    • 0029803499 scopus 로고    scopus 로고
    • Identification of two mutations in a compound heterozygous child with dihydrolioamide dehydrogenase deficiency
    • 61. Hong, Y.S., D.S. Kerr, W.J. Craigen, J. Tan, Y. Pan, M. Lusk & M.S. Patel. 1996. Identification of two mutations in a compound heterozygous child with dihydrolioamide dehydrogenase deficiency. Hum. Mol. Genet. 5: 1925-1930.
    • (1996) Hum. Mol. Genet. , vol.5 , pp. 1925-1930
    • Hong, Y.S.1    Kerr, D.S.2    Craigen, W.J.3    Tan, Y.4    Pan, Y.5    Lusk, M.6    Patel, M.S.7
  • 65
    • 0030835615 scopus 로고    scopus 로고
    • Inborn errors of the Krebs cycle: A group of unusual mitochondrial diseases in human
    • 65. Bourgeron, R.P., B. Parfait, D. Chretien, A. Munnich & A. Rotig. 1997. Inborn errors of the Krebs cycle: a group of unusual mitochondrial diseases in human. Biochim. Biophys. Acta. 1361: 185-197.
    • (1997) Biochim. Biophys. Acta. , vol.1361 , pp. 185-197
    • Bourgeron, R.P.1    Parfait, B.2    Chretien, D.3    Munnich, A.4    Rotig, A.5
  • 66
    • 0031445917 scopus 로고    scopus 로고
    • Targeted disruption of the murine dihydrolipoamide dehydrogenase gene (Dld) results in perigastrulation lethality
    • 66. Johnson, M.T., H.S. Yang, T. Magnuson & M.S. Patel. 1997. Targeted disruption of the murine dihydrolipoamide dehydrogenase gene (Dld) results in perigastrulation lethality. Proc. Nat. Acad. Sci. USA 94: 14512-14517.
    • (1997) Proc. Nat. Acad. Sci. USA , vol.94 , pp. 14512-14517
    • Johnson, M.T.1    Yang, H.S.2    Magnuson, T.3    Patel, M.S.4
  • 67
    • 0027384549 scopus 로고
    • 2-Ketoglutarate dehydrogenase deficiency, a rare cause of primary hyperlactataemia: Report of a new case
    • 67. Collombet, J.M., P. Divry, M. Mathieu & P. Guibaud. 1993. 2-Ketoglutarate dehydrogenase deficiency, a rare cause of primary hyperlactataemia: report of a new case. J. Inher. Metab. Dis. 16: 821-825.
    • (1993) J. Inher. Metab. Dis. , vol.16 , pp. 821-825
    • Collombet, J.M.1    Divry, P.2    Mathieu, M.3    Guibaud, P.4
  • 69
    • 0033054177 scopus 로고    scopus 로고
    • The friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis
    • 69. Wong, A., J. Yang, P. Cavadini, C. Gellera, B. Lonnerdal, F. Taroni & G. Cortopassi. 1999. The Friedreich's ataxia mutation confers cellular sensitivity to oxidant stress which is rescued by chelators of iron and calcium and inhibitors of apoptosis. Hum. Mol. Genet. 8(3): 425-30.
    • (1999) Hum. Mol. Genet. , vol.8 , Issue.3 , pp. 425-430
    • Wong, A.1    Yang, J.2    Cavadini, P.3    Gellera, C.4    Lonnerdal, B.5    Taroni, F.6    Cortopassi, G.7
  • 70
    • 0017143791 scopus 로고
    • Decreased activities of the pyruvate and ketoglutarate dehydrogenase complexes in fibroblasts from five patients with Fredreich's ataxia
    • 70. Blass, J.P., R.A.P. Kark, N. Menon & S.H. Harris. 1976. Decreased activities of the pyruvate and ketoglutarate dehydrogenase complexes in fibroblasts from five patients with Fredreich's ataxia. N. Engl. J. Med. 295: 62-66.
    • (1976) N. Engl. J. Med. , vol.295 , pp. 62-66
    • Blass, J.P.1    Kark, R.A.P.2    Menon, N.3    Harris, S.H.4
  • 73
    • 0031614996 scopus 로고    scopus 로고
    • Molecular genetics of the hereditary ataxias
    • 73. Pandolfo, M. & L. Montermini. 1998. Molecular genetics of the hereditary ataxias. Adv. Genet. 38: 31-68.
    • (1998) Adv. Genet. , vol.38 , pp. 31-68
    • Pandolfo, M.1    Montermini, L.2
  • 75
    • 0030812593 scopus 로고    scopus 로고
    • Glutathione-S-transferase constructs containing medium to large polyglutamine inserts are substrates of guinea pig liver transglutaminase: Does transglutaminase play a role in the pathogenesis of expanded CAG/Poly Q neurodegenerative diseases?
    • 75. Cooper, A.J.L., K.-F.R. Sheu, J.R. Burke, O. Onodera, W.J. Strittmatter, A.D. Roses & J.P. Blass. 1997. Glutathione-S-transferase constructs containing medium to large polyglutamine inserts are substrates of guinea pig liver transglutaminase: does transglutaminase play a role in the pathogenesis of expanded CAG/Poly Q neurodegenerative diseases? Proc. Natl. Acad. Sci. USA 94: 12604-12609.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12604-12609
    • Cooper, A.J.L.1    Sheu, K.-F.R.2    Burke, J.R.3    Onodera, O.4    Strittmatter, W.J.5    Roses, A.D.6    Blass, J.P.7
  • 79
    • 0028176592 scopus 로고
    • An immunohistochemical study on α-ketoglutarate dehydrogenase complex in Parkinson's disease
    • 79. Mizuno, Y., S. Matuda & H. Yoshino. 1994. An immunohistochemical study on α-ketoglutarate dehydrogenase complex in Parkinson's disease. Ann. Neurol. 35: 204-210.
    • (1994) Ann. Neurol. , vol.35 , pp. 204-210
    • Mizuno, Y.1    Matuda, S.2    Yoshino, H.3
  • 80
    • 0031891886 scopus 로고    scopus 로고
    • Association between the gene encoding the E2 subunit of α-ketoglutarate dehydrogenase complex and Parkinson's disease
    • 80. Kobayashi, T., H. Matsumine, S. Matuda & Y. Misuno. 1998. Association between the gene encoding the E2 subunit of α-ketoglutarate dehydrogenase complex and Parkinson's disease. Ann. Neurol. 43: 120-123.
    • (1998) Ann. Neurol. , vol.43 , pp. 120-123
    • Kobayashi, T.1    Matsumine, H.2    Matuda, S.3    Misuno, Y.4
  • 81
    • 0031861864 scopus 로고    scopus 로고
    • Absence of vascular dementia in an autopsy series from a dementia clinic
    • 81. Nolan, K.A., M.M. Lino, A.W. Seligman & J.P. Blass. 1998. Absence of vascular dementia in an autopsy series from a dementia clinic. J. Am. Geriatr. Soc. 46: 597-604.
    • (1998) J. Am. Geriatr. Soc. , vol.46 , pp. 597-604
    • Nolan, K.A.1    Lino, M.M.2    Seligman, A.W.3    Blass, J.P.4
  • 83
    • 0030915855 scopus 로고    scopus 로고
    • Oxidative stress hypothesis in Alzheimer's disease
    • 83. Markesbery, W.R. 1997. Oxidative stress hypothesis in Alzheimer's disease. Free Radical Biol. Med. 123: 134-147.
    • (1997) Free Radical Biol. Med. , vol.123 , pp. 134-147
    • Markesbery, W.R.1
  • 84
    • 0029884010 scopus 로고    scopus 로고
    • Brain protein and α-ketoglutarate dehydrogenase complex activity in Alzheimer's disease
    • 84. Mastrogiacoma, F., J.G. Lindsay, L. Bettendorff, J. Rice & S.J. Kish. 1996. Brain protein and α-ketoglutarate dehydrogenase complex activity in Alzheimer's disease. Ann. Neurol. 39: 592-598.
    • (1996) Ann. Neurol. , vol.39 , pp. 592-598
    • Mastrogiacoma, F.1    Lindsay, J.G.2    Bettendorff, L.3    Rice, J.4    Kish, S.J.5
  • 85
    • 0025650037 scopus 로고
    • Thiamine-dependent enzyme changes in temporal cortex of patients with Alzheimer's disease
    • 85. Butterworth, R.F. & A.M. Besnard. 1990. Thiamine-dependent enzyme changes in temporal cortex of patients with Alzheimer's disease. Metab. Brain Dis. 5: 179-184.
    • (1990) Metab. Brain Dis. , vol.5 , pp. 179-184
    • Butterworth, R.F.1    Besnard, A.M.2
  • 86
    • 85084767998 scopus 로고
    • Chemical neuroanatomy of energy metabolism: Immunohistochemical studies in relation to selective vulnerability
    • 86. Ko, L., K-F.R. Sheu & J.P. Blass. 1993. Chemical neuroanatomy of energy metabolism: immunohistochemical studies in relation to selective vulnerability. J. Neurochem. 61: S70.
    • (1993) J. Neurochem. , vol.61
    • Ko, L.1    Sheu, K.-F.R.2    Blass, J.P.3
  • 87
    • 0030709194 scopus 로고    scopus 로고
    • Inherent abnormalities in oxidative metabolism n Alzheimer's disease: Interaction with vascular abnormalities
    • 87. Blass, J.P., K.F. Sheu, S. Piacentini & S. Sorbi. 1997. Inherent abnormalities in oxidative metabolism n Alzheimer's disease: interaction with vascular abnormalities. Ann. N.Y. Acad. Sci. 826: 382-385.
    • (1997) Ann. N.Y. Acad. Sci. , vol.826 , pp. 382-385
    • Blass, J.P.1    Sheu, K.F.2    Piacentini, S.3    Sorbi, S.4
  • 89
    • 4243808616 scopus 로고    scopus 로고
    • Reductions in a key mitochondrial enzyme in brains from Alzheimer's Disease patients correlate with a clinical dementia rating
    • and submitted
    • 89. Gibson, G.E., V. Haroutunian, L.C.H. Park, H. Zhang, R. Mohs R.K-F. Sheu & J.P. Blass. 1999. Reductions in a key mitochondrial enzyme in brains from Alzheimer's Disease patients correlate with a clinical dementia rating. J. Neurochem. 73: S23; and submitted.
    • (1999) J. Neurochem. , vol.73
    • Gibson, G.E.1    Haroutunian, V.2    Park, L.C.H.3    Zhang, H.4    Mohs, R.5    Sheu, R.K.-F.6    Blass, J.P.7
  • 91
    • 0019142890 scopus 로고
    • Glycolytic enzymes from human autoptic brain cortex: Normal aged and demented cases
    • 91. Iwangoff, P., R. Armbruster, A. Enz & W. Meier-Ruge. 1980. Glycolytic enzymes from human autoptic brain cortex: normal aged and demented cases. Mech. Ageing Deve.l 14: 203-209.
    • (1980) Mech. Ageing Deve.l , vol.14 , pp. 203-209
    • Iwangoff, P.1    Armbruster, R.2    Enz, A.3    Meier-Ruge, W.4
  • 93
  • 94
    • 0016777499 scopus 로고
    • The metabolism of ketone bodies in developing human brain: Development of ketone-body - Utilizing enzymes and ketone bodies as precursors for lipid synthesis
    • 94. Patel, M.S., C.A. Johnson, R. Rajan & O.E. Owen. 1975. The metabolism of ketone bodies in developing human brain: development of ketone-body - utilizing enzymes and ketone bodies as precursors for lipid synthesis. J. Neurochem. 25: 905-908.
    • (1975) J. Neurochem. , vol.25 , pp. 905-908
    • Patel, M.S.1    Johnson, C.A.2    Rajan, R.3    Owen, O.E.4
  • 96
    • 0020685951 scopus 로고
    • Decreased pyruvate dehydrogenase complex activity in Huntington and Alzheimer brain
    • 96. Sorbi, S., E.D. Bird & J.P. Blass. 1983. Decreased pyruvate dehydrogenase complex activity in Huntington and Alzheimer brain. Ann. Neurol. 13: 72-78.
    • (1983) Ann. Neurol. , vol.13 , pp. 72-78
    • Sorbi, S.1    Bird, E.D.2    Blass, J.P.3
  • 97
    • 0023084649 scopus 로고
    • Glutamate and malate dehydrogenase activities in Joseph disease and olivopontocerebellar atrophy
    • 97. Grossman, A., R.N. Rosenberg & L. Warmoth. 1987. Glutamate and malate dehydrogenase activities in Joseph disease and olivopontocerebellar atrophy. Neurology 37: 106-111.
    • (1987) Neurology , vol.37 , pp. 106-111
    • Grossman, A.1    Rosenberg, R.N.2    Warmoth, L.3


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