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Volumn 276, Issue 42, 2001, Pages 38329-38336

A Trail of Research from Lipoic Acid to α-Keto Acid Dehydrogenase Complexes

Author keywords

[No Author keywords available]

Indexed keywords

2 OXOACID; OXIDOREDUCTASE; THIOCTIC ACID; 2 OXOISOVALERATE DEHYDROGENASE (LIPOAMIDE); MULTIENZYME COMPLEX;

EID: 0035914303     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.R100026200     Document Type: Review
Times cited : (217)

References (10)
  • 1
    • 0002908647 scopus 로고
    • Crystalline α-lipoic acid: A catalytic agent associated with pyruvate dehydrogenase
    • Reed, L. J., DeBusk, B. G., Gunsalus, I. C., and Hornberger, C. S., Jr. (1951) Crystalline α-lipoic acid: a catalytic agent associated with pyruvate dehydrogenase. Science 114, 93-94
    • (1951) Science , vol.114 , pp. 93-94
    • Reed, L.J.1    DeBusk, B.G.2    Gunsalus, I.C.3    Hornberger C.S., Jr.4
  • 2
    • 0001390623 scopus 로고
    • Studies on the nature of protein-bound lipoic acid
    • Nawa, H., Brady, W. T., Koike, M., and Reed, L. J. (1960) Studies on the nature of protein-bound lipoic acid. J. Am. Chem. Soc. 82, 896-903
    • (1960) J. Am. Chem. Soc. , vol.82 , pp. 896-903
    • Nawa, H.1    Brady, W.T.2    Koike, M.3    Reed, L.J.4
  • 3
    • 0001121612 scopus 로고
    • α-Keto acid dehydrogenation complexes. I. Purification and properties of pyruvate and α-ketoglutarate dehydrogenation complexes of Escherichia coli
    • Koike, M., Reed, L. J., and Carroll, W. R. (1960) α-Keto acid dehydrogenation complexes. I. Purification and properties of pyruvate and α-ketoglutarate dehydrogenation complexes of Escherichia coli. J. Biol. Chem. 235, 1924-1930
    • (1960) J. Biol. Chem. , vol.235 , pp. 1924-1930
    • Koike, M.1    Reed, L.J.2    Carroll, W.R.3
  • 4
    • 0010426629 scopus 로고
    • α-Keto acid dehydrogenation complexes. IV. Resolution and reconstitution of the Escherichia coli pyruvate dehydrogenation complex
    • Koike, M., Reed, L. J., and Carroll, W. R. (1963) α-Keto acid dehydrogenation complexes. IV. Resolution and reconstitution of the Escherichia coli pyruvate dehydrogenation complex. J. Biol. Chem. 238, 30-39
    • (1963) J. Biol. Chem. , vol.238 , pp. 30-39
    • Koike, M.1    Reed, L.J.2    Carroll, W.R.3
  • 5
    • 0018292437 scopus 로고
    • Subunit structure of dihydrolipoyl transacetylase component of pyruvate dehydrogenase complex from Escherichia coli
    • Bleile, D. M., Munk, P., Oliver, R. M., and Reed, L. J. (1979) Subunit structure of dihydrolipoyl transacetylase component of pyruvate dehydrogenase complex from Escherichia coli. Proc. Natl. Acad. Sci. U. S. A. 76, 4385-4389
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 4385-4389
    • Bleile, D.M.1    Munk, P.2    Oliver, R.M.3    Reed, L.J.4
  • 6
    • 0014461121 scopus 로고
    • α-Keto acid dehydrogenase complexes. X. Regulation of the activity of the pyruvate dehydrogenase complex from beef kidney mitochondria by phosphorylation and dephosphorylation
    • Linn, T. C., Pettit, F. H., and Reed, L. J. (1969) α-Keto acid dehydrogenase complexes. X. Regulation of the activity of the pyruvate dehydrogenase complex from beef kidney mitochondria by phosphorylation and dephosphorylation. Proc. Natl. Acad. Sci. U. S. A. 62, 234-241
    • (1969) Proc. Natl. Acad. Sci. U. S. A. , vol.62 , pp. 234-241
    • Linn, T.C.1    Pettit, F.H.2    Reed, L.J.3
  • 7
    • 0015293102 scopus 로고
    • α-Keto acid dehydrogenase complexes. XV. Purification and properties of the component enzymes of the pyruvate dehydrogenase complexes from bovine kidney and heart
    • Linn, T. C., Pelley, J. W., Pettit, F. H., Hucho, F., Randall, D. D., and Reed, L. J. (1972) α-Keto acid dehydrogenase complexes. XV. Purification and properties of the component enzymes of the pyruvate dehydrogenase complexes from bovine kidney and heart. Arch. Biochem. Biophys. 148, 327-342
    • (1972) Arch. Biochem. Biophys. , vol.148 , pp. 327-342
    • Linn, T.C.1    Pelley, J.W.2    Pettit, F.H.3    Hucho, F.4    Randall, D.D.5    Reed, L.J.6
  • 8
    • 0029899870 scopus 로고    scopus 로고
    • Role of the regulatory subunit of bovine pyruvate dehydrogenase phosphatase
    • Yan, J., Lawson, J. E., and Reed, L. J. (1996) Role of the regulatory subunit of bovine pyruvate dehydrogenase phosphatase. Proc. Natl. Acad. Sci. U. S. A. 93, 4953-4956
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 4953-4956
    • Yan, J.1    Lawson, J.E.2    Reed, L.J.3
  • 10
    • 0035877764 scopus 로고    scopus 로고
    • Direct evidence for the size and conformational variability of the pyruvate dehydrogenase complex revealed by three-dimensional electron microscopy
    • Zhou, Z. H., Liao, W., Cheng, R. H., Lawson, J. E., McCarthy, D. B., Reed, L. J., and Stoops, J. K. (2001) Direct evidence for the size and conformational variability of the pyruvate dehydrogenase complex revealed by three-dimensional electron microscopy. J. Biol. Chem. 276, 21704-21713
    • (2001) J. Biol. Chem. , vol.276 , pp. 21704-21713
    • Zhou, Z.H.1    Liao, W.2    Cheng, R.H.3    Lawson, J.E.4    McCarthy, D.B.5    Reed, L.J.6    Stoops, J.K.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.