메뉴 건너뛰기




Volumn , Issue , 2008, Pages 149-165

Pyruvate dehydrogenase complex regulation and lipoic acid

Author keywords

[No Author keywords available]

Indexed keywords


EID: 71549155062     PISSN: None     EISSN: None     Source Type: Book    
DOI: None     Document Type: Chapter
Times cited : (4)

References (67)
  • 1
    • 0032904416 scopus 로고    scopus 로고
    • Alpha-lipoic acid treatment decreases serum lactate and pyruvate concentrations and improves glucose effectiveness in lean and obese patients with type 2 diabetes
    • Konrad, T. et al. Alpha-lipoic acid treatment decreases serum lactate and pyruvate concentrations and improves glucose effectiveness in lean and obese patients with type 2 diabetes, Diabetes Care 22, 280, 1999.
    • (1999) Diabetes Care , vol.22 , pp. 280
    • Konrad, T.1
  • 2
    • 0032840875 scopus 로고    scopus 로고
    • Oral administration of RAC-alpha-lipoic acid modulates insulin sensitivity in patients with type-2 diabetes mellitus: A placebo-controlled pilot trial
    • Jacob, S. et al. Oral administration of RAC-alpha-lipoic acid modulates insulin sensitivity in patients with type-2 diabetes mellitus: A placebo-controlled pilot trial, Free Radic. Biol. Med. 27, 309, 1999.
    • (1999) Free Radic. Biol. Med , vol.27 , pp. 309
    • Jacob, S.1
  • 3
    • 0036070514 scopus 로고    scopus 로고
    • Antioxidant and prooxidant activities of alphalipoic acid and dihydrolipoic acid
    • Moini, H., Packer, L., and Saris, N.E. Antioxidant and prooxidant activities of alphalipoic acid and dihydrolipoic acid, Toxicol. Appl. Pharmacol. 182, 84, 2002.
    • (2002) Toxicol. Appl. Pharmacol , vol.182 , pp. 84
    • Moini, H.1    Packer, L.2    Saris, N.E.3
  • 4
    • 0034987312 scopus 로고    scopus 로고
    • The antihyperglycemic drug alpha-lipoic acid stimulates glucose uptake via both GLUT4 translocation and GLUT4 activation: Potential role of p38 mitogen-activated protein kinase in GLUT4 activation
    • Konrad, D. et al. The antihyperglycemic drug alpha-lipoic acid stimulates glucose uptake via both GLUT4 translocation and GLUT4 activation: Potential role of p38 mitogen-activated protein kinase in GLUT4 activation, Diabetes 50, 1464, 2001.
    • (2001) Diabetes , vol.50 , pp. 1464
    • Konrad, D.1
  • 5
    • 0037082117 scopus 로고    scopus 로고
    • R-alpha-lipoic acid action on cell redox status, the insulin receptor, and glucose uptake in 3T3-L1 adipocytes
    • Moini, H. et al. R-alpha-lipoic acid action on cell redox status, the insulin receptor, and glucose uptake in 3T3-L1 adipocytes, Arch. Biochem. Biophys. 397, 384, 2002.
    • (2002) Arch. Biochem. Biophys , vol.397 , pp. 384
    • Moini, H.1
  • 6
    • 8644274038 scopus 로고    scopus 로고
    • R-lipoic acid inhibits mammalian pyruvate dehydrogenase kinase
    • Korotchkina, L.G., Sidhu, S., and Patel, M.S. R-lipoic acid inhibits mammalian pyruvate dehydrogenase kinase, Free Radic Res. 38, 1083, 2004.
    • (2004) Free Radic Res , vol.38 , pp. 1083
    • Korotchkina, L.G.1    Sidhu, S.2    Patel, M.S.3
  • 7
    • 0035341962 scopus 로고    scopus 로고
    • Protection by thiols of the mitochondrial complexes from 4-hydroxy-2-nonenal
    • Korotchkina, L.G. et al. Protection by thiols of the mitochondrial complexes from 4-hydroxy-2-nonenal, Free Radic. Biol. Med. 30, 992, 2001.
    • (2001) Free Radic. Biol. Med , vol.30 , pp. 992
    • Korotchkina, L.G.1
  • 8
    • 0842284605 scopus 로고    scopus 로고
    • Effect of R(+)alpha-lipoic acid on pyruvate metabolism and fatty acid oxidation in rat hepatocytes
    • Walgren, J.L. et al. Effect of R(+)alpha-lipoic acid on pyruvate metabolism and fatty acid oxidation in rat hepatocytes, Metabolism: Clin. & Exper. 53, 16, 2004.
    • (2004) Metabolism: Clin. & Exper , vol.53 , pp. 16
    • Walgren, J.L.1
  • 9
    • 0034773628 scopus 로고    scopus 로고
    • Molecular aspects of lipoic acid in the prevention of diabetes complications
    • Packer, L., Kraemer, K., and Rimbach, G. Molecular aspects of lipoic acid in the prevention of diabetes complications, Nutrition 17, 888, 2001.
    • (2001) Nutrition , vol.17 , pp. 888
    • Packer, L.1    Kraemer, K.2    Rimbach, G.3
  • 10
    • 4143097091 scopus 로고    scopus 로고
    • The biochemistry of the pyruvate dehydrogenase complex
    • Patel, M.S. and Korotchkina, L.G. The biochemistry of the pyruvate dehydrogenase complex, Biochem. Mol. Biol. Educ. 31, 5, 2003.
    • (2003) Biochem. Mol. Biol. Educ , vol.31 , pp. 5
    • Patel, M.S.1    Korotchkina, L.G.2
  • 11
    • 0032054899 scopus 로고    scopus 로고
    • Alpha-lipoic acid in liver metabolism and disease
    • Bustamante, J. et al. Alpha-lipoic acid in liver metabolism and disease, Free Radic. Biol. Med. 24, 1023, 1998.
    • (1998) Free Radic. Biol. Med , vol.24 , pp. 1023
    • Bustamante, J.1
  • 12
    • 1342325393 scopus 로고    scopus 로고
    • Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and their capacities to bind the E1 and E3 components
    • Hiromasa, Y. et al. Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and their capacities to bind the E1 and E3 components, J. Biol. Chem. 279, 6921, 2004.
    • (2004) J. Biol. Chem , vol.279 , pp. 6921
    • Hiromasa, Y.1
  • 13
    • 0030877451 scopus 로고    scopus 로고
    • Dihydrolipoamide dehydrogenase-binding protein of the human pyruvate dehydrogenase complex. DNA-derived amino acid sequence, expression, and reconstitution of the pyruvate dehydrogenase complex
    • Harris, R.A. et al. Dihydrolipoamide dehydrogenase-binding protein of the human pyruvate dehydrogenase complex. DNA-derived amino acid sequence, expression, and reconstitution of the pyruvate dehydrogenase complex, J. Biol. Chem. 272, 19746, 1997.
    • (1997) J. Biol. Chem , vol.272 , pp. 19746
    • Harris, R.A.1
  • 14
    • 0035224979 scopus 로고    scopus 로고
    • Distinct regulatory properties of pyruvate dehydrogenase kinase and phosphatase isoforms
    • Roche, T.E. et al. Distinct regulatory properties of pyruvate dehydrogenase kinase and phosphatase isoforms, Progr. Nucl. Acid Res. Molec. Biol. 70, 33, 2001.
    • (2001) Progr. Nucl. Acid Res. Molec. Biol , vol.70 , pp. 33
    • Roche, T.E.1
  • 15
    • 0038418364 scopus 로고    scopus 로고
    • Structural basis for flip-flop action of thiamin pyrophosphatedependent enzymes revealed by human pyruvate dehydrogenase
    • Ciszak, E.M. et al. Structural basis for flip-flop action of thiamin pyrophosphatedependent enzymes revealed by human pyruvate dehydrogenase, J. Biol. Chem. 278, 21240, 2003.
    • (2003) J. Biol. Chem , vol.278 , pp. 21240
    • Ciszak, E.M.1
  • 16
    • 0031781602 scopus 로고    scopus 로고
    • Three-dimensional structure of the major autoantigen in primary biliary cirrhosis
    • Howard, M.J. et al. Three-dimensional structure of the major autoantigen in primary biliary cirrhosis, Gastroenterology 115, 139, 1998.
    • (1998) Gastroenterology , vol.115 , pp. 139
    • Howard, M.J.1
  • 17
    • 20444475852 scopus 로고    scopus 로고
    • Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations
    • Brautigam, C.A. et al. Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations, J. Mol. Biol. 350, 543, 2005.
    • (2005) J. Mol. Biol , vol.350 , pp. 543
    • Brautigam, C.A.1
  • 18
    • 33644869456 scopus 로고    scopus 로고
    • How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in human pyruvate dehydrogenase complex, J
    • Ciszak, E.M. et al. How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in human pyruvate dehydrogenase complex, J. Biol. Chem. 281, 648, 2006.
    • (2006) Biol. Chem , vol.281 , pp. 648
    • Ciszak, E.M.1
  • 19
    • 0035813145 scopus 로고    scopus 로고
    • Structure of pyruvate dehydrogenase kinase. Novel folding pattern for a serine protein kinase
    • Steussy, C.N. et al. Structure of pyruvate dehydrogenase kinase. Novel folding pattern for a serine protein kinase, J. Biol. Chem. 276, 37443, 2001.
    • (2001) J. Biol. Chem , vol.276 , pp. 37443
    • Steussy, C.N.1
  • 20
    • 30744469862 scopus 로고    scopus 로고
    • Regulatory roles of the N-terminal domain based on crystal structures of human pyruvate dehydrogenase kinase 2 containing physiological and synthetic ligands
    • Knoechel, T.R. et al. Regulatory roles of the N-terminal domain based on crystal structures of human pyruvate dehydrogenase kinase 2 containing physiological and synthetic ligands, Biochemistry 45, 402, 2006.
    • (2006) Biochemistry , vol.45 , pp. 402
    • Knoechel, T.R.1
  • 21
    • 20044390617 scopus 로고    scopus 로고
    • Crystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complex
    • Kato, M. et al. Crystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complex, EMBO J. 24, 1763, 2005.
    • (2005) EMBO J , vol.24 , pp. 1763
    • Kato, M.1
  • 22
    • 0026510711 scopus 로고
    • Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex
    • Mattevi, A. et al. Atomic structure of the cubic core of the pyruvate dehydrogenase multienzyme complex, Science 255, 1544, 1992.
    • (1992) Science , vol.255 , pp. 1544
    • Mattevi, A.1
  • 23
    • 0033573917 scopus 로고    scopus 로고
    • Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes
    • Izard, T. et al. Principles of quasi-equivalence and Euclidean geometry govern the assembly of cubic and dodecahedral cores of pyruvate dehydrogenase complexes, Proc. Natl. Acad. Sci. U.S. A. 96, 1240, 1999.
    • (1999) Proc. Natl. Acad. Sci. U.S. A , vol.96 , pp. 1240
    • Izard, T.1
  • 24
    • 0035909958 scopus 로고    scopus 로고
    • The remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexes
    • Zhou, Z.H. et al. The remarkable structural and functional organization of the eukaryotic pyruvate dehydrogenase complexes, Proc. Natl. Acad. Sci. U.S.A. 98, 14802, 2001.
    • (2001) Proc. Natl. Acad. Sci. U.S.A , vol.98 , pp. 14802
    • Zhou, Z.H.1
  • 25
    • 33750731272 scopus 로고    scopus 로고
    • Acetylphosphinate is the most potent mechanism-based substrate inhibitor of both the human and E. coli pyruvate dehydrogenase components of the pyruvate dehydrogenase complex
    • Nemeria, N.S. et al. Acetylphosphinate is the most potent mechanism-based substrate inhibitor of both the human and E. coli pyruvate dehydrogenase components of the pyruvate dehydrogenase complex, Bioorg. Chem. 34, 362, 2006.
    • (2006) Bioorg. Chem , vol.34 , pp. 362
    • Nemeria, N.S.1
  • 26
    • 33750370889 scopus 로고    scopus 로고
    • Direct kinetic evidence for half-of-the-sites reactivity in the E1 component of the human pyruvate dehydrogenase multienzyme complex through alternating sites cofactor activation
    • Seifert, F. et al. Direct kinetic evidence for half-of-the-sites reactivity in the E1 component of the human pyruvate dehydrogenase multienzyme complex through alternating sites cofactor activation, Biochemistry 45, 12775, 2006.
    • (2006) Biochemistry , vol.45 , pp. 12775
    • Seifert, F.1
  • 27
    • 33846041174 scopus 로고    scopus 로고
    • The 1',4'-iminopyrimidine tautomer of thiamin diphosphate is poised for catalysis in asymmetric active centers on enzymes
    • Nemeria, N. et al. The 1',4'-iminopyrimidine tautomer of thiamin diphosphate is poised for catalysis in asymmetric active centers on enzymes, Proc. Natl. Acad. Sci. U.S.A. 104, 78, 2007.
    • (2007) Proc. Natl. Acad. Sci. U.S.A , vol.104 , pp. 78
    • Nemeria, N.1
  • 28
    • 0017808017 scopus 로고
    • Regulation of pig heart pyruvate dehydrogenase by phosphorylation. Studies on the subunit and phosphorylation stoichiometries
    • Sugden, P.H. and Randle, P.J. Regulation of pig heart pyruvate dehydrogenase by phosphorylation. Studies on the subunit and phosphorylation stoichiometries, Biochem. J. 173, 659, 1978.
    • (1978) Biochem. J , vol.173 , pp. 659
    • Sugden, P.H.1    Randle, P.J.2
  • 29
    • 0029062935 scopus 로고
    • Mutagenesis studies of the phosphorylation sites of recombinant human pyruvate dehydrogenase. Site-specific regulation
    • Korotchkina, L.G. and Patel, M.S. Mutagenesis studies of the phosphorylation sites of recombinant human pyruvate dehydrogenase. Site-specific regulation, J. Biol. Chem. 270, 14297, 1995.
    • (1995) J. Biol. Chem , vol.270 , pp. 14297
    • Korotchkina, L.G.1    Patel, M.S.2
  • 30
    • 33645958257 scopus 로고    scopus 로고
    • Regulation of the pyruvate dehydrogenase complex
    • Patel, M.S. and Korotchkina, L.G. Regulation of the pyruvate dehydrogenase complex, Biochem. Soc. Trans. 34, 217, 2006.
    • (2006) Biochem. Soc. Trans , vol.34 , pp. 217
    • Patel, M.S.1    Korotchkina, L.G.2
  • 31
    • 0018096874 scopus 로고
    • Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heart
    • Yeaman, S.J. et al. Sites of phosphorylation on pyruvate dehydrogenase from bovine kidney and heart, Biochemistry 17, 2364, 1978.
    • (1978) Biochemistry , vol.17 , pp. 2364
    • Yeaman, S.J.1
  • 32
    • 0023245015 scopus 로고
    • The human pyruvate dehydrogenase complex. Isolation of cDNA clones for the E1 alpha subunit, sequence analysis, and characterization of the mRNA
    • Dahl, H.H. et al. The human pyruvate dehydrogenase complex. Isolation of cDNA clones for the E1 alpha subunit, sequence analysis, and characterization of the mRNA, J. Biol. Chem., 262, 7398, 1987.
    • (1987) J. Biol. Chem , vol.262 , pp. 7398
    • Dahl, H.H.1
  • 33
    • 0035937145 scopus 로고    scopus 로고
    • Probing the mechanism of inactivation of human pyruvate dehydrogenase by phosphorylation of three sites
    • Korotchkina, L.G. and Patel, M.S. Probing the mechanism of inactivation of human pyruvate dehydrogenase by phosphorylation of three sites, J. Biol. Chem. 276, 5731, 2001.
    • (2001) J. Biol. Chem , vol.276 , pp. 5731
    • Korotchkina, L.G.1    Patel, M.S.2
  • 34
    • 0031972736 scopus 로고    scopus 로고
    • Evidence for existence of tissue-specific regulation of the mammalian pyruvate dehydrogenase complex
    • Bowker-Kinley, M.M. et al. Evidence for existence of tissue-specific regulation of the mammalian pyruvate dehydrogenase complex, Biochem. J. 329, 191, 1998.
    • (1998) Biochem. J , vol.329 , pp. 191
    • Bowker-Kinley, M.M.1
  • 35
    • 9544245935 scopus 로고    scopus 로고
    • Cloning and characterization of PDK4 on 7q21.3 encoding a fourth pyruvate dehydrogenase kinase isoenzyme in human
    • Rowles, J. et al. Cloning and characterization of PDK4 on 7q21.3 encoding a fourth pyruvate dehydrogenase kinase isoenzyme in human, J. Biol. Chem. 271, 22376, 1996.
    • (1996) J. Biol. Chem , vol.271 , pp. 22376
    • Rowles, J.1
  • 36
    • 0035813150 scopus 로고    scopus 로고
    • Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase
    • Korotchkina, L.G. and Patel, M.S. Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase, J. Biol. Chem. 276, 37223, 2001.
    • (2001) J. Biol. Chem , vol.276 , pp. 37223
    • Korotchkina, L.G.1    Patel, M.S.2
  • 37
    • 0035882093 scopus 로고    scopus 로고
    • Regulation of pyruvate dehydrogenase activity through phosphorylation at multiple sites
    • Kolobova, E. et al. Regulation of pyruvate dehydrogenase activity through phosphorylation at multiple sites, Biochem. J. 358, 69, 2001.
    • (2001) Biochem. J , vol.358 , pp. 69
    • Kolobova, E.1
  • 38
    • 0032504147 scopus 로고    scopus 로고
    • Isoenzymes of pyruvate dehydrogenase phosphatase. DNA-derived amino acid sequences, expression and regulation
    • Huang, B. et al. Isoenzymes of pyruvate dehydrogenase phosphatase. DNA-derived amino acid sequences, expression and regulation, J. Biol. Chem. 273, 17680, 1998.
    • (1998) J. Biol. Chem , vol.273 , pp. 17680
    • Huang, B.1
  • 39
    • 0037983739 scopus 로고    scopus 로고
    • Starvation and diabetes reduce the amount of pyruvate dehydrogenase phosphatase in rat heart and kidney
    • Huang, B. et al. Starvation and diabetes reduce the amount of pyruvate dehydrogenase phosphatase in rat heart and kidney, Diabetes 52, 1371, 2003.
    • (2003) Diabetes , vol.52 , pp. 1371
    • Huang, B.1
  • 40
    • 1242351259 scopus 로고    scopus 로고
    • Characterization of the isozymes of pyruvate dehydrogenase phosphatase: Implications for the regulation of pyruvate dehydrogenase activity
    • Karpova, T. et al. Characterization of the isozymes of pyruvate dehydrogenase phosphatase: Implications for the regulation of pyruvate dehydrogenase activity, Biochim. Biophys. Acta 1652, 126, 2003.
    • (2003) Biochim. Biophys. Acta , vol.1652 , pp. 126
    • Karpova, T.1
  • 41
    • 0034993356 scopus 로고    scopus 로고
    • Control of pyruvate dehydrogenase kinase gene expression
    • Harris, R.A., Huang, B., and Wu, P. Control of pyruvate dehydrogenase kinase gene expression, Adv. Enzyme Regul. 41, 269, 2001.
    • (2001) Adv. Enzyme Regul , vol.41 , pp. 269
    • Harris, R.A.1    Huang, B.2    Wu, P.3
  • 42
    • 0031973056 scopus 로고    scopus 로고
    • Starvation and diabetes increase the amount of pyruvate dehydrogenase kinase isoenzyme 4 in rat heart
    • Wu, P. et al. Starvation and diabetes increase the amount of pyruvate dehydrogenase kinase isoenzyme 4 in rat heart, Biochem. J. 329, 197, 1998.
    • (1998) Biochem. J , vol.329 , pp. 197
    • Wu, P.1
  • 43
    • 0034282947 scopus 로고    scopus 로고
    • Starvation increases the amount of pyruvate dehydrogenase kinase in several mammalian tissues
    • Wu, P. et al. Starvation increases the amount of pyruvate dehydrogenase kinase in several mammalian tissues, Arch. Biochem. Biophys. 381, 1, 2000.
    • (2000) Arch. Biochem. Biophys , vol.381 , pp. 1
    • Wu, P.1
  • 44
    • 0036634105 scopus 로고    scopus 로고
    • Therapeutic potential of the mammalian pyruvate dehydrogenase kinases in the prevention of hyperglycaemia
    • Sugden, M.C. and Holness, M.J. Therapeutic potential of the mammalian pyruvate dehydrogenase kinases in the prevention of hyperglycaemia, Curr. Drug Targets- Imm. Endocr. Met. Dis. 2, 151, 2002.
    • (2002) Curr. Drug Targets- Imm. Endocr. Met. Dis , vol.2 , pp. 151
    • Sugden, M.C.1    Holness, M.J.2
  • 45
    • 4143146340 scopus 로고    scopus 로고
    • Downregulation of the skeletal muscle pyruvate dehydrogenase complex in the Otsuka Long-Evans Tokushima fatty rat both before and after the onset of diabetes mellitus
    • Bajotto, G. et al. Downregulation of the skeletal muscle pyruvate dehydrogenase complex in the Otsuka Long-Evans Tokushima fatty rat both before and after the onset of diabetes mellitus, Life Sci. 75, 2117, 2004.
    • (2004) Life Sci , vol.75 , pp. 2117
    • Bajotto, G.1
  • 46
    • 9644274305 scopus 로고    scopus 로고
    • Mechanisms responsible for regulation of pyruvate dehydrogenase kinase 4 gene expression
    • Kwon, H.S. and Harris, R.A. Mechanisms responsible for regulation of pyruvate dehydrogenase kinase 4 gene expression, Adv. Enzyme Regul. 44, 109, 2004.
    • (2004) Adv. Enzyme Regul , vol.44 , pp. 109
    • Kwon, H.S.1    Harris, R.A.2
  • 47
    • 0035976925 scopus 로고    scopus 로고
    • Activation and mitochondrial translocation of protein kinase CS are necessary for insulin stimulation of pyruvate dehydrogenase complex activity in muscle and liver cells
    • Caruso, M. et al. Activation and mitochondrial translocation of protein kinase CS are necessary for insulin stimulation of pyruvate dehydrogenase complex activity in muscle and liver cells, J. Biol. Chem. 276, 45088, 2001.
    • (2001) J. Biol. Chem , vol.276 , pp. 45088
    • Caruso, M.1
  • 48
    • 0037440203 scopus 로고    scopus 로고
    • Insulin stimulation of pyruvate dehydrogenase in adipocytes involves two distinct signalling pathways
    • Johnson, S.A. and Denton, R.M. Insulin stimulation of pyruvate dehydrogenase in adipocytes involves two distinct signalling pathways, Biochem. J. 369, 351, 2003.
    • (2003) Biochem. J , vol.369 , pp. 351
    • Johnson, S.A.1    Denton, R.M.2
  • 49
    • 0037103751 scopus 로고    scopus 로고
    • Interaction between the individual isoenzymes of pyruvate dehydrogenase kinase and the inner lipoyl-bearing domain of transacetylase component of pyruvate dehydrogenase complex
    • Tuganova, A., Boulatnikov, I., and Popov, K.M. Interaction between the individual isoenzymes of pyruvate dehydrogenase kinase and the inner lipoyl-bearing domain of transacetylase component of pyruvate dehydrogenase complex, Biochem. J. 366, 129, 2002.
    • (2002) Biochem. J , vol.366 , pp. 129
    • Tuganova, A.1    Boulatnikov, I.2    Popov, K.M.3
  • 50
    • 0037351228 scopus 로고    scopus 로고
    • Essential roles of lipoyl domains in the activated function and control of pyruvate dehydrogenase kinases and phosphatase isoform 1
    • Roche, T.E. et al. Essential roles of lipoyl domains in the activated function and control of pyruvate dehydrogenase kinases and phosphatase isoform 1, Eur. J. Biochem. 270, 1050, 2003.
    • (2003) Eur. J. Biochem , vol.270 , pp. 1050
    • Roche, T.E.1
  • 51
    • 17144395149 scopus 로고    scopus 로고
    • Role of protein-protein interactions in the regulation of pyruvate dehydrogenase kinase activity
    • Tuganova, A. and Popov, K.M. Role of protein-protein interactions in the regulation of pyruvate dehydrogenase kinase activity, Biochem. J. 387, 147, 2005.
    • (2005) Biochem. J , vol.387 , pp. 147
    • Tuganova, A.1    Popov, K.M.2
  • 52
    • 0034717278 scopus 로고    scopus 로고
    • Marked differences between two isoforms of human pyruvate dehydrogenase kinase
    • Baker, J.C. et al. Marked differences between two isoforms of human pyruvate dehydrogenase kinase, J. Biol. Chem. 275, 15773, 2000.
    • (2000) J. Biol. Chem , vol.275 , pp. 15773
    • Baker, J.C.1
  • 53
    • 0141483394 scopus 로고    scopus 로고
    • Facilitated interaction between the pyruvate dehydrogenase kinase isoform 2 and the dihydrolipoyl acetyltransferase
    • Hiromasa, Y. and Roche, T.E. Facilitated interaction between the pyruvate dehydrogenase kinase isoform 2 and the dihydrolipoyl acetyltransferase, J. Biol. Chem. 278, 33681, 2003.
    • (2003) J. Biol. Chem , vol.278 , pp. 33681
    • Hiromasa, Y.1    Roche, T.E.2
  • 54
    • 6344226530 scopus 로고    scopus 로고
    • Pyruvate dehydrogenase kinase isoform 2 activity stimulated by speeding up the rate of dissociation of ADP
    • Bao, H. et al. Pyruvate dehydrogenase kinase isoform 2 activity stimulated by speeding up the rate of dissociation of ADP, Biochemistry 43, 13442, 2004.
    • (2004) Biochemistry , vol.43 , pp. 13442
    • Bao, H.1
  • 55
    • 33744956372 scopus 로고    scopus 로고
    • Ligand-induced effects on pyruvate dehydrogenase kinase isoform 2
    • Hiromasa, Y., Hu, L., and Roche, T.E. Ligand-induced effects on pyruvate dehydrogenase kinase isoform 2, J. Biol. Chem. 281, 12568, 2006.
    • (2006) J. Biol. Chem , vol.281 , pp. 12568
    • Hiromasa, Y.1    Hu, L.2    Roche, T.E.3
  • 56
    • 9744285671 scopus 로고    scopus 로고
    • Formation of a complex of the catalytic subunit of pyruvate dehydrogenase phosphatase isoform 1 (PDP1c) and the L2 domain forms a Ca2th binding site and captures PDP1c as a monomer
    • Turkan, A., Hiromasa, Y., and Roche, T.E. Formation of a complex of the catalytic subunit of pyruvate dehydrogenase phosphatase isoform 1 (PDP1c) and the L2 domain forms a Ca2th binding site and captures PDP1c as a monomer, Biochemistry 43, 15073, 2004.
    • (2004) Biochemistry , vol.43 , pp. 15073
    • Turkan, A.1    Hiromasa, Y.2    Roche, T.E.3
  • 57
    • 0041976916 scopus 로고    scopus 로고
    • Alpha-lipoic acid decreases thiol reactivity of the insulin receptor and protein tyrosine phosphatase 1B in 3T3-L1 adipocytes
    • Cho, K.J. et al. Alpha-lipoic acid decreases thiol reactivity of the insulin receptor and protein tyrosine phosphatase 1B in 3T3-L1 adipocytes, Biochem. Pharmacol. 66, 849, 2003.
    • (2003) Biochem. Pharmacol , vol.66 , pp. 849
    • Cho, K.J.1
  • 58
    • 33847631240 scopus 로고    scopus 로고
    • A-Lipoic acid as a directly binding activator of the insulin receptor: Protection from hepatocyte apoptosis
    • Diesel, B. et al. a-Lipoic acid as a directly binding activator of the insulin receptor: Protection from hepatocyte apoptosis, Biochemistry 46, 2146, 2007.
    • (2007) Biochemistry , vol.46 , pp. 2146
    • Diesel, B.1
  • 59
    • 0028897754 scopus 로고
    • Alpha-lipoic acid prevents buthionine sulfoximine-induced cataract formation in newborn rats
    • Maitra, I. et al. Alpha-lipoic acid prevents buthionine sulfoximine-induced cataract formation in newborn rats, Free Radic. Biol. Med. 18, 823, 1995.
    • (1995) Free Radic. Biol. Med , vol.18 , pp. 823
    • Maitra, I.1
  • 60
    • 0032902482 scopus 로고    scopus 로고
    • Alpha-lipoic acid reduces expression of vascular cell adhesion molecule-1 and endothelial adhesion of human monocytes after stimulation with advanced glycation end products
    • Kunt, T. et al. Alpha-lipoic acid reduces expression of vascular cell adhesion molecule-1 and endothelial adhesion of human monocytes after stimulation with advanced glycation end products, Clin. Sci. (Lond.) 96, 75, 1999.
    • (1999) Clin. Sci. (Lond.) , vol.96 , pp. 75
    • Kunt, T.1
  • 61
    • 0034107946 scopus 로고    scopus 로고
    • Effects of alpha-lipoic acid on microcirculation in patients with peripheral diabetic neuropathy
    • Haak, E. et al. Effects of alpha-lipoic acid on microcirculation in patients with peripheral diabetic neuropathy, Exp. Clin. Endocrinol. Diabetes 108, 168, 2000.
    • (2000) Exp. Clin. Endocrinol. Diabetes , vol.108 , pp. 168
    • Haak, E.1
  • 62
    • 33646382095 scopus 로고    scopus 로고
    • Free radical-mediated neurotoxicity may be caused by inhibition of mitochondrial dehydrogenases in vitro and in vivo
    • Sheline, C.T. and Wei, L. Free radical-mediated neurotoxicity may be caused by inhibition of mitochondrial dehydrogenases in vitro and in vivo, Neuroscience 140, 235, 2006.
    • (2006) Neuroscience , vol.140 , pp. 235
    • Sheline, C.T.1    Wei, L.2
  • 63
    • 0030589626 scopus 로고    scopus 로고
    • Reactive oxygen species-mediated inactivation of pyruvate dehydrogenase
    • Tabatabaie, T., Potts, J.D., and Floyd, R.A. Reactive oxygen species-mediated inactivation of pyruvate dehydrogenase, Arch. Biochem. Biophys. 336, 290, 1996.
    • (1996) Arch. Biochem. Biophys , vol.336 , pp. 290
    • Tabatabaie, T.1    Potts, J.D.2    Floyd, R.A.3
  • 64
    • 0032972698 scopus 로고    scopus 로고
    • The inhibitory effects of lipoic compounds on mammalian pyruvate dehydrogenase complex and its catalytic components
    • Hong, Y.S. et al. The inhibitory effects of lipoic compounds on mammalian pyruvate dehydrogenase complex and its catalytic components, Free Radic. Biol. Med. 26, 685, 1999.
    • (1999) Free Radic. Biol. Med , vol.26 , pp. 685
    • Hong, Y.S.1
  • 65
    • 0032512411 scopus 로고    scopus 로고
    • Inhibition of NADH-linked mitochondrial respiration by 4-hydroxy-2-nonenal
    • Humphries, K.M., Yoo, Y., and Szweda, L.I. Inhibition of NADH-linked mitochondrial respiration by 4-hydroxy-2-nonenal, Biochemistry 37, 552, 1998.
    • (1998) Biochemistry , vol.37 , pp. 552
    • Humphries, K.M.1    Yoo, Y.2    Szweda, L.I.3
  • 66
    • 0022339431 scopus 로고
    • Lipoic acid and diabetes II: Mode of action of lipoic acid
    • Gandhi, V.M. et al. Lipoic acid and diabetes II: Mode of action of lipoic acid, J. Biosci. 9, 117, 1985.
    • (1985) J. Biosci , vol.9 , pp. 117
    • Gandhi, V.M.1
  • 67
    • 6344294845 scopus 로고    scopus 로고
    • Pyruvate dehydrogenase kinase isoform 2 activity limited and further inhibited by slowing down the rate of dissociation of ADP
    • Bao, H. et al. Pyruvate dehydrogenase kinase isoform 2 activity limited and further inhibited by slowing down the rate of dissociation of ADP, Biochemistry 43, 13432, 2004.
    • (2004) Biochemistry , vol.43 , pp. 13432
    • Bao, H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.