메뉴 건너뛰기




Volumn 54, Issue 1, 2015, Pages 69-82

Elucidation of the interaction loci of the human pyruvate dehydrogenase complex e2·E3BP core with pyruvate dehydrogenase kinase 1 and kinase 2 by h/d exchange mass spectrometry and nuclear magnetic resonance

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ENZYMES; MASS SPECTROMETRY; PROTEINS; SPECTROMETRY;

EID: 84921270898     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi5013113     Document Type: Article
Times cited : (16)

References (81)
  • 1
    • 0035914303 scopus 로고    scopus 로고
    • A trial of research from lipoic acid to α-keto acid dehydrogenase complexes
    • Reed, L. J. (2001) A trial of research from lipoic acid to α-keto acid dehydrogenase complexes J. Biol. Chem. 276, 38329-38336
    • (2001) J. Biol. Chem. , vol.276 , pp. 38329-38336
    • Reed, L.J.1
  • 2
    • 0026079562 scopus 로고
    • Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: A paradigm in the design of a multifunctional protein
    • Perham, R. N. (1991) Domains, motifs, and linkers in 2-oxo acid dehydrogenase multienzyme complexes: A paradigm in the design of a multifunctional protein Biochemistry 30, 8501-8512
    • (1991) Biochemistry , vol.30 , pp. 8501-8512
    • Perham, R.N.1
  • 3
    • 0025221771 scopus 로고
    • Molecular biology and biochemistry of pyruvate dehydrogenase complexes
    • Patel, M. S. and Roche, T. E. (1990) Molecular biology and biochemistry of pyruvate dehydrogenase complexes FASEB J. 14, 3224-3233
    • (1990) FASEB J. , vol.14 , pp. 3224-3233
    • Patel, M.S.1    Roche, T.E.2
  • 5
    • 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 capacities to bind E1 and E3 components
    • Hiromasa, Y., Fujisawa, T., Aso, Y., and Roche, T. E. (2004) Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and capacities to bind E1 and E3 components J. Biol. Chem. 279, 6921-6933
    • (2004) J. Biol. Chem. , vol.279 , pp. 6921-6933
    • Hiromasa, Y.1    Fujisawa, T.2    Aso, Y.3    Roche, T.E.4
  • 6
    • 34247131735 scopus 로고    scopus 로고
    • Pyruvate dehydrogenase kinase regulatory mechanisms and inhibition in treating diabetes, heart ischemia, and cancer
    • Roche, T. E. and Hiromasa, Y. (2007) Pyruvate dehydrogenase kinase regulatory mechanisms and inhibition in treating diabetes, heart ischemia, and cancer Cell. Mol. Life Sci. 64, 830-849
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 830-849
    • Roche, T.E.1    Hiromasa, Y.2
  • 7
  • 8
    • 39749140372 scopus 로고    scopus 로고
    • Specific ion influence on self-association of pyruvate dehydrogenase kinase isoform 2 (PDHK2), binding of PDHK2 to the L2 lipoyl domain, and effects of the lipoyl group-binding site inhibitor, Nov3r
    • Hiromasa, Y., Yan, X., and Roche, T. (2008) Specific ion influence on self-association of pyruvate dehydrogenase kinase isoform 2 (PDHK2), binding of PDHK2 to the L2 lipoyl domain, and effects of the lipoyl group-binding site inhibitor, Nov3r Biochemistry 47, 2312-2324
    • (2008) Biochemistry , vol.47 , pp. 2312-2324
    • Hiromasa, Y.1    Yan, X.2    Roche, T.3
  • 9
    • 0036377351 scopus 로고    scopus 로고
    • Regulation of the activity of the pyruvate dehydrogenase complex
    • Harris, R. A., Bowker-Kenley, M. M., Huang, B., and Wu, P. (2002) Regulation of the activity of the pyruvate dehydrogenase complex Adv. Enzyme Regul. 42, 249-259
    • (2002) Adv. Enzyme Regul. , vol.42 , pp. 249-259
    • Harris, R.A.1    Bowker-Kenley, M.M.2    Huang, B.3    Wu, P.4
  • 10
    • 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., Hiromasa, Y., Turkan, A., Gong, X., Peng, T., Yan, X., Kasten, S. A., Bao, H., and Dong, J. (2003) Essential roles of lipoyl domains in the activated function and control of pyruvate dehydrogenase kinases and phosphatase isoform 1 Eur. J. Biochem. 270, 1050-1056
    • (2003) Eur. J. Biochem. , vol.270 , pp. 1050-1056
    • Roche, T.E.1    Hiromasa, Y.2    Turkan, A.3    Gong, X.4    Peng, T.5    Yan, X.6    Kasten, S.A.7    Bao, H.8    Dong, J.9
  • 11
    • 0032504147 scopus 로고    scopus 로고
    • Isoenzymes of pyruvate dehydrogenase phosphatase: DNA-derived amino acid sequences, expression, and regulation
    • Huang, B., Gudi, R., Wu, P., Harris, R. A., Hamilton, J., and Popov, K. M. (1998) Isoenzymes of pyruvate dehydrogenase phosphatase: DNA-derived amino acid sequences, expression, and regulation J. Biol. Chem. 273, 17680-17688
    • (1998) J. Biol. Chem. , vol.273 , pp. 17680-17688
    • Huang, B.1    Gudi, R.2    Wu, P.3    Harris, R.A.4    Hamilton, J.5    Popov, K.M.6
  • 12
    • 67649718388 scopus 로고    scopus 로고
    • Subunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complex
    • Brautigam, C. A., Wynn, R. M., Chuang, J. L., and Chuang, D. T. (2009) Subunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complex J. Biol. Chem. 284, 13086-13098
    • (2009) J. Biol. Chem. , vol.284 , pp. 13086-13098
    • Brautigam, C.A.1    Wynn, R.M.2    Chuang, J.L.3    Chuang, D.T.4
  • 13
    • 0038418364 scopus 로고    scopus 로고
    • Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase
    • Ciszak, E. M., Korotchkina, L. G., Dominiak, P. M., Sidhu, S., and Patel, M. S. (2003) Structural basis for flip-flop action of thiamin pyrophosphate-dependent enzymes revealed by human pyruvate dehydrogenase J. Biol. Chem. 278, 21240-21246
    • (2003) J. Biol. Chem. , vol.278 , pp. 21240-21246
    • Ciszak, E.M.1    Korotchkina, L.G.2    Dominiak, P.M.3    Sidhu, S.4    Patel, M.S.5
  • 15
    • 33644869456 scopus 로고    scopus 로고
    • How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex
    • Ciszak, E. M., Makal, A., Hong, Y. S., Vettaikkorumakankauv, A. K., Korotchkina, L. G., and Patel, M. S. (2006) How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex J. Biol. Chem. 281, 648-655
    • (2006) J. Biol. Chem. , vol.281 , pp. 648-655
    • Ciszak, E.M.1    Makal, A.2    Hong, Y.S.3    Vettaikkorumakankauv, A.K.4    Korotchkina, L.G.5    Patel, M.S.6
  • 16
    • 33644842641 scopus 로고    scopus 로고
    • Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex
    • Brautigam, C. A., Wynn, R. M., Chuang, J. L., Machius, M., Tomchick, D. R., and Chuang, D. T. (2006) Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex Structure 14, 611-621
    • (2006) Structure , vol.14 , pp. 611-621
    • Brautigam, C.A.1    Wynn, R.M.2    Chuang, J.L.3    Machius, M.4    Tomchick, D.R.5    Chuang, D.T.6
  • 17
    • 34249702932 scopus 로고    scopus 로고
    • Phosphorylation of serine 264 impedes active site accessibility in the E1 component of the human pyruvate dehydrogenase multienzyme complex
    • Seifert, F., Ciszak, E., Korotchkina, L., Golbik, R., Spinka, M., Dominiak, P., Sidhu, S., Brauer, J., Patel, M. S., and Tittmann, K. (2007) Phosphorylation of serine 264 impedes active site accessibility in the E1 component of the human pyruvate dehydrogenase multienzyme complex Biochemistry 46, 6277-6287
    • (2007) Biochemistry , vol.46 , pp. 6277-6287
    • Seifert, F.1    Ciszak, E.2    Korotchkina, L.3    Golbik, R.4    Spinka, M.5    Dominiak, P.6    Sidhu, S.7    Brauer, J.8    Patel, M.S.9    Tittmann, K.10
  • 18
    • 57049114930 scopus 로고    scopus 로고
    • Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: Role of disordered phosphorylation loops
    • Kato, M., Wynn, R. M., Chuang, J. L., Tso, S.-C., Machius, M., Li, J., and Chuang, D. T. (2008) Structural basis for inactivation of the human pyruvate dehydrogenase complex by phosphorylation: role of disordered phosphorylation loops Structure 16, 1849-1859
    • (2008) Structure , vol.16 , pp. 1849-1859
    • Kato, M.1    Wynn, R.M.2    Chuang, J.L.3    Tso, S.-C.4    Machius, M.5    Li, J.6    Chuang, D.T.7
  • 19
    • 37549066690 scopus 로고    scopus 로고
    • Structures of the human pyruvate dehydrogenase complex cores: A highly conserved catalytic center with flexible N-terminal domains
    • Yu, X., Hiromasa, Y., Tsen, H., Stoops, J. K., Roche, T. E., and Zhou, Z. H. (2008) Structures of the human pyruvate dehydrogenase complex cores: A highly conserved catalytic center with flexible N-terminal domains Structure 16, 104-114
    • (2008) Structure , vol.16 , pp. 104-114
    • Yu, X.1    Hiromasa, Y.2    Tsen, H.3    Stoops, J.K.4    Roche, T.E.5    Zhou, Z.H.6
  • 21
    • 4143097091 scopus 로고    scopus 로고
    • The biochemistry of the pyruvate dehydrogenase Complex
    • Patel, M. S. and Korotchkina, L. G. (2003) The biochemistry of the pyruvate dehydrogenase Complex Biochem. Mol. Biol. Educ. 31, 5-15
    • (2003) Biochem. Mol. Biol. Educ. , vol.31 , pp. 5-15
    • Patel, M.S.1    Korotchkina, L.G.2
  • 22
    • 33645958257 scopus 로고    scopus 로고
    • Regulation of pyruvate dehydrogenase complex
    • Patel, M. S. and Korotchkina, L. G. (2006) Regulation of pyruvate dehydrogenase complex Biochem. Soc. Trans. 34, 217-222
    • (2006) Biochem. Soc. Trans. , vol.34 , pp. 217-222
    • Patel, M.S.1    Korotchkina, L.G.2
  • 23
    • 0035882093 scopus 로고    scopus 로고
    • Regulation of pyruvate dehydrogenase activity through phosphorylation at multiple sites
    • Kolobova, E., Tuganova, A., Boulatnikov, I., and Popov, K. M. (2001) Regulation of pyruvate dehydrogenase activity through phosphorylation at multiple sites Biochem. J. 358, 69-77
    • (2001) Biochem. J. , vol.358 , pp. 69-77
    • Kolobova, E.1    Tuganova, A.2    Boulatnikov, I.3    Popov, K.M.4
  • 24
    • 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. (2001) Probing the mechanism of inactivation of human pyruvate dehydrogenase by phosphorylation of three sites J. Biol. Chem. 276, 5731-5738
    • (2001) J. Biol. Chem. , vol.276 , pp. 5731-5738
    • Korotchkina, L.G.1    Patel, M.S.2
  • 25
    • 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. (2001) Site specificity of four pyruvate dehydrogenase kinase isoenzymes toward the three phosphorylation sites of human pyruvate dehydrogenase J. Biol. Chem. 276, 37223-37229
    • (2001) J. Biol. Chem. , vol.276 , pp. 37223-37229
    • Korotchkina, L.G.1    Patel, M.S.2
  • 26
    • 0022311019 scopus 로고
    • Regulation of mammalian pyruvate α-keto acid dehydrogenase complexes by phosphorylation-dephosphorylation
    • Reed, L. J., Damuni, Z., and Merryfield, M. L. (1985) Regulation of mammalian pyruvate α-keto acid dehydrogenase complexes by phosphorylation-dephosphorylation Curr. Top. Cell. Regul. 27, 41-49
    • (1985) Curr. Top. Cell. Regul. , vol.27 , pp. 41-49
    • Reed, L.J.1    Damuni, Z.2    Merryfield, M.L.3
  • 27
    • 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, M. M., Popov, K. M., and Harris, R. A. (1999) Mechanism responsible for inactivation of skeletal muscle pyruvate dehydrogenase complex in starvation and diabetes Diabetes 48, 1593-1599
    • (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
  • 28
    • 0034074642 scopus 로고    scopus 로고
    • Targeting upregulation of pyruvate dehydrogenase kinase (PDK)-4 in slow-twitch skeletal muscle underlies the state of modification of the regulatory characteristics of PDK induced by high-fat feeding
    • Holness, M. J., Kraus, A., Harris, R. A., and Sugden, M. C. (2000) Targeting upregulation of pyruvate dehydrogenase kinase (PDK)-4 in slow-twitch skeletal muscle underlies the state of modification of the regulatory characteristics of PDK induced by high-fat feeding Diabetes 49, 775-781
    • (2000) Diabetes , vol.49 , pp. 775-781
    • Holness, M.J.1    Kraus, A.2    Harris, R.A.3    Sugden, M.C.4
  • 29
    • 1842475551 scopus 로고    scopus 로고
    • Protein kinase B-α inhibits human pyruvate dehydrogenase kinase-4 gene induction by dexamethasone through inactivation of FOXO transcription factors
    • Kwon, H. S., Huang, B., Unterman, T. G., and Harris, R. A. (2004) Protein kinase B-α inhibits human pyruvate dehydrogenase kinase-4 gene induction by dexamethasone through inactivation of FOXO transcription factors Diabetes 53, 899-910
    • (2004) Diabetes , vol.53 , pp. 899-910
    • Kwon, H.S.1    Huang, B.2    Unterman, T.G.3    Harris, R.A.4
  • 30
    • 0028979684 scopus 로고
    • Mammalian α-keto acid dehydrogenase complexes gene regulation and genetic defects
    • Patel, M. S. and Harris, R. A. (1995) Mammalian α-keto acid dehydrogenase complexes gene regulation and genetic defects FASEB J. 9, 1164-1172
    • (1995) FASEB J. , vol.9 , pp. 1164-1172
    • Patel, M.S.1    Harris, R.A.2
  • 32
    • 84862528520 scopus 로고    scopus 로고
    • The spectrum of pyruvate dehydrogenase complex deficiency: Clinical, biochemical and genetic features in 371 patients
    • Patel, K. P., OBrien, T. W., Subramony, S. H., Shuster, J., and Stacpoole, P. W. (2012) The spectrum of pyruvate dehydrogenase complex deficiency: Clinical, biochemical and genetic features in 371 patients Mol. Genet. Metab. 106, 385-394
    • (2012) Mol. Genet. Metab. , vol.106 , pp. 385-394
    • Patel, K.P.1    Obrien, T.W.2    Subramony, S.H.3    Shuster, J.4    Stacpoole, P.W.5
  • 33
    • 84896316278 scopus 로고    scopus 로고
    • Regulation of pyruvate metabolism in metabolic-related diseases
    • Jeoung, N. H., Harris, C. R., and Harris, R. A. (2014) Regulation of pyruvate metabolism in metabolic-related diseases Rev. Endocr. Metab. Disord. 15, 99-110
    • (2014) Rev. Endocr. Metab. Disord. , vol.15 , pp. 99-110
    • Jeoung, N.H.1    Harris, C.R.2    Harris, R.A.3
  • 34
    • 66249108601 scopus 로고    scopus 로고
    • Understanding the Warburg effect: The metabolic requirements of cell proliferation
    • Vander Heiden, M. G., Cantley, L. C., and Thompson, C. B. (2009) Understanding the Warburg effect: The metabolic requirements of cell proliferation Science 324, 1029-1033
    • (2009) Science , vol.324 , pp. 1029-1033
    • Vander Heiden, M.G.1    Cantley, L.C.2    Thompson, C.B.3
  • 35
    • 84872198918 scopus 로고    scopus 로고
    • Mitochondrial redox signaling and cancer invasiveness
    • Enns, L. and Ladiges, W. (2012) Mitochondrial redox signaling and cancer invasiveness J. Bioenerg. Biomembr. 44, 635-638
    • (2012) J. Bioenerg. Biomembr. , vol.44 , pp. 635-638
    • Enns, L.1    Ladiges, W.2
  • 37
    • 84255187587 scopus 로고    scopus 로고
    • Flicking the Warburg switch-tyrosine phosphorylation of pyruvate dehydrogenase kinase regulates mitochondrial activity in cancer cells
    • Schulze, A. and Downward, J. (2011) Flicking the Warburg switch-tyrosine phosphorylation of pyruvate dehydrogenase kinase regulates mitochondrial activity in cancer cells Mol. Cell 44, 846-848
    • (2011) Mol. Cell , vol.44 , pp. 846-848
    • Schulze, A.1    Downward, J.2
  • 38
    • 84879391226 scopus 로고    scopus 로고
    • Pyruvate as a pivot point for oncogene-induced senescence
    • Olenchock, B. and Vander Heiden, M. G. (2013) Pyruvate as a pivot point for oncogene-induced senescence Cell 153, 1429-1430
    • (2013) Cell , vol.153 , pp. 1429-1430
    • Olenchock, B.1    Vander Heiden, M.G.2
  • 41
    • 84873665609 scopus 로고    scopus 로고
    • Expression of pyruvate dehydrogenase kinase-1 in gastric cancer as a potential therapeutic target
    • Hur, H., Xuan, Y., Kim, Y. B., Lee, G., Shim, W., Yun, J., Ham, I. H., and Han, S. U. (2013) Expression of pyruvate dehydrogenase kinase-1 in gastric cancer as a potential therapeutic target Int. J. Oncol. 42, 44-54
    • (2013) Int. J. Oncol. , vol.42 , pp. 44-54
    • Hur, H.1    Xuan, Y.2    Kim, Y.B.3    Lee, G.4    Shim, W.5    Yun, J.6    Ham, I.H.7    Han, S.U.8
  • 42
    • 84883271078 scopus 로고    scopus 로고
    • Pyruvate dehydrogenase kinase as a novel therapeutic target in oncology
    • Sutendra, G. and Michelakis, E. D. (2013) Pyruvate dehydrogenase kinase as a novel therapeutic target in oncology Front. Oncol. 3, 38
    • (2013) Front. Oncol. , vol.3 , pp. 38
    • Sutendra, G.1    Michelakis, E.D.2
  • 43
    • 33644622570 scopus 로고    scopus 로고
    • HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption
    • Papandreou, I., Cairns, R. A., Fontana, L., Lim, A. L., and Denko, N. C. (2006) HIF-1 mediates adaptation to hypoxia by actively downregulating mitochondrial oxygen consumption Cell Metab. 3, 187-197
    • (2006) Cell Metab. , vol.3 , pp. 187-197
    • Papandreou, I.1    Cairns, R.A.2    Fontana, L.3    Lim, A.L.4    Denko, N.C.5
  • 44
    • 33644614520 scopus 로고    scopus 로고
    • HIF-1-mediated expression of pyruvate dehydrogenase kinase: A metabolic switch required for cellular adaptation to hypoxia
    • Kim, J. W., Tchernyshyov, I., Semenza, G. L., and Dang, C. V. (2006) HIF-1-mediated expression of pyruvate dehydrogenase kinase: A metabolic switch required for cellular adaptation to hypoxia Cell Metab. 3, 177-185
    • (2006) Cell Metab. , vol.3 , pp. 177-185
    • Kim, J.W.1    Tchernyshyov, I.2    Semenza, G.L.3    Dang, C.V.4
  • 47
    • 57649130593 scopus 로고    scopus 로고
    • Induction of pyruvate dehydrogenase kinase-3 by hypoxia-inducible factor-1 promotes metabolic switch and drug resistance
    • Lu, C. W., Lin, S. C., Chen, K. F., Lai, Y. Y., and Tsai, S. J. (2008) Induction of pyruvate dehydrogenase kinase-3 by hypoxia-inducible factor-1 promotes metabolic switch and drug resistance J. Biol. Chem. 283, 28106-28114
    • (2008) J. Biol. Chem. , vol.283 , pp. 28106-28114
    • Lu, C.W.1    Lin, S.C.2    Chen, K.F.3    Lai, Y.Y.4    Tsai, S.J.5
  • 50
    • 53049103850 scopus 로고    scopus 로고
    • Dichloroacetate (DCA) as a potential metabolic targeting therapy for cancer
    • Michelakis, E. D., Webster, L., and Mackey, J. R. (2008) Dichloroacetate (DCA) as a potential metabolic targeting therapy for cancer Br. J. Cancer 99, 989-994
    • (2008) Br. J. Cancer , vol.99 , pp. 989-994
    • Michelakis, E.D.1    Webster, L.2    Mackey, J.R.3
  • 52
    • 34547683384 scopus 로고    scopus 로고
    • Distinct structural mechanisms for inhibition of pyruvate dehydrogenase kinase isoforms by AZD7545, dichloroacetate, and radicicol
    • Kato, M., Li, J., Chuang, J. L., and Chuang, D. T. (2007) Distinct structural mechanisms for inhibition of pyruvate dehydrogenase kinase isoforms by AZD7545, dichloroacetate, and radicicol Structure 15, 992-1004
    • (2007) Structure , vol.15 , pp. 992-1004
    • Kato, M.1    Li, J.2    Chuang, J.L.3    Chuang, D.T.4
  • 53
    • 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., Tucker, A. D., Robinson, C. M., Phillips, C., Taylor, W., Bungay, P. J., Kasten, S. A., Roche, T. E., and Brown, D. G. (2006) Regulatory roles of the N-terminal domain based on crystal structures of human pyruvate dehydrogenase kinase 2 containing physiological and synthetic ligands Biochemistry 45, 402-415
    • (2006) Biochemistry , vol.45 , pp. 402-415
    • Knoechel, T.R.1    Tucker, A.D.2    Robinson, C.M.3    Phillips, C.4    Taylor, W.5    Bungay, P.J.6    Kasten, S.A.7    Roche, T.E.8    Brown, D.G.9
  • 55
    • 34547124821 scopus 로고    scopus 로고
    • Recognition of the inner lipoyl-bearing domain of dihydrolipoyl transacetylase and of the blood glucose-lowering compound AZD7545 by pyruvate dehydrogenase kinase 2
    • Tuganova, A., Klyuyeva, A., and Popov, K. M. (2007) Recognition of the inner lipoyl-bearing domain of dihydrolipoyl transacetylase and of the blood glucose-lowering compound AZD7545 by pyruvate dehydrogenase kinase 2 Biochemistry 46, 8592-8602
    • (2007) Biochemistry , vol.46 , pp. 8592-8602
    • Tuganova, A.1    Klyuyeva, A.2    Popov, K.M.3
  • 56
    • 0346245917 scopus 로고    scopus 로고
    • AZD7545, a novel inhibitor of pyruvate dehydrogenase kinase 2 (PDK2), activates pyruvate dehydrogenase in vivo and improves blood glucose control in obese (fa/fa) Zucker rats
    • Mayers, R. M., Butlin, R. J., Kligour, E., Leighton, B., Martin, D., Myatt, J., Orme, J. P., and Holloway, B. P. (2003) AZD7545, a novel inhibitor of pyruvate dehydrogenase kinase 2 (PDK2), activates pyruvate dehydrogenase in vivo and improves blood glucose control in obese (fa/fa) Zucker rats Biochem. Soc. Trans. 31 (Part 6) 1165-1167
    • (2003) Biochem. Soc. Trans. , vol.31 , Issue.PART 6 , pp. 1165-1167
    • Mayers, R.M.1    Butlin, R.J.2    Kligour, E.3    Leighton, B.4    Martin, D.5    Myatt, J.6    Orme, J.P.7    Holloway, B.P.8
  • 60
    • 47049091759 scopus 로고    scopus 로고
    • Structural and functional insights into the molecular mechanisms responsible for the regulation of pyruvate dehydrogenase kinase 2
    • Green, T., Grigorian, A., Klyuyeva, A., Tuganova, A., Luo, M., and Popov, K. M. (2008) Structural and functional insights into the molecular mechanisms responsible for the regulation of pyruvate dehydrogenase kinase 2 J. Biol. Chem. 283, 15789-15798
    • (2008) J. Biol. Chem. , vol.283 , pp. 15789-15798
    • Green, T.1    Grigorian, A.2    Klyuyeva, A.3    Tuganova, A.4    Luo, M.5    Popov, K.M.6
  • 61
    • 20044390617 scopus 로고    scopus 로고
    • Crystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complex
    • Kato, M., Chuang, J. L., Tso, S. C., Wynn, R. M., and Chuang, D. T. (2005) Crystal structure of pyruvate dehydrogenase kinase 3 bound to lipoyl domain 2 of human pyruvate dehydrogenase complex EMBO J. 24, 1763-1774
    • (2005) EMBO J. , vol.24 , pp. 1763-1774
    • Kato, M.1    Chuang, J.L.2    Tso, S.C.3    Wynn, R.M.4    Chuang, D.T.5
  • 62
    • 34250202192 scopus 로고    scopus 로고
    • Crystal structure of an asymmetric complex of pyruvate dehydrogenase kinase 3 with lipoyl domain 2 and its biological implications
    • Devedjiev, Y., Steussy, C. N., and Vassylyev, D. G. (2007) Crystal structure of an asymmetric complex of pyruvate dehydrogenase kinase 3 with lipoyl domain 2 and its biological implications J. Mol. Biol. 370, 407-416
    • (2007) J. Mol. Biol. , vol.370 , pp. 407-416
    • Devedjiev, Y.1    Steussy, C.N.2    Vassylyev, D.G.3
  • 63
    • 54449099754 scopus 로고    scopus 로고
    • Pyruvate dehydrogenase kinase-4 structures reveal a metastable open conformation fostering robus core-free basal activity
    • Wynn, R. M., Kato, M., Chuang, J. L., Tso, S. C., Li, J., and Chuang, D. T. (2008) Pyruvate dehydrogenase kinase-4 structures reveal a metastable open conformation fostering robus core-free basal activity J. Biol. Chem. 283, 25305-25315
    • (2008) J. Biol. Chem. , vol.283 , pp. 25305-25315
    • Wynn, R.M.1    Kato, M.2    Chuang, J.L.3    Tso, S.C.4    Li, J.5    Chuang, D.T.6
  • 64
    • 0031972736 scopus 로고    scopus 로고
    • Evidence for existence of tissue-specific regulation of the mammalian pyruvate dehydrogenase complex
    • Bowker-Kinley, M. M., Davis, W. I., Wu, P., Harris, R. A., and Popov, K. M. (1998) Evidence for existence of tissue-specific regulation of the mammalian pyruvate dehydrogenase complex Biochem. J. 329, 191-196
    • (1998) Biochem. J. , vol.329 , pp. 191-196
    • Bowker-Kinley, M.M.1    Davis, W.I.2    Wu, P.3    Harris, R.A.4    Popov, K.M.5
  • 65
    • 0034282947 scopus 로고    scopus 로고
    • Starvation increases the amount of pyruvate dehydrogenase kinase in several mammalian tissues
    • Wu, P., Blair, P. V., Sato, J., Jaskiewicz, J., Popov, K. M., and Harris, R. A. (2000) Starvation increases the amount of pyruvate dehydrogenase kinase in several mammalian tissues Arch. Biochem. Biophys. 381, 1-7
    • (2000) Arch. Biochem. Biophys. , vol.381 , pp. 1-7
    • Wu, P.1    Blair, P.V.2    Sato, J.3    Jaskiewicz, J.4    Popov, K.M.5    Harris, R.A.6
  • 66
    • 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., Tucker, A. D., Robinson, C. M., Phillips, C., Taylor, W., Bungay, P. J., Kasten, S. A., Roche, T. E., and Brown, D. G. (2006) Regulatory Roles of the N-Terminal Domain Based on Crystal Structures of Human Pyruvate Dehydrogenase Kinase 2 Containing Physiological and Synthetic Ligands Biochemistry 45, 402-415
    • (2006) Biochemistry , vol.45 , pp. 402-415
    • Knoechel, T.R.1    Tucker, A.D.2    Robinson, C.M.3    Phillips, C.4    Taylor, W.5    Bungay, P.J.6    Kasten, S.A.7    Roche, T.E.8    Brown, D.G.9
  • 69
    • 84878214190 scopus 로고    scopus 로고
    • Insight to the Interaction of the Dihydrolipoamide Acetyltransferase (E2) Core with the Peripheral Components in the Escherichia coli Pyruvate Dehydrogenase Complex via Multifaceted Structural Approaches
    • Chandrasekhar, K., Wang, J., Arjunan, P., Sax, M., Park, Y.-H., Nemeria, N. S., Kumaran, S., Song, J., Jordan, F., and Furey, W. (2013) Insight to the Interaction of the Dihydrolipoamide Acetyltransferase (E2) Core with the Peripheral Components in the Escherichia coli Pyruvate Dehydrogenase Complex via Multifaceted Structural Approaches J. Biol. Chem. 288, 15402-15417
    • (2013) J. Biol. Chem. , vol.288 , pp. 15402-15417
    • Chandrasekhar, K.1    Wang, J.2    Arjunan, P.3    Sax, M.4    Park, Y.-H.5    Nemeria, N.S.6    Kumaran, S.7    Song, J.8    Jordan, F.9    Furey, W.10
  • 71
    • 33751337111 scopus 로고    scopus 로고
    • Semi-automated data processing of hydrogen exchange mass spectra using HX-Express
    • Weis, D., Engen, J., and Kass, I. (2006) Semi-automated data processing of hydrogen exchange mass spectra using HX-Express J. Am. Soc. Mass Spectrom. 17, 1700-1703
    • (2006) J. Am. Soc. Mass Spectrom. , vol.17 , pp. 1700-1703
    • Weis, D.1    Engen, J.2    Kass, I.3
  • 73
    • 0027250665 scopus 로고
    • Primary structure effects on peptide group hydrogen exchange
    • Bai, Y., Milne, J. S., Mayne, L., and Englander, S. W. (1993) Primary structure effects on peptide group hydrogen exchange Proteins 17, 75-86
    • (1993) Proteins , vol.17 , pp. 75-86
    • Bai, Y.1    Milne, J.S.2    Mayne, L.3    Englander, S.W.4
  • 75
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: A multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 77
  • 78
    • 79954629044 scopus 로고    scopus 로고
    • MSTools: Web based application for visualization and presentation of HXMS data
    • Kavan, D. and Man, P. (2011) MSTools: Web based application for visualization and presentation of HXMS data Int. J. Mass Spectrom. 302, 53-58
    • (2011) Int. J. Mass Spectrom. , vol.302 , pp. 53-58
    • Kavan, D.1    Man, P.2
  • 79
    • 32044468940 scopus 로고    scopus 로고
    • The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics
    • Ferguson, N., Sharpe, T. D., Johnson, C. M., and Fersht, A. R. (2006) The transition state for folding of a peripheral subunit-binding domain contains robust and ionic-strength dependent characteristics J. Mol. Biol. 356, 1237-1247
    • (2006) J. Mol. Biol. , vol.356 , pp. 1237-1247
    • Ferguson, N.1    Sharpe, T.D.2    Johnson, C.M.3    Fersht, A.R.4
  • 81
    • 33846331962 scopus 로고    scopus 로고
    • Distinct modes of recognition of the lipoyl domain as substrate by the E1 and E3 components of the pyruvate dehydrogebase multienzyme complex
    • Fries, M., Stott, K. M., Reynilds, S., and Perham, R. N. (2007) Distinct modes of recognition of the lipoyl domain as substrate by the E1 and E3 components of the pyruvate dehydrogebase multienzyme complex J. Mol. Biol. 366, 132-139
    • (2007) J. Mol. Biol. , vol.366 , pp. 132-139
    • Fries, M.1    Stott, K.M.2    Reynilds, S.3    Perham, R.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.