메뉴 건너뛰기




Volumn 1857, Issue 8, 2016, Pages 1086-1101

Succinate, an intermediate in metabolism, signal transduction, ROS, hypoxia, and tumorigenesis

Author keywords

Cancer; HIF1 alpha; Substrate level phosphorylation; Succinate dehydrogenase; Succinate receptor

Indexed keywords

ITACONIC ACID; REACTIVE OXYGEN METABOLITE; SUCCINIC ACID; G PROTEIN COUPLED RECEPTOR; HIF1A PROTEIN, HUMAN; HYPOXIA INDUCIBLE FACTOR 1ALPHA; PROTEIN SUBUNIT; SUCCINATE DEHYDROGENASE;

EID: 84961130018     PISSN: 00052728     EISSN: 18792650     Source Type: Journal    
DOI: 10.1016/j.bbabio.2016.03.012     Document Type: Article
Times cited : (395)

References (231)
  • 1
    • 33646380409 scopus 로고    scopus 로고
    • The role of an astrocytic NADPH oxidase in the neurotoxicity of amyloid beta peptides
    • [1] Abramov, A.Y., Duchen, M.R., The role of an astrocytic NADPH oxidase in the neurotoxicity of amyloid beta peptides. Philos. Trans. R. Soc. Lond. Ser. B Biol. Sci. 360 (2005), 2309–2314.
    • (2005) Philos. Trans. R. Soc. Lond. Ser. B Biol. Sci. , vol.360 , pp. 2309-2314
    • Abramov, A.Y.1    Duchen, M.R.2
  • 2
    • 46349104861 scopus 로고    scopus 로고
    • Mechanisms underlying the loss of mitochondrial membrane potential in glutamate excitotoxicity
    • [2] Abramov, A.Y., Duchen, M.R., Mechanisms underlying the loss of mitochondrial membrane potential in glutamate excitotoxicity. Biochim. Biophys. Acta 1777 (2008), 953–964.
    • (2008) Biochim. Biophys. Acta , vol.1777 , pp. 953-964
    • Abramov, A.Y.1    Duchen, M.R.2
  • 3
    • 0013651376 scopus 로고
    • The metabolism of itaconic acid by liver mitochondria
    • [3] ADLER, J., WANG, S.F., Lardy, H.A., The metabolism of itaconic acid by liver mitochondria. J. Biol. Chem. 229 (1957), 865–879.
    • (1957) J. Biol. Chem. , vol.229 , pp. 865-879
    • ADLER, J.1    WANG, S.F.2    Lardy, H.A.3
  • 6
    • 0037205652 scopus 로고    scopus 로고
    • Physical and chemical interactions in cold gelation of food proteins
    • [6] Alting, A.C., de Jongh, H.H., Visschers, R.W., Simons, J.W., Physical and chemical interactions in cold gelation of food proteins. J. Agric. Food Chem. 50 (2002), 4682–4689.
    • (2002) J. Agric. Food Chem. , vol.50 , pp. 4682-4689
    • Alting, A.C.1    de Jongh, H.H.2    Visschers, R.W.3    Simons, J.W.4
  • 8
    • 80053387828 scopus 로고    scopus 로고
    • An overview of gamma-hydroxybutyric acid: pharmacodynamics, pharmacokinetics, toxic effects, addiction, analytical methods, and interpretation of results
    • [8] Andresen, H., Aydin, B.E., Mueller, A., Iwersen-Bergmann, S., An overview of gamma-hydroxybutyric acid: pharmacodynamics, pharmacokinetics, toxic effects, addiction, analytical methods, and interpretation of results. Drug Test. Anal. 3 (2011), 560–568.
    • (2011) Drug Test. Anal. , vol.3 , pp. 560-568
    • Andresen, H.1    Aydin, B.E.2    Mueller, A.3    Iwersen-Bergmann, S.4
  • 10
    • 17144422877 scopus 로고    scopus 로고
    • Mitochondrial metabolism of reactive oxygen species
    • [10] Andreyev, A.Y., Kushnareva, Y.E., Starkov, A.A., Mitochondrial metabolism of reactive oxygen species. Biochem. Mosc. 70 (2005), 200–214.
    • (2005) Biochem. Mosc. , vol.70 , pp. 200-214
    • Andreyev, A.Y.1    Kushnareva, Y.E.2    Starkov, A.A.3
  • 11
    • 84921328745 scopus 로고    scopus 로고
    • Effect of varying degrees of succinylation on the functional and morphological properties of starch from acha (Digitaria exilis Kippis Stapf)
    • [11] Arueya, G.L., Oyewale, T.M., Effect of varying degrees of succinylation on the functional and morphological properties of starch from acha (Digitaria exilis Kippis Stapf). Food Chem. 177 (2015), 258–266.
    • (2015) Food Chem. , vol.177 , pp. 258-266
    • Arueya, G.L.1    Oyewale, T.M.2
  • 12
    • 0034964421 scopus 로고    scopus 로고
    • Gene mutations in the succinate dehydrogenase subunit SDHB cause susceptibility to familial pheochromocytoma and to familial paraganglioma
    • [12] Astuti, D., Latif, F., Dallol, A., Dahia, P.L., Douglas, F., George, E., Skoldberg, F., Husebye, E.S., Eng, C., Maher, E.R., Gene mutations in the succinate dehydrogenase subunit SDHB cause susceptibility to familial pheochromocytoma and to familial paraganglioma. Am. J. Hum. Genet. 69 (2001), 49–54.
    • (2001) Am. J. Hum. Genet. , vol.69 , pp. 49-54
    • Astuti, D.1    Latif, F.2    Dallol, A.3    Dahia, P.L.4    Douglas, F.5    George, E.6    Skoldberg, F.7    Husebye, E.S.8    Eng, C.9    Maher, E.R.10
  • 13
    • 3342880690 scopus 로고    scopus 로고
    • A role for heme in Alzheimer's disease: heme binds amyloid beta and has altered metabolism
    • [13] Atamna, H., Frey, W.H., A role for heme in Alzheimer's disease: heme binds amyloid beta and has altered metabolism. Proc. Natl. Acad. Sci. U. S. A. 101 (2004), 11153–11158.
    • (2004) Proc. Natl. Acad. Sci. U. S. A. , vol.101 , pp. 11153-11158
    • Atamna, H.1    Frey, W.H.2
  • 14
    • 0035930604 scopus 로고    scopus 로고
    • Heme deficiency selectively interrupts assembly of mitochondrial complex IV in human fibroblasts: revelance to aging
    • [14] Atamna, H., Liu, J., Ames, B.N., Heme deficiency selectively interrupts assembly of mitochondrial complex IV in human fibroblasts: revelance to aging. J. Biol. Chem. 276 (2001), 48410–48416.
    • (2001) J. Biol. Chem. , vol.276 , pp. 48410-48416
    • Atamna, H.1    Liu, J.2    Ames, B.N.3
  • 15
    • 33845999254 scopus 로고    scopus 로고
    • Biotin deficiency inhibits heme synthesis and impairs mitochondria in human lung fibroblasts
    • [15] Atamna, H., Newberry, J., Erlitzki, R., Schultz, C.S., Ames, B.N., Biotin deficiency inhibits heme synthesis and impairs mitochondria in human lung fibroblasts. J. Nutr. 137 (2007), 25–30.
    • (2007) J. Nutr. , vol.137 , pp. 25-30
    • Atamna, H.1    Newberry, J.2    Erlitzki, R.3    Schultz, C.S.4    Ames, B.N.5
  • 16
    • 0016689082 scopus 로고
    • The use of acetylated ferricytochrome c for the detection of superoxide radicals produced in biological membranes
    • [16] Azzi, A., Montecucco, C., Richter, C., The use of acetylated ferricytochrome c for the detection of superoxide radicals produced in biological membranes. Biochem. Biophys. Res. Commun. 65 (1975), 597–603.
    • (1975) Biochem. Biophys. Res. Commun. , vol.65 , pp. 597-603
    • Azzi, A.1    Montecucco, C.2    Richter, C.3
  • 17
    • 0031721246 scopus 로고    scopus 로고
    • Localization at complex I and mechanism of the higher free radical production of brain nonsynaptic mitochondria in the short-lived rat than in the longevous pigeon
    • [17] Barja, G., Herrero, A., Localization at complex I and mechanism of the higher free radical production of brain nonsynaptic mitochondria in the short-lived rat than in the longevous pigeon. J. Bioenerg. Biomembr. 30 (1998), 235–243.
    • (1998) J. Bioenerg. Biomembr. , vol.30 , pp. 235-243
    • Barja, G.1    Herrero, A.2
  • 20
    • 0018664824 scopus 로고
    • Influence of some biological pyrimidines on the succinate cycle during and after cerebral ischemia
    • [20] Benzi, G., Arrigoni, E., Marzatico, F., Villa, R.F., Influence of some biological pyrimidines on the succinate cycle during and after cerebral ischemia. Biochem. Pharmacol. 28 (1979), 2545–2550.
    • (1979) Biochem. Pharmacol. , vol.28 , pp. 2545-2550
    • Benzi, G.1    Arrigoni, E.2    Marzatico, F.3    Villa, R.F.4
  • 21
    • 0020062174 scopus 로고
    • Relationships between gamma-aminobutyrate and succinate cycles during and after cerebral ischemia
    • [21] Benzi, G., Pastoris, O., Dossena, M., Relationships between gamma-aminobutyrate and succinate cycles during and after cerebral ischemia. J. Neurosci. Res. 7 (1982), 193–201.
    • (1982) J. Neurosci. Res. , vol.7 , pp. 193-201
    • Benzi, G.1    Pastoris, O.2    Dossena, M.3
  • 22
    • 84939248947 scopus 로고    scopus 로고
    • The mitochondrial permeability transition pore: channel formation by F-ATP synthase, integration in signal transduction, and role in pathophysiology
    • [22] Bernardi, P., Rasola, A., Forte, M., Lippe, G., The mitochondrial permeability transition pore: channel formation by F-ATP synthase, integration in signal transduction, and role in pathophysiology. Physiol. Rev. 95 (2015), 1111–1155.
    • (2015) Physiol. Rev. , vol.95 , pp. 1111-1155
    • Bernardi, P.1    Rasola, A.2    Forte, M.3    Lippe, G.4
  • 23
    • 0020376270 scopus 로고
    • Mitochondrial lipid peroxidation by cumene hydroperoxide and its prevention by succinate
    • [23] Bindoli, A., Cavallini, L., Jocelyn, P., Mitochondrial lipid peroxidation by cumene hydroperoxide and its prevention by succinate. Biochim. Biophys. Acta 681 (1982), 496–503.
    • (1982) Biochim. Biophys. Acta , vol.681 , pp. 496-503
    • Bindoli, A.1    Cavallini, L.2    Jocelyn, P.3
  • 24
    • 0031282497 scopus 로고    scopus 로고
    • Multiple levels of regulation of Escherichia coli succinyl-CoA synthetase
    • [24] Birney, M., Um, H., Klein, C., Multiple levels of regulation of Escherichia coli succinyl-CoA synthetase. Arch. Biochem. Biophys. 347 (1997), 103–112.
    • (1997) Arch. Biochem. Biophys. , vol.347 , pp. 103-112
    • Birney, M.1    Um, H.2    Klein, C.3
  • 25
    • 0029923401 scopus 로고    scopus 로고
    • Novel mechanisms of Escherichia coli succinyl-coenzyme A synthetase regulation
    • [25] Birney, M., Um, H.D., Klein, C., Novel mechanisms of Escherichia coli succinyl-coenzyme A synthetase regulation. J. Bacteriol. 178 (1996), 2883–2889.
    • (1996) J. Bacteriol. , vol.178 , pp. 2883-2889
    • Birney, M.1    Um, H.D.2    Klein, C.3
  • 26
    • 1642581653 scopus 로고    scopus 로고
    • Hypoxic gene activation by lipopolysaccharide in macrophages: implication of hypoxia-inducible factor 1alpha
    • [26] Blouin, C.C., Page, E.L., Soucy, G.M., Richard, D.E., Hypoxic gene activation by lipopolysaccharide in macrophages: implication of hypoxia-inducible factor 1alpha. Blood 103 (2004), 1124–1130.
    • (2004) Blood , vol.103 , pp. 1124-1130
    • Blouin, C.C.1    Page, E.L.2    Soucy, G.M.3    Richard, D.E.4
  • 27
    • 84897967621 scopus 로고    scopus 로고
    • Molecular mechanisms of cell death: central implication of ATP synthase in mitochondrial permeability transition
    • [27] Bonora, M., Wieckowski, M.R., Chinopoulos, C., Kepp, O., Kroemer, G., Galluzzi, L., Pinton, P., Molecular mechanisms of cell death: central implication of ATP synthase in mitochondrial permeability transition. Oncogene 34 (2015), 1475–1486.
    • (2015) Oncogene , vol.34 , pp. 1475-1486
    • Bonora, M.1    Wieckowski, M.R.2    Chinopoulos, C.3    Kepp, O.4    Kroemer, G.5    Galluzzi, L.6    Pinton, P.7
  • 28
    • 76949137843 scopus 로고
    • The inhibitory effects of itaconic acid in vitro and in vivo
    • [28] BOOTH, A.N., TAYLOR, J., WILSON, R.H., DEEDS, F., The inhibitory effects of itaconic acid in vitro and in vivo. J. Biol. Chem. 195 (1952), 697–702.
    • (1952) J. Biol. Chem. , vol.195 , pp. 697-702
    • BOOTH, A.N.1    TAYLOR, J.2    WILSON, R.H.3    DEEDS, F.4
  • 30
    • 33751528825 scopus 로고    scopus 로고
    • High frequency of SDHB germline mutations in patients with malignant catecholamine-producing paragangliomas: implications for genetic testing
    • [30] Brouwers, F.M., Eisenhofer, G., Tao, J.J., Kant, J.A., Adams, K.T., Linehan, W.M., Pacak, K., High frequency of SDHB germline mutations in patients with malignant catecholamine-producing paragangliomas: implications for genetic testing. J. Clin. Endocrinol. Metab. 91 (2006), 4505–4509.
    • (2006) J. Clin. Endocrinol. Metab. , vol.91 , pp. 4505-4509
    • Brouwers, F.M.1    Eisenhofer, G.2    Tao, J.J.3    Kant, J.A.4    Adams, K.T.5    Linehan, W.M.6    Pacak, K.7
  • 32
    • 0019001723 scopus 로고
    • Low-level chemiluminescence of hydroperoxide-supplemented cytochrome c
    • [32] Cadenas, E., Boveris, A., Chance, B., Low-level chemiluminescence of hydroperoxide-supplemented cytochrome c. Biochem. J. 187 (1980), 131–140.
    • (1980) Biochem. J. , vol.187 , pp. 131-140
    • Cadenas, E.1    Boveris, A.2    Chance, B.3
  • 35
    • 0021167390 scopus 로고
    • +/ADP-induced lipid peroxidation in heart and liver submitochondrial particles. mechanisms of protection by succinate
    • +/ADP-induced lipid peroxidation in heart and liver submitochondrial particles. mechanisms of protection by succinate. Biochim. Biophys. Acta 795 (1984), 466–472.
    • (1984) Biochim. Biophys. Acta , vol.795 , pp. 466-472
    • Cavallini, L.1    Valente, M.2    Bindoli, A.3
  • 36
    • 70450239624 scopus 로고    scopus 로고
    • Inhibition of succinate dehydrogenase dysregulates histone modification in mammalian cells
    • [36] Cervera, A.M., Bayley, J.P., Devilee, P., McCreath, K.J., Inhibition of succinate dehydrogenase dysregulates histone modification in mammalian cells. Mol. Cancer, 8, 2009, 89.
    • (2009) Mol. Cancer , vol.8 , pp. 89
    • Cervera, A.M.1    Bayley, J.P.2    Devilee, P.3    McCreath, K.J.4
  • 37
    • 72949139589 scopus 로고
    • The interaction of energy and electron transfer reactions in mitochondria. I. General properties and nature of the products of succinate-linked reduction of pyridine nucleotide
    • [37] Chance, B., Hollunger, G., The interaction of energy and electron transfer reactions in mitochondria. I. General properties and nature of the products of succinate-linked reduction of pyridine nucleotide. J. Biol. Chem. 236 (1961), 1534–1543.
    • (1961) J. Biol. Chem. , vol.236 , pp. 1534-1543
    • Chance, B.1    Hollunger, G.2
  • 38
    • 0025948834 scopus 로고
    • GABA: an excitatory transmitter in early postnatal life
    • [38] Cherubini, E., Gaiarsa, J.L., Ben-Ari, Y., GABA: an excitatory transmitter in early postnatal life. Trends Neurosci. 14 (1991), 515–519.
    • (1991) Trends Neurosci. , vol.14 , pp. 515-519
    • Cherubini, E.1    Gaiarsa, J.L.2    Ben-Ari, Y.3
  • 39
    • 79955629653 scopus 로고    scopus 로고
    • Mitochondrial consumption of cytosolic ATP: not so fast
    • [39] Chinopoulos, C., Mitochondrial consumption of cytosolic ATP: not so fast. FEBS Lett. 585 (2011), 1255–1259.
    • (2011) FEBS Lett. , vol.585 , pp. 1255-1259
    • Chinopoulos, C.1
  • 40
    • 80053634617 scopus 로고    scopus 로고
    • The “B space” of mitochondrial phosphorylation
    • [40] Chinopoulos, C., The “B space” of mitochondrial phosphorylation. J. Neurosci. Res. 89 (2011), 1897–1904.
    • (2011) J. Neurosci. Res. , vol.89 , pp. 1897-1904
    • Chinopoulos, C.1
  • 41
    • 84879605512 scopus 로고    scopus 로고
    • Which way does the citric acid cycle turn during hypoxia? The critical role of alpha-ketoglutarate dehydrogenase complex
    • [41] Chinopoulos, C., Which way does the citric acid cycle turn during hypoxia? The critical role of alpha-ketoglutarate dehydrogenase complex. J. Neurosci. Res. 91 (2013), 1030–1043.
    • (2013) J. Neurosci. Res. , vol.91 , pp. 1030-1043
    • Chinopoulos, C.1
  • 42
    • 71849096530 scopus 로고    scopus 로고
    • Mitochondria as ATP consumers in cellular pathology
    • [42] Chinopoulos, C., Adam-Vizi, V., Mitochondria as ATP consumers in cellular pathology. Biochim. Biophys. Acta 1802 (2010), 221–227.
    • (2010) Biochim. Biophys. Acta , vol.1802 , pp. 221-227
    • Chinopoulos, C.1    Adam-Vizi, V.2
  • 44
    • 84901420208 scopus 로고    scopus 로고
    • Measurement of ADP–ATP exchange in relation to mitochondrial transmembrane potential and oxygen consumption
    • [44] Chinopoulos, C., Kiss, G., Kawamata, H., Starkov, A.A., Measurement of ADP–ATP exchange in relation to mitochondrial transmembrane potential and oxygen consumption. Methods Enzymol. 542 (2014), 333–348.
    • (2014) Methods Enzymol. , vol.542 , pp. 333-348
    • Chinopoulos, C.1    Kiss, G.2    Kawamata, H.3    Starkov, A.A.4
  • 46
    • 0034724389 scopus 로고    scopus 로고
    • Expression analysis with oligonucleotide microarrays reveals that MYC regulates genes involved in growth, cell cycle, signaling, and adhesion
    • [46] Coller, H.A., Grandori, C., Tamayo, P., Colbert, T., Lander, E.S., Eisenman, R.N., Golub, T.R., Expression analysis with oligonucleotide microarrays reveals that MYC regulates genes involved in growth, cell cycle, signaling, and adhesion. Proc. Natl. Acad. Sci. U. S. A. 97 (2000), 3260–3265.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 3260-3265
    • Coller, H.A.1    Grandori, C.2    Tamayo, P.3    Colbert, T.4    Lander, E.S.5    Eisenman, R.N.6    Golub, T.R.7
  • 47
    • 84937572123 scopus 로고    scopus 로고
    • Itaconic acid: the surprising role of an industrial compound as a mammalian antimicrobial metabolite
    • [47] Cordes, T., Michelucci, A., Hiller, K., Itaconic acid: the surprising role of an industrial compound as a mammalian antimicrobial metabolite. Annu. Rev. Nutr. 35 (2015), 451–473.
    • (2015) Annu. Rev. Nutr. , vol.35 , pp. 451-473
    • Cordes, T.1    Michelucci, A.2    Hiller, K.3
  • 49
    • 0018595957 scopus 로고
    • Inhibition by propionyl-coenzyme A of N-acetylglutamate synthetase in rat liver mitochondria. A possible explanation for hyperammonemia in propionic and methylmalonic acidemia
    • [49] Coude, F.X., Sweetman, L., Nyhan, W.L., Inhibition by propionyl-coenzyme A of N-acetylglutamate synthetase in rat liver mitochondria. A possible explanation for hyperammonemia in propionic and methylmalonic acidemia. J. Clin. Invest. 64 (1979), 1544–1551.
    • (1979) J. Clin. Invest. , vol.64 , pp. 1544-1551
    • Coude, F.X.1    Sweetman, L.2    Nyhan, W.L.3
  • 50
    • 30944439522 scopus 로고    scopus 로고
    • Unravelling the brain targets of gamma-hydroxybutyric acid
    • [50] Crunelli, V., Emri, Z., Leresche, N., Unravelling the brain targets of gamma-hydroxybutyric acid. Curr. Opin. Pharmacol. 6 (2006), 44–52.
    • (2006) Curr. Opin. Pharmacol. , vol.6 , pp. 44-52
    • Crunelli, V.1    Emri, Z.2    Leresche, N.3
  • 52
    • 0032471513 scopus 로고    scopus 로고
    • Getting to the nucleus of mitochondrial disorders: identification of respiratory chain-enzyme genes causing Leigh syndrome
    • [52] Dahl, H.H., Getting to the nucleus of mitochondrial disorders: identification of respiratory chain-enzyme genes causing Leigh syndrome. Am. J. Hum. Genet. 63 (1998), 1594–1597.
    • (1998) Am. J. Hum. Genet. , vol.63 , pp. 1594-1597
    • Dahl, H.H.1
  • 56
    • 0009732710 scopus 로고
    • Studies on succinate dehydrogenase. I. Spectral properties of the purified enzyme and formation of enzyme-competitive inhibitor complexes
    • [56] Dervartanian, D.V., Veeger, C., Studies on succinate dehydrogenase. I. Spectral properties of the purified enzyme and formation of enzyme-competitive inhibitor complexes. Biochim. Biophys. Acta 92 (1964), 233–247.
    • (1964) Biochim. Biophys. Acta , vol.92 , pp. 233-247
    • Dervartanian, D.V.1    Veeger, C.2
  • 57
    • 77956250065 scopus 로고    scopus 로고
    • 2 removal in brain mitochondria via the thioredoxin/peroxiredoxin system
    • 2 removal in brain mitochondria via the thioredoxin/peroxiredoxin system. J. Biol. Chem. 285 (2010), 27850–27858.
    • (2010) J. Biol. Chem. , vol.285 , pp. 27850-27858
    • Drechsel, D.A.1    Patel, M.2
  • 58
    • 84875710000 scopus 로고    scopus 로고
    • Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning
    • [58] Drose, S., Differential effects of complex II on mitochondrial ROS production and their relation to cardioprotective pre- and postconditioning. Biochim. Biophys. Acta 1827 (2013), 578–587.
    • (2013) Biochim. Biophys. Acta , vol.1827 , pp. 578-587
    • Drose, S.1
  • 59
    • 0027510585 scopus 로고
    • Inhibition of succinate dehydrogenase and beta-hydroxybutyrate dehydrogenase activities by methylmalonate in brain and liver of developing rats
    • [59] Dutra, J.C., Dutra-Filho, C.S., Cardozo, S.E., Wannmacher, C.M., Sarkis, J.J., Wajner, M., Inhibition of succinate dehydrogenase and beta-hydroxybutyrate dehydrogenase activities by methylmalonate in brain and liver of developing rats. J. Inherit. Metab. Dis. 16 (1993), 147–153.
    • (1993) J. Inherit. Metab. Dis. , vol.16 , pp. 147-153
    • Dutra, J.C.1    Dutra-Filho, C.S.2    Cardozo, S.E.3    Wannmacher, C.M.4    Sarkis, J.J.5    Wajner, M.6
  • 61
    • 0016203839 scopus 로고
    • Comparative studies on 3-oxo acid coenzyme A transferase from various rat tissues
    • [61] Fenselau, A., Wallis, K., Comparative studies on 3-oxo acid coenzyme A transferase from various rat tissues. Biochem. J. 142 (1974), 619–627.
    • (1974) Biochem. J. , vol.142 , pp. 619-627
    • Fenselau, A.1    Wallis, K.2
  • 62
    • 0016280296 scopus 로고
    • Substrate specificity and mechanism of action of acetoacetate coenzyme A transferase from rat heart
    • [62] Fenselau, A., Wallis, K., Substrate specificity and mechanism of action of acetoacetate coenzyme A transferase from rat heart. Biochemistry 13 (1974), 3884–3888.
    • (1974) Biochemistry , vol.13 , pp. 3884-3888
    • Fenselau, A.1    Wallis, K.2
  • 63
    • 0016302480 scopus 로고
    • Influence of complete ischemia on glycolytic metabolites, citric acid cycle intermediates, and associated amino acids in the rat cerebral cortex
    • [63] Folbergrova, J., Ljunggren, B., Norberg, K., Siesjo, B.K., Influence of complete ischemia on glycolytic metabolites, citric acid cycle intermediates, and associated amino acids in the rat cerebral cortex. Brain Res. 80 (1974), 265–279.
    • (1974) Brain Res. , vol.80 , pp. 265-279
    • Folbergrova, J.1    Ljunggren, B.2    Norberg, K.3    Siesjo, B.K.4
  • 64
    • 84982072085 scopus 로고
    • Zur kenntniss der spezifität von dehydrasen iii über das verhalten halogensubstituierter bernsteinsäuren sowie einiger anderer bernsteinsäure- und malonsäure-derivate gegenüber succinodehydrase
    • [64] Franke, W., Holz, E., Zur kenntniss der spezifität von dehydrasen iii über das verhalten halogensubstituierter bernsteinsäuren sowie einiger anderer bernsteinsäure- und malonsäure-derivate gegenüber succinodehydrase. Justus Liebigs Ann. Chem. 608 (1957), 168–194.
    • (1957) Justus Liebigs Ann. Chem. , vol.608 , pp. 168-194
    • Franke, W.1    Holz, E.2
  • 65
    • 0034705332 scopus 로고    scopus 로고
    • Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase
    • [65] Fraser, M.E., James, M.N., Bridger, W.A., Wolodko, W.T., Phosphorylated and dephosphorylated structures of pig heart, GTP-specific succinyl-CoA synthetase. J. Mol. Biol. 299 (2000), 1325–1339.
    • (2000) J. Mol. Biol. , vol.299 , pp. 1325-1339
    • Fraser, M.E.1    James, M.N.2    Bridger, W.A.3    Wolodko, W.T.4
  • 66
    • 33745003285 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharide induces HIF-1 activation in human monocytes via p44/42 MAPK and NF-kappaB
    • [66] Frede, S., Stockmann, C., Freitag, P., Fandrey, J., Bacterial lipopolysaccharide induces HIF-1 activation in human monocytes via p44/42 MAPK and NF-kappaB. Biochem. J. 396 (2006), 517–527.
    • (2006) Biochem. J. , vol.396 , pp. 517-527
    • Frede, S.1    Stockmann, C.2    Freitag, P.3    Fandrey, J.4
  • 68
    • 0034068564 scopus 로고    scopus 로고
    • Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia
    • [68] Furuyama, K., Sassa, S., Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia. J. Clin. Invest. 105 (2000), 757–764.
    • (2000) J. Clin. Invest. , vol.105 , pp. 757-764
    • Furuyama, K.1    Sassa, S.2
  • 70
    • 84935831609 scopus 로고    scopus 로고
    • Alpha-ketoglutarate dehydrogenase complex-dependent succinylation of proteins in neurons and neuronal cell lines
    • [70] Gibson, G.E., Xu, H., Chen, H.L., Chen, W., Denton, T.T., Zhang, S., Alpha-ketoglutarate dehydrogenase complex-dependent succinylation of proteins in neurons and neuronal cell lines. J. Neurochem. 134 (2015), 86–96.
    • (2015) J. Neurochem. , vol.134 , pp. 86-96
    • Gibson, G.E.1    Xu, H.2    Chen, H.L.3    Chen, W.4    Denton, T.T.5    Zhang, S.6
  • 71
    • 0035213138 scopus 로고    scopus 로고
    • The R22X mutation of the SDHD gene in hereditary paraganglioma abolishes the enzymatic activity of complex II in the mitochondrial respiratory chain and activates the hypoxia pathway
    • [71] Gimenez-Roqueplo, A.P., Favier, J., Rustin, P., Mourad, J.J., Plouin, P.F., Corvol, P., Rotig, A., Jeunemaitre, X., The R22X mutation of the SDHD gene in hereditary paraganglioma abolishes the enzymatic activity of complex II in the mitochondrial respiratory chain and activates the hypoxia pathway. Am. J. Hum. Genet. 69 (2001), 1186–1197.
    • (2001) Am. J. Hum. Genet. , vol.69 , pp. 1186-1197
    • Gimenez-Roqueplo, A.P.1    Favier, J.2    Rustin, P.3    Mourad, J.J.4    Plouin, P.F.5    Corvol, P.6    Rotig, A.7    Jeunemaitre, X.8
  • 72
    • 0017111352 scopus 로고
    • Effect of propionic acid on fatty acid oxidation and ureagenesis
    • [72] Glasgow, A.M., Chase, H.P., Effect of propionic acid on fatty acid oxidation and ureagenesis. Pediatr. Res. 10 (1976), 683–686.
    • (1976) Pediatr. Res. , vol.10 , pp. 683-686
    • Glasgow, A.M.1    Chase, H.P.2
  • 74
    • 65449185779 scopus 로고    scopus 로고
    • Functional study in a yeast model of a novel succinate dehydrogenase subunit B gene germline missense mutation (C191Y) diagnosed in a patient affected by a glomus tumor
    • [74] Goffrini, P., Ercolino, T., Panizza, E., Giache, V., Cavone, L., Chiarugi, A., Dima, V., Ferrero, I., Mannelli, M., Functional study in a yeast model of a novel succinate dehydrogenase subunit B gene germline missense mutation (C191Y) diagnosed in a patient affected by a glomus tumor. Hum. Mol. Genet. 18 (2009), 1860–1868.
    • (2009) Hum. Mol. Genet. , vol.18 , pp. 1860-1868
    • Goffrini, P.1    Ercolino, T.2    Panizza, E.3    Giache, V.4    Cavone, L.5    Chiarugi, A.6    Dima, V.7    Ferrero, I.8    Mannelli, M.9
  • 75
    • 84875736482 scopus 로고    scopus 로고
    • Respiratory chain complex II as general sensor for apoptosis
    • [75] Grimm, S., Respiratory chain complex II as general sensor for apoptosis. Biochim. Biophys. Acta 1827 (2013), 565–572.
    • (2013) Biochim. Biophys. Acta , vol.1827 , pp. 565-572
    • Grimm, S.1
  • 76
    • 37849022071 scopus 로고    scopus 로고
    • Loss of the SdhB, but not the SdhA, subunit of complex II triggers reactive oxygen species-dependent hypoxia-inducible factor activation and tumorigenesis
    • [76] Guzy, R.D., Sharma, B., Bell, E., Chandel, N.S., Schumacker, P.T., Loss of the SdhB, but not the SdhA, subunit of complex II triggers reactive oxygen species-dependent hypoxia-inducible factor activation and tumorigenesis. Mol. Cell. Biol. 28 (2008), 718–731.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 718-731
    • Guzy, R.D.1    Sharma, B.2    Bell, E.3    Chandel, N.S.4    Schumacker, P.T.5
  • 77
    • 84920000941 scopus 로고    scopus 로고
    • Inhibition of succinate dehydrogenase by the mitochondrial chaperone TRAP1 has anti-oxidant and anti-apoptotic effects on tumor cells
    • [77] Guzzo, G., Sciacovelli, M., Bernardi, P., Rasola, A., Inhibition of succinate dehydrogenase by the mitochondrial chaperone TRAP1 has anti-oxidant and anti-apoptotic effects on tumor cells. Oncotarget 5 (2014), 11897–11908.
    • (2014) Oncotarget , vol.5 , pp. 11897-11908
    • Guzzo, G.1    Sciacovelli, M.2    Bernardi, P.3    Rasola, A.4
  • 78
    • 0343052744 scopus 로고    scopus 로고
    • Succinate: quinone oxidoreductases. Variations on a conserved theme
    • [78] Hagerhall, C., Succinate: quinone oxidoreductases. Variations on a conserved theme. Biochim. Biophys. Acta 1320 (1997), 107–141.
    • (1997) Biochim. Biophys. Acta , vol.1320 , pp. 107-141
    • Hagerhall, C.1
  • 79
    • 0015160543 scopus 로고
    • The inhibition by methylmalonic acid of malate transport by the dicarboxylate carrier in rat liver mitochondria. A possible explantation for hypoglycemia in methylmalonic aciduria
    • [79] Halperin, M.L., Schiller, C.M., Fritz, I.B., The inhibition by methylmalonic acid of malate transport by the dicarboxylate carrier in rat liver mitochondria. A possible explantation for hypoglycemia in methylmalonic aciduria. J. Clin. Invest. 50 (1971), 2276–2282.
    • (1971) J. Clin. Invest. , vol.50 , pp. 2276-2282
    • Halperin, M.L.1    Schiller, C.M.2    Fritz, I.B.3
  • 81
    • 2442649129 scopus 로고    scopus 로고
    • Citric acid cycle intermediates as ligands for orphan G-protein-coupled receptors
    • [81] He, W., Miao, F.J., Lin, D.C., Schwandner, R.T., Wang, Z., Gao, J., Chen, J.L., Tian, H., Ling, L., Citric acid cycle intermediates as ligands for orphan G-protein-coupled receptors. Nature 429 (2004), 188–193.
    • (2004) Nature , vol.429 , pp. 188-193
    • He, W.1    Miao, F.J.2    Lin, D.C.3    Schwandner, R.T.4    Wang, Z.5    Gao, J.6    Chen, J.L.7    Tian, H.8    Ling, L.9
  • 82
    • 84939131092 scopus 로고    scopus 로고
    • Succinate dehydrogenase loss in familial paraganglioma: biochemistry, genetics, and epigenetics
    • [82] Her, Y.F., Maher, L.J. III, Succinate dehydrogenase loss in familial paraganglioma: biochemistry, genetics, and epigenetics. Int. J. Endocrinol., 2015, 2015, 296167.
    • (2015) Int. J. Endocrinol. , vol.2015 , pp. 296167
    • Her, Y.F.1    Maher, L.J.2
  • 83
    • 0019464634 scopus 로고
    • Glyoxylate bypass enzymes in Yersinia species and multiple forms of isocitrate lyase in Yersinia pestis
    • [83] Hillier, S., Charnetzky, W.T., Glyoxylate bypass enzymes in Yersinia species and multiple forms of isocitrate lyase in Yersinia pestis. J. Bacteriol. 145 (1981), 452–458.
    • (1981) J. Bacteriol. , vol.145 , pp. 452-458
    • Hillier, S.1    Charnetzky, W.T.2
  • 84
    • 0016332611 scopus 로고
    • Inhibition of glycine-serine interconversion in cultured human fibroblasts by products of isoleucine catabolism
    • [84] Hillman, R.E., Otto, E.F., Inhibition of glycine-serine interconversion in cultured human fibroblasts by products of isoleucine catabolism. Pediatr. Res. 8 (1974), 941–945.
    • (1974) Pediatr. Res. , vol.8 , pp. 941-945
    • Hillman, R.E.1    Otto, E.F.2
  • 85
    • 0015904941 scopus 로고
    • Inhibition of glycine oxidation in cultured fibroblasts by isoleucine
    • [85] Hillman, R.E., Sowers, L.H., Cohen, J.L., Inhibition of glycine oxidation in cultured fibroblasts by isoleucine. Pediatr. Res. 7 (1973), 945–947.
    • (1973) Pediatr. Res. , vol.7 , pp. 945-947
    • Hillman, R.E.1    Sowers, L.H.2    Cohen, J.L.3
  • 87
    • 0018956583 scopus 로고
    • Human brain aldehyde reductases: relationship to succinic semialdehyde reductase and aldose reductase
    • [87] Hoffman, P.L., Wermuth, B., von Wartburg, J.P., Human brain aldehyde reductases: relationship to succinic semialdehyde reductase and aldose reductase. J. Neurochem. 35 (1980), 354–366.
    • (1980) J. Neurochem. , vol.35 , pp. 354-366
    • Hoffman, P.L.1    Wermuth, B.2    von Wartburg, J.P.3
  • 88
    • 11244279161 scopus 로고    scopus 로고
    • A mutation in the SDHC gene of complex II increases oxidative stress, resulting in apoptosis and tumorigenesis
    • [88] Ishii, T., Yasuda, K., Akatsuka, A., Hino, O., Hartman, P.S., Ishii, N., A mutation in the SDHC gene of complex II increases oxidative stress, resulting in apoptosis and tumorigenesis. Cancer Res. 65 (2005), 203–209.
    • (2005) Cancer Res. , vol.65 , pp. 203-209
    • Ishii, T.1    Yasuda, K.2    Akatsuka, A.3    Hino, O.4    Hartman, P.S.5    Ishii, N.6
  • 90
    • 0032538549 scopus 로고    scopus 로고
    • Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes
    • [90] Johnson, J.D., Mehus, J.G., Tews, K., Milavetz, B.I., Lambeth, D.O., Genetic evidence for the expression of ATP- and GTP-specific succinyl-CoA synthetases in multicellular eucaryotes. J. Biol. Chem. 273 (1998), 27580–27586.
    • (1998) J. Biol. Chem. , vol.273 , pp. 27580-27586
    • Johnson, J.D.1    Mehus, J.G.2    Tews, K.3    Milavetz, B.I.4    Lambeth, D.O.5
  • 91
    • 0028168469 scopus 로고
    • Net glucose production from acetone in isolated murine hepatocytes. The effect of different pretreatments of mice
    • [91] Kalapos, M.P., Mandl, J., Banhegyi, G., Antoni, F., Garzo, T., Net glucose production from acetone in isolated murine hepatocytes. The effect of different pretreatments of mice. Int. J. Biochem. 26 (1994), 1069–1079.
    • (1994) Int. J. Biochem. , vol.26 , pp. 1069-1079
    • Kalapos, M.P.1    Mandl, J.2    Banhegyi, G.3    Antoni, F.4    Garzo, T.5
  • 92
    • 35348887850 scopus 로고    scopus 로고
    • Regulation of tumor cell mitochondrial homeostasis by an organelle-specific Hsp90 chaperone network
    • [92] Kang, B.H., Plescia, J., Dohi, T., Rosa, J., Doxsey, S.J., Altieri, D.C., Regulation of tumor cell mitochondrial homeostasis by an organelle-specific Hsp90 chaperone network. Cell 131 (2007), 257–270.
    • (2007) Cell , vol.131 , pp. 257-270
    • Kang, B.H.1    Plescia, J.2    Dohi, T.3    Rosa, J.4    Doxsey, S.J.5    Altieri, D.C.6
  • 94
    • 79959964863 scopus 로고    scopus 로고
    • Succinic semialdehyde dehydrogenase: biochemical-molecular-clinical disease mechanisms, redox regulation, and functional significance
    • [94] Kim, K.J., Pearl, P.L., Jensen, K., Snead, O.C., Malaspina, P., Jakobs, C., Gibson, K.M., Succinic semialdehyde dehydrogenase: biochemical-molecular-clinical disease mechanisms, redox regulation, and functional significance. Antioxid. Redox Signal. 15 (2011), 691–718.
    • (2011) Antioxid. Redox Signal. , vol.15 , pp. 691-718
    • Kim, K.J.1    Pearl, P.L.2    Jensen, K.3    Snead, O.C.4    Malaspina, P.5    Jakobs, C.6    Gibson, K.M.7
  • 96
    • 0019989177 scopus 로고
    • Nonenzymic protein modification: a general phenomenon?
    • [96] Kirschenbaum, D.M., Nonenzymic protein modification: a general phenomenon?. Med. Hypotheses 8 (1982), 491–493.
    • (1982) Med. Hypotheses , vol.8 , pp. 491-493
    • Kirschenbaum, D.M.1
  • 98
    • 84901049781 scopus 로고    scopus 로고
    • Mitochondrial diaphorases as NAD(+) donors to segments of the citric acid cycle that support substrate-level phosphorylation yielding ATP during respiratory inhibition
    • [98] Kiss, G., Konrad, C., Pour-Ghaz, I., Mansour, J.J., Nemeth, B., Starkov, A.A., Adam-Vizi, V., Chinopoulos, C., Mitochondrial diaphorases as NAD(+) donors to segments of the citric acid cycle that support substrate-level phosphorylation yielding ATP during respiratory inhibition. FASEB J. 28 (2014), 1682–1697.
    • (2014) FASEB J. , vol.28 , pp. 1682-1697
    • Kiss, G.1    Konrad, C.2    Pour-Ghaz, I.3    Mansour, J.J.4    Nemeth, B.5    Starkov, A.A.6    Adam-Vizi, V.7    Chinopoulos, C.8
  • 99
    • 52049113898 scopus 로고    scopus 로고
    • The ADP and ATP transport in mitochondria and its carrier
    • [99] Klingenberg, M., The ADP and ATP transport in mitochondria and its carrier. Biochim. Biophys. Acta 1778 (2008), 1978–2021.
    • (2008) Biochim. Biophys. Acta , vol.1778 , pp. 1978-2021
    • Klingenberg, M.1
  • 100
    • 0030729851 scopus 로고    scopus 로고
    • High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria
    • [100] Korshunov, S.S., Skulachev, V.P., Starkov, A.A., High protonic potential actuates a mechanism of production of reactive oxygen species in mitochondria. FEBS Lett. 416 (1997), 15–18.
    • (1997) FEBS Lett. , vol.416 , pp. 15-18
    • Korshunov, S.S.1    Skulachev, V.P.2    Starkov, A.A.3
  • 102
    • 0014040410 scopus 로고
    • The action of gamma-aminobutyric acid on cortical neurones
    • [102] Krnjevic, K., Schwartz, S., The action of gamma-aminobutyric acid on cortical neurones. Exp. Brain Res. 3 (1967), 320–336.
    • (1967) Exp. Brain Res. , vol.3 , pp. 320-336
    • Krnjevic, K.1    Schwartz, S.2
  • 103
    • 82155192318 scopus 로고    scopus 로고
    • Functional regulation of HIF-1alpha under normoxia—is there more than post-translational regulation?
    • [103] Kuschel, A., Simon, P., Tug, S., Functional regulation of HIF-1alpha under normoxia—is there more than post-translational regulation?. J. Cell. Physiol. 227 (2012), 514–524.
    • (2012) J. Cell. Physiol. , vol.227 , pp. 514-524
    • Kuschel, A.1    Simon, P.2    Tug, S.3
  • 104
    • 0034781986 scopus 로고    scopus 로고
    • Analysis of dicarboxylic acids by tandem mass spectrometry. High-throughput quantitative measurement of methylmalonic acid in serum, plasma, and urine
    • [104] Kushnir, M.M., Komaromy-Hiller, G., Shushan, B., Urry, F.M., Roberts, W.L., Analysis of dicarboxylic acids by tandem mass spectrometry. High-throughput quantitative measurement of methylmalonic acid in serum, plasma, and urine. Clin. Chem. 47 (2001), 1993–2002.
    • (2001) Clin. Chem. , vol.47 , pp. 1993-2002
    • Kushnir, M.M.1    Komaromy-Hiller, G.2    Shushan, B.3    Urry, F.M.4    Roberts, W.L.5
  • 105
    • 79953292975 scopus 로고    scopus 로고
    • Highly sensitive GC/MS/MS method for quantitation of amino and nonamino organic acids
    • [105] Kvitvang, H.F., Andreassen, T., Adam, T., Villas-Boas, S.G., Bruheim, P., Highly sensitive GC/MS/MS method for quantitation of amino and nonamino organic acids. Anal. Chem. 83 (2011), 2705–2711.
    • (2011) Anal. Chem. , vol.83 , pp. 2705-2711
    • Kvitvang, H.F.1    Andreassen, T.2    Adam, T.3    Villas-Boas, S.G.4    Bruheim, P.5
  • 108
    • 67349267341 scopus 로고    scopus 로고
    • Mutations in the heme b-binding residue of SDHC inhibit assembly of respiratory chain complex II in mammalian cells
    • [108] Lemarie, A., Grimm, S., Mutations in the heme b-binding residue of SDHC inhibit assembly of respiratory chain complex II in mammalian cells. Mitochondrion 9 (2009), 254–260.
    • (2009) Mitochondrion , vol.9 , pp. 254-260
    • Lemarie, A.1    Grimm, S.2
  • 109
    • 78651282654 scopus 로고    scopus 로고
    • Specific disintegration of complex II succinate:ubiquinone oxidoreductase links pH changes to oxidative stress for apoptosis induction
    • [109] Lemarie, A., Huc, L., Pazarentzos, E., Mahul-Mellier, A.L., Grimm, S., Specific disintegration of complex II succinate:ubiquinone oxidoreductase links pH changes to oxidative stress for apoptosis induction. Cell Death Differ. 18 (2011), 338–349.
    • (2011) Cell Death Differ. , vol.18 , pp. 338-349
    • Lemarie, A.1    Huc, L.2    Pazarentzos, E.3    Mahul-Mellier, A.L.4    Grimm, S.5
  • 110
    • 84891388086 scopus 로고    scopus 로고
    • Succinate-to-fumarate ratio as a new metabolic marker to detect the presence of SDHB/D-related paraganglioma: initial experimental and ex vivo findings
    • [110] Lendvai, N., Pawlosky, R., Bullova, P., Eisenhofer, G., Patocs, A., Veech, R.L., Pacak, K., Succinate-to-fumarate ratio as a new metabolic marker to detect the presence of SDHB/D-related paraganglioma: initial experimental and ex vivo findings. Endocrinology 155 (2014), 27–32.
    • (2014) Endocrinology , vol.155 , pp. 27-32
    • Lendvai, N.1    Pawlosky, R.2    Bullova, P.3    Eisenhofer, G.4    Patocs, A.5    Veech, R.L.6    Pacak, K.7
  • 114
    • 0028773636 scopus 로고
    • Structural variation in heme enzymes: a comparative analysis of peroxidase and P450 crystal structures
    • [114] Li, H., Poulos, T.L., Structural variation in heme enzymes: a comparative analysis of peroxidase and P450 crystal structures. Structure 2 (1994), 461–464.
    • (1994) Structure , vol.2 , pp. 461-464
    • Li, H.1    Poulos, T.L.2
  • 115
    • 84872705578 scopus 로고    scopus 로고
    • Identification of the kinetic mechanism of succinyl-CoA synthetase
    • [115] Li, X., Wu, F., Beard, D.A., Identification of the kinetic mechanism of succinyl-CoA synthetase. Biosci. Rep. 33 (2013), 145–163.
    • (2013) Biosci. Rep. , vol.33 , pp. 145-163
    • Li, X.1    Wu, F.2    Beard, D.A.3
  • 116
    • 0023658399 scopus 로고
    • Mitochondrial phosphate carrier. Functional role of its SH groups and interrelations within the carrier unit
    • [116] Ligeti, E., Fonyo, A., Mitochondrial phosphate carrier. Functional role of its SH groups and interrelations within the carrier unit. Eur. J. Biochem. 167 (1987), 167–173.
    • (1987) Eur. J. Biochem. , vol.167 , pp. 167-173
    • Ligeti, E.1    Fonyo, A.2
  • 117
    • 0024573558 scopus 로고
    • Phosphate transport protein of rat heart mitochondria: location of its SH-groups and exploration of their environment
    • [117] Ligeti, E., Fonyo, A., Phosphate transport protein of rat heart mitochondria: location of its SH-groups and exploration of their environment. Biochim. Biophys. Acta 973 (1989), 170–175.
    • (1989) Biochim. Biophys. Acta , vol.973 , pp. 170-175
    • Ligeti, E.1    Fonyo, A.2
  • 119
    • 0029868750 scopus 로고    scopus 로고
    • The role of iron–sulfur clusters in in vivo hydroxyl radical production
    • [119] Liochev, S.L., The role of iron–sulfur clusters in in vivo hydroxyl radical production. Free Radic. Res. 25 (1996), 369–384.
    • (1996) Free Radic. Res. , vol.25 , pp. 369-384
    • Liochev, S.L.1
  • 120
    • 39349105090 scopus 로고    scopus 로고
    • Expanding chemical biology of 2-oxoglutarate oxygenases
    • [120] Loenarz, C., Schofield, C.J., Expanding chemical biology of 2-oxoglutarate oxygenases. Nat. Chem. Biol. 4 (2008), 152–156.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 152-156
    • Loenarz, C.1    Schofield, C.J.2
  • 121
    • 84876889621 scopus 로고    scopus 로고
    • What a difference a hydroxyl makes: mutant IDH, (R)-2-hydroxyglutarate, and cancer
    • [121] Losman, J.A., Kaelin, W.G. Jr., What a difference a hydroxyl makes: mutant IDH, (R)-2-hydroxyglutarate, and cancer. Genes Dev. 27 (2013), 836–852.
    • (2013) Genes Dev. , vol.27 , pp. 836-852
    • Losman, J.A.1    Kaelin, W.G.2
  • 122
    • 0347419242 scopus 로고    scopus 로고
    • Developmental up-regulation of KCC2 in the absence of GABAergic and glutamatergic transmission
    • [122] Ludwig, A., Li, H., Saarma, M., Kaila, K., Rivera, C., Developmental up-regulation of KCC2 in the absence of GABAergic and glutamatergic transmission. Eur. J. Neurosci. 18 (2003), 3199–3206.
    • (2003) Eur. J. Neurosci. , vol.18 , pp. 3199-3206
    • Ludwig, A.1    Li, H.2    Saarma, M.3    Kaila, K.4    Rivera, C.5
  • 123
    • 34147099624 scopus 로고    scopus 로고
    • A Chinese family with familial paraganglioma syndrome due to succinate dehydrogenase deficiency
    • [123] Ma, R.C., Lam, C.W., Chan, W.B., So, W.Y., Tong, S.F., Chow, C.C., Cockram, C.S., A Chinese family with familial paraganglioma syndrome due to succinate dehydrogenase deficiency. Hong. Kong. Med. J. 13 (2007), 151–154.
    • (2007) Hong. Kong. Med. J. , vol.13 , pp. 151-154
    • Ma, R.C.1    Lam, C.W.2    Chan, W.B.3    So, W.Y.4    Tong, S.F.5    Chow, C.C.6    Cockram, C.S.7
  • 124
    • 0027395911 scopus 로고
    • Regulation of gamma-aminobutyric acid synthesis in the brain
    • [124] Martin, D.L., Rimvall, K., Regulation of gamma-aminobutyric acid synthesis in the brain. J. Neurochem. 60 (1993), 395–407.
    • (1993) J. Neurochem. , vol.60 , pp. 395-407
    • Martin, D.L.1    Rimvall, K.2
  • 125
    • 84929505550 scopus 로고    scopus 로고
    • Targeted disruption of the SUCNR1 metabolic receptor leads to dichotomous effects on obesity
    • [125] McCreath, K.J., Espada, S., Galvez, B.G., Benito, M., de, M.A., Sepulveda, P., Cervera, A.M., Targeted disruption of the SUCNR1 metabolic receptor leads to dichotomous effects on obesity. Diabetes 64 (2015), 1154–1167.
    • (2015) Diabetes , vol.64 , pp. 1154-1167
    • McCreath, K.J.1    Espada, S.2    Galvez, B.G.3    Benito, M.4    de, M.A.5    Sepulveda, P.6    Cervera, A.M.7
  • 126
    • 0017404916 scopus 로고
    • Itaconate, an isocitrate lyase-directed inhibitor in Pseudomonas indigofera
    • [126] McFadden, B.A., Purohit, S., Itaconate, an isocitrate lyase-directed inhibitor in Pseudomonas indigofera. J. Bacteriol. 131 (1977), 136–144.
    • (1977) J. Bacteriol. , vol.131 , pp. 136-144
    • McFadden, B.A.1    Purohit, S.2
  • 127
    • 0023782890 scopus 로고
    • Control of mitochondrial respiration in muscle
    • [127] McMillin, J.B., Pauly, D.F., Control of mitochondrial respiration in muscle. Mol. Cell. Biochem. 81 (1988), 121–129.
    • (1988) Mol. Cell. Biochem. , vol.81 , pp. 121-129
    • McMillin, J.B.1    Pauly, D.F.2
  • 128
    • 34548386693 scopus 로고    scopus 로고
    • Familial gastrointestinal stromal tumors and germ-line mutations
    • [128] McWhinney, S.R., Pasini, B., Stratakis, C.A., Familial gastrointestinal stromal tumors and germ-line mutations. N. Engl. J. Med. 357 (2007), 1054–1056.
    • (2007) N. Engl. J. Med. , vol.357 , pp. 1054-1056
    • McWhinney, S.R.1    Pasini, B.2    Stratakis, C.A.3
  • 129
    • 0004206488 scopus 로고
    • Chemical modification of proteins
    • Holden-Day
    • [129] Means, G.E., Feeney, R.E., Chemical modification of proteins. 1971, Holden-Day.
    • (1971)
    • Means, G.E.1    Feeney, R.E.2
  • 130
    • 70449720998 scopus 로고    scopus 로고
    • Modeling of ATP–ADP steady-state exchange rate mediated by the adenine nucleotide translocase in isolated mitochondria
    • [130] Metelkin, E., Demin, O., Kovacs, Z., Chinopoulos, C., Modeling of ATP–ADP steady-state exchange rate mediated by the adenine nucleotide translocase in isolated mitochondria. FEBS J. 276 (2009), 6942–6955.
    • (2009) FEBS J. , vol.276 , pp. 6942-6955
    • Metelkin, E.1    Demin, O.2    Kovacs, Z.3    Chinopoulos, C.4
  • 132
    • 84899473768 scopus 로고    scopus 로고
    • Succinate: a metabolic signal in inflammation
    • [132] Mills, E., O'Neill, L.A., Succinate: a metabolic signal in inflammation. Trends Cell Biol. 24 (2014), 313–320.
    • (2014) Trends Cell Biol. , vol.24 , pp. 313-320
    • Mills, E.1    O'Neill, L.A.2
  • 133
    • 0029789256 scopus 로고    scopus 로고
    • GAT-3, a high-affinity GABA plasma membrane transporter, is localized to astrocytic processes, and it is not confined to the vicinity of GABAergic synapses in the cerebral cortex
    • [133] Minelli, A., DeBiasi, S., Brecha, N.C., Zuccarello, L.V., Conti, F., GAT-3, a high-affinity GABA plasma membrane transporter, is localized to astrocytic processes, and it is not confined to the vicinity of GABAergic synapses in the cerebral cortex. J. Neurosci. 16 (1996), 6255–6264.
    • (1996) J. Neurosci. , vol.16 , pp. 6255-6264
    • Minelli, A.1    DeBiasi, S.2    Brecha, N.C.3    Zuccarello, L.V.4    Conti, F.5
  • 136
    • 0020067705 scopus 로고
    • Alteration of inner-membrane components and damage to electron-transfer activities of bovine heart submitochondrial particles induced by NADPH-dependent lipid peroxidation
    • [136] Narabayashi, H., Takeshige, K., Minakami, S., Alteration of inner-membrane components and damage to electron-transfer activities of bovine heart submitochondrial particles induced by NADPH-dependent lipid peroxidation. Biochem. J. 202 (1982), 97–105.
    • (1982) Biochem. J. , vol.202 , pp. 97-105
    • Narabayashi, H.1    Takeshige, K.2    Minakami, S.3
  • 139
    • 84871107379 scopus 로고    scopus 로고
    • Mitochondrial protein acylation and intermediary metabolism: regulation by sirtuins and implications for metabolic disease
    • [139] Newman, J.C., He, W., Verdin, E., Mitochondrial protein acylation and intermediary metabolism: regulation by sirtuins and implications for metabolic disease. J. Biol. Chem. 287 (2012), 42436–42443.
    • (2012) J. Biol. Chem. , vol.287 , pp. 42436-42443
    • Newman, J.C.1    He, W.2    Verdin, E.3
  • 141
    • 0004064798 scopus 로고    scopus 로고
    • Bioenergetics
    • Academic Press
    • [141] Nicholls, D.G., Ferguson, S.J., Bioenergetics. 2002, Academic Press.
    • (2002)
    • Nicholls, D.G.1    Ferguson, S.J.2
  • 142
    • 0033767445 scopus 로고    scopus 로고
    • Mutations in SDHC cause autosomal dominant paraganglioma, type 3
    • [142] Niemann, S., Muller, U., Mutations in SDHC cause autosomal dominant paraganglioma, type 3. Nat. Genet. 26 (2000), 268–270.
    • (2000) Nat. Genet. , vol.26 , pp. 268-270
    • Niemann, S.1    Muller, U.2
  • 144
    • 0017810263 scopus 로고
    • Do mitochondria produce oxygen radicals in vivo?
    • [144] Nohl, H., Hegner, D., Do mitochondria produce oxygen radicals in vivo?. Eur. J. Biochem. 82 (1978), 563–567.
    • (1978) Eur. J. Biochem. , vol.82 , pp. 563-567
    • Nohl, H.1    Hegner, D.2
  • 145
    • 84938201044 scopus 로고    scopus 로고
    • Oncometabolites: tailoring our genes
    • [145] Nowicki, S., Gottlieb, E., Oncometabolites: tailoring our genes. FEBS J. 282 (2015), 2796–2805.
    • (2015) FEBS J. , vol.282 , pp. 2796-2805
    • Nowicki, S.1    Gottlieb, E.2
  • 146
    • 0019876977 scopus 로고
    • Thermodynamic and electron paramagnetic resonance characterization of flavin in succinate dehydrogenase
    • [146] Ohnishi, T., King, T.E., Salerno, J.C., Blum, H., Bowyer, J.R., Maida, T., Thermodynamic and electron paramagnetic resonance characterization of flavin in succinate dehydrogenase. J. Biol. Chem. 256 (1981), 5577–5582.
    • (1981) J. Biol. Chem. , vol.256 , pp. 5577-5582
    • Ohnishi, T.1    King, T.E.2    Salerno, J.C.3    Blum, H.4    Bowyer, J.R.5    Maida, T.6
  • 147
    • 43149121085 scopus 로고    scopus 로고
    • Disorders caused by deficiency of succinate-CoA ligase
    • [147] Ostergaard, E., Disorders caused by deficiency of succinate-CoA ligase. J. Inherit. Metab. Dis. 31 (2008), 226–229.
    • (2008) J. Inherit. Metab. Dis. , vol.31 , pp. 226-229
    • Ostergaard, E.1
  • 149
    • 2642675784 scopus 로고
    • Polyfunctional dinitrophenyl haptens as reagents for elicitation of immediate type allergic skin responses
    • [149] Parker, C.W., Kern, M., EISEN, H.N., Polyfunctional dinitrophenyl haptens as reagents for elicitation of immediate type allergic skin responses. J. Exp. Med. 115 (1962), 789–801.
    • (1962) J. Exp. Med. , vol.115 , pp. 789-801
    • Parker, C.W.1    Kern, M.2    EISEN, H.N.3
  • 151
    • 66849143816 scopus 로고    scopus 로고
    • SDH mutations in tumorigenesis and inherited endocrine tumours: lesson from the phaeochromocytoma–paraganglioma syndromes
    • [151] Pasini, B., Stratakis, C.A., SDH mutations in tumorigenesis and inherited endocrine tumours: lesson from the phaeochromocytoma–paraganglioma syndromes. J. Intern. Med. 266 (2009), 19–42.
    • (2009) J. Intern. Med. , vol.266 , pp. 19-42
    • Pasini, B.1    Stratakis, C.A.2
  • 152
    • 0017815434 scopus 로고
    • Caenorhabditis elegans and Ascaris suum: inhibition of isocitrate lyase by itaconate
    • [152] Patel, T.R., McFadden, B.A., Caenorhabditis elegans and Ascaris suum: inhibition of isocitrate lyase by itaconate. Exp. Parasitol. 44 (1978), 262–268.
    • (1978) Exp. Parasitol. , vol.44 , pp. 262-268
    • Patel, T.R.1    McFadden, B.A.2
  • 153
    • 84876758617 scopus 로고    scopus 로고
    • Metabolic pathways in immune cell activation and quiescence
    • [153] Pearce, E.L., Pearce, E.J., Metabolic pathways in immune cell activation and quiescence. Immunity 38 (2013), 633–643.
    • (2013) Immunity , vol.38 , pp. 633-643
    • Pearce, E.L.1    Pearce, E.J.2
  • 156
    • 0024282355 scopus 로고
    • Analysis of mechanisms of free-energy coupling and uncoupling by inhibitor titrations: theory, computer modeling and experiments
    • [156] Petronilli, V., Azzone, G.F., Pietrobon, D., Analysis of mechanisms of free-energy coupling and uncoupling by inhibitor titrations: theory, computer modeling and experiments. Biochim. Biophys. Acta 932 (1988), 306–324.
    • (1988) Biochim. Biophys. Acta , vol.932 , pp. 306-324
    • Petronilli, V.1    Azzone, G.F.2    Pietrobon, D.3
  • 157
    • 70350710639 scopus 로고    scopus 로고
    • Succinyl-CoA synthetase is a phosphate target for the activation of mitochondrial metabolism
    • [157] Phillips, D., Aponte, A.M., French, S.A., Chess, D.J., Balaban, R.S., Succinyl-CoA synthetase is a phosphate target for the activation of mitochondrial metabolism. Biochemistry 48 (2009), 7140–7149.
    • (2009) Biochemistry , vol.48 , pp. 7140-7149
    • Phillips, D.1    Aponte, A.M.2    French, S.A.3    Chess, D.J.4    Balaban, R.S.5
  • 158
    • 0035914218 scopus 로고    scopus 로고
    • Elevation of AKR7A2 (succinic semialdehyde reductase) in neurodegenerative disease
    • [158] Picklo, M.J. Sr., Olson, S.J., Hayes, J.D., Markesbery, W.R., Montine, T.J., Elevation of AKR7A2 (succinic semialdehyde reductase) in neurodegenerative disease. Brain Res. 916 (2001), 229–238.
    • (2001) Brain Res. , vol.916 , pp. 229-238
    • Picklo, M.J.1    Olson, S.J.2    Hayes, J.D.3    Markesbery, W.R.4    Montine, T.J.5
  • 159
    • 84904915102 scopus 로고    scopus 로고
    • Genetically modeled mice with mutations in mitochondrial metabolic enzymes for the study of cancer
    • [159] Piruat, J.I., Millan-Ucles, A., Genetically modeled mice with mutations in mitochondrial metabolic enzymes for the study of cancer. Front Oncol., 4, 2014, 200.
    • (2014) Front Oncol. , vol.4 , pp. 200
    • Piruat, J.I.1    Millan-Ucles, A.2
  • 160
    • 10044296222 scopus 로고    scopus 로고
    • The mitochondrial SDHD gene is required for early embryogenesis, and its partial deficiency results in persistent carotid body glomus cell activation with full responsiveness to hypoxia
    • [160] Piruat, J.I., Pintado, C.O., Ortega-Saenz, P., Roche, M., Lopez-Barneo, J., The mitochondrial SDHD gene is required for early embryogenesis, and its partial deficiency results in persistent carotid body glomus cell activation with full responsiveness to hypoxia. Mol. Cell. Biol. 24 (2004), 10933–10940.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 10933-10940
    • Piruat, J.I.1    Pintado, C.O.2    Ortega-Saenz, P.3    Roche, M.4    Lopez-Barneo, J.5
  • 163
    • 80052419584 scopus 로고    scopus 로고
    • The mechanism of superoxide production by the antimycin-inhibited mitochondrial Q-cycle
    • [163] Quinlan, C.L., Gerencser, A.A., Treberg, J.R., Brand, M.D., The mechanism of superoxide production by the antimycin-inhibited mitochondrial Q-cycle. J. Biol. Chem. 286 (2011), 31361–31372.
    • (2011) J. Biol. Chem. , vol.286 , pp. 31361-31372
    • Quinlan, C.L.1    Gerencser, A.A.2    Treberg, J.R.3    Brand, M.D.4
  • 164
    • 84864540083 scopus 로고    scopus 로고
    • Mitochondrial complex II can generate reactive oxygen species at high rates in both the forward and reverse reactions
    • [164] Quinlan, C.L., Orr, A.L., Perevoshchikova, I.V., Treberg, J.R., Ackrell, B.A., Brand, M.D., Mitochondrial complex II can generate reactive oxygen species at high rates in both the forward and reverse reactions. J. Biol. Chem. 287 (2012), 27255–27264.
    • (2012) J. Biol. Chem. , vol.287 , pp. 27255-27264
    • Quinlan, C.L.1    Orr, A.L.2    Perevoshchikova, I.V.3    Treberg, J.R.4    Ackrell, B.A.5    Brand, M.D.6
  • 165
    • 84907095476 scopus 로고    scopus 로고
    • Exploring the association of succinate dehydrogenase complex mutations with lymphoid malignancies
    • [165] Renella, R., Carnevale, J., Schneider, K.A., Hornick, J.L., Rana, H.Q., Janeway, K.A., Exploring the association of succinate dehydrogenase complex mutations with lymphoid malignancies. Familial Cancer 13 (2014), 507–511.
    • (2014) Familial Cancer , vol.13 , pp. 507-511
    • Renella, R.1    Carnevale, J.2    Schneider, K.A.3    Hornick, J.L.4    Rana, H.Q.5    Janeway, K.A.6
  • 167
    • 0015830590 scopus 로고
    • Heterogeneity of NADPH-dependent aldehyde reductase from human and rat brain
    • [167] Ris, M.M., von Wartburg, J.P., Heterogeneity of NADPH-dependent aldehyde reductase from human and rat brain. Eur. J. Biochem. 37 (1973), 69–77.
    • (1973) Eur. J. Biochem. , vol.37 , pp. 69-77
    • Ris, M.M.1    von Wartburg, J.P.2
  • 168
    • 71149117826 scopus 로고    scopus 로고
    • Localization of the succinate receptor in the distal nephron and its signaling in polarized MDCK cells
    • [168] Robben, J.H., Fenton, R.A., Vargas, S.L., Schweer, H., Peti-Peterdi, J., Deen, P.M., Milligan, G., Localization of the succinate receptor in the distal nephron and its signaling in polarized MDCK cells. Kidney Int. 76 (2009), 1258–1267.
    • (2009) Kidney Int. , vol.76 , pp. 1258-1267
    • Robben, J.H.1    Fenton, R.A.2    Vargas, S.L.3    Schweer, H.4    Peti-Peterdi, J.5    Deen, P.M.6    Milligan, G.7
  • 169
    • 0025672728 scopus 로고
    • ATP depletion and mitochondrial functional loss during ischemia in slow and fast heart-rate hearts
    • [169] Rouslin, W., Broge, C.W., Grupp, I.L., ATP depletion and mitochondrial functional loss during ischemia in slow and fast heart-rate hearts. Am. J. Phys. 259 (1990), H1759–H1766.
    • (1990) Am. J. Phys. , vol.259 , pp. H1759-H1766
    • Rouslin, W.1    Broge, C.W.2    Grupp, I.L.3
  • 170
    • 0022515008 scopus 로고
    • Effects of oligomycin and acidosis on rates of ATP depletion in ischemic heart muscle
    • [170] Rouslin, W., Erickson, J.L., Solaro, R.J., Effects of oligomycin and acidosis on rates of ATP depletion in ischemic heart muscle. Am. J. Phys. 250 (1986), H503–H508.
    • (1986) Am. J. Phys. , vol.250 , pp. H503-H508
    • Rouslin, W.1    Erickson, J.L.2    Solaro, R.J.3
  • 173
    • 0019326469 scopus 로고
    • Studies on the stabilized ubisemiquinone species in the succinate-cytochrome c reductase segment of the intact mitochondrial membrane system
    • [173] Salerno, J.C., Ohnishi, T., Studies on the stabilized ubisemiquinone species in the succinate-cytochrome c reductase segment of the intact mitochondrial membrane system. Biochem. J. 192 (1980), 769–781.
    • (1980) Biochem. J. , vol.192 , pp. 769-781
    • Salerno, J.C.1    Ohnishi, T.2
  • 174
    • 84942372787 scopus 로고    scopus 로고
    • 2-Oxoglutarate-dependent dioxygenases are sensors of energy metabolism, oxygen availability, and iron homeostasis: potential role in the regulation of aging process
    • [174] Salminen, A., Kauppinen, A., Kaarniranta, K., 2-Oxoglutarate-dependent dioxygenases are sensors of energy metabolism, oxygen availability, and iron homeostasis: potential role in the regulation of aging process. Cell. Mol. Life Sci. 72 (2015), 3897–3914.
    • (2015) Cell. Mol. Life Sci. , vol.72 , pp. 3897-3914
    • Salminen, A.1    Kauppinen, A.2    Kaarniranta, K.3
  • 175
    • 84956644437 scopus 로고    scopus 로고
    • Inborn metabolic diseases: diagnosis and treatment
    • Springer
    • [175] Saudubray, J.M., van den Berghe, G., Walter, J.H., Inborn metabolic diseases: diagnosis and treatment. 2011, Springer.
    • (2011)
    • Saudubray, J.M.1    van den Berghe, G.2    Walter, J.H.3
  • 178
    • 0016140139 scopus 로고
    • Pyruvate carboxylase. Studies of activator-independent catalysis and of the specificity of activation by acyl derivatives of coenzyme A for the enzyme from rat liver
    • [178] Scrutton, M.C., Pyruvate carboxylase. Studies of activator-independent catalysis and of the specificity of activation by acyl derivatives of coenzyme A for the enzyme from rat liver. J. Biol. Chem. 249 (1974), 7057–7067.
    • (1974) J. Biol. Chem. , vol.249 , pp. 7057-7067
    • Scrutton, M.C.1
  • 179
    • 0014216556 scopus 로고
    • Pyruvate carboxylase. IX. Some properties of the activation by certain acyl derivatives of coenzyme A
    • [179] Scrutton, M.C., Utter, M.F., Pyruvate carboxylase. IX. Some properties of the activation by certain acyl derivatives of coenzyme A. J. Biol. Chem. 242 (1967), 1723–1735.
    • (1967) J. Biol. Chem. , vol.242 , pp. 1723-1735
    • Scrutton, M.C.1    Utter, M.F.2
  • 181
    • 33745591371 scopus 로고    scopus 로고
    • Redox stress is not essential for the pseudo-hypoxic phenotype of succinate dehydrogenase deficient cells
    • [181] Selak, M.A., Duran, R.V., Gottlieb, E., Redox stress is not essential for the pseudo-hypoxic phenotype of succinate dehydrogenase deficient cells. Biochim. Biophys. Acta 1757 (2006), 567–572.
    • (2006) Biochim. Biophys. Acta , vol.1757 , pp. 567-572
    • Selak, M.A.1    Duran, R.V.2    Gottlieb, E.3
  • 182
    • 0035834789 scopus 로고    scopus 로고
    • A defect in the cytochrome b large subunit in complex II causes both superoxide anion overproduction and abnormal energy metabolism in Caenorhabditis elegans
    • [182] Senoo-Matsuda, N., Yasuda, K., Tsuda, M., Ohkubo, T., Yoshimura, S., Nakazawa, H., Hartman, P.S., Ishii, N., A defect in the cytochrome b large subunit in complex II causes both superoxide anion overproduction and abnormal energy metabolism in Caenorhabditis elegans. J. Biol. Chem. 276 (2001), 41553–41558.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41553-41558
    • Senoo-Matsuda, N.1    Yasuda, K.2    Tsuda, M.3    Ohkubo, T.4    Yoshimura, S.5    Nakazawa, H.6    Hartman, P.S.7    Ishii, N.8
  • 183
    • 34247339729 scopus 로고    scopus 로고
    • Putrescine as an important source of GABA in the postnatal rat subventricular zone
    • [183] Sequerra, E.B., Gardino, P., Hedin-Pereira, C., de Mello, F.G., Putrescine as an important source of GABA in the postnatal rat subventricular zone. Neuroscience 146 (2007), 489–493.
    • (2007) Neuroscience , vol.146 , pp. 489-493
    • Sequerra, E.B.1    Gardino, P.2    Hedin-Pereira, C.3    de Mello, F.G.4
  • 184
    • 0020787536 scopus 로고
    • Initial-velocity kinetics of succinoyl-coenzyme A-3-oxo acid coenzyme A-transferase from sheep kidney
    • [184] Sharp, J.A., Edwards, M.R., Initial-velocity kinetics of succinoyl-coenzyme A-3-oxo acid coenzyme A-transferase from sheep kidney. Biochem. J. 213 (1983), 179–185.
    • (1983) Biochem. J. , vol.213 , pp. 179-185
    • Sharp, J.A.1    Edwards, M.R.2
  • 187
    • 36249005491 scopus 로고    scopus 로고
    • Succinate inhibition of alpha-ketoglutarate-dependent enzymes in a yeast model of paraganglioma
    • [187] Smith, E.H., Janknecht, R., Maher, L.J. III, Succinate inhibition of alpha-ketoglutarate-dependent enzymes in a yeast model of paraganglioma. Hum. Mol. Genet. 16 (2007), 3136–3148.
    • (2007) Hum. Mol. Genet. , vol.16 , pp. 3136-3148
    • Smith, E.H.1    Janknecht, R.2    Maher, L.J.3
  • 188
    • 0032416442 scopus 로고    scopus 로고
    • Two isoforms of glutamate decarboxylase: why?
    • [188] Soghomonian, J.J., Martin, D.L., Two isoforms of glutamate decarboxylase: why?. Trends Pharmacol. Sci. 19 (1998), 500–505.
    • (1998) Trends Pharmacol. Sci. , vol.19 , pp. 500-505
    • Soghomonian, J.J.1    Martin, D.L.2
  • 189
    • 0016273538 scopus 로고
    • Oxygen radicals and hydrogen peroxide in rat brain mitochondria
    • [189] Sorgato, M.C., Sartorelli, L., Loschen, G., Azzi, A., Oxygen radicals and hydrogen peroxide in rat brain mitochondria. FEBS Lett. 45 (1974), 92–95.
    • (1974) FEBS Lett. , vol.45 , pp. 92-95
    • Sorgato, M.C.1    Sartorelli, L.2    Loschen, G.3    Azzi, A.4
  • 190
    • 84896718850 scopus 로고    scopus 로고
    • Heterogeneous cellular distribution of glutamate dehydrogenase in brain and in non-neural tissues
    • [190] Spanaki, C., Kotzamani, D., Petraki, Z., Drakos, E., Plaitakis, A., Heterogeneous cellular distribution of glutamate dehydrogenase in brain and in non-neural tissues. Neurochem. Res. 39 (2014), 500–515.
    • (2014) Neurochem. Res. , vol.39 , pp. 500-515
    • Spanaki, C.1    Kotzamani, D.2    Petraki, Z.3    Drakos, E.4    Plaitakis, A.5
  • 191
    • 0034693690 scopus 로고    scopus 로고
    • Are mitochondria a permanent source of reactive oxygen species?
    • [191] Staniek, K., Nohl, H., Are mitochondria a permanent source of reactive oxygen species?. Biochim. Biophys. Acta 1460 (2000), 268–275.
    • (2000) Biochim. Biophys. Acta , vol.1460 , pp. 268-275
    • Staniek, K.1    Nohl, H.2
  • 193
    • 0018824270 scopus 로고
    • Failure of the normal ureagenic response to amino acids in organic acid-loaded rats. Proposed mechanism for the hyperammonemia of propionic and methylmalonic acidemia
    • [193] Stewart, P.M., Walser, M., Failure of the normal ureagenic response to amino acids in organic acid-loaded rats. Proposed mechanism for the hyperammonemia of propionic and methylmalonic acidemia. J. Clin. Invest. 66 (1980), 484–492.
    • (1980) J. Clin. Invest. , vol.66 , pp. 484-492
    • Stewart, P.M.1    Walser, M.2
  • 196
    • 21244503033 scopus 로고    scopus 로고
    • Crystal structure of mitochondrial respiratory membrane protein complex II
    • [196] Sun, F., Huo, X., Zhai, Y., Wang, A., Xu, J., Su, D., Bartlam, M., Rao, Z., Crystal structure of mitochondrial respiratory membrane protein complex II. Cell 121 (2005), 1043–1057.
    • (2005) Cell , vol.121 , pp. 1043-1057
    • Sun, F.1    Huo, X.2    Zhai, Y.3    Wang, A.4    Xu, J.5    Su, D.6    Bartlam, M.7    Rao, Z.8
  • 197
    • 34848866025 scopus 로고    scopus 로고
    • Ubiquinone-binding site mutations in the Saccharomyces cerevisiae succinate dehydrogenase generate superoxide and lead to the accumulation of succinate
    • [197] Szeto, S.S., Reinke, S.N., Sykes, B.D., Lemire, B.D., Ubiquinone-binding site mutations in the Saccharomyces cerevisiae succinate dehydrogenase generate superoxide and lead to the accumulation of succinate. J. Biol. Chem. 282 (2007), 27518–27526.
    • (2007) J. Biol. Chem. , vol.282 , pp. 27518-27526
    • Szeto, S.S.1    Reinke, S.N.2    Sykes, B.D.3    Lemire, B.D.4
  • 199
    • 33947530604 scopus 로고    scopus 로고
    • Clinical presentations, biochemical phenotypes, and genotype–phenotype correlations in patients with succinate dehydrogenase subunit B-associated pheochromocytomas and paragangliomas
    • [199] Timmers, H.J., Kozupa, A., Eisenhofer, G., Raygada, M., Adams, K.T., Solis, D., Lenders, J.W., Pacak, K., Clinical presentations, biochemical phenotypes, and genotype–phenotype correlations in patients with succinate dehydrogenase subunit B-associated pheochromocytomas and paragangliomas. J. Clin. Endocrinol. Metab. 92 (2007), 779–786.
    • (2007) J. Clin. Endocrinol. Metab. , vol.92 , pp. 779-786
    • Timmers, H.J.1    Kozupa, A.2    Eisenhofer, G.3    Raygada, M.4    Adams, K.T.5    Solis, D.6    Lenders, J.W.7    Pacak, K.8
  • 200
    • 0028884492 scopus 로고
    • Methylmalonic acid inhibits respiration in rat liver mitochondria
    • [200] Toyoshima, S., Watanabe, F., Saido, H., Miyatake, K., Nakano, Y., Methylmalonic acid inhibits respiration in rat liver mitochondria. J. Nutr. 125 (1995), 2846–2850.
    • (1995) J. Nutr. , vol.125 , pp. 2846-2850
    • Toyoshima, S.1    Watanabe, F.2    Saido, H.3    Miyatake, K.4    Nakano, Y.5
  • 201
    • 0034671429 scopus 로고    scopus 로고
    • Inhibition of Krebs cycle enzymes by hydrogen peroxide: a key role of [alpha]-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress
    • [201] Tretter, L., Adam-Vizi, V., Inhibition of Krebs cycle enzymes by hydrogen peroxide: a key role of [alpha]-ketoglutarate dehydrogenase in limiting NADH production under oxidative stress. J. Neurosci. 20 (2000), 8972–8979.
    • (2000) J. Neurosci. , vol.20 , pp. 8972-8979
    • Tretter, L.1    Adam-Vizi, V.2
  • 202
    • 4544226082 scopus 로고    scopus 로고
    • Generation of reactive oxygen species in the reaction catalyzed by alpha-ketoglutarate dehydrogenase
    • [202] Tretter, L., Adam-Vizi, V., Generation of reactive oxygen species in the reaction catalyzed by alpha-ketoglutarate dehydrogenase. J. Neurosci. 24 (2004), 7771–7778.
    • (2004) J. Neurosci. , vol.24 , pp. 7771-7778
    • Tretter, L.1    Adam-Vizi, V.2
  • 203
    • 84925388552 scopus 로고    scopus 로고
    • Measurement of ROS homeostasis in isolated mitochondria
    • [203] Tretter, L., Ambrus, A., Measurement of ROS homeostasis in isolated mitochondria. Methods Enzymol. 547 (2014), 199–223.
    • (2014) Methods Enzymol. , vol.547 , pp. 199-223
    • Tretter, L.1    Ambrus, A.2
  • 204
    • 0023097348 scopus 로고
    • Effect of succinate on mitochondrial lipid peroxidation. 2. The protective effect of succinate against functional and structural changes induced by lipid peroxidation
    • [204] Tretter, L., Szabados, G., Ando, A., Horvath, I., Effect of succinate on mitochondrial lipid peroxidation. 2. The protective effect of succinate against functional and structural changes induced by lipid peroxidation. J. Bioenerg. Biomembr. 19 (1987), 31–44.
    • (1987) J. Bioenerg. Biomembr. , vol.19 , pp. 31-44
    • Tretter, L.1    Szabados, G.2    Ando, A.3    Horvath, I.4
  • 206
    • 0025358947 scopus 로고
    • The protonmotive Q cycle. Energy transduction by coupling of proton translocation to electron transfer by the cytochrome bc1 complex
    • [206] Trumpower, B.L., The protonmotive Q cycle. Energy transduction by coupling of proton translocation to electron transfer by the cytochrome bc1 complex. J. Biol. Chem. 265 (1990), 11409–11412.
    • (1990) J. Biol. Chem. , vol.265 , pp. 11409-11412
    • Trumpower, B.L.1
  • 207
    • 0021861044 scopus 로고
    • Studies on the succinate dehydrogenating system. Isolation and properties of the mitochondrial succinate-ubiquinone reductase
    • [207] Tushurashvili, P.R., Gavrikova, E.V., Ledenev, A.N., Vinogradov, A.D., Studies on the succinate dehydrogenating system. Isolation and properties of the mitochondrial succinate-ubiquinone reductase. Biochim. Biophys. Acta 809 (1985), 145–159.
    • (1985) Biochim. Biophys. Acta , vol.809 , pp. 145-159
    • Tushurashvili, P.R.1    Gavrikova, E.V.2    Ledenev, A.N.3    Vinogradov, A.D.4
  • 208
    • 0027365338 scopus 로고
    • Evidence for allosteric regulation of succinyl-CoA synthetase
    • [208] Um, H.D., Klein, C., Evidence for allosteric regulation of succinyl-CoA synthetase. Biochem. J. 295:Pt 3 (1993), 821–826.
    • (1993) Biochem. J. , vol.295 , pp. 821-826
    • Um, H.D.1    Klein, C.2
  • 209
    • 10744232949 scopus 로고    scopus 로고
    • Homozygous Gly555Glu mutation in the nuclear-encoded 70 kDa flavoprotein gene causes instability of the respiratory chain complex II
    • [209] Van, C.R., Seneca, S., Smet, J., Van, H.R., Gerlo, E., Devreese, B., Van, B.J., Leroy, J.G., De, M.L., Lissens, W., Homozygous Gly555Glu mutation in the nuclear-encoded 70 kDa flavoprotein gene causes instability of the respiratory chain complex II. Am. J. Med. Genet. A 120A (2003), 13–18.
    • (2003) Am. J. Med. Genet. A , vol.120A , pp. 13-18
    • Van, C.R.1    Seneca, S.2    Smet, J.3    Van, H.R.4    Gerlo, E.5    Devreese, B.6    Van, B.J.7    Leroy, J.G.8    De, M.L.9    Lissens, W.10
  • 211
    • 84861830661 scopus 로고    scopus 로고
    • Central role of GABA in neuron–glia interactions
    • [211] Velez-Fort, M., Audinat, E., Angulo, M.C., Central role of GABA in neuron–glia interactions. Neuroscientist 18 (2012), 237–250.
    • (2012) Neuroscientist , vol.18 , pp. 237-250
    • Velez-Fort, M.1    Audinat, E.2    Angulo, M.C.3
  • 212
    • 78649328799 scopus 로고    scopus 로고
    • Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling
    • [212] Verdin, E., Hirschey, M.D., Finley, L.W., Haigis, M.C., Sirtuin regulation of mitochondria: energy production, apoptosis, and signaling. Trends Biochem. Sci. 35 (2010), 669–675.
    • (2010) Trends Biochem. Sci. , vol.35 , pp. 669-675
    • Verdin, E.1    Hirschey, M.D.2    Finley, L.W.3    Haigis, M.C.4
  • 213
    • 0032716145 scopus 로고    scopus 로고
    • The regeneration of reduced glutathione in rat forebrain mitochondria identifies metabolic pathways providing the NADPH required
    • [213] Vogel, R., Wiesinger, H., Hamprecht, B., Dringen, R., The regeneration of reduced glutathione in rat forebrain mitochondria identifies metabolic pathways providing the NADPH required. Neurosci. Lett. 275 (1999), 97–100.
    • (1999) Neurosci. Lett. , vol.275 , pp. 97-100
    • Vogel, R.1    Wiesinger, H.2    Hamprecht, B.3    Dringen, R.4
  • 214
    • 84898012702 scopus 로고    scopus 로고
    • Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases
    • [214] Wagner, G.R., Hirschey, M.D., Nonenzymatic protein acylation as a carbon stress regulated by sirtuin deacylases. Mol. Cell 54 (2014), 5–16.
    • (2014) Mol. Cell , vol.54 , pp. 5-16
    • Wagner, G.R.1    Hirschey, M.D.2
  • 215
    • 84885155285 scopus 로고    scopus 로고
    • Widespread and enzyme-independent Nepsilon-acetylation and Nepsilon-succinylation of proteins in the chemical conditions of the mitochondrial matrix
    • [215] Wagner, G.R., Payne, R.M., Widespread and enzyme-independent Nepsilon-acetylation and Nepsilon-succinylation of proteins in the chemical conditions of the mitochondrial matrix. J. Biol. Chem. 288 (2013), 29036–29045.
    • (2013) J. Biol. Chem. , vol.288 , pp. 29036-29045
    • Wagner, G.R.1    Payne, R.M.2
  • 216
    • 84922376793 scopus 로고    scopus 로고
    • GABAergic system in the endocrine pancreas: a new target for diabetes treatment
    • [216] Wan, Y., Wang, Q., Prud'homme, G.J., GABAergic system in the endocrine pancreas: a new target for diabetes treatment. Diabetes Metab Syndr. Obes. 8 (2015), 79–87.
    • (2015) Diabetes Metab Syndr. Obes. , vol.8 , pp. 79-87
    • Wan, Y.1    Wang, Q.2    Prud'homme, G.J.3
  • 217
    • 0013667597 scopus 로고
    • The pathway of itaconate metabolism by liver mitochondria
    • [217] WANG, S.F., ADLER, J., Lardy, H.A., The pathway of itaconate metabolism by liver mitochondria. J. Biol. Chem. 236 (1961), 26–30.
    • (1961) J. Biol. Chem. , vol.236 , pp. 26-30
    • WANG, S.F.1    ADLER, J.2    Lardy, H.A.3
  • 218
    • 0036525722 scopus 로고    scopus 로고
    • Construction of heme enzymes: four approaches
    • [218] Watanabe, Y., Construction of heme enzymes: four approaches. Curr. Opin. Chem. Biol. 6 (2002), 208–216.
    • (2002) Curr. Opin. Chem. Biol. , vol.6 , pp. 208-216
    • Watanabe, Y.1
  • 220
    • 84883307077 scopus 로고    scopus 로고
    • Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation
    • [220] Weinert, B.T., Scholz, C., Wagner, S.A., Iesmantavicius, V., Su, D., Daniel, J.A., Choudhary, C., Lysine succinylation is a frequently occurring modification in prokaryotes and eukaryotes and extensively overlaps with acetylation. Cell Rep. 4 (2013), 842–851.
    • (2013) Cell Rep. , vol.4 , pp. 842-851
    • Weinert, B.T.1    Scholz, C.2    Wagner, S.A.3    Iesmantavicius, V.4    Su, D.5    Daniel, J.A.6    Choudhary, C.7
  • 221
    • 77954611048 scopus 로고    scopus 로고
    • Metabolomic patterns in glioblastoma and changes during radiotherapy: a clinical microdialysis study
    • [221] Wibom, C., Surowiec, I., Moren, L., Bergstrom, P., Johansson, M., Antti, H., Bergenheim, A.T., Metabolomic patterns in glioblastoma and changes during radiotherapy: a clinical microdialysis study. J. Proteome Res. 9 (2010), 2909–2919.
    • (2010) J. Proteome Res. , vol.9 , pp. 2909-2919
    • Wibom, C.1    Surowiec, I.2    Moren, L.3    Bergstrom, P.4    Johansson, M.5    Antti, H.6    Bergenheim, A.T.7
  • 222
    • 0027157645 scopus 로고
    • Phosphate affects the distribution of flux control among the enzymes of oxidative phosphorylation in rat skeletal muscle mitochondria
    • [222] Wisniewski, E., Kunz, W.S., Gellerich, F.N., Phosphate affects the distribution of flux control among the enzymes of oxidative phosphorylation in rat skeletal muscle mitochondria. J. Biol. Chem. 268 (1993), 9343–9346.
    • (1993) J. Biol. Chem. , vol.268 , pp. 9343-9346
    • Wisniewski, E.1    Kunz, W.S.2    Gellerich, F.N.3
  • 223
    • 0035970294 scopus 로고    scopus 로고
    • An expressed sequence tag (EST) data mining strategy succeeding in the discovery of new G-protein coupled receptors
    • [223] Wittenberger, T., Schaller, H.C., Hellebrand, S., An expressed sequence tag (EST) data mining strategy succeeding in the discovery of new G-protein coupled receptors. J. Mol. Biol. 307 (2001), 799–813.
    • (2001) J. Mol. Biol. , vol.307 , pp. 799-813
    • Wittenberger, T.1    Schaller, H.C.2    Hellebrand, S.3
  • 224
    • 84862632865 scopus 로고    scopus 로고
    • Inhibition of alpha-KG-dependent histone and DNA demethylases by fumarate and succinate that are accumulated in mutations of FH and SDH tumor suppressors
    • [224] Xiao, M., Yang, H., Xu, W., Ma, S., Lin, H., Zhu, H., Liu, L., Liu, Y., Yang, C., Xu, Y., Zhao, S., Ye, D., Xiong, Y., Guan, K.L., Inhibition of alpha-KG-dependent histone and DNA demethylases by fumarate and succinate that are accumulated in mutations of FH and SDH tumor suppressors. Genes Dev. 26 (2012), 1326–1338.
    • (2012) Genes Dev. , vol.26 , pp. 1326-1338
    • Xiao, M.1    Yang, H.2    Xu, W.3    Ma, S.4    Lin, H.5    Zhu, H.6    Liu, L.7    Liu, Y.8    Yang, C.9    Xu, Y.10    Zhao, S.11    Ye, D.12    Xiong, Y.13    Guan, K.L.14
  • 226
    • 84911465693 scopus 로고    scopus 로고
    • Triggering the succinate receptor GPR91 enhances pressure overload-induced right ventricular hypertrophy
    • [226] Yang, L., Yu, D., Fan, H.H., Feng, Y., Hu, L., Zhang, W.Y., Zhou, K., Mo, X.M., Triggering the succinate receptor GPR91 enhances pressure overload-induced right ventricular hypertrophy. Int. J. Clin. Exp. Pathol. 7 (2014), 5415–5428.
    • (2014) Int. J. Clin. Exp. Pathol. , vol.7 , pp. 5415-5428
    • Yang, L.1    Yu, D.2    Fan, H.H.3    Feng, Y.4    Hu, L.5    Zhang, W.Y.6    Zhou, K.7    Mo, X.M.8
  • 227
    • 84922742515 scopus 로고    scopus 로고
    • Influence of succinylation on the conformation of yak casein micelles
    • [227] Yang, M., Cui, N., Fang, Y., Shi, Y., Yang, J., Wang, J., Influence of succinylation on the conformation of yak casein micelles. Food Chem. 179 (2015), 246–252.
    • (2015) Food Chem. , vol.179 , pp. 246-252
    • Yang, M.1    Cui, N.2    Fang, Y.3    Shi, Y.4    Yang, J.5    Wang, J.6
  • 228
    • 34249022235 scopus 로고    scopus 로고
    • Snapshot: genetic mouse models of cancer
    • [228] Zender, L., Zuber, J., Lowe, S.W., Snapshot: genetic mouse models of cancer. Cell, 129, 2007, 838.
    • (2007) Cell , vol.129 , pp. 838
    • Zender, L.1    Zuber, J.2    Lowe, S.W.3
  • 229
    • 78650516004 scopus 로고    scopus 로고
    • Identification of lysine succinylation as a new post-translational modification
    • [229] Zhang, Z., Tan, M., Xie, Z., Dai, L., Chen, Y., Zhao, Y., Identification of lysine succinylation as a new post-translational modification. Nat. Chem. Biol. 7 (2011), 58–63.
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 58-63
    • Zhang, Z.1    Tan, M.2    Xie, Z.3    Dai, L.4    Chen, Y.5    Zhao, Y.6
  • 230
    • 1842431424 scopus 로고    scopus 로고
    • Study of succinylated food proteins by Raman spectroscopy
    • [230] Zhao, Y., Ma, C.Y., Yuen, S.N., Phillips, D.L., Study of succinylated food proteins by Raman spectroscopy. J. Agric. Food Chem. 52 (2004), 1815–1823.
    • (2004) J. Agric. Food Chem. , vol.52 , pp. 1815-1823
    • Zhao, Y.1    Ma, C.Y.2    Yuen, S.N.3    Phillips, D.L.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.