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Volumn 9, Issue 11, 2014, Pages

Metabolic profiling of alternative NAD biosynthetic routes in mouse tissues

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE NUCLEOTIDE; GLUTAMIC ACID; GLUTAMINE; ISOENZYME; NICOTINAMIDE NUCLEOTIDE ADENYLYLTRANSFERASE; NICOTINIC ACID ADENINE DINUCLEOTIDE PHOSPHATE; PHOSPHATE; POLYPHOSPHATE; NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINIC ACID ADENINE DINUCLEOTIDE;

EID: 84912572145     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0113939     Document Type: Article
Times cited : (121)

References (64)
  • 2
    • 80054771657 scopus 로고    scopus 로고
    • The role of mammalian sirtuins in the regulation of metabolism, aging, and longevity
    • Satoh A, Stein L, Imai S (2011) The role of mammalian sirtuins in the regulation of metabolism, aging, and longevity. Handb Exp Pharmacol 206: 125-162.
    • (2011) Handb Exp Pharmacol , vol.206 , pp. 125-162
    • Satoh, A.1    Stein, L.2    Imai, S.3
  • 3
    • 0023219685 scopus 로고
    • Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate
    • Clapper DL, Walseth TF, Dargie PJ, Lee HC (1987) Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate. J Biol Chem 262: 9561-9568.
    • (1987) J Biol Chem , vol.262 , pp. 9561-9568
    • Clapper, D.L.1    Walseth, T.F.2    Dargie, P.J.3    Lee, H.C.4
  • 4
    • 84883491871 scopus 로고    scopus 로고
    • The importance of NAMPT/NAD/SIRT1 in the systemic regulation of metabolism and ageing
    • Imai S, Yoshino J (2013) The importance of NAMPT/NAD/SIRT1 in the systemic regulation of metabolism and ageing. Diabetes Obes Metab 15: 26-33.
    • (2013) Diabetes Obes Metab , vol.15 , pp. 26-33
    • Imai, S.1    Yoshino, J.2
  • 6
    • 52049117617 scopus 로고    scopus 로고
    • Enzymology of mammalian NAD metabolism in health and disease
    • Magni G, Orsomando G, Raffelli N, Ruggieri S (2008) Enzymology of mammalian NAD metabolism in health and disease. Front Biosci 13: 6135-6154.
    • (2008) Front Biosci , vol.13 , pp. 6135-6154
    • Magni, G.1    Orsomando, G.2    Raffelli, N.3    Ruggieri, S.4
  • 8
    • 79957944139 scopus 로고    scopus 로고
    • NMN/NaMN adenylyltransferase (NMNAT) and NAD kinase (NADK) inhibitors: Chemistry and potential therapeutic applications
    • Petrelli R, Felczak K, Cappellacci L (2011) NMN/NaMN adenylyltransferase (NMNAT) and NAD kinase (NADK) inhibitors: chemistry and potential therapeutic applications. Curr Med Chem 18: 1973-1992.
    • (2011) Curr Med Chem , vol.18 , pp. 1973-1992
    • Petrelli, R.1    Felczak, K.2    Cappellacci, L.3
  • 9
    • 79953165649 scopus 로고    scopus 로고
    • Synthesis and biological activity of novel N6-substituted and 2, N6-disubstituted adenine ribo- and 3′-C-methyl-ribonucleosides as antitumor agents
    • Cappellacci L, Petrelli R, Franchetti P, Vita P, Kusumanchi P, et al. (2011) Synthesis and biological activity of novel N6-substituted and 2, N6-disubstituted adenine ribo- and 3′-C-methyl-ribonucleosides as antitumor agents. Eur J Med Chem 46: 1499-1504.
    • (2011) Eur J Med Chem , vol.46 , pp. 1499-1504
    • Cappellacci, L.1    Petrelli, R.2    Franchetti, P.3    Vita, P.4    Kusumanchi, P.5
  • 10
  • 11
    • 84884596730 scopus 로고    scopus 로고
    • Diversification of NAD biological role: The importance of location
    • Di Stefano M, Conforti L (2013) Diversification of NAD biological role: the importance of location. Febs J 280: 4711-4728.
    • (2013) Febs J , vol.280 , pp. 4711-4728
    • Di Stefano, M.1    Conforti, L.2
  • 12
    • 84867877340 scopus 로고    scopus 로고
    • The NAD metabolome - A key determinant of cancer cell biology
    • Chiarugi A, Dolle C, Felici R, Ziegler M (2012) The NAD metabolome - a key determinant of cancer cell biology. Nat Rev Cancer 12: 741-752.
    • (2012) Nat Rev Cancer , vol.12 , pp. 741-752
    • Chiarugi, A.1    Dolle, C.2    Felici, R.3    Ziegler, M.4
  • 14
    • 70449213670 scopus 로고
    • Biosynthesis of diphosphopyridine nucleotide. II. Enzymatic aspects
    • Preiss J, Handler P (1958) Biosynthesis of diphosphopyridine nucleotide. II. Enzymatic aspects. J Biol Chem 233: 493-500.
    • (1958) J Biol Chem , vol.233 , pp. 493-500
    • Preiss, J.1    Handler, P.2
  • 15
    • 1842534935 scopus 로고    scopus 로고
    • Structure and function of nicotinamide mononucleotide adenylyltransferase
    • Magni G, Amici A, Emanuelli M, Orsomando G, Raffaelli N, et al. (2004) Structure and function of nicotinamide mononucleotide adenylyltransferase. Curr Med Chem 11: 873-885.
    • (2004) Curr Med Chem , vol.11 , pp. 873-885
    • Magni, G.1    Amici, A.2    Emanuelli, M.3    Orsomando, G.4    Raffaelli, N.5
  • 16
    • 27744501798 scopus 로고    scopus 로고
    • Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms
    • Berger F, Lau C, Dahlmann M, Ziegler M (2005) Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms. J Biol Chem 280: 36334-36341.
    • (2005) J Biol Chem , vol.280 , pp. 36334-36341
    • Berger, F.1    Lau, C.2    Dahlmann, M.3    Ziegler, M.4
  • 17
    • 68949210360 scopus 로고    scopus 로고
    • Nicotinamide/nicotinic acid mononucleotide adenylyltransferase, new insights into an ancient enzyme
    • Zhai RG, Rizzi M, Garavaglia S (2009) Nicotinamide/nicotinic acid mononucleotide adenylyltransferase, new insights into an ancient enzyme. Cell Mol Life Sci 66: 2805-2818.
    • (2009) Cell Mol Life Sci , vol.66 , pp. 2805-2818
    • Zhai, R.G.1    Rizzi, M.2    Garavaglia, S.3
  • 18
    • 84871751837 scopus 로고    scopus 로고
    • Simultaneous single-sample determination of NMNAT isozyme activities in mouse tissues
    • Orsomando G, Cialabrini L, Amici A, Mazzola F, Ruggieri S, et al. (2012) Simultaneous single-sample determination of NMNAT isozyme activities in mouse tissues. PLoS One 7: e53271.
    • (2012) PLoS One , vol.7 , pp. e53271
    • Orsomando, G.1    Cialabrini, L.2    Amici, A.3    Mazzola, F.4    Ruggieri, S.5
  • 19
    • 34247500849 scopus 로고    scopus 로고
    • Initial-rate kinetics of human NMN-adenylyltransferases: Substrate and metal ion specificity, inhibition by products and multisubstrate analogues, and isozyme contributions to NAD+ biosynthesis
    • Sorci L, Cimadamore F, Scotti S, Petrelli R, Cappellacci L, et al. (2007) Initial-rate kinetics of human NMN-adenylyltransferases: substrate and metal ion specificity, inhibition by products and multisubstrate analogues, and isozyme contributions to NAD+ biosynthesis. Biochemistry 46: 4912-4922.
    • (2007) Biochemistry , vol.46 , pp. 4912-4922
    • Sorci, L.1    Cimadamore, F.2    Scotti, S.3    Petrelli, R.4    Cappellacci, L.5
  • 21
    • 79960605733 scopus 로고    scopus 로고
    • Reducing expression of NAD+ synthesizing enzyme NMNAT1 does not affect the rate of Wallerian degeneration
    • Conforti L, Janeckova L, Wagner D, Mazzola F, Cialabrini L, et al. (2011) Reducing expression of NAD+ synthesizing enzyme NMNAT1 does not affect the rate of Wallerian degeneration. Febs J 278: 2666-2679.
    • (2011) Febs J , vol.278 , pp. 2666-2679
    • Conforti, L.1    Janeckova, L.2    Wagner, D.3    Mazzola, F.4    Cialabrini, L.5
  • 22
    • 0042377362 scopus 로고    scopus 로고
    • Eukaryotic NAD+ synthetase Qns1 contains an essential, obligate intramolecular thiol glutamine amidotransferase domain related to nitrilase
    • Bieganowski P, Pace HC, Brenner C (2003) Eukaryotic NAD+ synthetase Qns1 contains an essential, obligate intramolecular thiol glutamine amidotransferase domain related to nitrilase. J Biol Chem 278: 33049-33055.
    • (2003) J Biol Chem , vol.278 , pp. 33049-33055
    • Bieganowski, P.1    Pace, H.C.2    Brenner, C.3
  • 23
    • 33846922557 scopus 로고    scopus 로고
    • A subsystems-based approach to the identification of drug targets in bacterial pathogens
    • Osterman AL, Begley TP (2007) A subsystems-based approach to the identification of drug targets in bacterial pathogens. Prog Drug Res 64: 133-170.
    • (2007) Prog Drug Res , vol.64 , pp. 133-170
    • Osterman, A.L.1    Begley, T.P.2
  • 24
    • 84881500396 scopus 로고    scopus 로고
    • Rescue of peripheral and CNS axon defects in mice lacking NMNAT2
    • Gilley J, Adalbert R, Yu G, Coleman MP (2013) Rescue of peripheral and CNS axon defects in mice lacking NMNAT2. J Neurosci 33: 13410-13424.
    • (2013) J Neurosci , vol.33 , pp. 13410-13424
    • Gilley, J.1    Adalbert, R.2    Yu, G.3    Coleman, M.P.4
  • 25
    • 84889001380 scopus 로고    scopus 로고
    • Model of tryptophan metabolism, readily scalable using tissue-specific gene expression data
    • Stavrum AK, Heiland I, Schuster S, Puntervoll P, Ziegler M (2013) Model of tryptophan metabolism, readily scalable using tissue-specific gene expression data. J Biol Chem 288: 34555-34566.
    • (2013) J Biol Chem , vol.288 , pp. 34555-34566
    • Stavrum, A.K.1    Heiland, I.2    Schuster, S.3    Puntervoll, P.4    Ziegler, M.5
  • 27
    • 0035195636 scopus 로고    scopus 로고
    • Wallerian degeneration of injured axons and synapses is delayed by a Ube4b/Nmnat chimeric gene
    • Mack TG, Reiner M, Beirowski B, Mi W, Emanuelli M, et al. (2001) Wallerian degeneration of injured axons and synapses is delayed by a Ube4b/Nmnat chimeric gene. Nat Neurosci 4: 1199-1206.
    • (2001) Nat Neurosci , vol.4 , pp. 1199-1206
    • Mack, T.G.1    Reiner, M.2    Beirowski, B.3    Mi, W.4    Emanuelli, M.5
  • 28
    • 77649295811 scopus 로고    scopus 로고
    • NAD+ metabolite levels as a function of vitamins and calorie restriction: Evidence for different mechanisms of longevity
    • Evans C, Bogan KL, Song P, Burant CF, Kennedy RT, et al. (2010) NAD+ metabolite levels as a function of vitamins and calorie restriction: evidence for different mechanisms of longevity. BMC Chem Biol 10: 2.
    • (2010) BMC Chem Biol , vol.10 , pp. 2
    • Evans, C.1    Bogan, K.L.2    Song, P.3    Burant, C.F.4    Kennedy, R.T.5
  • 29
    • 33646150202 scopus 로고    scopus 로고
    • The simultaneous measurement of nicotinamide adenine dinucleotide and related compounds by liquid chromatography/electrospray ionization tandem mass spectrometry
    • Yamada K, Hara N, Shibata T, Osago H, Tsuchiya M (2006) The simultaneous measurement of nicotinamide adenine dinucleotide and related compounds by liquid chromatography/electrospray ionization tandem mass spectrometry. Anal Biochem 352: 282-285.
    • (2006) Anal Biochem , vol.352 , pp. 282-285
    • Yamada, K.1    Hara, N.2    Shibata, T.3    Osago, H.4    Tsuchiya, M.5
  • 30
    • 64049094455 scopus 로고    scopus 로고
    • Detection and pharmacological modulation of nicotinamide mononucleotide (NMN) in vitro and in vivo
    • Formentini L, Moroni F, Chiarugi A (2009) Detection and pharmacological modulation of nicotinamide mononucleotide (NMN) in vitro and in vivo. Biochem Pharmacol 77: 1612-1620.
    • (2009) Biochem Pharmacol , vol.77 , pp. 1612-1620
    • Formentini, L.1    Moroni, F.2    Chiarugi, A.3
  • 31
    • 84862022077 scopus 로고    scopus 로고
    • The NAD(+) precursor nicotinamide riboside enhances oxidative metabolism and protects against high-fat diet-induced obesity
    • Canto C, Houtkooper RH, Pirinen E, Youn DY, Oosterveer MH, et al. (2012) The NAD(+) precursor nicotinamide riboside enhances oxidative metabolism and protects against high-fat diet-induced obesity. Cell Metab 15: 838-847.
    • (2012) Cell Metab , vol.15 , pp. 838-847
    • Canto, C.1    Houtkooper, R.H.2    Pirinen, E.3    Youn, D.Y.4    Oosterveer, M.H.5
  • 32
    • 0014029054 scopus 로고
    • The pyridine nucleotide cycle
    • Gholson RK (1966) The pyridine nucleotide cycle. Nature 212: 933-935.
    • (1966) Nature , vol.212 , pp. 933-935
    • Gholson, R.K.1
  • 33
    • 0015500271 scopus 로고
    • The management of nicotinamide and nicotinic acid in the mouse
    • Collins PB, Chaykin S (1972) The management of nicotinamide and nicotinic acid in the mouse. J Biol Chem 247: 778-783.
    • (1972) J Biol Chem , vol.247 , pp. 778-783
    • Collins, P.B.1    Chaykin, S.2
  • 34
    • 0025134583 scopus 로고
    • Importance of nicotinamide as an NAD precursor in the human erythrocyte
    • Micheli V, Simmonds HA, Sestini S, Ricci C (1990) Importance of nicotinamide as an NAD precursor in the human erythrocyte. Arch Biochem Biophys 283: 40-45.
    • (1990) Arch Biochem Biophys , vol.283 , pp. 40-45
    • Micheli, V.1    Simmonds, H.A.2    Sestini, S.3    Ricci, C.4
  • 35
    • 62149148872 scopus 로고    scopus 로고
    • Nicotinamide phosphoribosyltransferase (Nampt): A link between NAD biology, metabolism, and diseases
    • Imai S (2009) Nicotinamide phosphoribosyltransferase (Nampt): a link between NAD biology, metabolism, and diseases. Curr Pharm Des 15: 20-28.
    • (2009) Curr Pharm des , vol.15 , pp. 20-28
    • Imai, S.1
  • 36
    • 79957549799 scopus 로고    scopus 로고
    • Pathways and subcellular compartmentation of NAD biosynthesis in human cells: From entry of extracellular precursors to mitochondrial NAD generation
    • Nikiforov A, Dolle C, Niere M, Ziegler M (2011) Pathways and subcellular compartmentation of NAD biosynthesis in human cells: from entry of extracellular precursors to mitochondrial NAD generation. J Biol Chem 286: 21767-21778.
    • (2011) J Biol Chem , vol.286 , pp. 21767-21778
    • Nikiforov, A.1    Dolle, C.2    Niere, M.3    Ziegler, M.4
  • 37
    • 0029012892 scopus 로고
    • Assay methods for nicotinamide mononucleotide adenylyltransferase of wide applicability
    • Balducci E, Emanuelli M, Raffaelli N, Ruggieri S, Amici A, et al. (1995) Assay methods for nicotinamide mononucleotide adenylyltransferase of wide applicability. Anal Biochem 228: 64-68.
    • (1995) Anal Biochem , vol.228 , pp. 64-68
    • Balducci, E.1    Emanuelli, M.2    Raffaelli, N.3    Ruggieri, S.4    Amici, A.5
  • 38
    • 62549094038 scopus 로고    scopus 로고
    • Nicotinamide mononucleotide synthetase is the key enzyme for an alternative route of NAD biosynthesis in Francisella tularensis
    • Sorci L, Martynowski D, Rodionov DA, Eyobo Y, Zogaj X, et al. (2009) Nicotinamide mononucleotide synthetase is the key enzyme for an alternative route of NAD biosynthesis in Francisella tularensis. Proc Natl Acad Sci U S A 106: 3083-3088.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 3083-3088
    • Sorci, L.1    Martynowski, D.2    Rodionov, D.A.3    Eyobo, Y.4    Zogaj, X.5
  • 39
    • 0026409264 scopus 로고
    • High-performance liquid chromatographic determination of pyrophosphate in the presence of a 20,000-fold excess of orthophosphate
    • Yoza N, Akazaki I, Nakazato T, Ueda N, Kodama H, et al. (1991) High-performance liquid chromatographic determination of pyrophosphate in the presence of a 20,000-fold excess of orthophosphate. Anal Biochem 199: 279-285.
    • (1991) Anal Biochem , vol.199 , pp. 279-285
    • Yoza, N.1    Akazaki, I.2    Nakazato, T.3    Ueda, N.4    Kodama, H.5
  • 40
    • 0016192094 scopus 로고
    • Thermodynamic parameters for the hydrolysis of inorganic pyrophosphate at pH 7.4 as a function of (Mg2+), (K+), and ionic strength determined from equilibrium studies of the reaction
    • Flodgaard H, Fleron P (1974) Thermodynamic parameters for the hydrolysis of inorganic pyrophosphate at pH 7.4 as a function of (Mg2+), (K+), and ionic strength determined from equilibrium studies of the reaction. J Biol Chem 249: 3465-3474.
    • (1974) J Biol Chem , vol.249 , pp. 3465-3474
    • Flodgaard, H.1    Fleron, P.2
  • 41
    • 0037081860 scopus 로고    scopus 로고
    • A novel cycling assay for cellular cADP-ribose with nanomolar sensitivity
    • Graeff R, Lee HC (2002) A novel cycling assay for cellular cADP-ribose with nanomolar sensitivity. Biochem J 361: 379-384.
    • (2002) Biochem J , vol.361 , pp. 379-384
    • Graeff, R.1    Lee, H.C.2
  • 43
    • 0025263919 scopus 로고
    • Partial purification and properties of nicotinamide adenine dinucleotide synthetase from human erythrocytes: Evidence that enzyme activity is a sensitive indicator of lead exposure
    • Zerez CR, Wong MD, Tanaka KR (1990) Partial purification and properties of nicotinamide adenine dinucleotide synthetase from human erythrocytes: evidence that enzyme activity is a sensitive indicator of lead exposure. Blood 75: 1576-1582.
    • (1990) Blood , vol.75 , pp. 1576-1582
    • Zerez, C.R.1    Wong, M.D.2    Tanaka, K.R.3
  • 44
    • 0037500302 scopus 로고    scopus 로고
    • Molecular identification of human glutamine- and ammonia-dependent NAD synthetases. Carbon-nitrogen hydrolase domain confers glutamine dependency
    • Hara N, Yamada K, Terashima M, Osago H, Shimoyama M, et al. (2003) Molecular identification of human glutamine- and ammonia-dependent NAD synthetases. Carbon-nitrogen hydrolase domain confers glutamine dependency. J Biol Chem 278: 10914-10921.
    • (2003) J Biol Chem , vol.278 , pp. 10914-10921
    • Hara, N.1    Yamada, K.2    Terashima, M.3    Osago, H.4    Shimoyama, M.5
  • 45
    • 0033591302 scopus 로고    scopus 로고
    • Hypoxanthine-guanine phosphoribosyltransferase deficiency and erythrocyte synthesis of pyridine coenzymes
    • Micheli V, Sestini S, Rocchigiani M, Jacomelli G, Manzoni F, et al. (1999) Hypoxanthine-guanine phosphoribosyltransferase deficiency and erythrocyte synthesis of pyridine coenzymes. Life Sci 64: 2479-2487.
    • (1999) Life Sci , vol.64 , pp. 2479-2487
    • Micheli, V.1    Sestini, S.2    Rocchigiani, M.3    Jacomelli, G.4    Manzoni, F.5
  • 46
    • 77953139085 scopus 로고    scopus 로고
    • Unique expression pattern of human nicotinamide mononucleotide adenylyltransferase isozymes in red blood cells
    • Di Stefano M, Galassi L, Magni G (2010) Unique expression pattern of human nicotinamide mononucleotide adenylyltransferase isozymes in red blood cells. Blood Cells Mol Dis 45: 33-39.
    • (2010) Blood Cells Mol Dis , vol.45 , pp. 33-39
    • Di Stefano, M.1    Galassi, L.2    Magni, G.3
  • 47
    • 0035808313 scopus 로고    scopus 로고
    • Molecular cloning, chromosomal localization, tissue mRNA levels, bacterial expression, and enzymatic properties of human NMN adenylyltransferase
    • Emanuelli M, Carnevali F, Saccucci F, Pierella F, Amici A, et al. (2001) Molecular cloning, chromosomal localization, tissue mRNA levels, bacterial expression, and enzymatic properties of human NMN adenylyltransferase. J Biol Chem 276: 406-412.
    • (2001) J Biol Chem , vol.276 , pp. 406-412
    • Emanuelli, M.1    Carnevali, F.2    Saccucci, F.3    Pierella, F.4    Amici, A.5
  • 48
    • 0038644836 scopus 로고    scopus 로고
    • Structural characterization of a human cytosolic NMN/NaMN adenylyltransferase and implication in human NAD biosynthesis
    • Zhang X, Kurnasov OV, Karthikeyan S, Grishin NV, Osterman AL, et al. (2003) Structural characterization of a human cytosolic NMN/NaMN adenylyltransferase and implication in human NAD biosynthesis. J Biol Chem 278: 13503-13511.
    • (2003) J Biol Chem , vol.278 , pp. 13503-13511
    • Zhang, X.1    Kurnasov, O.V.2    Karthikeyan, S.3    Grishin, N.V.4    Osterman, A.L.5
  • 49
    • 0942279500 scopus 로고    scopus 로고
    • Characterization of human brain nicotinamide 5′-mononucleotide adenylyltransferase-2 and expression in human pancreas
    • Yalowitz JA, Xiao S, Biju MP, Antony AC, Cummings OW, et al. (2004) Characterization of human brain nicotinamide 5′-mononucleotide adenylyltransferase-2 and expression in human pancreas. Biochem J 377: 317-326.
    • (2004) Biochem J , vol.377 , pp. 317-326
    • Yalowitz, J.A.1    Xiao, S.2    Biju, M.P.3    Antony, A.C.4    Cummings, O.W.5
  • 51
    • 0000198395 scopus 로고
    • Concentrations of Metabolites in Animal Tisuues
    • Bergmeyer HU, , editor., Academic Press, Inc: Verlag Chemie Weinheim
    • Williamson DH, Brosnan JT (1974) Concentrations of Metabolites in Animal Tisuues. In: Bergmeyer HU, , editor., Methods of Enzymatic Analysis. Academic Press, Inc: Verlag Chemie Weinheim. pp. 2267-2300.
    • (1974) Methods of Enzymatic Analysis , pp. 2267-2300
    • Williamson, D.H.1    Brosnan, J.T.2
  • 52
    • 0001166474 scopus 로고
    • Reversible enzymatic synthesis of diphosphopyridine nucleotide and inorganic pyrophosphate
    • Kornberg A (1950) Reversible enzymatic synthesis of diphosphopyridine nucleotide and inorganic pyrophosphate. J Biol Chem 182: 779-793.
    • (1950) J Biol Chem , vol.182 , pp. 779-793
    • Kornberg, A.1
  • 53
    • 0032531011 scopus 로고    scopus 로고
    • A novel deamido-NAD+-binding site revealed by the trapped NAD-adenylate intermediate in the NAD+ synthetase structure
    • Rizzi M, Bolognesi M, Coda A (1998) A novel deamido-NAD+-binding site revealed by the trapped NAD-adenylate intermediate in the NAD+ synthetase structure. Structure 6: 1129-1140.
    • (1998) Structure , vol.6 , pp. 1129-1140
    • Rizzi, M.1    Bolognesi, M.2    Coda, A.3
  • 54
    • 0029113318 scopus 로고
    • Standard free energy change for the hydrolysis of the alpha, beta-phosphoanhydride bridge in ATP
    • Frey PA, Arabshahi A (1995) Standard free energy change for the hydrolysis of the alpha, beta-phosphoanhydride bridge in ATP. Biochemistry 34: 11307-11310.
    • (1995) Biochemistry , vol.34 , pp. 11307-11310
    • Frey, P.A.1    Arabshahi, A.2
  • 55
    • 0017275889 scopus 로고
    • Magnitude and significance of NAD turnover in human cell line D98/AH2
    • Rechsteiner M, Hillyard D, Olivera BM (1976) Magnitude and significance of NAD turnover in human cell line D98/AH2. Nature 259: 695-696.
    • (1976) Nature , vol.259 , pp. 695-696
    • Rechsteiner, M.1    Hillyard, D.2    Olivera, B.M.3
  • 56
    • 0014082605 scopus 로고
    • The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver
    • Williamson DH, Lund P, Krebs HA (1967) The redox state of free nicotinamide-adenine dinucleotide in the cytoplasm and mitochondria of rat liver. Biochem J 103: 514-527.
    • (1967) Biochem J , vol.103 , pp. 514-527
    • Williamson, D.H.1    Lund, P.2    Krebs, H.A.3
  • 57
    • 0015278655 scopus 로고
    • Control of the redox state of the nicotinamide-adenine dinucleotide couple in rat liver cytoplasm
    • Stubbs M, Veech RL, Krebs HA (1972) Control of the redox state of the nicotinamide-adenine dinucleotide couple in rat liver cytoplasm. Biochem J 126: 59-65.
    • (1972) Biochem J , vol.126 , pp. 59-65
    • Stubbs, M.1    Veech, R.L.2    Krebs, H.A.3
  • 58
    • 84876987935 scopus 로고    scopus 로고
    • Subcellular localization determines the stability and axon protective capacity of axon survival factor Nmnat2
    • Milde S, Gilley J, Coleman MP (2013) Subcellular localization determines the stability and axon protective capacity of axon survival factor Nmnat2. PLoS Biol 11: e1001539.
    • (2013) PLoS Biol , vol.11 , pp. e1001539
    • Milde, S.1    Gilley, J.2    Coleman, M.P.3
  • 59
    • 84901848955 scopus 로고    scopus 로고
    • Effective treatment of mitochondrial myopathy by nicotinamide riboside, a vitamin B3
    • Khan NA, Auranen M, Paetau I, Pirinen E, Euro L, et al. (2014) Effective treatment of mitochondrial myopathy by nicotinamide riboside, a vitamin B3. EMBO Mol Med 6: 721-731.
    • (2014) EMBO Mol Med , vol.6 , pp. 721-731
    • Khan, N.A.1    Auranen, M.2    Paetau, I.3    Pirinen, E.4    Euro, L.5
  • 60
    • 77955276934 scopus 로고    scopus 로고
    • Nrk2b-mediated NAD+ production regulates cell adhesion and is required for muscle morphogenesis in vivo: Nrk2b and NAD+ in muscle morphogenesis
    • Goody MF, Kelly MW, Lessard KN, Khalil A, Henry CA (2010) Nrk2b-mediated NAD+ production regulates cell adhesion and is required for muscle morphogenesis in vivo: Nrk2b and NAD+ in muscle morphogenesis. Dev Biol 344: 809-826.
    • (2010) Dev Biol , vol.344 , pp. 809-826
    • Goody, M.F.1    Kelly, M.W.2    Lessard, K.N.3    Khalil, A.4    Henry, C.A.5
  • 61
    • 84886664594 scopus 로고    scopus 로고
    • Enzymes that control the conversion of L-tryptophan-nicotinamide and the urinary excretion ratio (N(1)-methyl-2-pyridone-5-carboxamide + N(1)-methyl-4-pyridone-3-carboxamide)/N(1)-methylnicotinamide in mice
    • Shibata K, Morita N, Shibata Y, Fukuwatari T (2013) Enzymes that control the conversion of L-tryptophan-nicotinamide and the urinary excretion ratio (N(1)-methyl-2-pyridone-5-carboxamide + N(1)-methyl-4-pyridone-3-carboxamide)/N(1)-methylnicotinamide in mice. Biosci Biotechnol Biochem 77: 2105-2111.
    • (2013) Biosci Biotechnol Biochem , vol.77 , pp. 2105-2111
    • Shibata, K.1    Morita, N.2    Shibata, Y.3    Fukuwatari, T.4
  • 62
    • 84901446681 scopus 로고    scopus 로고
    • Deficiency of Nicotinamide Mononucleotide Adenylyltransferase 3 (Nmnat3) Causes Hemolytic Anemia by Altering the Glycolytic Flow in Mature Erythrocytes
    • Hikosaka K, Ikutani M, Shito M, Kazuma K, Gulshan M, et al . (2014) Deficiency of Nicotinamide Mononucleotide Adenylyltransferase 3 (Nmnat3) Causes Hemolytic Anemia by Altering the Glycolytic Flow in Mature Erythrocytes. J Biol Chem 289: 14796-14811.
    • (2014) J Biol Chem , vol.289 , pp. 14796-14811
    • Hikosaka, K.1    Ikutani, M.2    Shito, M.3    Kazuma, K.4    Gulshan, M.5    Al, E.6
  • 63
    • 0027304771 scopus 로고
    • Nicotinamide mononucleotide adenylyltransferase activity in human erythrocytes
    • Sestini S, Ricci C, Micheli V, Pompucci G (1993) Nicotinamide mononucleotide adenylyltransferase activity in human erythrocytes. Arch Biochem Biophys 302: 206-211.
    • (1993) Arch Biochem Biophys , vol.302 , pp. 206-211
    • Sestini, S.1    Ricci, C.2    Micheli, V.3    Pompucci, G.4
  • 64
    • 84859582577 scopus 로고    scopus 로고
    • Quinolinic acid, the inescapable neurotoxin
    • Guillemin GJ (2012) Quinolinic acid, the inescapable neurotoxin. Febs J 279: 1356-1365.
    • (2012) Febs J , vol.279 , pp. 1356-1365
    • Guillemin, G.J.1


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