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Volumn 1854, Issue 9, 2015, Pages 1138-1149

Regulation of NAD biosynthetic enzymes modulates NAD-sensing processes to shape mammalian cell physiology under varying biological cues

Author keywords

Enzyme regulation; NAD biosynthesis; Nicotinamide phosphoribosyltransferase; Nicotinamide riboside kinase; Nicotinic acid phosphoribosyltransferase; Quinolinate phosphoribosyltransferase

Indexed keywords

NICOTINAMIDE ADENINE DINUCLEOTIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE NUCLEOSIDASE; NICOTINAMIDE PHOSPHORIBOSYLTRANSFERASE; NICOTINAMIDE RIBOSIDE; NICOTINATE PHOSPHORIBOSYLTRANSFERASE; PHOSPHORIBOSYLTRANSFERASE; QUINOLINATE PHOSPHORIBOSYLTRANSFERASE; SIRTUIN; UNCLASSIFIED DRUG; GLYCOSYLTRANSFERASE; NICOTINATE-NUCLEOTIDE DIPHOSPHORYLASE (CARBOXYLATING);

EID: 84937524287     PISSN: 15709639     EISSN: 18781454     Source Type: Journal    
DOI: 10.1016/j.bbapap.2015.02.021     Document Type: Review
Times cited : (69)

References (174)
  • 1
    • 84865525580 scopus 로고    scopus 로고
    • Regulation of cell survival and death by pyridine nucleotides
    • S. Oka, C.P. Hsu, and J. Sadoshima Regulation of cell survival and death by pyridine nucleotides Circ. Res. 111 2012 611 627
    • (2012) Circ. Res. , vol.111 , pp. 611-627
    • Oka, S.1    Hsu, C.P.2    Sadoshima, J.3
  • 2
    • 84886723521 scopus 로고    scopus 로고
    • Poly(ADP-ribose): PARadigms and PARadoxes
    • A. Burkle, and L. Virag Poly(ADP-ribose): PARadigms and PARadoxes Mol. Aspects Med. 34 2013 1046 1065
    • (2013) Mol. Aspects Med. , vol.34 , pp. 1046-1065
    • Burkle, A.1    Virag, L.2
  • 3
    • 84880324619 scopus 로고    scopus 로고
    • Expanding functions of intracellular resident mono-ADP-ribosylation in cell physiology
    • K.L. Feijs, P. Verheugd, and B. Luscher Expanding functions of intracellular resident mono-ADP-ribosylation in cell physiology FEBS J. 280 2013 3519 3529
    • (2013) FEBS J. , vol.280 , pp. 3519-3529
    • Feijs, K.L.1    Verheugd, P.2    Luscher, B.3
  • 4
    • 84927757448 scopus 로고    scopus 로고
    • Roles and mechanisms of the CD38/cyclic adenosine diphosphate ribose/Ca(2 +) signaling pathway
    • W. Wei, R. Graeff, and J. Yue Roles and mechanisms of the CD38/cyclic adenosine diphosphate ribose/Ca(2 +) signaling pathway World J. Biol. Chem. 5 2014 58 67
    • (2014) World J. Biol. Chem. , vol.5 , pp. 58-67
    • Wei, W.1    Graeff, R.2    Yue, J.3
  • 10
    • 0020980976 scopus 로고
    • Poly(ADP-ribose) polymerase mediates the suicide response to massive DNA damage: studies in normal and DNA-repair defective cells
    • N.A. Berger, J.L. Sims, D.M. Catino, and S.J. Berger Poly(ADP-ribose) polymerase mediates the suicide response to massive DNA damage: studies in normal and DNA-repair defective cells Princess Takamatsu Symp. 13 1983 219 226
    • (1983) Princess Takamatsu Symp. , vol.13 , pp. 219-226
    • Berger, N.A.1    Sims, J.L.2    Catino, D.M.3    Berger, S.J.4
  • 12
    • 83455206803 scopus 로고    scopus 로고
    • Targeting sirtuin 1 to improve metabolism: all you need is NAD(+)?
    • C. Canto, and J. Auwerx Targeting sirtuin 1 to improve metabolism: all you need is NAD(+)? Pharmacol. Rev. 64 2012 166 187
    • (2012) Pharmacol. Rev. , vol.64 , pp. 166-187
    • Canto, C.1    Auwerx, J.2
  • 13
  • 14
    • 84880879892 scopus 로고    scopus 로고
    • NAD(+) metabolism: a therapeutic target for age-related metabolic disease
    • L. Mouchiroud, R.H. Houtkooper, and J. Auwerx NAD(+) metabolism: a therapeutic target for age-related metabolic disease Crit. Rev. Biochem. Mol. Biol. 48 2014 397 408
    • (2014) Crit. Rev. Biochem. Mol. Biol. , vol.48 , pp. 397-408
    • Mouchiroud, L.1    Houtkooper, R.H.2    Auwerx, J.3
  • 15
    • 84884702166 scopus 로고    scopus 로고
    • Cellular NAD depletion and decline of SIRT1 activity play critical roles in PARP-1-mediated acute epileptic neuronal death in vitro
    • S. Wang, X. Yang, Y. Lin, X. Qiu, H. Li, X. Zhao, L. Cao, X. Liu, Y. Pang, X. Wang, and Z. Chi Cellular NAD depletion and decline of SIRT1 activity play critical roles in PARP-1-mediated acute epileptic neuronal death in vitro Brain Res. 1535 2013 14 23
    • (2013) Brain Res. , vol.1535 , pp. 14-23
    • Wang, S.1    Yang, X.2    Lin, Y.3    Qiu, X.4    Li, H.5    Zhao, X.6    Cao, L.7    Liu, X.8    Pang, Y.9    Wang, X.10    Chi, Z.11
  • 16
    • 84859248021 scopus 로고    scopus 로고
    • DNA damage in Nijmegen Breakage Syndrome cells leads to PARP hyperactivation and increased oxidative stress
    • H. Krenzlin, I. Demuth, B. Salewsky, P. Wessendorf, K. Weidele, A. Burkle, and M. Digweed DNA damage in Nijmegen Breakage Syndrome cells leads to PARP hyperactivation and increased oxidative stress PLoS Genet. 8 2012 e1002557
    • (2012) PLoS Genet. , vol.8
    • Krenzlin, H.1    Demuth, I.2    Salewsky, B.3    Wessendorf, P.4    Weidele, K.5    Burkle, A.6    Digweed, M.7
  • 17
    • 80051670852 scopus 로고    scopus 로고
    • + depletion or PAR polymer formation: which plays the role of executioner in ischaemic cell death?
    • + depletion or PAR polymer formation: which plays the role of executioner in ischaemic cell death? Acta Physiol. (Oxf) 203 2011 225 234
    • (2011) Acta Physiol. (Oxf) , vol.203 , pp. 225-234
    • Siegel, C.1    McCullough, L.D.2
  • 19
    • 77955657563 scopus 로고    scopus 로고
    • Ex vivo supplementation with nicotinic acid enhances cellular poly(ADP-ribosyl)ation and improves cell viability in human peripheral blood mononuclear cells
    • K. Weidele, A. Kunzmann, M. Schmitz, S. Beneke, and A. Burkle Ex vivo supplementation with nicotinic acid enhances cellular poly(ADP-ribosyl)ation and improves cell viability in human peripheral blood mononuclear cells Biochem. Pharmacol. 80 2010 1103 1112
    • (2010) Biochem. Pharmacol. , vol.80 , pp. 1103-1112
    • Weidele, K.1    Kunzmann, A.2    Schmitz, M.3    Beneke, S.4    Burkle, A.5
  • 20
    • 84860263053 scopus 로고    scopus 로고
    • Prevention of traumatic brain injury-induced neuron death by intranasal delivery of nicotinamide adenine dinucleotide
    • S.J. Won, B.Y. Choi, B.H. Yoo, M. Sohn, W. Ying, R.A. Swanson, and S.W. Suh Prevention of traumatic brain injury-induced neuron death by intranasal delivery of nicotinamide adenine dinucleotide J. Neurotrauma 29 2012 1401 1409
    • (2012) J. Neurotrauma , vol.29 , pp. 1401-1409
    • Won, S.J.1    Choi, B.Y.2    Yoo, B.H.3    Sohn, M.4    Ying, W.5    Swanson, R.A.6    Suh, S.W.7
  • 23
    • 0032558401 scopus 로고    scopus 로고
    • The reaction mechanism for CD38. A single intermediate is responsible for cyclization, hydrolysis, and base-exchange chemistries
    • A.A. Sauve, C. Munshi, H.C. Lee, and V.L. Schramm The reaction mechanism for CD38. A single intermediate is responsible for cyclization, hydrolysis, and base-exchange chemistries Biochemistry 37 1998 13239 13249
    • (1998) Biochemistry , vol.37 , pp. 13239-13249
    • Sauve, A.A.1    Munshi, C.2    Lee, H.C.3    Schramm, V.L.4
  • 24
    • 84866366579 scopus 로고    scopus 로고
    • The membrane-bound enzyme CD38 exists in two opposing orientations
    • Y.J. Zhao, C.M. Lam, and H.C. Lee The membrane-bound enzyme CD38 exists in two opposing orientations Sci. Signal. 5 2012 ra67
    • (2012) Sci. Signal. , vol.5 , pp. ra67
    • Zhao, Y.J.1    Lam, C.M.2    Lee, H.C.3
  • 26
    • 84898988575 scopus 로고    scopus 로고
    • Revealing CD38 cellular localization using a cell permeable, mechanism-based fluorescent small-molecule probe
    • J.H. Shrimp, J. Hu, M. Dong, B.S. Wang, R. MacDonald, H. Jiang, Q. Hao, A. Yen, and H. Lin Revealing CD38 cellular localization using a cell permeable, mechanism-based fluorescent small-molecule probe J. Am. Chem. Soc. 136 2014 5656 5663
    • (2014) J. Am. Chem. Soc. , vol.136 , pp. 5656-5663
    • Shrimp, J.H.1    Hu, J.2    Dong, M.3    Wang, B.S.4    MacDonald, R.5    Jiang, H.6    Hao, Q.7    Yen, A.8    Lin, H.9
  • 29
    • 36049038217 scopus 로고    scopus 로고
    • The enzyme CD38 (a NAD glycohydrolase, EC 3.2.2.5) is necessary for the development of diet-induced obesity
    • M.T. Barbosa, S.M. Soares, C.M. Novak, D. Sinclair, J.A. Levine, P. Aksoy, and E.N. Chini The enzyme CD38 (a NAD glycohydrolase, EC 3.2.2.5) is necessary for the development of diet-induced obesity FASEB J. 21 2007 3629 3639
    • (2007) FASEB J. , vol.21 , pp. 3629-3639
    • Barbosa, M.T.1    Soares, S.M.2    Novak, C.M.3    Sinclair, D.4    Levine, J.A.5    Aksoy, P.6    Chini, E.N.7
  • 30
    • 84893854576 scopus 로고    scopus 로고
    • Overexpression of CD38 decreases cellular NAD levels and alters the expression of proteins involved in energy metabolism and antioxidant defense
    • Y. Hu, H. Wang, Q. Wang, and H. Deng Overexpression of CD38 decreases cellular NAD levels and alters the expression of proteins involved in energy metabolism and antioxidant defense J. Proteome Res. 13 2014 786 795
    • (2014) J. Proteome Res. , vol.13 , pp. 786-795
    • Hu, Y.1    Wang, H.2    Wang, Q.3    Deng, H.4
  • 33
    • 33846704323 scopus 로고    scopus 로고
    • Retinoic acid-induced CD38 antigen promotes leukemia cells attachment and interferon-gamma/interleukin-1beta-dependent apoptosis of endothelial cells: implications in the etiology of retinoic acid syndrome
    • Y. Gao, L.H. Camacho, and K. Mehta Retinoic acid-induced CD38 antigen promotes leukemia cells attachment and interferon-gamma/interleukin-1beta-dependent apoptosis of endothelial cells: implications in the etiology of retinoic acid syndrome Leuk. Res. 31 2007 455 463
    • (2007) Leuk. Res. , vol.31 , pp. 455-463
    • Gao, Y.1    Camacho, L.H.2    Mehta, K.3
  • 35
  • 37
    • 84906854282 scopus 로고    scopus 로고
    • MicroRNA-708 regulates CD38 expression through signaling pathways JNK MAP kinase and PTEN/AKT in human airway smooth muscle cells
    • M. Dileepan, J.A. Jude, S.P. Rao, T.F. Walseth, R.A. Panettieri, S. Subramanian, and M.S. Kannan MicroRNA-708 regulates CD38 expression through signaling pathways JNK MAP kinase and PTEN/AKT in human airway smooth muscle cells Respir. Res. 15 2014 107
    • (2014) Respir. Res. , vol.15 , pp. 107
    • Dileepan, M.1    Jude, J.A.2    Rao, S.P.3    Walseth, T.F.4    Panettieri, R.A.5    Subramanian, S.6    Kannan, M.S.7
  • 38
    • 33748681284 scopus 로고    scopus 로고
    • Cyclic ADP-ribose is a second messenger in the lipopolysaccharide-stimulated activation of murine N9 microglial cell line
    • L. Franco, N. Bodrato, I. Moreschi, C. Usai, S. Bruzzone, S. Scarf i, E. Zocchi, and A. De Flora Cyclic ADP-ribose is a second messenger in the lipopolysaccharide-stimulated activation of murine N9 microglial cell line J. Neurochem. 99 2006 165 176
    • (2006) J. Neurochem. , vol.99 , pp. 165-176
    • Franco, L.1    Bodrato, N.2    Moreschi, I.3    Usai, C.4    Bruzzone, S.5    Scarfi, S.6    Zocchi, E.7    De Flora, A.8
  • 39
    • 84889667056 scopus 로고    scopus 로고
    • Large changes in NAD levels associated with CD38 expression during HL-60 cell differentiation
    • Z.N. Al-Abady, B. Durante, A.J. Moody, and R.A. Billington Large changes in NAD levels associated with CD38 expression during HL-60 cell differentiation Biochem. Biophys. Res. Commun. 442 2013 51 55
    • (2013) Biochem. Biophys. Res. Commun. , vol.442 , pp. 51-55
    • Al-Abady, Z.N.1    Durante, B.2    Moody, A.J.3    Billington, R.A.4
  • 40
    • 84895127938 scopus 로고    scopus 로고
    • SIRT1 metabolic actions: integrating recent advances from mouse models
    • M. Boutant, and C. Canto SIRT1 metabolic actions: integrating recent advances from mouse models Mol. Metab. 3 2014 5 18
    • (2014) Mol. Metab. , vol.3 , pp. 5-18
    • Boutant, M.1    Canto, C.2
  • 41
    • 84883476818 scopus 로고    scopus 로고
    • Sirt1 extends life span and delays aging in mice through the regulation of Nk2 homeobox 1 in the DMH and LH
    • A. Satoh, C.S. Brace, N. Rensing, P. Cliften, D.F. Wozniak, E.D. Herzog, K.A. Yamada, and S. Imai Sirt1 extends life span and delays aging in mice through the regulation of Nk2 homeobox 1 in the DMH and LH Cell Metab. 18 2013 416 430
    • (2013) Cell Metab. , vol.18 , pp. 416-430
    • Satoh, A.1    Brace, C.S.2    Rensing, N.3    Cliften, P.4    Wozniak, D.F.5    Herzog, E.D.6    Yamada, K.A.7    Imai, S.8
  • 42
    • 78751663378 scopus 로고    scopus 로고
    • SIRT1 modulation as a novel approach to the treatment of diseases of aging
    • C.A. Blum, J.L. Ellis, C. Loh, P.Y. Ng, R.B. Perni, and R.L. Stein SIRT1 modulation as a novel approach to the treatment of diseases of aging J. Med. Chem. 54 2011 417 432
    • (2011) J. Med. Chem. , vol.54 , pp. 417-432
    • Blum, C.A.1    Ellis, J.L.2    Loh, C.3    Ng, P.Y.4    Perni, R.B.5    Stein, R.L.6
  • 43
    • 0034687694 scopus 로고    scopus 로고
    • Silent information regulator 2 family of NAD-dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose
    • K.G. Tanner, J. Landry, R. Sternglanz, and J.M. Denu Silent information regulator 2 family of NAD-dependent histone/protein deacetylases generates a unique product, 1-O-acetyl-ADP-ribose Proc. Natl. Acad. Sci. U. S. A. 97 2000 14178 14182
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 14178-14182
    • Tanner, K.G.1    Landry, J.2    Sternglanz, R.3    Denu, J.M.4
  • 44
    • 0037160097 scopus 로고    scopus 로고
    • Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1
    • K.J. Bitterman, R.M. Anderson, H.Y. Cohen, M. Latorre-Esteves, and D.A. Sinclair Inhibition of silencing and accelerated aging by nicotinamide, a putative negative regulator of yeast sir2 and human SIRT1 J. Biol. Chem. 277 2002 45099 45107
    • (2002) J. Biol. Chem. , vol.277 , pp. 45099-45107
    • Bitterman, K.J.1    Anderson, R.M.2    Cohen, H.Y.3    Latorre-Esteves, M.4    Sinclair, D.A.5
  • 49
    • 43049121395 scopus 로고    scopus 로고
    • Glucose restriction inhibits skeletal myoblast differentiation by activating SIRT1 through AMPK-mediated regulation of Nampt
    • M. Fulco, Y. Cen, P. Zhao, E.P. Hoffman, M.W. McBurney, A.A. Sauve, and V. Sartorelli Glucose restriction inhibits skeletal myoblast differentiation by activating SIRT1 through AMPK-mediated regulation of Nampt Dev. Cell 14 2008 661 673
    • (2008) Dev. Cell , vol.14 , pp. 661-673
    • Fulco, M.1    Cen, Y.2    Zhao, P.3    Hoffman, E.P.4    McBurney, M.W.5    Sauve, A.A.6    Sartorelli, V.7
  • 50
    • 14544282413 scopus 로고    scopus 로고
    • Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1
    • J.T. Rodgers, C. Lerin, W. Haas, S.P. Gygi, B.M. Spiegelman, and P. Puigserver Nutrient control of glucose homeostasis through a complex of PGC-1alpha and SIRT1 Nature 434 2005 113 118
    • (2005) Nature , vol.434 , pp. 113-118
    • Rodgers, J.T.1    Lerin, C.2    Haas, W.3    Gygi, S.P.4    Spiegelman, B.M.5    Puigserver, P.6
  • 52
    • 80053920774 scopus 로고    scopus 로고
    • Nicotinamide mononucleotide, a key NAD(+) intermediate, treats the pathophysiology of diet- and age-induced diabetes in mice
    • J. Yoshino, K.F. Mills, M.J. Yoon, and S. Imai Nicotinamide mononucleotide, a key NAD(+) intermediate, treats the pathophysiology of diet- and age-induced diabetes in mice Cell Metab. 14 2011 528 536
    • (2011) Cell Metab. , vol.14 , pp. 528-536
    • Yoshino, J.1    Mills, K.F.2    Yoon, M.J.3    Imai, S.4
  • 54
    • 84917671255 scopus 로고    scopus 로고
    • Regulation of SIRT2-dependent alpha-tubulin deacetylation by cellular NAD levels
    • R.H. Skoge, C. Dolle, and M. Ziegler Regulation of SIRT2-dependent alpha-tubulin deacetylation by cellular NAD levels DNA Repair (Amst) 2014
    • (2014) DNA Repair (Amst)
    • Skoge, R.H.1    Dolle, C.2    Ziegler, M.3
  • 59
    • 38349112898 scopus 로고    scopus 로고
    • Age-associated loss of Sirt1-mediated enhancement of glucose-stimulated insulin secretion in beta cell-specific Sirt1-overexpressing (BESTO) mice
    • K.M. Ramsey, K.F. Mills, A. Satoh, and S. Imai Age-associated loss of Sirt1-mediated enhancement of glucose-stimulated insulin secretion in beta cell-specific Sirt1-overexpressing (BESTO) mice Aging Cell 7 2008 78 88
    • (2008) Aging Cell , vol.7 , pp. 78-88
    • Ramsey, K.M.1    Mills, K.F.2    Satoh, A.3    Imai, S.4
  • 60
    • 82455212299 scopus 로고    scopus 로고
    • Nicotinamide mononucleotide protects against pro-inflammatory cytokine-mediated impairment of mouse islet function
    • P.W. Caton, J. Kieswich, M.M. Yaqoob, M.J. Holness, and M.C. Sugden Nicotinamide mononucleotide protects against pro-inflammatory cytokine-mediated impairment of mouse islet function Diabetologia 54 2011 3083 3092
    • (2011) Diabetologia , vol.54 , pp. 3083-3092
    • Caton, P.W.1    Kieswich, J.2    Yaqoob, M.M.3    Holness, M.J.4    Sugden, M.C.5
  • 64
    • 84875245617 scopus 로고    scopus 로고
    • Nicotinamide riboside restores cognition through an upregulation of proliferator-activated receptor-gamma coactivator 1alpha regulated beta-secretase 1 degradation and mitochondrial gene expression in Alzheimer's mouse models
    • B. Gong, Y. Pan, P. Vempati, W. Zhao, L. Knable, L. Ho, J. Wang, M. Sastre, K. Ono, A.A. Sauve, and G.M. Pasinetti Nicotinamide riboside restores cognition through an upregulation of proliferator-activated receptor-gamma coactivator 1alpha regulated beta-secretase 1 degradation and mitochondrial gene expression in Alzheimer's mouse models Neurobiol. Aging 34 2013 1581 1588
    • (2013) Neurobiol. Aging , vol.34 , pp. 1581-1588
    • Gong, B.1    Pan, Y.2    Vempati, P.3    Zhao, W.4    Knable, L.5    Ho, L.6    Wang, J.7    Sastre, M.8    Ono, K.9    Sauve, A.A.10    Pasinetti, G.M.11
  • 65
    • 84919694179 scopus 로고    scopus 로고
    • Activation of SIRT3 by the NAD(+) precursor nicotinamide riboside protects from noise-induced hearing loss
    • K.D. Brown, S. Maqsood, J.Y. Huang, Y. Pan, W. Harkcom, W. Li, A. Sauve, E. Verdin, and S.R. Jaffrey Activation of SIRT3 by the NAD(+) precursor nicotinamide riboside protects from noise-induced hearing loss Cell Metab. 20 2014 1059 1068
    • (2014) Cell Metab. , vol.20 , pp. 1059-1068
    • Brown, K.D.1    Maqsood, S.2    Huang, J.Y.3    Pan, Y.4    Harkcom, W.5    Li, W.6    Sauve, A.7    Verdin, E.8    Jaffrey, S.R.9
  • 67
    • 84884596730 scopus 로고    scopus 로고
    • Diversification of NAD biological role: the importance of location
    • M. Di Stefano, and L. Conforti Diversification of NAD biological role: the importance of location FEBS J. 280 2013 4711 4728
    • (2013) FEBS J. , vol.280 , pp. 4711-4728
    • Di Stefano, M.1    Conforti, L.2
  • 70
    • 79961085079 scopus 로고    scopus 로고
    • Nicotinamide phosphoribosyltransferase/visfatin does not catalyze nicotinamide mononucleotide formation in blood plasma
    • N. Hara, K. Yamada, T. Shibata, H. Osago, and M. Tsuchiya Nicotinamide phosphoribosyltransferase/visfatin does not catalyze nicotinamide mononucleotide formation in blood plasma PLoS One 6 2011 e22781
    • (2011) PLoS One , vol.6
    • Hara, N.1    Yamada, K.2    Shibata, T.3    Osago, H.4    Tsuchiya, M.5
  • 74
    • 71749096624 scopus 로고    scopus 로고
    • Identification of Isn1 and Sdt1 as glucose- and vitamin-regulated nicotinamide mononucleotide and nicotinic acid mononucleotide [corrected] 5′-nucleotidases responsible for production of nicotinamide riboside and nicotinic acid riboside
    • K.L. Bogan, C. Evans, P. Belenky, P. Song, C.F. Burant, R. Kennedy, and C. Brenner Identification of Isn1 and Sdt1 as glucose- and vitamin-regulated nicotinamide mononucleotide and nicotinic acid mononucleotide [corrected] 5′-nucleotidases responsible for production of nicotinamide riboside and nicotinic acid riboside J. Biol. Chem. 284 2009 34861 34869
    • (2009) J. Biol. Chem. , vol.284 , pp. 34861-34869
    • Bogan, K.L.1    Evans, C.2    Belenky, P.3    Song, P.4    Burant, C.F.5    Kennedy, R.6    Brenner, C.7
  • 75
    • 84888626285 scopus 로고    scopus 로고
    • Targeted, LCMS-based metabolomics for quantitative measurement of NAD(+) metabolites
    • S.A. Trammell, and C. Brenner Targeted, LCMS-based metabolomics for quantitative measurement of NAD(+) metabolites Comput. Struct. Biotechnol. J. 4 2013 e201301012
    • (2013) Comput. Struct. Biotechnol. J. , vol.4
    • Trammell, S.A.1    Brenner, C.2
  • 76
    • 50949120914 scopus 로고    scopus 로고
    • + precursor vitamins in human nutrition
    • + precursor vitamins in human nutrition Annu. Rev. Nutr. 28 2008 115 130
    • (2008) Annu. Rev. Nutr. , vol.28 , pp. 115-130
    • Bogan, K.L.1    Brenner, C.2
  • 77
    • 84055223632 scopus 로고    scopus 로고
    • The high-resolution crystal structure of periplasmic Haemophilus influenzae NAD nucleotidase reveals a novel enzymatic function of human CD73 related to NAD metabolism
    • S. Garavaglia, S. Bruzzone, C. Cassani, L. Canella, G. Allegrone, L. Sturla, E. Mannino, E. Millo, A. De Flora, and M. Rizzi The high-resolution crystal structure of periplasmic Haemophilus influenzae NAD nucleotidase reveals a novel enzymatic function of human CD73 related to NAD metabolism Biochem. J. 441 2012 131 141
    • (2012) Biochem. J. , vol.441 , pp. 131-141
    • Garavaglia, S.1    Bruzzone, S.2    Cassani, C.3    Canella, L.4    Allegrone, G.5    Sturla, L.6    Mannino, E.7    Millo, E.8    De Flora, A.9    Rizzi, M.10
  • 80
    • 84889046051 scopus 로고    scopus 로고
    • NAD biosynthesis in humans - enzymes, metabolites and therapeutic aspects
    • C. Dolle, R.H. Skoge, M.R. Vanlinden, and M. Ziegler NAD biosynthesis in humans - enzymes, metabolites and therapeutic aspects Curr. Top. Med. Chem. 13 2013 2907 2917
    • (2013) Curr. Top. Med. Chem. , vol.13 , pp. 2907-2917
    • Dolle, C.1    Skoge, R.H.2    Vanlinden, M.R.3    Ziegler, M.4
  • 81
    • 10944270187 scopus 로고    scopus 로고
    • The NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase regulates Sir2 activity in mammalian cells
    • J.R. Revollo, A.A. Grimm, and S. Imai The NAD biosynthesis pathway mediated by nicotinamide phosphoribosyltransferase regulates Sir2 activity in mammalian cells J. Biol. Chem. 279 2004 50754 50763
    • (2004) J. Biol. Chem. , vol.279 , pp. 50754-50763
    • Revollo, J.R.1    Grimm, A.A.2    Imai, S.3
  • 86
    • 79952537492 scopus 로고    scopus 로고
    • Nicotinamide phosphoribosyltransferase protects against ischemic stroke through SIRT1-dependent adenosine monophosphate-activated kinase pathway
    • P. Wang, T.Y. Xu, Y.F. Guan, W.W. Tian, B. Viollet, Y.C. Rui, Q.W. Zhai, D.F. Su, and C.Y. Miao Nicotinamide phosphoribosyltransferase protects against ischemic stroke through SIRT1-dependent adenosine monophosphate-activated kinase pathway Ann. Neurol. 69 2011 360 374
    • (2011) Ann. Neurol. , vol.69 , pp. 360-374
    • Wang, P.1    Xu, T.Y.2    Guan, Y.F.3    Tian, W.W.4    Viollet, B.5    Rui, Y.C.6    Zhai, Q.W.7    Su, D.F.8    Miao, C.Y.9
  • 88
    • 84155160707 scopus 로고    scopus 로고
    • Pre-B-cell colony-enhancing factor exerts a neuronal protection through its enzymatic activity and the reduction of mitochondrial dysfunction in in vitro ischemic models
    • J. Bi, H. Li, S.Q. Ye, and S. Ding Pre-B-cell colony-enhancing factor exerts a neuronal protection through its enzymatic activity and the reduction of mitochondrial dysfunction in in vitro ischemic models J. Neurochem. 120 2012 334 346
    • (2012) J. Neurochem. , vol.120 , pp. 334-346
    • Bi, J.1    Li, H.2    Ye, S.Q.3    Ding, S.4
  • 91
    • 33748174151 scopus 로고    scopus 로고
    • Stimulation of nicotinamide adenine dinucleotide biosynthetic pathways delays axonal degeneration after axotomy
    • Y. Sasaki, T. Araki, and J. Milbrandt Stimulation of nicotinamide adenine dinucleotide biosynthetic pathways delays axonal degeneration after axotomy J. Neurosci. 26 2006 8484 8491
    • (2006) J. Neurosci. , vol.26 , pp. 8484-8491
    • Sasaki, Y.1    Araki, T.2    Milbrandt, J.3
  • 93
    • 84867417683 scopus 로고    scopus 로고
    • Nicotinamide phosphoribosyltransferase may be involved in age-related brain diseases
    • L.Y. Liu, F. Wang, X.Y. Zhang, P. Huang, Y.B. Lu, E.Q. Wei, and W.P. Zhang Nicotinamide phosphoribosyltransferase may be involved in age-related brain diseases PLoS One 7 2012 e44933
    • (2012) PLoS One , vol.7
    • Liu, L.Y.1    Wang, F.2    Zhang, X.Y.3    Huang, P.4    Lu, Y.B.5    Wei, E.Q.6    Zhang, W.P.7
  • 95
    • 63549150420 scopus 로고    scopus 로고
    • Nicotinamide phosphoribosyltransferase imparts human endothelial cells with extended replicative lifespan and enhanced angiogenic capacity in a high glucose environment
    • N.M. Borradaile, and J.G. Pickering Nicotinamide phosphoribosyltransferase imparts human endothelial cells with extended replicative lifespan and enhanced angiogenic capacity in a high glucose environment Aging Cell 8 2009 100 112
    • (2009) Aging Cell , vol.8 , pp. 100-112
    • Borradaile, N.M.1    Pickering, J.G.2
  • 97
    • 0242526050 scopus 로고    scopus 로고
    • FK866, a highly specific noncompetitive inhibitor of nicotinamide phosphoribosyltransferase, represents a novel mechanism for induction of tumor cell apoptosis
    • M. Hasmann, and I. Schemainda FK866, a highly specific noncompetitive inhibitor of nicotinamide phosphoribosyltransferase, represents a novel mechanism for induction of tumor cell apoptosis Cancer Res. 63 2003 7436 7442
    • (2003) Cancer Res. , vol.63 , pp. 7436-7442
    • Hasmann, M.1    Schemainda, I.2
  • 101
    • 79952007931 scopus 로고    scopus 로고
    • NAMPT overexpression in prostate cancer and its contribution to tumor cell survival and stress response
    • B. Wang, M.K. Hasan, E. Alvarado, H. Yuan, H. Wu, and W.Y. Chen NAMPT overexpression in prostate cancer and its contribution to tumor cell survival and stress response Oncogene 30 2011 907 921
    • (2011) Oncogene , vol.30 , pp. 907-921
    • Wang, B.1    Hasan, M.K.2    Alvarado, E.3    Yuan, H.4    Wu, H.5    Chen, W.Y.6
  • 102
    • 84863090408 scopus 로고    scopus 로고
    • Nicotinamide phosphoribosyl transferase (Nampt) is required for de novo lipogenesis in tumor cells
    • S.C. Bowlby, M.J. Thomas, R.B. D'Agostino Jr., and S.J. Kridel Nicotinamide phosphoribosyl transferase (Nampt) is required for de novo lipogenesis in tumor cells PLoS One 7 2012 e40195
    • (2012) PLoS One , vol.7
    • Bowlby, S.C.1    Thomas, M.J.2    D'Agostino, R.B.3    Kridel, S.J.4
  • 103
    • 58149316660 scopus 로고    scopus 로고
    • Nicotinamide phosphoribosyl transferase/pre-B cell colony-enhancing factor/visfatin is required for lymphocyte development and cellular resistance to genotoxic stress
    • A. Rongvaux, M. Galli, S. Denanglaire, F. Van Gool, P.L. Dreze, C. Szpirer, F. Bureau, F. Andris, and O. Leo Nicotinamide phosphoribosyl transferase/pre-B cell colony-enhancing factor/visfatin is required for lymphocyte development and cellular resistance to genotoxic stress J. Immunol. 181 2008 4685 4695
    • (2008) J. Immunol. , vol.181 , pp. 4685-4695
    • Rongvaux, A.1    Galli, M.2    Denanglaire, S.3    Van Gool, F.4    Dreze, P.L.5    Szpirer, C.6    Bureau, F.7    Andris, F.8    Leo, O.9
  • 104
    • 75149160970 scopus 로고    scopus 로고
    • The nicotinamide phosphoribosyltransferase: a molecular link between metabolism, inflammation, and cancer
    • M. Galli, F. Van Gool, A. Rongvaux, F. Andris, and O. Leo The nicotinamide phosphoribosyltransferase: a molecular link between metabolism, inflammation, and cancer Cancer Res. 70 2010 8 11
    • (2010) Cancer Res. , vol.70 , pp. 8-11
    • Galli, M.1    Van Gool, F.2    Rongvaux, A.3    Andris, F.4    Leo, O.5
  • 105
    • 48249105497 scopus 로고    scopus 로고
    • Pharmacological inhibition of nicotinamide phosphoribosyltransferase/visfatin enzymatic activity identifies a new inflammatory pathway linked to NAD
    • N. Busso, M. Karababa, M. Nobile, A. Rolaz, F. Van Gool, M. Galli, O. Leo, A. So, and T. De Smedt Pharmacological inhibition of nicotinamide phosphoribosyltransferase/visfatin enzymatic activity identifies a new inflammatory pathway linked to NAD PLoS One 3 2008 e2267
    • (2008) PLoS One , vol.3
    • Busso, N.1    Karababa, M.2    Nobile, M.3    Rolaz, A.4    Van Gool, F.5    Galli, M.6    Leo, O.7    So, A.8    De Smedt, T.9
  • 107
    • 44449124774 scopus 로고    scopus 로고
    • Pre-B cell colony-enhancing factor (PBEF)/visfatin: a novel mediator of innate immunity
    • T. Luk, Z. Malam, and J.C. Marshall Pre-B cell colony-enhancing factor (PBEF)/visfatin: a novel mediator of innate immunity J. Leukoc. Biol. 83 2008 804 816
    • (2008) J. Leukoc. Biol. , vol.83 , pp. 804-816
    • Luk, T.1    Malam, Z.2    Marshall, J.C.3
  • 108
    • 84884714145 scopus 로고    scopus 로고
    • Pre-B cell colony enhancing factor (PBEF), a cytokine with multiple physiological functions
    • Z. Sun, H. Lei, and Z. Zhang Pre-B cell colony enhancing factor (PBEF), a cytokine with multiple physiological functions Cytokine Growth Factor Rev. 24 2013 433 442
    • (2013) Cytokine Growth Factor Rev. , vol.24 , pp. 433-442
    • Sun, Z.1    Lei, H.2    Zhang, Z.3
  • 109
    • 0027958452 scopus 로고
    • Cloning and characterization of the cDNA encoding a novel human pre-B-cell colony-enhancing factor
    • B. Samal, Y. Sun, G. Stearns, C. Xie, S. Suggs, and I. McNiece Cloning and characterization of the cDNA encoding a novel human pre-B-cell colony-enhancing factor Mol. Cell. Biol. 14 1994 1431 1437
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1431-1437
    • Samal, B.1    Sun, Y.2    Stearns, G.3    Xie, C.4    Suggs, S.5    McNiece, I.6
  • 110
    • 0036856578 scopus 로고    scopus 로고
    • Pre-B-cell colony-enhancing factor, whose expression is up-regulated in activated lymphocytes, is a nicotinamide phosphoribosyltransferase, a cytosolic enzyme involved in NAD biosynthesis
    • A. Rongvaux, R.J. Shea, M.H. Mulks, D. Gigot, J. Urbain, O. Leo, and F. Andris Pre-B-cell colony-enhancing factor, whose expression is up-regulated in activated lymphocytes, is a nicotinamide phosphoribosyltransferase, a cytosolic enzyme involved in NAD biosynthesis Eur. J. Immunol. 32 2002 3225 3234
    • (2002) Eur. J. Immunol. , vol.32 , pp. 3225-3234
    • Rongvaux, A.1    Shea, R.J.2    Mulks, M.H.3    Gigot, D.4    Urbain, J.5    Leo, O.6    Andris, F.7
  • 112
    • 79951968731 scopus 로고    scopus 로고
    • Nicotinamide phosphoribosyltransferase in human diseases
    • L.Q. Zhang, D.P. Heruth, and S.Q. Ye Nicotinamide phosphoribosyltransferase in human diseases J. Bioanal. Biomed. 3 2011 13 25
    • (2011) J. Bioanal. Biomed. , vol.3 , pp. 13-25
    • Zhang, L.Q.1    Heruth, D.P.2    Ye, S.Q.3
  • 113
    • 84864269536 scopus 로고    scopus 로고
    • Visfatin/NAMPT: a multifaceted molecule with diverse roles in physiology and pathophysiology
    • T.B. Dahl, S. Holm, P. Aukrust, and B. Halvorsen Visfatin/NAMPT: a multifaceted molecule with diverse roles in physiology and pathophysiology Annu. Rev. Nutr. 32 2012 229 243
    • (2012) Annu. Rev. Nutr. , vol.32 , pp. 229-243
    • Dahl, T.B.1    Holm, S.2    Aukrust, P.3    Halvorsen, B.4
  • 115
    • 52049098545 scopus 로고    scopus 로고
    • Visfatin: structure, function and relation to diabetes mellitus and other dysfunctions
    • E. Adeghate Visfatin: structure, function and relation to diabetes mellitus and other dysfunctions Curr. Med. Chem. 15 2008 1851 1862
    • (2008) Curr. Med. Chem. , vol.15 , pp. 1851-1862
    • Adeghate, E.1
  • 116
    • 0035062540 scopus 로고    scopus 로고
    • Genomic organization of the gene coding for human pre-B-cell colony enhancing factor and expression in human fetal membranes
    • S. Ognjanovic, S. Bao, S.Y. Yamamoto, J. Garibay-Tupas, B. Samal, and G.D. Bryant-Greenwood Genomic organization of the gene coding for human pre-B-cell colony enhancing factor and expression in human fetal membranes J. Mol. Endocrinol. 26 2001 107 117
    • (2001) J. Mol. Endocrinol. , vol.26 , pp. 107-117
    • Ognjanovic, S.1    Bao, S.2    Yamamoto, S.Y.3    Garibay-Tupas, J.4    Samal, B.5    Bryant-Greenwood, G.D.6
  • 117
    • 33745894354 scopus 로고    scopus 로고
    • Regulation of pre-B cell colony-enhancing factor by STAT-3-dependent interleukin-6 trans-signaling: implications in the pathogenesis of rheumatoid arthritis
    • M.A. Nowell, P.J. Richards, C.A. Fielding, S. Ognjanovic, N. Topley, A.S. Williams, G. Bryant-Greenwood, and S.A. Jones Regulation of pre-B cell colony-enhancing factor by STAT-3-dependent interleukin-6 trans-signaling: implications in the pathogenesis of rheumatoid arthritis Arthritis Rheum. 54 2006 2084 2095
    • (2006) Arthritis Rheum. , vol.54 , pp. 2084-2095
    • Nowell, M.A.1    Richards, P.J.2    Fielding, C.A.3    Ognjanovic, S.4    Topley, N.5    Williams, A.S.6    Bryant-Greenwood, G.7    Jones, S.A.8
  • 118
    • 0033959206 scopus 로고    scopus 로고
    • Fetal membrane distention: I. Differentially expressed genes regulated by acute distention in amniotic epithelial (WISH) cells
    • E. Nemeth, L.S. Tashima, Z. Yu, and G.D. Bryant-Greenwood Fetal membrane distention: I. Differentially expressed genes regulated by acute distention in amniotic epithelial (WISH) cells Am. J. Obstet. Gynecol. 182 2000 50 59
    • (2000) Am. J. Obstet. Gynecol. , vol.182 , pp. 50-59
    • Nemeth, E.1    Tashima, L.S.2    Yu, Z.3    Bryant-Greenwood, G.D.4
  • 121
    • 34347385041 scopus 로고    scopus 로고
    • Visfatin expression is hormonally regulated by metabolic and sex hormones in 3T3-L1 pre-adipocytes and adipocytes
    • R. MacLaren, W. Cui, and K. Cianflone Visfatin expression is hormonally regulated by metabolic and sex hormones in 3T3-L1 pre-adipocytes and adipocytes Diabetes Obes. Metab. 9 2007 490 497
    • (2007) Diabetes Obes. Metab. , vol.9 , pp. 490-497
    • MacLaren, R.1    Cui, W.2    Cianflone, K.3
  • 122
    • 33745826960 scopus 로고    scopus 로고
    • Hypoxic induction of human visfatin gene is directly mediated by hypoxia-inducible factor-1
    • S.K. Bae, S.R. Kim, J.G. Kim, J.Y. Kim, T.H. Koo, H.O. Jang, I. Yun, M.A. Yoo, and M.K. Bae Hypoxic induction of human visfatin gene is directly mediated by hypoxia-inducible factor-1 FEBS Lett. 580 2006 4105 4113
    • (2006) FEBS Lett. , vol.580 , pp. 4105-4113
    • Bae, S.K.1    Kim, S.R.2    Kim, J.G.3    Kim, J.Y.4    Koo, T.H.5    Jang, H.O.6    Yun, I.7    Yoo, M.A.8    Bae, M.K.9
  • 123
    • 84905046221 scopus 로고    scopus 로고
    • Visfatin promotes cell and tumor growth by upregulating Notch1 in breast cancer
    • H.J. Park, S.R. Kim, S.S. Kim, H.J. Wee, M.K. Bae, M.H. Ryu, and S.K. Bae Visfatin promotes cell and tumor growth by upregulating Notch1 in breast cancer Oncotarget 5 2014 5087 5099
    • (2014) Oncotarget , vol.5 , pp. 5087-5099
    • Park, H.J.1    Kim, S.R.2    Kim, S.S.3    Wee, H.J.4    Bae, M.K.5    Ryu, M.H.6    Bae, S.K.7
  • 124
    • 79954576666 scopus 로고    scopus 로고
    • Hepatic FoxOs regulate lipid metabolism via modulation of expression of the nicotinamide phosphoribosyltransferase gene
    • R. Tao, D. Wei, H. Gao, Y. Liu, R.A. DePinho, and X.C. Dong Hepatic FoxOs regulate lipid metabolism via modulation of expression of the nicotinamide phosphoribosyltransferase gene J. Biol. Chem. 286 2011 14681 14690
    • (2011) J. Biol. Chem. , vol.286 , pp. 14681-14690
    • Tao, R.1    Wei, D.2    Gao, H.3    Liu, Y.4    Depinho, R.A.5    Dong, X.C.6
  • 127
    • 79951772967 scopus 로고    scopus 로고
    • Energy sensing by the AMP-activated protein kinase and its effects on muscle metabolism
    • D.G. Hardie Energy sensing by the AMP-activated protein kinase and its effects on muscle metabolism Proc. Nutr. Soc. 70 2007 92 99
    • (2007) Proc. Nutr. Soc. , vol.70 , pp. 92-99
    • Hardie, D.G.1
  • 128
    • 80055051189 scopus 로고    scopus 로고
    • Metformin opposes impaired AMPK and SIRT1 function and deleterious changes in core clock protein expression in white adipose tissue of genetically-obese db/db mice
    • P.W. Caton, J. Kieswich, M.M. Yaqoob, M.J. Holness, and M.C. Sugden Metformin opposes impaired AMPK and SIRT1 function and deleterious changes in core clock protein expression in white adipose tissue of genetically-obese db/db mice Diabetes Obes. Metab. 13 2011 1097 1104
    • (2011) Diabetes Obes. Metab. , vol.13 , pp. 1097-1104
    • Caton, P.W.1    Kieswich, J.2    Yaqoob, M.M.3    Holness, M.J.4    Sugden, M.C.5
  • 136
    • 65249087389 scopus 로고    scopus 로고
    • SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle
    • T. Nakagawa, D.J. Lomb, M.C. Haigis, and L. Guarente SIRT5 deacetylates carbamoyl phosphate synthetase 1 and regulates the urea cycle Cell 137 2009 560 570
    • (2009) Cell , vol.137 , pp. 560-570
    • Nakagawa, T.1    Lomb, D.J.2    Haigis, M.C.3    Guarente, L.4
  • 137
    • 79957549799 scopus 로고    scopus 로고
    • Pathways and subcellular compartmentation of NAD biosynthesis in human cells: from entry of extracellular precursors to mitochondrial NAD generation
    • A. Nikiforov, C. Dolle, M. Niere, and M. Ziegler Pathways and subcellular compartmentation of NAD biosynthesis in human cells: from entry of extracellular precursors to mitochondrial NAD generation J. Biol. Chem. 286 2011 21767 21778
    • (2011) J. Biol. Chem. , vol.286 , pp. 21767-21778
    • Nikiforov, A.1    Dolle, C.2    Niere, M.3    Ziegler, M.4
  • 138
    • 69549117127 scopus 로고    scopus 로고
    • A phosphoenzyme mimic, overlapping catalytic sites and reaction coordinate motion for human NAMPT
    • E.S. Burgos, M.C. Ho, S.C. Almo, and V.L. Schramm A phosphoenzyme mimic, overlapping catalytic sites and reaction coordinate motion for human NAMPT Proc. Natl. Acad. Sci. U. S. A. 106 2009 13748 13753
    • (2009) Proc. Natl. Acad. Sci. U. S. A. , vol.106 , pp. 13748-13753
    • Burgos, E.S.1    Ho, M.C.2    Almo, S.C.3    Schramm, V.L.4
  • 139
    • 54349088713 scopus 로고    scopus 로고
    • Weak coupling of ATP hydrolysis to the chemical equilibrium of human nicotinamide phosphoribosyltransferase
    • E.S. Burgos, and V.L. Schramm Weak coupling of ATP hydrolysis to the chemical equilibrium of human nicotinamide phosphoribosyltransferase Biochemistry 47 2008 11086 11096
    • (2008) Biochemistry , vol.47 , pp. 11086-11096
    • Burgos, E.S.1    Schramm, V.L.2
  • 140
    • 34547659990 scopus 로고    scopus 로고
    • Crystal structure of human nicotinamide riboside kinase
    • J.A. Khan, S. Xiang, and L. Tong Crystal structure of human nicotinamide riboside kinase Structure 15 2007 1005 1013
    • (2007) Structure , vol.15 , pp. 1005-1013
    • Khan, J.A.1    Xiang, S.2    Tong, L.3
  • 141
    • 0033611068 scopus 로고    scopus 로고
    • A novel muscle-specific beta 1 integrin binding protein (MIBP) that modulates myogenic differentiation
    • J. Li, R. Mayne, and C. Wu A novel muscle-specific beta 1 integrin binding protein (MIBP) that modulates myogenic differentiation J. Cell Biol. 147 1999 1391 1398
    • (1999) J. Cell Biol. , vol.147 , pp. 1391-1398
    • Li, J.1    Mayne, R.2    Wu, C.3
  • 142
    • 0042162890 scopus 로고    scopus 로고
    • The muscle integrin binding protein (MIBP) interacts with alpha7beta1 integrin and regulates cell adhesion and laminin matrix deposition
    • J. Li, H. Rao, D. Burkin, S.J. Kaufman, and C. Wu The muscle integrin binding protein (MIBP) interacts with alpha7beta1 integrin and regulates cell adhesion and laminin matrix deposition Dev. Biol. 261 2003 209 219
    • (2003) Dev. Biol. , vol.261 , pp. 209-219
    • Li, J.1    Rao, H.2    Burkin, D.3    Kaufman, S.J.4    Wu, C.5
  • 144
    • 33846463399 scopus 로고    scopus 로고
    • Tissue expression and biochemical characterization of human 2-amino 3-carboxymuconate 6-semialdehyde decarboxylase, a key enzyme in tryptophan catabolism
    • L. Pucci, S. Perozzi, F. Cimadamore, G. Orsomando, and N. Raffaelli Tissue expression and biochemical characterization of human 2-amino 3-carboxymuconate 6-semialdehyde decarboxylase, a key enzyme in tryptophan catabolism FEBS J. 274 2007 827 840
    • (2007) FEBS J. , vol.274 , pp. 827-840
    • Pucci, L.1    Perozzi, S.2    Cimadamore, F.3    Orsomando, G.4    Raffaelli, N.5
  • 145
    • 0000558155 scopus 로고
    • Studies on the biosynthesis of nicotinamide adenine dinucleotide. II. A role of picolinic carboxylase in the biosynthesis of nicotinamide adenine dinucleotide from tryptophan in mammals
    • M. Ikeda, H. Tsuji, S. Nakamura, A. Ichiyama, Y. Nishizuka, and O. Hayaishi Studies on the biosynthesis of nicotinamide adenine dinucleotide. II. A role of picolinic carboxylase in the biosynthesis of nicotinamide adenine dinucleotide from tryptophan in mammals J. Biol. Chem. 240 1965 1395 1401
    • (1965) J. Biol. Chem. , vol.240 , pp. 1395-1401
    • Ikeda, M.1    Tsuji, H.2    Nakamura, S.3    Ichiyama, A.4    Nishizuka, Y.5    Hayaishi, O.6
  • 148
    • 0042762821 scopus 로고    scopus 로고
    • Inhibition of indoleamine 2,3-dioxygenase activity in IFN-gamma stimulated astroglioma cells decreases intracellular NAD levels
    • R. Grant, and V. Kapoor Inhibition of indoleamine 2,3-dioxygenase activity in IFN-gamma stimulated astroglioma cells decreases intracellular NAD levels Biochem. Pharmacol. 66 2003 1033 1036
    • (2003) Biochem. Pharmacol. , vol.66 , pp. 1033-1036
    • Grant, R.1    Kapoor, V.2
  • 149
    • 0033915898 scopus 로고    scopus 로고
    • IDO induction in IFN-gamma activated astroglia: a role in improving cell viability during oxidative stress
    • R.S. Grant, H. Naif, M. Espinosa, and V. Kapoor IDO induction in IFN-gamma activated astroglia: a role in improving cell viability during oxidative stress Redox Rep. 5 2000 101 104
    • (2000) Redox Rep. , vol.5 , pp. 101-104
    • Grant, R.S.1    Naif, H.2    Espinosa, M.3    Kapoor, V.4
  • 150
    • 0033485301 scopus 로고    scopus 로고
    • Evidence for increased de novo synthesis of NAD in immune-activated RAW264.7 macrophages: a self-protective mechanism?
    • R.S. Grant, R. Passey, G. Matanovic, G. Smythe, and V. Kapoor Evidence for increased de novo synthesis of NAD in immune-activated RAW264.7 macrophages: a self-protective mechanism? Arch. Biochem. Biophys. 372 1999 1 7
    • (1999) Arch. Biochem. Biophys. , vol.372 , pp. 1-7
    • Grant, R.S.1    Passey, R.2    Matanovic, G.3    Smythe, G.4    Kapoor, V.5
  • 151
    • 84859741613 scopus 로고    scopus 로고
    • Effects of kynurenine pathway inhibition on NAD metabolism and cell viability in human primary astrocytes and neurons
    • N. Braidy, G.J. Guillemin, and R. Grant Effects of kynurenine pathway inhibition on NAD metabolism and cell viability in human primary astrocytes and neurons Int. J. Tryptophan Res. 4 2011 29 37
    • (2011) Int. J. Tryptophan Res. , vol.4 , pp. 29-37
    • Braidy, N.1    Guillemin, G.J.2    Grant, R.3
  • 153
    • 84910142746 scopus 로고    scopus 로고
    • Novel assay for simultaneous measurement of pyridine mononucleotides synthesizing activities allows dissection of the NAD(+) biosynthetic machinery in mammalian cells
    • F. Zamporlini, S. Ruggieri, F. Mazzola, A. Amici, G. Orsomando, and N. Raffaelli Novel assay for simultaneous measurement of pyridine mononucleotides synthesizing activities allows dissection of the NAD(+) biosynthetic machinery in mammalian cells FEBS J. 281 2014 5104 5119
    • (2014) FEBS J. , vol.281 , pp. 5104-5119
    • Zamporlini, F.1    Ruggieri, S.2    Mazzola, F.3    Amici, A.4    Orsomando, G.5    Raffaelli, N.6
  • 154
    • 0037789537 scopus 로고    scopus 로고
    • Peripheral distribution of kynurenine metabolites and activity of kynurenine pathway enzymes in renal failure
    • D. Pawlak, A. Tankiewicz, T. Matys, and W. Buczko Peripheral distribution of kynurenine metabolites and activity of kynurenine pathway enzymes in renal failure J. Physiol. Pharmacol. 54 2003 175 189
    • (2003) J. Physiol. Pharmacol. , vol.54 , pp. 175-189
    • Pawlak, D.1    Tankiewicz, A.2    Matys, T.3    Buczko, W.4
  • 155
    • 65349094683 scopus 로고    scopus 로고
    • QPRT: a potential marker for follicular thyroid carcinoma including minimal invasive variant; a gene expression, RNA and immunohistochemical study
    • N. Hinsch, M. Frank, C. Doring, C. Vorlander, and M.L. Hansmann QPRT: a potential marker for follicular thyroid carcinoma including minimal invasive variant; a gene expression, RNA and immunohistochemical study BMC Cancer 9 2009 93
    • (2009) BMC Cancer , vol.9 , pp. 93
    • Hinsch, N.1    Frank, M.2    Doring, C.3    Vorlander, C.4    Hansmann, M.L.5
  • 158
    • 0021832252 scopus 로고
    • Quinolinic acid phosphoribosyltransferase in human and rat brain: activity in Huntington's disease and in quinolinate-lesioned rat striatum
    • A.C. Foster, W.O. Whetsell Jr., E.D. Bird, and R. Schwarcz Quinolinic acid phosphoribosyltransferase in human and rat brain: activity in Huntington's disease and in quinolinate-lesioned rat striatum Brain Res. 336 1985 207 214
    • (1985) Brain Res. , vol.336 , pp. 207-214
    • Foster, A.C.1    Whetsell, W.O.2    Bird, E.D.3    Schwarcz, R.4
  • 159
    • 0026078274 scopus 로고
    • Quinolinic acid catabolism is increased in cerebellum of patients with dominantly inherited olivopontocerebellar atrophy
    • S.J. Kish, F. Du, D.A. Parks, Y. Robitaille, M.J. Ball, L. Schut, O. Hornykiewicz, and R. Schwarcz Quinolinic acid catabolism is increased in cerebellum of patients with dominantly inherited olivopontocerebellar atrophy Ann. Neurol. 29 1991 100 104
    • (1991) Ann. Neurol. , vol.29 , pp. 100-104
    • Kish, S.J.1    Du, F.2    Parks, D.A.3    Robitaille, Y.4    Ball, M.J.5    Schut, L.6    Hornykiewicz, O.7    Schwarcz, R.8
  • 160
    • 0027295833 scopus 로고
    • Kynurenine pathway enzymes in a rat model of chronic epilepsy: immunohistochemical study of activated glial cells
    • F. Du, J. Williamson, E. Bertram, E. Lothman, E. Okuno, and R. Schwarcz Kynurenine pathway enzymes in a rat model of chronic epilepsy: immunohistochemical study of activated glial cells Neuroscience 55 1993 975 989
    • (1993) Neuroscience , vol.55 , pp. 975-989
    • Du, F.1    Williamson, J.2    Bertram, E.3    Lothman, E.4    Okuno, E.5    Schwarcz, R.6
  • 161
    • 84876449074 scopus 로고    scopus 로고
    • Expression of tryptophan 2,3-dioxygenase and production of kynurenine pathway metabolites in triple transgenic mice and human Alzheimer's disease brain
    • W. Wu, J.A. Nicolazzo, L. Wen, R. Chung, R. Stankovic, S.S. Bao, C.K. Lim, B.J. Brew, K.M. Cullen, and G.J. Guillemin Expression of tryptophan 2,3-dioxygenase and production of kynurenine pathway metabolites in triple transgenic mice and human Alzheimer's disease brain PLoS One 8 2013 e59749
    • (2013) PLoS One , vol.8
    • Wu, W.1    Nicolazzo, J.A.2    Wen, L.3    Chung, R.4    Stankovic, R.5    Bao, S.S.6    Lim, C.K.7    Brew, B.J.8    Cullen, K.M.9    Guillemin, G.J.10
  • 163
    • 84872167755 scopus 로고    scopus 로고
    • Establishment of true niacin deficiency in quinolinic acid phosphoribosyltransferase knockout mice
    • M. Terakata, T. Fukuwatari, M. Sano, N. Nakao, R. Sasaki, S. Fukuoka, and K. Shibata Establishment of true niacin deficiency in quinolinic acid phosphoribosyltransferase knockout mice J. Nutr. 142 2012 2148 2153
    • (2012) J. Nutr. , vol.142 , pp. 2148-2153
    • Terakata, M.1    Fukuwatari, T.2    Sano, M.3    Nakao, N.4    Sasaki, R.5    Fukuoka, S.6    Shibata, K.7
  • 164
    • 34748882326 scopus 로고    scopus 로고
    • Structural and kinetic characterization of quinolinate phosphoribosyltransferase (hQPRTase) from Homo sapiens
    • H. Liu, K. Woznica, G. Catton, A. Crawford, N. Botting, and J.H. Naismith Structural and kinetic characterization of quinolinate phosphoribosyltransferase (hQPRTase) from Homo sapiens J. Mol. Biol. 373 2007 755 763
    • (2007) J. Mol. Biol. , vol.373 , pp. 755-763
    • Liu, H.1    Woznica, K.2    Catton, G.3    Crawford, A.4    Botting, N.5    Naismith, J.H.6
  • 165
    • 0001112709 scopus 로고
    • The enzymatic conversion of quinolinate to nicotinic acid mononucleotide in mammalian liver
    • R.K. Gholson, I. Ueda, N. Ogasawara, and L.M. Henderson The enzymatic conversion of quinolinate to nicotinic acid mononucleotide in mammalian liver J. Biol. Chem. 239 1964 1208 1214
    • (1964) J. Biol. Chem. , vol.239 , pp. 1208-1214
    • Gholson, R.K.1    Ueda, I.2    Ogasawara, N.3    Henderson, L.M.4
  • 166
    • 0017086237 scopus 로고
    • Inhibition of hog liver crystalline quinolinate phosphoribosyltransferase by nucleotides, quinolinate analogues and sulfhydryl reagents
    • H. Taguchi, and K. Iwai Inhibition of hog liver crystalline quinolinate phosphoribosyltransferase by nucleotides, quinolinate analogues and sulfhydryl reagents Agric. Biol. Chem. 40 1976 385 389
    • (1976) Agric. Biol. Chem. , vol.40 , pp. 385-389
    • Taguchi, H.1    Iwai, K.2
  • 167
    • 0015500271 scopus 로고
    • The management of nicotinamide and nicotinic acid in the mouse
    • P.B. Collins, and S. Chaykin The management of nicotinamide and nicotinic acid in the mouse J. Biol. Chem. 247 1972 778 783
    • (1972) J. Biol. Chem. , vol.247 , pp. 778-783
    • Collins, P.B.1    Chaykin, S.2
  • 168
    • 0029050644 scopus 로고
    • + and poly(ADP-ribose) levels but do not affect diethylnitrosamine-induced altered hepatic foci in Fischer-344 rats
    • + and poly(ADP-ribose) levels but do not affect diethylnitrosamine-induced altered hepatic foci in Fischer-344 rats J. Nutr. 125 1995 1455 1461
    • (1995) J. Nutr. , vol.125 , pp. 1455-1461
    • Jackson, T.M.1    Rawling, J.M.2    Roebuck, B.D.3    Kirkland, J.B.4
  • 169
    • 34548329953 scopus 로고    scopus 로고
    • Elevation of cellular NAD levels by nicotinic acid and involvement of nicotinic acid phosphoribosyltransferase in human cells
    • N. Hara, K. Yamada, T. Shibata, H. Osago, T. Hashimoto, and M. Tsuchiya Elevation of cellular NAD levels by nicotinic acid and involvement of nicotinic acid phosphoribosyltransferase in human cells J. Biol. Chem. 282 2007 24574 24582
    • (2007) J. Biol. Chem. , vol.282 , pp. 24574-24582
    • Hara, N.1    Yamada, K.2    Shibata, T.3    Osago, H.4    Hashimoto, T.5    Tsuchiya, M.6
  • 170
    • 84855840670 scopus 로고    scopus 로고
    • Characterization of human nicotinate phosphoribosyltransferase: kinetic studies, structure prediction and functional analysis by site-directed mutagenesis
    • L. Galassi, M. Di Stefano, L. Brunetti, G. Orsomando, A. Amici, S. Ruggieri, and G. Magni Characterization of human nicotinate phosphoribosyltransferase: kinetic studies, structure prediction and functional analysis by site-directed mutagenesis Biochimie 94 2012 300 309
    • (2012) Biochimie , vol.94 , pp. 300-309
    • Galassi, L.1    Di Stefano, M.2    Brunetti, L.3    Orsomando, G.4    Amici, A.5    Ruggieri, S.6    Magni, G.7
  • 171
    • 0015877039 scopus 로고
    • Nicotinate phosphoribosyltransferase of human erythrocytes. Purification and properties
    • J. Niedel, and L.S. Dietrich Nicotinate phosphoribosyltransferase of human erythrocytes. Purification and properties J. Biol. Chem. 248 1973 3500 3505
    • (1973) J. Biol. Chem. , vol.248 , pp. 3500-3505
    • Niedel, J.1    Dietrich, L.S.2
  • 172
    • 0014669299 scopus 로고
    • Allosteric properties of bovine liver nicotinate phosphoribosyltransferase
    • L.D. Smith, and R.K. Gholson Allosteric properties of bovine liver nicotinate phosphoribosyltransferase J. Biol. Chem. 244 1969 68 71
    • (1969) J. Biol. Chem. , vol.244 , pp. 68-71
    • Smith, L.D.1    Gholson, R.K.2
  • 173
    • 0032821997 scopus 로고    scopus 로고
    • Energy coupling through molecular discrimination: nicotinate phosphoribosyltransferase
    • C.T. Grubmeyer, J.W. Gross, and M. Rajavel Energy coupling through molecular discrimination: nicotinate phosphoribosyltransferase Methods Enzymol. 308 1999 28 48
    • (1999) Methods Enzymol. , vol.308 , pp. 28-48
    • Grubmeyer, C.T.1    Gross, J.W.2    Rajavel, M.3
  • 174
    • 0015138604 scopus 로고
    • Inhibition of nicotinate phosphoribosyltransferase in human platelet lysate by nicotinic acid analogs
    • Z.N. Gaut, and H.M. Solomon Inhibition of nicotinate phosphoribosyltransferase in human platelet lysate by nicotinic acid analogs Biochem. Pharmacol. 20 1971 2903 2906
    • (1971) Biochem. Pharmacol. , vol.20 , pp. 2903-2906
    • Gaut, Z.N.1    Solomon, H.M.2


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