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Volumn 54, Issue 8, 2011, Pages 699-711

Cyclic ADP-ribose and NAADP: Fraternal twin messengers for calcium signaling

Author keywords

ADP ribosyl cyclase; cADPR; Calcium mobilization and signaling; CD38; cyclic ADP ribose; NAADP; nicotinic acid adenine dinucleotide phosphate

Indexed keywords

APLYSIA; BACTERIA (MICROORGANISMS); MAMMALIA; MUS;

EID: 79960629413     PISSN: 16747305     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11427-011-4197-3     Document Type: Review
Times cited : (52)

References (161)
  • 1
    • 0020643801 scopus 로고
    • 2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1,4,5-trisphosphate
    • 2+ from a nonmitochondrial intracellular store in pancreatic acinar cells by inositol-1, 4, 5-trisphosphate. Nature, 1983, 306: 67-69.
    • (1983) Nature , vol.306 , pp. 67-69
    • Streb, H.1    Irvine, R.F.2    Berridge, M.J.3
  • 2
    • 0037069667 scopus 로고    scopus 로고
    • Structure of the inositol 1,4,5-trisphosphate receptor binding core in complex with its ligand
    • Bosanac I, Alattia J R, Mal T K, et al. Structure of the inositol 1, 4, 5-trisphosphate receptor binding core in complex with its ligand. Nature, 2002, 420: 696-700.
    • (2002) Nature , vol.420 , pp. 696-700
    • Bosanac, I.1    Alattia, J.R.2    Mal, T.K.3
  • 3
    • 0023219685 scopus 로고
    • Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate
    • Clapper D L, Walseth T F, Dargie P J, et al. Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate. J Biol Chem, 1987, 262: 9561-9568.
    • (1987) J Biol Chem , vol.262 , pp. 9561-9568
    • Clapper, D.L.1    Walseth, T.F.2    Dargie, P.J.3
  • 5
    • 0022270778 scopus 로고
    • +2-release from non-mitochondrial stores in sea urchin egg homogenates
    • +2-release from non-mitochondrial stores in sea urchin egg homogenates. J Biol Chem, 1985, 260: 13947-3954.
    • (1985) J Biol Chem , vol.260 , pp. 13947-13954
    • Clapper, D.L.1    Lee, H.C.2
  • 6
    • 0009032641 scopus 로고
    • The release of calcium in Arbacia eggs on fertilization
    • Mazia D. The release of calcium in Arbacia eggs on fertilization. J Cell Comp, 1937, Physiol, 10: 291-304.
    • (1937) J Cell Comp , vol.10 , pp. 291-304
    • Mazia, D.1
  • 7
    • 0028402138 scopus 로고
    • The crystal structure of cyclic ADP-ribose
    • Lee H C, Aarhus R, Levitt D. The crystal structure of cyclic ADP-ribose. Nature Struct Biol, 1994, 1: 143-144.
    • (1994) Nature Struct Biol , vol.1 , pp. 143-144
    • Lee, H.C.1    Aarhus, R.2    Levitt, D.3
  • 9
    • 1942485471 scopus 로고    scopus 로고
    • Medicinal chemistry and pharmacology of cyclic ADP-ribose
    • Potter B V L, Walseth T F. Medicinal chemistry and pharmacology of cyclic ADP-ribose. Curr Mol Med, 2004, 4: 303-312.
    • (2004) Curr Mol Med , vol.4 , pp. 303-312
    • Potter, B.V.L.1    Walseth, T.F.2
  • 10
    • 0025831860 scopus 로고
    • Determination of endogenous levels of cyclic ADP-ribose in rat tissues
    • Walseth T F, Aarhus R, Zeleznikar R J Jr., et al. Determination of endogenous levels of cyclic ADP-ribose in rat tissues. Biochim Biophys Acta, 1991, 1094: 113-120.
    • (1991) Biochim Biophys Acta , vol.1094 , pp. 113-120
    • Walseth, T.F.1    Aarhus, R.2    Zeleznikar Jr., R.J.3
  • 11
    • 0028950282 scopus 로고
    • A derivative of NADP mobilizes calcium stores insensitive to inositol trisphosphate and cyclic ADP-ribose
    • Lee H C, Aarhus R. A derivative of NADP mobilizes calcium stores insensitive to inositol trisphosphate and cyclic ADP-ribose. J Biol Chem, 1995, 270: 2152-2157.
    • (1995) J Biol Chem , vol.270 , pp. 2152-2157
    • Lee, H.C.1    Aarhus, R.2
  • 12
    • 62549084244 scopus 로고    scopus 로고
    • Cyclic ADP-ribose links metabolism to multiple fission in the dinoflagellate Crypthecodinium cohnii
    • Lam C M, Yeung P K, Lee H C, et al. Cyclic ADP-ribose links metabolism to multiple fission in the dinoflagellate Crypthecodinium cohnii. Cell Cal, 2009, 45: 346-357.
    • (2009) Cell Cal , vol.45 , pp. 346-357
    • Lam, C.M.1    Yeung, P.K.2    Lee, H.C.3
  • 13
    • 0034682499 scopus 로고    scopus 로고
    • Calcium release from the endoplasmic reticulum of higher plants elicited by the NADP metabolite nicotinic acid adenine dinucleotide phosphate
    • Navazio L, Bewell M A, Siddiqua A, et al. Calcium release from the endoplasmic reticulum of higher plants elicited by the NADP metabolite nicotinic acid adenine dinucleotide phosphate. Proc Natl Acad Sci USA, 2000, 97: 8693-8698.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 8693-8698
    • Navazio, L.1    Bewell, M.A.2    Siddiqua, A.3
  • 14
    • 0031444350 scopus 로고    scopus 로고
    • Abscisic acid signaling through cyclic ADP-ribose in plants
    • Wu Y, Kuzma J, Marechal E, et al. Abscisic acid signaling through cyclic ADP-ribose in plants. Science, 1997, 278: 2126-2130.
    • (1997) Science , vol.278 , pp. 2126-2130
    • Wu, Y.1    Kuzma, J.2    Marechal, E.3
  • 15
    • 0037195094 scopus 로고    scopus 로고
    • Nicotinic acid-adenine dinucleotide phosphate-sensitive calcium stores initiate insulin signaling in human beta cells
    • Johnson J D, Misler S. Nicotinic acid-adenine dinucleotide phosphate-sensitive calcium stores initiate insulin signaling in human beta cells. Proc Natl Acad Sci USA, 2002, 99: 14566-14571.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 14566-14571
    • Johnson, J.D.1    Misler, S.2
  • 16
    • 0034170945 scopus 로고    scopus 로고
    • Extracellular cyclic ADP-ribose increases intracellular free calcium concentration and stimulates proliferation of human hemopoietic progenitors
    • Podesta M, Zocchi E, Pitto A, et al. Extracellular cyclic ADP-ribose increases intracellular free calcium concentration and stimulates proliferation of human hemopoietic progenitors. FASEB J, 2000, 14: 680-690.
    • (2000) FASEB J , vol.14 , pp. 680-690
    • Podesta, M.1    Zocchi, E.2    Pitto, A.3
  • 18
    • 0035195549 scopus 로고    scopus 로고
    • 2+ transients in fertilization of sea urchin eggs
    • 2+ transients in fertilization of sea urchin eggs. Dev, 2001, 128: 4405-4414.
    • (2001) Dev , vol.128 , pp. 4405-4414
    • Kuroda, R.1    Kontani, K.2    Kanda, Y.3
  • 19
    • 0012637873 scopus 로고    scopus 로고
    • The NO pathway acts late during the fertilization response in sea urchin eggs
    • Leckie C, Empson R, Becchetti A, et al. The NO pathway acts late during the fertilization response in sea urchin eggs. J Biol Chem, 2003, 278: 12247-12254.
    • (2003) J Biol Chem , vol.278 , pp. 12247-12254
    • Leckie, C.1    Empson, R.2    Becchetti, A.3
  • 20
    • 0025384609 scopus 로고
    • 2+ mobilizing activities of cyclic ADP-ribose and inositol trisphosphate
    • 2+ mobilizing activities of cyclic ADP-ribose and inositol trisphosphate. Cell Regul, 1990, 1: 279-290.
    • (1990) Cell Regul , vol.1 , pp. 279-290
    • Dargie, P.J.1    Agre, M.C.2    Lee, H.C.3
  • 21
    • 0027282375 scopus 로고
    • Redundant mechanisms of calcium-induced calcium release underlying calcium waves during fertilization of sea urchin eggs
    • Galione A, McDougall A, Busa W B, et al. Redundant mechanisms of calcium-induced calcium release underlying calcium waves during fertilization of sea urchin eggs. Science, 1993, 261: 348-352.
    • (1993) Science , vol.261 , pp. 348-352
    • Galione, A.1    McDougall, A.2    Busa, W.B.3
  • 22
    • 0027295646 scopus 로고
    • Calcium mobilization by dual receptors during fertilization of sea urchin eggs
    • Lee H C, Aarhus R, Walseth T F. Calcium mobilization by dual receptors during fertilization of sea urchin eggs. Science, 1993, 261: 352-355.
    • (1993) Science , vol.261 , pp. 352-355
    • Lee, H.C.1    Aarhus, R.2    Walseth, T.F.3
  • 23
    • 0037418583 scopus 로고    scopus 로고
    • Calcium signaling: NAADP ascends as a new messenger
    • Lee H C. Calcium signaling: NAADP ascends as a new messenger. Curr Biol, 2003, 13: R186-R188.
    • (2003) Curr Biol , vol.13 , pp. 186-188
    • Lee, H.C.1
  • 24
    • 26644460215 scopus 로고    scopus 로고
    • Nicotinic acid adenine dinucleotide phosphate (NAADP)-mediated calcium signaling
    • Lee H C. Nicotinic acid adenine dinucleotide phosphate (NAADP)-mediated calcium signaling. J Biol Chem, 2005, 280: 33693-33696.
    • (2005) J Biol Chem , vol.280 , pp. 33693-33696
    • Lee, H.C.1
  • 25
    • 0034744519 scopus 로고    scopus 로고
    • 2+ signaling evoked by cholecystokinin and acetylcholine: The roles of NAADP, cADPR, and IP3
    • 2+ signaling evoked by cholecystokinin and acetylcholine: The roles of NAADP, cADPR, and IP3. Annu Rev Physiol, 2001, 63: 99-117.
    • (2001) Annu Rev Physiol , vol.63 , pp. 99-117
    • Cancela, J.M.1
  • 26
    • 0033522228 scopus 로고    scopus 로고
    • 2+-signalling patterns by NAADP in pancreatic acinar cells
    • 2+-signalling patterns by NAADP in pancreatic acinar cells. Nature, 1999, 398: 74-76.
    • (1999) Nature , vol.398 , pp. 74-76
    • Cancela, J.M.1    Churchill, G.C.2    Galione, A.3
  • 29
    • 77957361860 scopus 로고    scopus 로고
    • 2+ signaling in the pancreatic beta-cell
    • 2+ signaling in the pancreatic beta-cell. Islets, 2010, 2: 323-330.
    • (2010) Islets , vol.2 , pp. 323-330
    • Arredouani, A.1    Evans, A.M.2    Ma, J.3
  • 32
    • 0026418298 scopus 로고
    • 2+ release in sea urchin egg homogenates: modulation by cyclic ADP-ribose
    • 2+ release in sea urchin egg homogenates: modulation by cyclic ADP-ribose. Science, 1991, 253: 1143-1146.
    • (1991) Science , vol.253 , pp. 1143-1146
    • Galione, A.1    Lee, H.C.2    Busa, W.B.3
  • 33
    • 0027518440 scopus 로고
    • Potentiation of calcium- and caffeine-induced calcium release by cyclic ADP-ribose
    • Lee H C. Potentiation of calcium- and caffeine-induced calcium release by cyclic ADP-ribose. J Biol Chem, 1993, 268: 293-299.
    • (1993) J Biol Chem , vol.268 , pp. 293-299
    • Lee, H.C.1
  • 35
    • 0030783094 scopus 로고    scopus 로고
    • 2+ release channel (ryanodine receptor) expressed in HEK293 cells
    • 2+ release channel (ryanodine receptor) expressed in HEK293 cells. J Biol Chem, 1997, 272: 24234-24246.
    • (1997) J Biol Chem , vol.272 , pp. 24234-24246
    • Chen, S.R.W.1    Li, X.L.2    Ebisawa, K.3
  • 36
    • 0034750136 scopus 로고    scopus 로고
    • Lack of effect of cADP-ribose and NAADP on the activity of skeletal muscle and heart ryanodine receptors
    • Copello J A, Qi Y, Jeyakumar L H, et al. Lack of effect of cADP-ribose and NAADP on the activity of skeletal muscle and heart ryanodine receptors. Cell Cal, 2001, 30: 269-284.
    • (2001) Cell Cal , vol.30 , pp. 269-284
    • Copello, J.A.1    Qi, Y.2    Jeyakumar, L.H.3
  • 37
    • 0028018016 scopus 로고
    • Cyclic ADP-ribose does not affect cardiac or skeletal muscle ryanodine receptors
    • Fruen B R, Mickelson J R, Shomer N H, et al. Cyclic ADP-ribose does not affect cardiac or skeletal muscle ryanodine receptors. FEBS Lett, 1994, 352: 123-126.
    • (1994) FEBS Lett , vol.352 , pp. 123-126
    • Fruen, B.R.1    Mickelson, J.R.2    Shomer, N.H.3
  • 38
    • 79959995018 scopus 로고    scopus 로고
    • Gain of Function of cardiac ryanodine receptor in a rat model of type 1 diabetes
    • doi: 10. 1093/cvr/cvr076
    • Tian C, Shao C H, Moore C J, et al. Gain of Function of cardiac ryanodine receptor in a rat model of type 1 diabetes. Cardiovasc Res, 2011, doi: 10. 1093/cvr/cvr076.
    • (2011) Cardiovasc Res
    • Tian, C.1    Shao, C.H.2    Moore, C.J.3
  • 39
    • 0032127196 scopus 로고    scopus 로고
    • Detection and functional characterization of ryanodine receptors from sea urchin eggs
    • Lokuta A J, Darszon A, Beltran C, et al. Detection and functional characterization of ryanodine receptors from sea urchin eggs. J Physiol, 1998, 510, 1: 155-164.
    • (1998) J Physiol , vol.510 , Issue.1 , pp. 155-164
    • Lokuta, A.J.1    Darszon, A.2    Beltran, C.3
  • 40
    • 0036087476 scopus 로고    scopus 로고
    • Role of FKBP12.6 in cADPR-induced activation of reconstituted ryanodine receptors from arterial smooth muscle
    • Tang W X, Chen Y F, Zou A P, et al. Role of FKBP12. 6 in cADPR-induced activation of reconstituted ryanodine receptors from arterial smooth muscle. Am J Physiol Heart Circ Physiol, 2002, 282: H1304-1310.
    • (2002) Am J Physiol Heart Circ Physiol , vol.282 , pp. 1304-1310
    • Tang, W.X.1    Chen, Y.F.2    Zou, A.P.3
  • 41
    • 0033200222 scopus 로고    scopus 로고
    • Effects of photoreleased cADP-ribose on calcium transients and calcium sparks in myocytes isolated from guinea-pig and rat ventricle
    • Cui Y, Galione A, Terrar D A. Effects of photoreleased cADP-ribose on calcium transients and calcium sparks in myocytes isolated from guinea-pig and rat ventricle. Biochem J, 1999, 342: 269-273.
    • (1999) Biochem J , vol.342 , pp. 269-273
    • Cui, Y.1    Galione, A.2    Terrar, D.A.3
  • 42
    • 34247376025 scopus 로고    scopus 로고
    • 2+ release and storage in cardiac myocytes isolated from guinea-pig and rat ventricle
    • 2+ release and storage in cardiac myocytes isolated from guinea-pig and rat ventricle. Cell Cal, 2007, 41: 537-546.
    • (2007) Cell Cal , vol.41 , pp. 537-546
    • Macgregor, A.T.1    Rakovic, S.2    Galione, A.3
  • 43
    • 71549136818 scopus 로고    scopus 로고
    • Dissociation of FKBP 12. 6 from ryanodine receptor type 2 is regulated by cyclic ADP-ribose but not ta-adrenergic stimulation in mouse cardiomyocytes
    • Zhang X, Tallini Y N, Chen Z, et al. Dissociation of FKBP 12. 6 from ryanodine receptor type 2 is regulated by cyclic ADP-ribose but not ta-adrenergic stimulation in mouse cardiomyocytes. Cardiovasc Res, 2009, 84: 253-262.
    • (2009) Cardiovasc Res , vol.84 , pp. 253-262
    • Zhang, X.1    Tallini, Y.N.2    Chen, Z.3
  • 44
    • 77952953014 scopus 로고    scopus 로고
    • Ca(2+) release induced by cADP-ribose is mediated by FKBP12.6 proteins in mouse bladder smooth muscle
    • Zheng J, Wenzhi B, Miao L, et al. Ca(2+) release induced by cADP-ribose is mediated by FKBP12. 6 proteins in mouse bladder smooth muscle. Cell Cal, 2010, 47: 449-457.
    • (2010) Cell Cal , vol.47 , pp. 449-457
    • Zheng, J.1    Wenzhi, B.2    Miao, L.3
  • 45
    • 79953173921 scopus 로고    scopus 로고
    • CADPR activates ryanodine receptors while NAADP activates two pore domain channels
    • Ogunbayo O A, Zhu Y, Rossi D, et al. cADPR activates ryanodine receptors while NAADP activates two pore domain channels. J Biol Chem, 2011, 286: 9136-9140.
    • (2011) J Biol Chem , vol.286 , pp. 9136-9140
    • Ogunbayo, O.A.1    Zhu, Y.2    Rossi, D.3
  • 46
    • 0028131433 scopus 로고
    • Cyclic ADP ribose activation of the ryanodine receptor is mediated by calmodulin
    • Lee H C, Aarhus R, Graeff R, et al. Cyclic ADP ribose activation of the ryanodine receptor is mediated by calmodulin. Nature, 1994, 370: 307-309.
    • (1994) Nature , vol.370 , pp. 307-309
    • Lee, H.C.1    Aarhus, R.2    Graeff, R.3
  • 47
    • 0028961777 scopus 로고
    • Sensitization of calcium-induced calcium release by cyclic ADP-ribose and calmodulin
    • Lee H C, Aarhus R, Graeff R M. Sensitization of calcium-induced calcium release by cyclic ADP-ribose and calmodulin. J Biol Chem, 1995, 270: 9060-9066.
    • (1995) J Biol Chem , vol.270 , pp. 9060-9066
    • Lee, H.C.1    Aarhus, R.2    Graeff, R.M.3
  • 53
    • 33646893027 scopus 로고    scopus 로고
    • 2+ dynamics and catecholamine release in acetylcholine-stimulated bovine adrenal chromaffin cells
    • 2+ dynamics and catecholamine release in acetylcholine-stimulated bovine adrenal chromaffin cells. J Pharmacol Sci, 2006, 101: 40-51.
    • (2006) J Pharmacol Sci , vol.101 , pp. 40-51
    • Morita, K.1    Kitayama, T.2    Kitayama, S.3
  • 54
    • 0030610008 scopus 로고    scopus 로고
    • 2+ entry induced by cyclic ADP-ribose in intact T-lymphocytes
    • 2+ entry induced by cyclic ADP-ribose in intact T-lymphocytes. J Biol Chem, 1997, 272: 8546-8550.
    • (1997) J Biol Chem , vol.272 , pp. 8546-8550
    • Guse, A.H.1    Berg, I.2    Dasilva, C.P.3
  • 55
    • 0035173647 scopus 로고    scopus 로고
    • Cyclic ADP-ribose production by CD38 regulates intracellular calcium release, extracellular calcium influx and chemotaxis in neutrophils and is required for bacterial clearance in vivo
    • Partida-Sanchez S, Cockayne D, Monard S, et al. Cyclic ADP-ribose production by CD38 regulates intracellular calcium release, extracellular calcium influx and chemotaxis in neutrophils and is required for bacterial clearance in vivo. Nature Med, 2001, 7: 1209-1216.
    • (2001) Nature Med , vol.7 , pp. 1209-1216
    • Partida-Sanchez, S.1    Cockayne, D.2    Monard, S.3
  • 56
    • 33646543034 scopus 로고    scopus 로고
    • TRPM2 activation by cyclic ADP-ribose at body temperature is involved in insulin secretion
    • Togashi K, Hara Y, Tominaga T, et al. TRPM2 activation by cyclic ADP-ribose at body temperature is involved in insulin secretion. EMBO J, 2006, 25: 1804-1815.
    • (2006) EMBO J , vol.25 , pp. 1804-1815
    • Togashi, K.1    Hara, Y.2    Tominaga, T.3
  • 57
    • 15944417442 scopus 로고    scopus 로고
    • Cyclic ADP-ribose and hydrogen peroxide synergize with ADP-ribose in the activation of TRPM2 channels
    • Kolisek M, Beck A, Fleig A, et al. Cyclic ADP-ribose and hydrogen peroxide synergize with ADP-ribose in the activation of TRPM2 channels. Mol Cell, 2005, 18: 61-69.
    • (2005) Mol Cell , vol.18 , pp. 61-69
    • Kolisek, M.1    Beck, A.2    Fleig, A.3
  • 58
    • 55349126396 scopus 로고    scopus 로고
    • Synergistic regulation of endogenous TRPM2 channels by adenine dinucleotides in primary human neutrophils
    • Lange I, Penner R, Fleig A, et al. Synergistic regulation of endogenous TRPM2 channels by adenine dinucleotides in primary human neutrophils. Cell Cal, 2008, 44: 604-615.
    • (2008) Cell Cal , vol.44 , pp. 604-615
    • Lange, I.1    Penner, R.2    Fleig, A.3
  • 60
    • 33646343224 scopus 로고    scopus 로고
    • Activation of T cell calcium influx by the second messenger ADP-ribose
    • Gasser A, Glassmeier G, Fliegert R, et al. Activation of T cell calcium influx by the second messenger ADP-ribose. J Biol Chem, 2005, 281: 2489-2496.
    • (2005) J Biol Chem , vol.281 , pp. 2489-2496
    • Gasser, A.1    Glassmeier, G.2    Fliegert, R.3
  • 61
    • 79960627552 scopus 로고    scopus 로고
    • Endogenous ADP-ribose enables calcium-regulated cation currents through TRPM2 channels in neutrophil granulocytes
    • Heiner I, Eisfeld J, Warnstedt M, et al. Endogenous ADP-ribose enables calcium-regulated cation currents through TRPM2 channels in neutrophil granulocytes. Biochem J, 2006, 9: 9.
    • (2006) Biochem J , vol.9 , pp. 9
    • Heiner, I.1    Eisfeld, J.2    Warnstedt, M.3
  • 62
    • 34748897412 scopus 로고    scopus 로고
    • Regulation of TRPM2 by extra- and intracellular calcium
    • Starkus J, Beck A, Fleig A, et al. Regulation of TRPM2 by extra- and intracellular calcium. J Gen Physiol, 2007, 4: 427-440.
    • (2007) J Gen Physiol , vol.4 , pp. 427-440
    • Starkus, J.1    Beck, A.2    Fleig, A.3
  • 63
    • 0035978751 scopus 로고    scopus 로고
    • ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology
    • Perraud A L, Fleig A, Dunn C A, et al. ADP-ribose gating of the calcium-permeable LTRPC2 channel revealed by Nudix motif homology. Nature, 2001, 411: 595-599.
    • (2001) Nature , vol.411 , pp. 595-599
    • Perraud, A.L.1    Fleig, A.2    Dunn, C.A.3
  • 64
    • 40949124783 scopus 로고    scopus 로고
    • Inhibition of the transient receptor potential cation channel TRPM2 by 2-aminoethoxydiphenyl borate (2-APB)
    • Togashi K, Inada H, Tominaga M. Inhibition of the transient receptor potential cation channel TRPM2 by 2-aminoethoxydiphenyl borate (2-APB). Br J Pharmacol, 2008, 153: 1324-1330.
    • (2008) Br J Pharmacol , vol.153 , pp. 1324-1330
    • Togashi, K.1    Inada, H.2    Tominaga, M.3
  • 65
    • 77954718588 scopus 로고    scopus 로고
    • Intracellular calcium elevation induced by extracellular application of cyclic-ADP-ribose or oxytocin is temperature-sensitive in rodent NG108-15 neuronal cells with or without exogenous expression of human oxytocin receptors
    • Amina S, Hashii M, Ma W J, et al. Intracellular calcium elevation induced by extracellular application of cyclic-ADP-ribose or oxytocin is temperature-sensitive in rodent NG108-15 neuronal cells with or without exogenous expression of human oxytocin receptors. J Neuroendocrinol, 2010, 5: 460-466.
    • (2010) J Neuroendocrinol , vol.5 , pp. 460-466
    • Amina, S.1    Hashii, M.2    Ma, W.J.3
  • 66
    • 33847398002 scopus 로고    scopus 로고
    • CD38 is critical for social behaviour by regulating oxytocin secretion
    • Jin D, Liu H X, Hirai H, et al. CD38 is critical for social behaviour by regulating oxytocin secretion. Nature, 2007, 446: 41-45.
    • (2007) Nature , vol.446 , pp. 41-45
    • Jin, D.1    Liu, H.X.2    Hirai, H.3
  • 67
    • 56249122605 scopus 로고    scopus 로고
    • Cyclic ADP-ribose-mediated expansion and stimulation of human mesenchymal stem cells by the plant hormone abscisic acid
    • Scarfi S, Ferraris C, Fruscione F, et al. Cyclic ADP-ribose-mediated expansion and stimulation of human mesenchymal stem cells by the plant hormone abscisic acid. Stem Cells, 2008, 11: 2855-2864.
    • (2008) Stem Cells , vol.11 , pp. 2855-2864
    • Scarfi, S.1    Ferraris, C.2    Fruscione, F.3
  • 68
    • 79960640911 scopus 로고    scopus 로고
    • Cyclic ADP ribose is a novel regulator of intracellular Ca(2+) oscillations in human bone marrow mesenchymal stem cells
    • doi: 10. 1111/j. 1582-4934. 2011. 01263. x
    • Tao R, Sun H Y, Lau C P, et al. Cyclic ADP ribose is a novel regulator of intracellular Ca(2+) oscillations in human bone marrow mesenchymal stem cells. J Cell Mol Med, 2011, doi: 10. 1111/j. 1582-4934. 2011. 01263. x.
    • (2011) J Cell Mol Med
    • Tao, R.1    Sun, H.Y.2    Lau, C.P.3
  • 71
    • 0030846558 scopus 로고    scopus 로고
    • Structural determinants of nicotinic acid adenine dinucleotide phosphate important for its calcium-mobilizing activity
    • Lee H C, Aarhus R. Structural determinants of nicotinic acid adenine dinucleotide phosphate important for its calcium-mobilizing activity. J Biol Chem, 1997, 272: 20378-20383.
    • (1997) J Biol Chem , vol.272 , pp. 20378-20383
    • Lee, H.C.1    Aarhus, R.2
  • 72
    • 0029706922 scopus 로고    scopus 로고
    • Modulator and messenger functions of cyclic ADP-ribose in calcium signaling
    • Lee H C. Modulator and messenger functions of cyclic ADP-ribose in calcium signaling. Re Prog Horm Res, 1996, 51: 355-88.
    • (1996) Re Prog Horm Res , vol.51 , pp. 355-388
    • Lee, H.C.1
  • 73
    • 0034496224 scopus 로고    scopus 로고
    • Functional visualization of the separate but interacting calcium stores sensitive to NAADP and cyclic ADP-ribose
    • Lee H C, Aarhus R. Functional visualization of the separate but interacting calcium stores sensitive to NAADP and cyclic ADP-ribose. J Cell Sci, 2000, 113: 4413-4420.
    • (2000) J Cell Sci , vol.113 , pp. 4413-4420
    • Lee, H.C.1    Aarhus, R.2
  • 74
    • 0037184523 scopus 로고    scopus 로고
    • 2+ from reserve granules, lysosome-related organelles, in sea urchin eggs
    • 2+ from reserve granules, lysosome-related organelles, in sea urchin eggs. Cell, 2002, 111: 703-708.
    • (2002) Cell , vol.111 , pp. 703-708
    • Churchill, G.C.1    Okada, Y.2    Thomas, J.M.3
  • 75
    • 11144227270 scopus 로고    scopus 로고
    • Lysosome-Sarcoplasmic reticulum junctions: A trigger zone for calcium signalling by NAADP and endothelin-1
    • Kinnear N P, Boittin F X, Thomas J M, et al. Lysosome-Sarcoplasmic reticulum junctions: A trigger zone for calcium signalling by NAADP and endothelin-1. J Biol Chem, 2004, 279: 54319-54326.
    • (2004) J Biol Chem , vol.279 , pp. 54319-54326
    • Kinnear, N.P.1    Boittin, F.X.2    Thomas, J.M.3
  • 76
    • 17844368321 scopus 로고    scopus 로고
    • The NAADP Receptor: New receptors or new regulation?
    • Galione A, Petersen O H. The NAADP Receptor: New receptors or new regulation? Mol Interv, 2005, 5: 73-79.
    • (2005) Mol Interv , vol.5 , pp. 73-79
    • Galione, A.1    Petersen, O.H.2
  • 77
    • 15244350821 scopus 로고    scopus 로고
    • 2+-activated channel TPC1 regulates germination and stomatal movement
    • 2+-activated channel TPC1 regulates germination and stomatal movement. Nature, 2005, 434: 404-408.
    • (2005) Nature , vol.434 , pp. 404-408
    • Peiter, E.1    Maathuis, F.J.2    Mills, L.N.3
  • 78
    • 67349287016 scopus 로고    scopus 로고
    • NAADP mobilizes calcium from acidic organelles through two-pore channels
    • Calcraft P J, Ruas M, Pan Z, et al. NAADP mobilizes calcium from acidic organelles through two-pore channels. Nature, 2009, 459: 596-601.
    • (2009) Nature , vol.459 , pp. 596-601
    • Calcraft, P.J.1    Ruas, M.2    Pan, Z.3
  • 79
    • 67749143745 scopus 로고    scopus 로고
    • Essential requirement for two-pore channel 1 in NAADP-mediated calcium signaling
    • Brailoiu E, Churamani D, Cai X, et al. Essential requirement for two-pore channel 1 in NAADP-mediated calcium signaling. J Cell Biol, 2009, 186: 201-209.
    • (2009) J Cell Biol , vol.186 , pp. 201-209
    • Brailoiu, E.1    Churamani, D.2    Cai, X.3
  • 82
    • 77951205549 scopus 로고    scopus 로고
    • 2+ signaling and endolysosomal trafficking
    • Mar 24. [Epub ahead of print]
    • 2+ signaling and endolysosomal trafficking. Curr Biol, 2010, Mar 24. [Epub ahead of print].
    • (2010) Curr Biol
    • Ruas, M.1    Rietdorf, K.2    Arredouani, A.3
  • 85
    • 0024381620 scopus 로고
    • 2+-mobilizing activity
    • 2+-mobilizing activity. J Biol Chem, 1989, 264: 11725-11731.
    • (1989) J Biol Chem , vol.264 , pp. 11725-11731
    • Rusinko, N.1    Lee, H.C.2
  • 86
    • 0026133769 scopus 로고
    • Purification and characterization of a molluscan egg-specific NADase, a second-messenger enzyme
    • Hellmich M R, Strumwasser F. Purification and characterization of a molluscan egg-specific NADase, a second-messenger enzyme. Cell Regul, 1991, 2: 193-202.
    • (1991) Cell Regul , vol.2 , pp. 193-202
    • Hellmich, M.R.1    Strumwasser, F.2
  • 87
    • 14844354701 scopus 로고
    • + into a calcium-mobilizing metabolite
    • + into a calcium-mobilizing metabolite. Cell Regul, 1991, 2: 203-209.
    • (1991) Cell Regul , vol.2 , pp. 203-209
    • Lee, H.C.1    Aarhus, R.2
  • 88
    • 0027944850 scopus 로고
    • Enzymatic synthesis and characterizations of cyclic GDP-ribose. A procedure for distinguishing enzymes with ADP-ribosyl cyclase activity
    • Graeff R M, Walseth T F, Fryxell K, et al. Enzymatic synthesis and characterizations of cyclic GDP-ribose. A procedure for distinguishing enzymes with ADP-ribosyl cyclase activity. J Biol Chem, 1994, 269: 30260-30267.
    • (1994) J Biol Chem , vol.269 , pp. 30260-30267
    • Graeff, R.M.1    Walseth, T.F.2    Fryxell, K.3
  • 89
    • 0026468136 scopus 로고
    • Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase and human lymphocyte antigen CD38
    • States D J, Walseth T F, Lee H C. Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase and human lymphocyte antigen CD38. Trends Biochem Sci, 1992, 17: 495.
    • (1992) Trends Biochem Sci , vol.17 , pp. 495
    • States, D.J.1    Walseth, T.F.2    Lee, H.C.3
  • 90
    • 0027763586 scopus 로고
    • Formation and hydrolysis of cyclic ADP-ribose catalyzed by lymphocyte antigen CD38
    • Howard M, Grimaldi J C, Bazan J F, et al. Formation and hydrolysis of cyclic ADP-ribose catalyzed by lymphocyte antigen CD38. Science, 1993, 262: 1056-1059.
    • (1993) Science , vol.262 , pp. 1056-1059
    • Howard, M.1    Grimaldi, J.C.2    Bazan, J.F.3
  • 91
    • 0027240645 scopus 로고
    • Production and hydrolysis of cyclic ADP-ribose at the outer surface of human erythrocytes
    • Lee H C, Zocchi E, Guida L, et al. Production and hydrolysis of cyclic ADP-ribose at the outer surface of human erythrocytes. Biochem Biophys Res Commun, 1993, 191: 639-645.
    • (1993) Biochem Biophys Res Commun , vol.191 , pp. 639-645
    • Lee, H.C.1    Zocchi, E.2    Guida, L.3
  • 92
    • 0027501559 scopus 로고
    • Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen CD38 and inhibition of the hydrolysis by ATP
    • Takasawa S, Tohgo A, Noguchi N, et al. Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen CD38 and inhibition of the hydrolysis by ATP. J Biol Chem, 1993, 268: 26052-26054.
    • (1993) J Biol Chem , vol.268 , pp. 26052-26054
    • Takasawa, S.1    Tohgo, A.2    Noguchi, N.3
  • 93
    • 0027892021 scopus 로고
    • Synthesis and degradation of cyclic ADP-ribose by NAD glycohydrolases
    • Kim H, Jacobson E L, Jacobson M K. Synthesis and degradation of cyclic ADP-ribose by NAD glycohydrolases. Science, 1993, 261: 1330-1333.
    • (1993) Science , vol.261 , pp. 1330-1333
    • Kim, H.1    Jacobson, E.L.2    Jacobson, M.K.3
  • 94
    • 0027937693 scopus 로고
    • GDP-ribosyl cyclase activity as a measure of CD38 induction by retinoic acid in HL-60 cells
    • Graeff R M, Mehta K, Lee H C. GDP-ribosyl cyclase activity as a measure of CD38 induction by retinoic acid in HL-60 cells. Biochem. Biophys Res Commun, 1994, 205: 722-727.
    • (1994) Biochem. Biophys Res Commun , vol.205 , pp. 722-727
    • Graeff, R.M.1    Mehta, K.2    Lee, H.C.3
  • 95
    • 0030024344 scopus 로고    scopus 로고
    • Fluorescent analogs of cyclic ADP-ribose: synthesis, spectral characterization, and use
    • Graeff R M, Walseth T F, Hill H K, et al. Fluorescent analogs of cyclic ADP-ribose: synthesis, spectral characterization, and use. Biochemistry, 1996, 35: 379-386.
    • (1996) Biochemistry , vol.35 , pp. 379-386
    • Graeff, R.M.1    Walseth, T.F.2    Hill, H.K.3
  • 96
    • 0037081860 scopus 로고    scopus 로고
    • A novel cycling assay for cellular cyclic ADP-ribose with nanomolar sensitivity
    • Graeff R, Lee H C. A novel cycling assay for cellular cyclic ADP-ribose with nanomolar sensitivity. Biochem J, 2002, 361: 379-384.
    • (2002) Biochem J , vol.361 , pp. 379-384
    • Graeff, R.1    Lee, H.C.2
  • 99
    • 12144285678 scopus 로고    scopus 로고
    • Regulation of dendritic cell trafficking by the ADP-ribosyl cyclase CD38; Impact on the development of humoral immunity
    • Partida-Sanchez S, Goodrich S, Kusser K, et al. Regulation of dendritic cell trafficking by the ADP-ribosyl cyclase CD38; Impact on the development of humoral immunity. Immunity, 2004, 20: 279-291.
    • (2004) Immunity , vol.20 , pp. 279-291
    • Partida-Sanchez, S.1    Goodrich, S.2    Kusser, K.3
  • 100
    • 0037336165 scopus 로고    scopus 로고
    • Disordered osteoclast formation and function in a CD38 (ADP-ribosyl cyclase)-deficient mouse establishes an essential role for CD38 in bone resorption
    • Sun L, Iqbal J, Dolgilevich S, et al. Disordered osteoclast formation and function in a CD38 (ADP-ribosyl cyclase)-deficient mouse establishes an essential role for CD38 in bone resorption. FASEB J, 2003, 17: 369-375.
    • (2003) FASEB J , vol.17 , pp. 369-375
    • Sun, L.1    Iqbal, J.2    Dolgilevich, S.3
  • 102
    • 1842556359 scopus 로고    scopus 로고
    • CD38 gene disruption inhibits the contraction induced by alpha-adrenoceptor stimulation in mouse aorta
    • Mitsui-Saito M, Kato I, Takasawa S, et al. CD38 gene disruption inhibits the contraction induced by alpha-adrenoceptor stimulation in mouse aorta. J Vet Med Sci, 2003, 65: 1325-1330.
    • (2003) J Vet Med Sci , vol.65 , pp. 1325-1330
    • Mitsui-Saito, M.1    Kato, I.2    Takasawa, S.3
  • 103
    • 10744226039 scopus 로고    scopus 로고
    • Deficit of CD38/cyclic ADP-ribose is differentially compensated in hearts by gender
    • Takahashi J, Kagaya Y, Kato I, et al. Deficit of CD38/cyclic ADP-ribose is differentially compensated in hearts by gender. Biochem Biophys Res Commun, 2003, 312: 434-440.
    • (2003) Biochem Biophys Res Commun , vol.312 , pp. 434-440
    • Takahashi, J.1    Kagaya, Y.2    Kato, I.3
  • 104
    • 50349083286 scopus 로고    scopus 로고
    • Evolution and function of the ADP ribosyl cyclase/CD38 gene family in physiology and pathology
    • Malavasi F, Deaglio S, Funaro A, et al. Evolution and function of the ADP ribosyl cyclase/CD38 gene family in physiology and pathology. Physiol Rev, 2008, 88: 841-886.
    • (2008) Physiol Rev , vol.88 , pp. 841-886
    • Malavasi, F.1    Deaglio, S.2    Funaro, A.3
  • 105
    • 0036795474 scopus 로고    scopus 로고
    • Nicotinic acid adenine dinucleotide phosphate (NAADP) is present at micromolar concentrations in sea urchin spermatozoa
    • Billington R A, Ho A, Genazzani A A. Nicotinic acid adenine dinucleotide phosphate (NAADP) is present at micromolar concentrations in sea urchin spermatozoa. J Physiol, 2002, 544. 1: 107-112.
    • (2002) J Physiol , vol.1 , pp. 107-112
    • Billington, R.A.1    Ho, A.2    Genazzani, A.A.3
  • 106
    • 0037458088 scopus 로고    scopus 로고
    • Sperm deliver a new second messenger: NAADP
    • Churchill G C, O'Neill J S, Masgrau R, et al. Sperm deliver a new second messenger: NAADP. Curr Biol, 2003, 13: 125-128.
    • (2003) Curr Biol , vol.13 , pp. 125-128
    • Churchill, G.C.1    O'Neill, J.S.2    Masgrau, R.3
  • 107
    • 2942753860 scopus 로고    scopus 로고
    • Determination of cellular nicotinic acid adenine dinucleotide phosphate (NAADP) levels
    • Churamani D, Carrey E A, Dickinson G D, et al. Determination of cellular nicotinic acid adenine dinucleotide phosphate (NAADP) levels. Biochem J, 2004, 380: 449-454.
    • (2004) Biochem J , vol.380 , pp. 449-454
    • Churamani, D.1    Carrey, E.A.2    Dickinson, G.D.3
  • 108
    • 0029616337 scopus 로고
    • ADP-ribosyl cyclase and CD38 catalyze the synthesis of a calcium-mobilizing metabolite from NADP
    • Aarhus R, Graeff R M, Dickey D M, et al. ADP-ribosyl cyclase and CD38 catalyze the synthesis of a calcium-mobilizing metabolite from NADP. J Biol Chem, 1995, 270: 30327-30333.
    • (1995) J Biol Chem , vol.270 , pp. 30327-30333
    • Aarhus, R.1    Graeff, R.M.2    Dickey, D.M.3
  • 109
    • 73649108888 scopus 로고    scopus 로고
    • 2+ signaling contributes to angiotensin II-induced activation of hepatic stellate cells: attenuation of hepatic fibrosis by CD38 ablation
    • 2+ signaling contributes to angiotensin II-induced activation of hepatic stellate cells: attenuation of hepatic fibrosis by CD38 ablation. J Biol Chem, 2010, 285: 576-582.
    • (2010) J Biol Chem , vol.285 , pp. 576-582
    • Kim, S.Y.1    Cho, B.H.2    Kim, U.H.3
  • 110
    • 77954376340 scopus 로고    scopus 로고
    • 2+ signaling in interleukin-8-treated lymphokine-activated killer cells
    • 2+ signaling in interleukin-8-treated lymphokine-activated killer cells. J Biol Chem, 2010, 285: 21877-21887.
    • (2010) J Biol Chem , vol.285 , pp. 21877-21887
    • Rah, S.Y.1    Mushtaq, M.2    Nam, T.S.3
  • 111
    • 78649670802 scopus 로고    scopus 로고
    • 2+ mobilization from lysosomes in pancreatic acinar cells
    • 2+ mobilization from lysosomes in pancreatic acinar cells. J Biol Chem, 2010, 285: 38251-38259.
    • (2010) J Biol Chem , vol.285 , pp. 38251-38259
    • Cosker, F.1    Cheviron, N.2    Yamasaki, M.3
  • 112
    • 0025265030 scopus 로고
    • Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface glycoprotein with an unusual discontinuous patern of expression during lymphocyte differentiation
    • Jackson D G, Bell J I. Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface glycoprotein with an unusual discontinuous patern of expression during lymphocyte differentiation. J Immunol, 1990, 144: 2811-2815.
    • (1990) J Immunol , vol.144 , pp. 2811-2815
    • Jackson, D.G.1    Bell, J.I.2
  • 113
    • 0029858306 scopus 로고    scopus 로고
    • Crystal structure of Aplysia ADP ribosyl cyclase, a homologue of the bifunctional ectozyme CD38
    • Prasad G S, McRee D E, Stura E A, et al. Crystal structure of Aplysia ADP ribosyl cyclase, a homologue of the bifunctional ectozyme CD38. Nature Struct Biol, 1996, 3: 957-964.
    • (1996) Nature Struct Biol , vol.3 , pp. 957-964
    • Prasad, G.S.1    McRee, D.E.2    Stura, E.A.3
  • 114
    • 0032506274 scopus 로고    scopus 로고
    • The homo-dimeric form of ADP-ribosyl cyclase in solution
    • Munshi C, Baumann C, Levitt D, et al. The homo-dimeric form of ADP-ribosyl cyclase in solution. Biochim Biophys Acta, 1998, 1388: 428-436.
    • (1998) Biochim Biophys Acta , vol.1388 , pp. 428-436
    • Munshi, C.1    Baumann, C.2    Levitt, D.3
  • 115
    • 0032719465 scopus 로고    scopus 로고
    • Characterization of the active site of ADP-ribosyl cyclase
    • Munshi C, Thiel D J, Mathews I I, et al. Characterization of the active site of ADP-ribosyl cyclase. J Biol Chem, 1999, 274: 30770-30777.
    • (1999) J Biol Chem , vol.274 , pp. 30770-30777
    • Munshi, C.1    Thiel, D.J.2    Mathews, I.I.3
  • 116
    • 24344490302 scopus 로고    scopus 로고
    • Crystal structure of human CD38 extracellular domain
    • Liu Q, Kriksunov I A, Graeff R, et al. Crystal structure of human CD38 extracellular domain. Structure, 2005, 13: 1331-1339.
    • (2005) Structure , vol.13 , pp. 1331-1339
    • Liu, Q.1    Kriksunov, I.A.2    Graeff, R.3
  • 117
    • 34047231298 scopus 로고    scopus 로고
    • Structural basis for formation and hydrolysis of calcium messenger cyclic ADP-ribose by human CD38
    • Liu Q, Kriksunov I A, Graeff R, et al. Structural basis for formation and hydrolysis of calcium messenger cyclic ADP-ribose by human CD38. J Biol Chem, 2007, 282: 5853-5861.
    • (2007) J Biol Chem , vol.282 , pp. 5853-5861
    • Liu, Q.1    Kriksunov, I.A.2    Graeff, R.3
  • 118
    • 58849105013 scopus 로고    scopus 로고
    • Conformational closure of the catalytic site of human CD38 induced by calcium
    • Liu Q, Graeff R, Kriksunov I A, et al. Conformational closure of the catalytic site of human CD38 induced by calcium. Biochemistry, 2008, 47: 13966-13973.
    • (2008) Biochemistry , vol.47 , pp. 13966-13973
    • Liu, Q.1    Graeff, R.2    Kriksunov, I.A.3
  • 119
    • 0034647497 scopus 로고    scopus 로고
    • Identification of the enzymatic active site of CD38 by site-directed mutagenesis
    • Munshi C, Aarhus R, Graeff R, et al. Identification of the enzymatic active site of CD38 by site-directed mutagenesis. J Biol Chem, 2000, 275: 21566-21571.
    • (2000) J Biol Chem , vol.275 , pp. 21566-21571
    • Munshi, C.1    Aarhus, R.2    Graeff, R.3
  • 120
    • 70350453607 scopus 로고    scopus 로고
    • Mechanism of cyclizing NAD to cyclic ADP-ribose by ADP-ribosyl cyclase and CD38
    • Graeff R, Liu Q, Kriksunov I A, et al. Mechanism of cyclizing NAD to cyclic ADP-ribose by ADP-ribosyl cyclase and CD38. J Biol Chem, 2009, 284: 27629-27636.
    • (2009) J Biol Chem , vol.284 , pp. 27629-27636
    • Graeff, R.1    Liu, Q.2    Kriksunov, I.A.3
  • 121
    • 0035853770 scopus 로고    scopus 로고
    • A single residue at the active site of CD38 determines its NAD cyclizing and hydrolyzing activities
    • Graeff R, Munshi C, Aarhus R, et al. A single residue at the active site of CD38 determines its NAD cyclizing and hydrolyzing activities. J Biol Chem, 2001, 276: 12169-12173.
    • (2001) J Biol Chem , vol.276 , pp. 12169-12173
    • Graeff, R.1    Munshi, C.2    Aarhus, R.3
  • 122
    • 33749409972 scopus 로고    scopus 로고
    • Acidic residues at the active sites of CD38 and ADP-ribosyl cyclase determine NAADP synthesis and hydrolysis activities
    • Graeff R, Liu Q, Kriksunov I A, et al. Acidic residues at the active sites of CD38 and ADP-ribosyl cyclase determine NAADP synthesis and hydrolysis activities. J Biol Chem, 2006, 281: 28951-28957.
    • (2006) J Biol Chem , vol.281 , pp. 28951-28957
    • Graeff, R.1    Liu, Q.2    Kriksunov, I.A.3
  • 123
    • 33845936792 scopus 로고    scopus 로고
    • Structural basis for the mechanistic understanding of human CD38 controlled multiple catalysis
    • Liu Q, Kriksunov I A, Graeff R, et al. Structural basis for the mechanistic understanding of human CD38 controlled multiple catalysis. J Biol Chem, 2006, 281: 32861-32869.
    • (2006) J Biol Chem , vol.281 , pp. 32861-32869
    • Liu, Q.1    Kriksunov, I.A.2    Graeff, R.3
  • 124
    • 53849148622 scopus 로고    scopus 로고
    • Covalent and noncovalent intermediates of an NAD utilizing enzyme, human CD38
    • Liu Q, Kriksunov I A, Jiang H, et al. Covalent and noncovalent intermediates of an NAD utilizing enzyme, human CD38. Chem Biol, 2008, 15: 1068-1078.
    • (2008) Chem Biol , vol.15 , pp. 1068-1078
    • Liu, Q.1    Kriksunov, I.A.2    Jiang, H.3
  • 125
    • 79251593960 scopus 로고    scopus 로고
    • Dynamic conformations of the CD38-mediated NAD cyclization captured in a single crystal
    • Zhang H, Graeff R, Chen Z, et al. Dynamic conformations of the CD38-mediated NAD cyclization captured in a single crystal. J Mol Biol, 2011, 405: 1070-1078.
    • (2011) J Mol Biol , vol.405 , pp. 1070-1078
    • Zhang, H.1    Graeff, R.2    Chen, Z.3
  • 127
    • 0027486946 scopus 로고
    • 2+ in sea urchin eggs by stimulating cyclic ADP-ribose synthesis
    • 2+ in sea urchin eggs by stimulating cyclic ADP-ribose synthesis. Nature, 1993, 365: 456-459.
    • (1993) Nature , vol.365 , pp. 456-459
    • Galione, A.1    White, A.2    Willmott, N.3
  • 128
    • 0030044293 scopus 로고    scopus 로고
    • Nitric oxide-induced mobilization of intracellular calcium via the cyclic ADP-ribose signaling pathway
    • Willmott N, Sethi J K, Walseth T F, et al. Nitric oxide-induced mobilization of intracellular calcium via the cyclic ADP-ribose signaling pathway. J Biol Chem, 1996, 271: 3699-705.
    • (1996) J Biol Chem , vol.271 , pp. 3699-3705
    • Willmott, N.1    Sethi, J.K.2    Walseth, T.F.3
  • 129
    • 0032079431 scopus 로고    scopus 로고
    • Differential regulation of nicotinic acid adenine dinucleotide phosphate and cADP-ribose production by cAMP and cGMP
    • Wilson H L, Galione A. Differential regulation of nicotinic acid adenine dinucleotide phosphate and cADP-ribose production by cAMP and cGMP. Biochem J, 1998, 331: 837-843.
    • (1998) Biochem J , vol.331 , pp. 837-843
    • Wilson, H.L.1    Galione, A.2
  • 130
    • 0031973097 scopus 로고    scopus 로고
    • Cyclic GMP-dependent and -independent effects on the synthesis of the calcium messengers cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate
    • Graeff R M, Franco L, De Flora A, et al. Cyclic GMP-dependent and -independent effects on the synthesis of the calcium messengers cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate. J Biol Chem, 1998, 273: 118-125.
    • (1998) J Biol Chem , vol.273 , pp. 118-125
    • Graeff, R.M.1    Franco, L.2    de Flora, A.3
  • 131
    • 0033616622 scopus 로고    scopus 로고
    • Evidence of a role for cyclic ADP-ribose in long-term synaptic depression in hippocampus
    • Reyes-Harde M, Empson R, Potter B V L, et al. Evidence of a role for cyclic ADP-ribose in long-term synaptic depression in hippocampus. Proc Natl Acad Sci USA, 1999, 96: 4061-4066.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 4061-4066
    • Reyes-Harde, M.1    Empson, R.2    Potter, B.V.L.3
  • 132
    • 79953295227 scopus 로고    scopus 로고
    • 2+ second messengers, IP3, NAADP and cADPR
    • 2+ second messengers, IP3, NAADP and cADPR. Islets, 2009, 1: 216-223.
    • (2009) Islets , vol.1 , pp. 216-223
    • Shawl, A.I.1    Park, K.H.2    Kim, U.H.3
  • 133
    • 0141446020 scopus 로고    scopus 로고
    • Hormonal control of ADP-ribosyl cyclase in pancreatic acinar cells from rat
    • Sternfeld L, Krause E, Guse A H, et al. Hormonal control of ADP-ribosyl cyclase in pancreatic acinar cells from rat. J Biol Chem, 2003, 36: 33629-33636.
    • (2003) J Biol Chem , vol.36 , pp. 33629-33636
    • Sternfeld, L.1    Krause, E.2    Guse, A.H.3
  • 134
    • 17044399698 scopus 로고    scopus 로고
    • ADP-ribosyl cyclase couples to cyclic AMP signaling in the cardiomyocytes
    • Xie G H, Rah S Y, Kim S J, et al. ADP-ribosyl cyclase couples to cyclic AMP signaling in the cardiomyocytes. Biochem Biophys Res Commun, 2005, 330: 1290-1298.
    • (2005) Biochem Biophys Res Commun , vol.330 , pp. 1290-1298
    • Xie, G.H.1    Rah, S.Y.2    Kim, S.J.3
  • 135
    • 34347266203 scopus 로고    scopus 로고
    • Abscisic acid is an endogenous cytokine in human granulocytes with cyclic ADP-ribose as second messenger
    • Bruzzone S, Moreschi I, Usai C, et al. Abscisic acid is an endogenous cytokine in human granulocytes with cyclic ADP-ribose as second messenger. Proc Natl Acad Sci USA, 2007, 104: 5759-5764.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 5759-5764
    • Bruzzone, S.1    Moreschi, I.2    Usai, C.3
  • 136
    • 67650549689 scopus 로고    scopus 로고
    • Abscisic acid released by human monocytes activates monocytes and vascular smooth muscle cell responses involved in atherogenesis
    • Magnone M, Bruzzone S, Guida L, et al. Abscisic acid released by human monocytes activates monocytes and vascular smooth muscle cell responses involved in atherogenesis. J Biol Chem, 2009, 284: 17808-17818.
    • (2009) J Biol Chem , vol.284 , pp. 17808-17818
    • Magnone, M.1    Bruzzone, S.2    Guida, L.3
  • 137
    • 31544466507 scopus 로고    scopus 로고
    • + regulates intracellular calcium levels and induces activation of human granulocytes
    • + regulates intracellular calcium levels and induces activation of human granulocytes. Biochem J, 2006, 393: 697-704.
    • (2006) Biochem J , vol.393 , pp. 697-704
    • Bruzzone, S.1    Moreschi, I.2    Guida, L.3
  • 138
    • 0030731286 scopus 로고    scopus 로고
    • The CD38/Cyclic ADP-ribose system-A topological paradox
    • De Flora A, Guida L, Franco L, et al. The CD38/Cyclic ADP-ribose system-A topological paradox. Int J Biochem Cell Biol, 1997, 29: 1149-1166.
    • (1997) Int J Biochem Cell Biol , vol.29 , pp. 1149-1166
    • de Flora, A.1    Guida, L.2    Franco, L.3
  • 140
    • 0035930624 scopus 로고    scopus 로고
    • + and cyclic ADP-ribose metabolism and regulates intracellular calcium in 3T3 fibroblasts
    • + and cyclic ADP-ribose metabolism and regulates intracellular calcium in 3T3 fibroblasts. J Biol Chem, 2001, 276: 48300-48308.
    • (2001) J Biol Chem , vol.276 , pp. 48300-48308
    • Bruzzone, S.1    Franco, L.2    Guida, L.3
  • 141
    • 0035235938 scopus 로고    scopus 로고
    • 2+-regulated transmembrane NAD+ fluxes in intact cells
    • 2+-regulated transmembrane NAD+ fluxes in intact cells. Faseb J, 2001, 15: 10-12.
    • (2001) Faseb J , vol.15 , pp. 10-12
    • Bruzzone, S.1    Guida, L.2    Zocchi, E.3
  • 142
    • 0037033120 scopus 로고    scopus 로고
    • Equilibrative and concentrative nucleoside transporters mediate influx of extracellular cyclic ADP-Ribose into 3T3 murine fibroblasts
    • Guida L, Bruzzone S, Sturla L, et al. Equilibrative and concentrative nucleoside transporters mediate influx of extracellular cyclic ADP-Ribose into 3T3 murine fibroblasts. J Biol Chem, 2002, 277: 47097-47105.
    • (2002) J Biol Chem , vol.277 , pp. 47097-47105
    • Guida, L.1    Bruzzone, S.2    Sturla, L.3
  • 143
    • 2542485304 scopus 로고    scopus 로고
    • Concentrative influx of functionally active cyclic ADP-ribose in dimethylsulfoxide-differen tiated HL-60 cells
    • Guida L, Franco L, Bruzzone S, et al. Concentrative influx of functionally active cyclic ADP-ribose in dimethylsulfoxide-differen tiated HL-60 cells. J Biol Chem, 2004, 279: 22066-22075.
    • (2004) J Biol Chem , vol.279 , pp. 22066-22075
    • Guida, L.1    Franco, L.2    Bruzzone, S.3
  • 144
    • 0030947213 scopus 로고    scopus 로고
    • Ultrastructural localization of CD38 immunoreactivity in rat brain
    • Yamada M, Mizuguchi M, Otsuka N, et al. Ultrastructural localization of CD38 immunoreactivity in rat brain. Brain Res, 1997, 756: 52-60.
    • (1997) Brain Res , vol.756 , pp. 52-60
    • Yamada, M.1    Mizuguchi, M.2    Otsuka, N.3
  • 145
    • 69249231115 scopus 로고    scopus 로고
    • CD38 regulation in activated astrocytes: Implications for neuroinflammation and HIV-1 brain infection
    • Kou W, Banerjee S, Eudy J, et al. CD38 regulation in activated astrocytes: Implications for neuroinflammation and HIV-1 brain infection. J Neurosci Res, 2009, 87: 2326-2339.
    • (2009) J Neurosci Res , vol.87 , pp. 2326-2339
    • Kou, W.1    Banerjee, S.2    Eudy, J.3
  • 146
    • 54149104220 scopus 로고    scopus 로고
    • 2+ Signaling occurs via second messenger release from intraorganelle synthesis sites
    • 2+ Signaling occurs via second messenger release from intraorganelle synthesis sites. Curr Biol, 2008, 18: 1612-1618.
    • (2008) Curr Biol , vol.18 , pp. 1612-1618
    • Davis, L.C.1    Morgan, A.J.2    Ruas, M.3
  • 148
    • 0034637449 scopus 로고    scopus 로고
    • Localization of the cyclic ADP-ribose-dependent calcium signaling pathway in hepatocyte nucleus
    • Khoo K M, Han M-K, Park J B, et al. Localization of the cyclic ADP-ribose-dependent calcium signaling pathway in hepatocyte nucleus. J Biol Chem, 2000, 275: 24807-24817.
    • (2000) J Biol Chem , vol.275 , pp. 24807-24817
    • Khoo, K.M.1    Han, M.-K.2    Park, J.B.3
  • 149
    • 9644263908 scopus 로고    scopus 로고
    • Nuclear CD38 in retinoic acid-induced HL-60 cells
    • Yalcintepe L, Albeniz I, Adin-Cinar S, et al. Nuclear CD38 in retinoic acid-induced HL-60 cells. Exper Cell Res, 2005, 303: 14-21.
    • (2005) Exper Cell Res , vol.303 , pp. 14-21
    • Yalcintepe, L.1    Albeniz, I.2    Adin-Cinar, S.3
  • 150
    • 4944228608 scopus 로고    scopus 로고
    • Topogenesis of membrane proteins at the endoplasmic reticulum
    • Higy M, Junne T, Spiess M. Topogenesis of membrane proteins at the endoplasmic reticulum. Biochemistry, 2004, 43: 12716-12722.
    • (2004) Biochemistry , vol.43 , pp. 12716-12722
    • Higy, M.1    Junne, T.2    Spiess, M.3
  • 151
    • 77954070546 scopus 로고    scopus 로고
    • Control of membrane protein topology by a single C-terminal residue
    • Seppala S, Slusky J S, Lloris-Garcera P, et al. Control of membrane protein topology by a single C-terminal residue. Science, 2010, 328: 1698-1700.
    • (2010) Science , vol.328 , pp. 1698-1700
    • Seppala, S.1    Slusky, J.S.2    Lloris-Garcera, P.3
  • 152
    • 0032488777 scopus 로고    scopus 로고
    • A transmembrane form of the prion protein in neurodegenerative disease
    • Hegde R S, Mastrianni J A, Scott M R, et al. A transmembrane form of the prion protein in neurodegenerative disease. Science, 1998, 279: 827-834.
    • (1998) Science , vol.279 , pp. 827-834
    • Hegde, R.S.1    Mastrianni, J.A.2    Scott, M.R.3
  • 153
    • 0032113448 scopus 로고    scopus 로고
    • Regulation of Protein topology by trans-acting factors at the endoplasmic reticulum
    • Hegde R S, Voigt S, Lingappa V R. Regulation of Protein topology by trans-acting factors at the endoplasmic reticulum. Mol Cell, 1998, 2: 85-91.
    • (1998) Mol Cell , vol.2 , pp. 85-91
    • Hegde, R.S.1    Voigt, S.2    Lingappa, V.R.3
  • 154
    • 16344395798 scopus 로고    scopus 로고
    • A transmembrane form of the prion protein is localized in the Golgi apparatus of neurons
    • Stewart R S, Harris D A. A transmembrane form of the prion protein is localized in the Golgi apparatus of neurons. J Biol Chem, 2005, 280: 15855-15864.
    • (2005) J Biol Chem , vol.280 , pp. 15855-15864
    • Stewart, R.S.1    Harris, D.A.2
  • 155
    • 0242412541 scopus 로고    scopus 로고
    • Mutational analysis of topological determinants in prion protein (PrP) and measurement of transmembrane and cytosolic PrP during prion infection
    • Stewart R S, Harris D A. Mutational analysis of topological determinants in prion protein (PrP) and measurement of transmembrane and cytosolic PrP during prion infection. J Biol Chem, 2003, 278: 45960-45968.
    • (2003) J Biol Chem , vol.278 , pp. 45960-45968
    • Stewart, R.S.1    Harris, D.A.2
  • 156
    • 2542469551 scopus 로고    scopus 로고
    • Protein disulfide bond formation in the cytoplasm during oxidative stress
    • Cumming R C, Andon N L, Haynes P A, et al. Protein disulfide bond formation in the cytoplasm during oxidative stress. J Biol Chem, 2004, 279: 21749-21758.
    • (2004) J Biol Chem , vol.279 , pp. 21749-21758
    • Cumming, R.C.1    Andon, N.L.2    Haynes, P.A.3
  • 157
    • 4744363388 scopus 로고    scopus 로고
    • Detection and mapping of widespread intermolecular protein disulfide formation during cardiac oxidative stress using proteomics with diagonal electrophoresis
    • Brennan J P, Wait R, Begum S, et al. Detection and mapping of widespread intermolecular protein disulfide formation during cardiac oxidative stress using proteomics with diagonal electrophoresis. J Biol Chem, 2004, 279: 41352-41360.
    • (2004) J Biol Chem , vol.279 , pp. 41352-41360
    • Brennan, J.P.1    Wait, R.2    Begum, S.3
  • 158
    • 0032189925 scopus 로고    scopus 로고
    • Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins
    • Stewart E J, Åslund F, Beckwith J. Disulfide bond formation in the Escherichia coli cytoplasm: an in vivo role reversal for the thioredoxins. EMBO J, 1998, 17: 5543-5550.
    • (1998) EMBO J , vol.17 , pp. 5543-5550
    • Stewart, E.J.1    Åslund, F.2    Beckwith, J.3
  • 159
    • 79959365485 scopus 로고    scopus 로고
    • Cytosolic CD38 forms intact disulfides and is active in elevating intracellular cyclic ADP-ribose
    • Zhao Y J, Zhang H M, Lam C M C, et al. Cytosolic CD38 forms intact disulfides and is active in elevating intracellular cyclic ADP-ribose. J Biol Chem, 2011, 286: 22170-22177.
    • (2011) J Biol Chem , vol.286 , pp. 22170-22177
    • Zhao, Y.J.1    Zhang, H.M.2    Lam, C.M.C.3
  • 160
    • 0006536415 scopus 로고
    • The alcoholic ferment of yeast-juice
    • Harden A, Young W J. The alcoholic ferment of yeast-juice. Proc R Soc London, 1906, 78: 369-375.
    • (1906) Proc R Soc London , vol.78 , pp. 369-375
    • Harden, A.1    Young, W.J.2
  • 161
    • 0011863707 scopus 로고
    • Pyridin, the hydrogen-transferring component of the fermentation enzymes (pyridine nucleotide)
    • Warburg O, Christian W. Pyridin, the hydrogen-transferring component of the fermentation enzymes (pyridine nucleotide). Biochem Z, 1936, 287: 291.
    • (1936) Biochem Z , vol.287 , pp. 291
    • Warburg, O.1    Christian, W.2


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