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Volumn 19, Issue 6, 2014, Pages 986-1002

The ADP-ribosyl cyclases - The current evolutionary state of the ARCs

Author keywords

ADP ribosyl cyclases; cADPR and NAADP; Evolution; NAD consuming enzymes; Protein family; Review

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSYL CYCLASE; ADP-RIBOSYL CYCLASE 2; CD38 ANTIGEN; GLYCOSYLPHOSPHATIDYLINOSITOL ANCHORED PROTEIN; LEUKOCYTE ANTIGEN; NICOTINAMIDE ADENINE DINUCLEOTIDE;

EID: 84904341525     PISSN: 27686701     EISSN: 27686698     Source Type: Journal    
DOI: 10.2741/4262     Document Type: Review
Times cited : (32)

References (119)
  • 2
    • 0024496833 scopus 로고
    • Structural determination of a cyclic metabolite of NAD+ with intracellular Ca2+-mobilizing activity
    • HC Lee, TF Walseth, GT Bratt, RN Hayes, DL Clapper: Structural determination of a cyclic metabolite of NAD+ with intracellular Ca2+-mobilizing activity. J Biol Chem 264, 1608-1615 (1989)
    • (1989) J Biol Chem , vol.264 , pp. 1608-1615
    • Lee, H.C.1    Walseth, T.F.2    Bratt, G.T.3    Hayes, R.N.4    Clapper, D.L.5
  • 3
    • 14844354701 scopus 로고
    • ADP-ribosyl cyclase: An enzyme that cyclizes NAD+ into a calcium-mobilizing metabolite
    • HC Lee, R Aarhus: ADP-ribosyl cyclase: an enzyme that cyclizes NAD+ into a calcium-mobilizing metabolite. Cell Regul 2, 203-209 (1991)
    • (1991) Cell Regul , vol.2 , pp. 203-209
    • Lee, H.C.1    Aarhus, R.2
  • 4
    • 0023219685 scopus 로고
    • Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate
    • DL Clapper, TF Walseth, PJ Dargie, HC Lee: Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate. J Biol Chem 262, 9561-9568 (1987)
    • (1987) J Biol Chem , vol.262 , pp. 9561-9568
    • Clapper, D.L.1    Walseth, T.F.2    Dargie, P.J.3    Lee, H.C.4
  • 5
    • 0025384609 scopus 로고
    • Comparison of Ca2+ mobilizing activities of cyclic ADP-ribose and inositol trisphosphate
    • PJ Dargie, MC Agre, HC Lee: Comparison of Ca2+ mobilizing activities of cyclic ADP-ribose and inositol trisphosphate. Cell Regul 1, 279-290 (1990)
    • (1990) Cell Regul , vol.1 , pp. 279-290
    • Dargie, P.J.1    Agre, M.C.2    Lee, H.C.3
  • 6
    • 0024381620 scopus 로고
    • Widespread occurrence in animal tissues of an enzyme catalyzing the conversion of NAD+ into a cyclic metabolite with intracellular Ca2+-mobilizing activity
    • N Rusinko, HC Lee: Widespread occurrence in animal tissues of an enzyme catalyzing the conversion of NAD+ into a cyclic metabolite with intracellular Ca2+-mobilizing activity. J Biol Chem 264, 11725-11731 (1989)
    • (1989) J Biol Chem , vol.264 , pp. 11725-11731
    • Rusinko, N.1    Lee, H.C.2
  • 7
    • 0026133769 scopus 로고
    • Purification and characterization of a molluscan egg-specific NADase, a second-messenger enzyme
    • MR Hellmich, F Strumwasser: Purification and characterization of a molluscan egg-specific NADase, a second-messenger enzyme. Cell Regul 2, 193-202 (1991)
    • (1991) Cell Regul , vol.2 , pp. 193-202
    • Hellmich, M.R.1    Strumwasser, F.2
  • 9
    • 0026468136 scopus 로고
    • Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase and human lymphocyte antigen CD38
    • DJ States, TF Walseth, HC Lee: Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase and human lymphocyte antigen CD38. Trends Biochem Sci 17, 495 (1992)
    • (1992) Trends Biochem Sci , vol.17 , pp. 495
    • States, D.J.1    Walseth, T.F.2    Lee, H.C.3
  • 10
    • 0018075060 scopus 로고
    • Studies of bovine erythrocyte NAD glycohydrolase
    • PH Pekala, BM Anderson: Studies of bovine erythrocyte NAD glycohydrolase. J Biol Chem 253, 7453-7459 (1978)
    • (1978) J Biol Chem , vol.253 , pp. 7453-7459
    • Pekala, P.H.1    Anderson, B.M.2
  • 11
    • 0033954107 scopus 로고    scopus 로고
    • Molecular cloning and functional expression of bovine spleen ecto-NAD+ glycohydrolase: Structural identity with human CD38
    • A Augustin, H Muller-Steffner, F Schuber: Molecular cloning and functional expression of bovine spleen ecto-NAD+ glycohydrolase: structural identity with human CD38. Biochem J 345, 43-52 (2000)
    • (2000) Biochem J , vol.345 , pp. 43-52
    • Augustin, A.1    Muller-Steffner, H.2    Schuber, F.3
  • 13
    • 84862027161 scopus 로고    scopus 로고
    • Identification of a major enzyme for the synthesis and hydrolysis of cyclic ADP-ribose in amphibian cells and evolutional conservation of the enzyme from human to invertebrate
    • T Ikeda, S Takasawa, N Noguchi, K Nata, A Yamauchi, I Takahashi, T Yoshikawa, A Sugawara, H Yonekura, H Okamoto: Identification of a major enzyme for the synthesis and hydrolysis of cyclic ADP-ribose in amphibian cells and evolutional conservation of the enzyme from human to invertebrate. Mol Cell Biochem 366, 69-80 (2012)
    • (2012) Mol Cell Biochem , vol.366 , pp. 69-80
    • Ikeda, T.1    Takasawa, S.2    Noguchi, N.3    Nata, K.4    Yamauchi, A.5    Takahashi, I.6    Yoshikawa, T.7    Sugawara, A.8    Yonekura, H.9    Okamoto, H.10
  • 16
    • 77953758506 scopus 로고    scopus 로고
    • A single residue in a novel ADP-ribosyl cyclase controls production of the calcium-mobilizing messengers cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate
    • L Ramakrishnan, H Muller-Steffner, C Bosc, VD Vacquier, F Schuber, M J Moutin, L Dale, S Patel: A single residue in a novel ADP-ribosyl cyclase controls production of the calcium-mobilizing messengers cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate. J Biol Chem 285, 19900-19909 (2010)
    • (2010) J Biol Chem , vol.285 , pp. 19900-19909
    • Ramakrishnan, L.1    Muller-Steffner, H.2    Bosc, C.3    Vacquier, V.D.4    Schuber, F.5    Moutin, M.J.6    Dale, L.7    Patel, S.8
  • 20
    • 56249122625 scopus 로고    scopus 로고
    • Investigating cADPR and NAADP in intact and broken cell preparations
    • AJ Morgan, A Galione: Investigating cADPR and NAADP in intact and broken cell preparations. Methods 46, 194-203 (2008)
    • (2008) Methods , vol.46 , pp. 194-203
    • Morgan, A.J.1    Galione, A.2
  • 21
    • 38649132338 scopus 로고    scopus 로고
    • Evo-devo: Variations on ancestral themes
    • EM De Robertis: Evo-devo: variations on ancestral themes. Cell 132, 185-195 (2008)
    • (2008) Cell , vol.132 , pp. 185-195
    • De Robertis, E.M.1
  • 22
    • 40549103781 scopus 로고    scopus 로고
    • Acoel development supports a simple planula-like urbilaterian
    • A Hejnol, MQ Martindale: Acoel development supports a simple planula-like urbilaterian. Philos Trans R Soc Lond B Biol Sci 363, 1493-1501 (2008)
    • (2008) Philos Trans R Soc Lond B Biol Sci , vol.363 , pp. 1493-1501
    • Hejnol, A.1    Martindale, M.Q.2
  • 23
    • 0031572588 scopus 로고    scopus 로고
    • Human CD38, a leukocyte receptor and ectoenzyme, is a member of a novel eukaryotic gene family of nicotinamide adenine dinucleotide+-converting enzymes: Extensive structural homology with the genes for murine bone marrow stromal cell antigen 1 and aplysian ADP-ribosyl cyclase
    • E Ferrero, F Malavasi: Human CD38, a leukocyte receptor and ectoenzyme, is a member of a novel eukaryotic gene family of nicotinamide adenine dinucleotide+-converting enzymes: extensive structural homology with the genes for murine bone marrow stromal cell antigen 1 and aplysian ADP-ribosyl cyclase. J Immunol 159, 3858-3865 (1997)
    • (1997) J Immunol , vol.159 , pp. 3858-3865
    • Ferrero, E.1    Malavasi, F.2
  • 24
  • 26
    • 0029857644 scopus 로고    scopus 로고
    • Genomic organization and chromosomal localization of the mouse Bp3 gene, a member of the CD38/ADP-ribosyl cyclase family
    • C Dong, D Willerford, FW Alt, MD Cooper: Genomic organization and chromosomal localization of the mouse Bp3 gene, a member of the CD38/ADP-ribosyl cyclase family. Immunogenetics 45, 35-43 (1996)
    • (1996) Immunogenetics , vol.45 , pp. 35-43
    • Dong, C.1    Willerford, D.2    Alt, F.W.3    Cooper, M.D.4
  • 29
    • 0013502347 scopus 로고    scopus 로고
    • Cyclic ADP-ribose and NAADP - A story of two calcium messengers
    • Ed: HC Lee, Kluwer Dordrecht, The Netherlands
    • HC Lee: Cyclic ADP-ribose and NAADP - A story of two calcium messengers. In: Cyclic ADP-ribose and NAADP - Structures, Metabolism and Functions. Ed: HC Lee, Kluwer Dordrecht, The Netherlands (2002)
    • (2002) Cyclic ADP-ribose and NAADP - Structures, Metabolism and Functions
    • Lee, H.C.1
  • 30
    • 0000493971 scopus 로고
    • Studies on the Mode of Action of Diphtheria Toxin. 2. Effect of Toxin on Amino Acid Incorporation in Cell-Free Systems
    • RJ Collier, AM Pappenheimer Jr: Studies on the Mode of Action of Diphtheria Toxin. 2. Effect of Toxin on Amino Acid Incorporation in Cell-Free Systems. J Exp Med 120, 1019-1039 (1964)
    • (1964) J Exp Med , vol.120 , pp. 1019-1039
    • Collier, R.J.1    Pappenheimer Jr., A.M.2
  • 31
    • 0343508071 scopus 로고
    • A primary metabolic change of fertilization: Interconversion of pyridine nucleotides
    • D Epel: A primary metabolic change of fertilization: interconversion of pyridine nucleotides. Biochemical and Biophysical Research Communications 17, 7 (1964)
    • (1964) Biochemical and Biophysical Research Communications , vol.17 , pp. 7
    • Epel, D.1
  • 32
    • 84878996231 scopus 로고    scopus 로고
    • The Cyclic ADP-Ribose/NAADP/CD38-Signaling Pathway: Past and Present
    • HC Lee: The Cyclic ADP-Ribose/NAADP/CD38-Signaling Pathway: Past and Present. Messenger 1, 16-33 (2012)
    • (2012) Messenger , vol.1 , pp. 16-33
    • Lee, H.C.1
  • 33
    • 79953153188 scopus 로고    scopus 로고
    • TRPM2: A multifunctional ion channel for calcium signalling
    • A Sumoza-Toledo, R Penner: TRPM2: a multifunctional ion channel for calcium signalling. J Physiol 589, 1515-1525 (2011)
    • (2011) J Physiol , vol.589 , pp. 1515-1525
    • Sumoza-Toledo, A.1    Penner, R.2
  • 34
    • 84857686131 scopus 로고    scopus 로고
    • Ancestral Ca2+ signaling machinery in early animal and fungal evolution
    • X Cai, DE Clapham: Ancestral Ca2+ signaling machinery in early animal and fungal evolution. Mol Biol Evol 29, 91-100 (2012)
    • (2012) Mol Biol Evol , vol.29 , pp. 91-100
    • Cai, X.1    Clapham, D.E.2
  • 36
    • 33845343261 scopus 로고    scopus 로고
    • Membrane-protein topology
    • G von Heijne: Membrane-protein topology. Nat Rev Mol Cell Biol 7, 909-918 (2006)
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 909-918
    • Von Heijne, G.1
  • 37
    • 70350446961 scopus 로고    scopus 로고
    • The biology of memory: A forty-year perspective
    • ER Kandel: The biology of memory: a forty-year perspective. J Neurosci 29, 12748-12756 (2009)
    • (2009) J Neurosci , vol.29 , pp. 12748-12756
    • Kandel, E.R.1
  • 38
    • 0032032393 scopus 로고    scopus 로고
    • Cyclic ADP-ribose and calcium-induced calcium release regulate neurotransmitter release at a cholinergic synapse of Aplysia
    • JP Mothet, P Fossier, FM Meunier, J Stinnakre, L Tauc, G Baux: Cyclic ADP-ribose and calcium-induced calcium release regulate neurotransmitter release at a cholinergic synapse of Aplysia. J Physiol 507, 405-414 (1998)
    • (1998) J Physiol , vol.507 , pp. 405-414
    • Mothet, J.P.1    Fossier, P.2    Meunier, F.M.3    Stinnakre, J.4    Tauc, L.5    Baux, G.6
  • 39
    • 55549097127 scopus 로고    scopus 로고
    • Regulation of nuclear Ca2+ signaling by translocation of the Ca2+ messenger synthesizing enzyme ADP-ribosyl cyclase during neuronal depolarization
    • S Bezin, G Charpentier, HC Lee, G Baux, P Fossier, JM Cancela: Regulation of nuclear Ca2+ signaling by translocation of the Ca2+ messenger synthesizing enzyme ADP-ribosyl cyclase during neuronal depolarization. J Biol Chem 283, 27859-27870 (2008)
    • (2008) J Biol Chem , vol.283 , pp. 27859-27870
    • Bezin, S.1    Charpentier, G.2    Lee, H.C.3    Baux, G.4    Fossier, P.5    Cancela, J.M.6
  • 40
    • 0029616337 scopus 로고
    • ADP-ribosyl cyclase and CD38 catalyze the synthesis of a calcium-mobilizing metabolite from NADP
    • R Aarhus, RM Graeff, DM Dickey, TF Walseth, HC Lee: ADP-ribosyl cyclase and CD38 catalyze the synthesis of a calcium-mobilizing metabolite from NADP. J Biol Chem 270, 30327-30333 (1995)
    • (1995) J Biol Chem , vol.270 , pp. 30327-30333
    • Aarhus, R.1    Graeff, R.M.2    Dickey, D.M.3    Walseth, T.F.4    Lee, H.C.5
  • 42
    • 84873188874 scopus 로고    scopus 로고
    • Calcium pathway machinery at fertilization in echinoderms
    • I Ramos, GM Wessel: Calcium pathway machinery at fertilization in echinoderms. Cell Calcium 53, 16-23 (2013)
    • (2013) Cell Calcium , vol.53 , pp. 16-23
    • Ramos, I.1    Wessel, G.M.2
  • 43
    • 79953770681 scopus 로고    scopus 로고
    • Enzymatic shaving of the tegument surface of live schistosomes for proteomic analysis: A rational approach to select vaccine candidates
    • W Castro-Borges, A Dowle, RS Curwen, J Thomas-Oates, RA Wilson: Enzymatic shaving of the tegument surface of live schistosomes for proteomic analysis: a rational approach to select vaccine candidates. PLoS Negl Trop Dis 5, e993 (2011)
    • (2011) PLoS Negl Trop Dis , vol.5
    • Castro-Borges, W.1    Dowle, A.2    Curwen, R.S.3    Thomas-Oates, J.4    Wilson, R.A.5
  • 44
    • 33749349245 scopus 로고    scopus 로고
    • Redesign of Schistosoma mansoni NAD+ catabolizing enzyme: Active site H103W mutation restores ADP-ribosyl cyclase activity
    • I Kuhn, E Kellenberger, D Rognan, FE Lund, H Muller-Steffner, F Schuber: Redesign of Schistosoma mansoni NAD+ catabolizing enzyme: active site H103W mutation restores ADP-ribosyl cyclase activity. Biochemistry 45, 11867-11878 (2006)
    • (2006) Biochemistry , vol.45 , pp. 11867-11878
    • Kuhn, I.1    Kellenberger, E.2    Rognan, D.3    Lund, F.E.4    Muller-Steffner, H.5    Schuber, F.6
  • 45
    • 84884679558 scopus 로고    scopus 로고
    • Schistosoma mansoni NAD catabolizing enzyme: Identification of key residues in catalysis
    • I Kuhn, E Kellenberger, F Schuber, H Muller-Steffner: Schistosoma mansoni NAD catabolizing enzyme: Identification of key residues in catalysis. Biochim Biophys Acta 1834, 2520-2527 (2013)
    • (2013) Biochim Biophys Acta , vol.1834 , pp. 2520-2527
    • Kuhn, I.1    Kellenberger, E.2    Schuber, F.3    Muller-Steffner, H.4
  • 46
    • 0026958382 scopus 로고
    • Molecular evidence linking hominid evolution to recent radiation of schistosomes (Platyhelminthes: Trematoda)
    • L Despres, D Imbert-Establet, C Combes, F Bonhomme: Molecular evidence linking hominid evolution to recent radiation of schistosomes (Platyhelminthes: Trematoda). Mol Phylogenet Evol 1, 295-304 (1992)
    • (1992) Mol Phylogenet Evol , vol.1 , pp. 295-304
    • Despres, L.1    Imbert-Establet, D.2    Combes, C.3    Bonhomme, F.4
  • 47
    • 57049129327 scopus 로고    scopus 로고
    • Praziquantel: Mechanisms of action, resistance and new derivatives for schistosomiasis
    • MJ Doenhoff, D Cioli, J Utzinger: Praziquantel: mechanisms of action, resistance and new derivatives for schistosomiasis. Curr Opin Infect Dis 21, 659-667 (2008)
    • (2008) Curr Opin Infect Dis , vol.21 , pp. 659-667
    • Doenhoff, M.J.1    Cioli, D.2    Utzinger, J.3
  • 49
    • 0025265030 scopus 로고
    • Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface glycoprotein with an unusual discontinuous pattern of expression during lymphocyte differentiation
    • DG Jackson, JI Bell: Isolation of a cDNA encoding the human CD38 (T10) molecule, a cell surface glycoprotein with an unusual discontinuous pattern of expression during lymphocyte differentiation. J Immunol 144, 2811-2815 (1990)
    • (1990) J Immunol , vol.144 , pp. 2811-2815
    • Jackson, D.G.1    Bell, J.I.2
  • 51
    • 0034304851 scopus 로고    scopus 로고
    • Lipid rafts and signal transduction
    • K Simons, D Toomre: Lipid rafts and signal transduction. Nat Rev Mol Cell Biol 1, 31-39 (2000)
    • (2000) Nat Rev Mol Cell Biol , vol.1 , pp. 31-39
    • Simons, K.1    Toomre, D.2
  • 52
    • 0021943992 scopus 로고
    • The modulated expression of Mo5, a human myelomonocytic plasma membrane antigen
    • RF Todd 3rd, JA Roach, MA Arnaout: The modulated expression of Mo5, a human myelomonocytic plasma membrane antigen. Blood 65, 964-973 (1985)
    • (1985) Blood , vol.65 , pp. 964-973
    • Todd III, R.F.1    Roach, J.A.2    Arnaout, M.A.3
  • 59
    • 84879014238 scopus 로고    scopus 로고
    • Effects of keratinocyte growth factor on skin epithelial differentiation of human amnion epithelial cells
    • SS Fatimah, GC Tan, K Chua, AE Tan, AG Nur Azurah, AR Hayati: Effects of keratinocyte growth factor on skin epithelial differentiation of human amnion epithelial cells. Burns 39, 905-915 (2013)
    • (2013) Burns , vol.39 , pp. 905-915
    • Fatimah, S.S.1    Tan, G.C.2    Chua, K.3    Tan, A.E.4    Nur Azurah, A.G.5    Hayati, A.R.6
  • 61
    • 0029818389 scopus 로고    scopus 로고
    • Stage-specific expression of mouse BST-1/BP-3 on the early B and T cell progenitors prior to gene rearrangement of antigen receptor
    • K Ishihara, Y Kobune, Y Okuyama, M Itoh, BO Lee, O Muraoka, T Hirano: Stage-specific expression of mouse BST-1/BP-3 on the early B and T cell progenitors prior to gene rearrangement of antigen receptor. Int Immunol 8, 1395-1404 (1996)
    • (1996) Int Immunol , vol.8 , pp. 1395-1404
    • Ishihara, K.1    Kobune, Y.2    Okuyama, Y.3    Itoh, M.4    Lee, B.O.5    Muraoka, O.6    Hirano, T.7
  • 62
    • 0032532046 scopus 로고    scopus 로고
    • Deletion of bone marrow stromal cell antigen-1 (CD157) gene impaired systemic thymus independent-2 antigen-induced IgG3 and mucosal TD antigen-elicited IgA responses
    • M Itoh, K Ishihara, T Hiroi, BO Lee, H Maeda, H Iijima, M Yanagita, H Kiyono, T Hirano: Deletion of bone marrow stromal cell antigen-1 (CD157) gene impaired systemic thymus independent-2 antigen-induced IgG3 and mucosal TD antigen-elicited IgA responses. J Immunol 161, 3974-3983 (1998)
    • (1998) J Immunol , vol.161 , pp. 3974-3983
    • Itoh, M.1    Ishihara, K.2    Hiroi, T.3    Lee, B.O.4    Maeda, H.5    Iijima, H.6    Yanagita, M.7    Kiyono, H.8    Hirano, T.9
  • 64
    • 84866366579 scopus 로고    scopus 로고
    • The membrane-bound enzyme CD38 exists in two opposing orientations
    • YJ Zhao, CM Lam, HC Lee: The membrane-bound enzyme CD38 exists in two opposing orientations. Sci Signal 5, ra67 (2012)
    • (2012) Sci Signal , vol.5
    • Zhao, Y.J.1    Lam, C.M.2    Lee, H.C.3
  • 67
    • 54849437726 scopus 로고    scopus 로고
    • CD38 is constitutively expressed in the nucleus of human hematopoietic cells
    • M Orciani, O Trubiani, S Guarnieri, E Ferrero, R Di Primio: CD38 is constitutively expressed in the nucleus of human hematopoietic cells. J Cell Biochem 105, 905-912 (2008)
    • (2008) J Cell Biochem , vol.105 , pp. 905-912
    • Orciani, M.1    Trubiani, O.2    Guarnieri, S.3    Ferrero, E.4    Di Primio, R.5
  • 68
    • 0030775072 scopus 로고    scopus 로고
    • Identification of bovine liver mitochondrial NAD+ glycohydrolase as ADP-ribosyl cyclase
    • M Ziegler, D Jorcke, M Schweiger: Identification of bovine liver mitochondrial NAD+ glycohydrolase as ADP-ribosyl cyclase. Biochem J 326, 401-405 (1997)
    • (1997) Biochem J , vol.326 , pp. 401-405
    • Ziegler, M.1    Jorcke, D.2    Schweiger, M.3
  • 69
    • 80051794561 scopus 로고    scopus 로고
    • CD38/ADP-ribosyl cyclase in the rat sublingual gland: Subcellular localization under resting and saliva-secreting conditions
    • W Masuda, E Jimi: CD38/ADP-ribosyl cyclase in the rat sublingual gland: subcellular localization under resting and saliva-secreting conditions. Arch Biochem Biophys 513, 131-139 (2011)
    • (2011) Arch Biochem Biophys , vol.513 , pp. 131-139
    • Masuda, W.1    Jimi, E.2
  • 72
    • 84867859797 scopus 로고    scopus 로고
    • Prostasomes are heterogeneous regarding size and appearance but affiliated to one DNA-containing exosome family
    • GK Ronquist, A Larsson, A Stavreus-Evers, G Ronquist: Prostasomes are heterogeneous regarding size and appearance but affiliated to one DNA-containing exosome family. Prostate 72, 1736-1745 (2012)
    • (2012) Prostate , vol.72 , pp. 1736-1745
    • Ronquist, G.K.1    Larsson, A.2    Stavreus-Evers, A.3    Ronquist, G.4
  • 75
    • 0035853770 scopus 로고    scopus 로고
    • A single residue at the active site of CD38 determines its NAD cyclizing and hydrolyzing activities
    • R Graeff, C Munshi, R Aarhus, M Johns, HC Lee: A single residue at the active site of CD38 determines its NAD cyclizing and hydrolyzing activities. J Biol Chem 276, 12169-12173 (2001)
    • (2001) J Biol Chem , vol.276 , pp. 12169-12173
    • Graeff, R.1    Munshi, C.2    Aarhus, R.3    Johns, M.4    Lee, H.C.5
  • 76
    • 84878497749 scopus 로고    scopus 로고
    • Human monogenic disease genes have frequently functionally redundant paralogs
    • WH Chen, XM Zhao, V van Noort, P Bork: Human monogenic disease genes have frequently functionally redundant paralogs. PLoS Comput Biol 9, e1003073 (2013)
    • (2013) PLoS Comput Biol , vol.9
    • Chen, W.H.1    Zhao, X.M.2    Van Noort, V.3    Bork, P.4
  • 81
    • 77953631698 scopus 로고    scopus 로고
    • The secret life of NAD+: An old metabolite controlling new metabolic signaling pathways
    • RH Houtkooper, C Canto, RJ Wanders, J Auwerx: The secret life of NAD+: an old metabolite controlling new metabolic signaling pathways. Endocr Rev 31, 194-223 (2010)
    • (2010) Endocr Rev , vol.31 , pp. 194-223
    • Houtkooper, R.H.1    Canto, C.2    Wanders, R.J.3    Auwerx, J.4
  • 85
    • 0034617096 scopus 로고    scopus 로고
    • Interaction of two classes of ADP-ribose transfer reactions in immune signaling
    • MK Han, YS Cho, YS Kim, CY Yim, UH Kim: Interaction of two classes of ADP-ribose transfer reactions in immune signaling. J Biol Chem 275, 20799-20805 (2000)
    • (2000) J Biol Chem , vol.275 , pp. 20799-20805
    • Han, M.K.1    Cho, Y.S.2    Kim, Y.S.3    Yim, C.Y.4    Kim, U.H.5
  • 86
    • 0034816206 scopus 로고    scopus 로고
    • Significance of ecto-cyclase activity of CD38 in insulin secretion of mouse pancreatic islet cells
    • NH An, MK Han, C Um, BH Park, BJ Park, HK Kim, UH Kim: Significance of ecto-cyclase activity of CD38 in insulin secretion of mouse pancreatic islet cells. Biochem Biophys Res Commun 282, 781-786 (2001)
    • (2001) Biochem Biophys Res Commun , vol.282 , pp. 781-786
    • An, N.H.1    Han, M.K.2    Um, C.3    Park, B.H.4    Park, B.J.5    Kim, H.K.6    Kim, U.H.7
  • 88
    • 34250855032 scopus 로고    scopus 로고
    • NAD+ released during inflammation participates in T cell homeostasis by inducing ART2-mediated death of naive T cells in vivo
    • S Adriouch, S Hubert, S Pechberty, F Koch-Nolte, F Haag, M Seman: NAD+ released during inflammation participates in T cell homeostasis by inducing ART2-mediated death of naive T cells in vivo. J Immunol 179, 186-194 (2007)
    • (2007) J Immunol , vol.179 , pp. 186-194
    • Adriouch, S.1    Hubert, S.2    Pechberty, S.3    Koch-Nolte, F.4    Haag, F.5    Seman, M.6
  • 89
    • 84865213154 scopus 로고    scopus 로고
    • NAD induces astrocyte calcium flux and cell death by ART2 and P2X7 pathway
    • J Wang, J Yang, P Liu, X Bi, C Li, K Zhu: NAD induces astrocyte calcium flux and cell death by ART2 and P2X7 pathway. Am J Pathol 181, 746-752 (2012)
    • (2012) Am J Pathol , vol.181 , pp. 746-752
    • Wang, J.1    Yang, J.2    Liu, P.3    Bi, X.4    Li, C.5    Zhu, K.6
  • 90
    • 33646386147 scopus 로고    scopus 로고
    • ADP-ribosylation of membrane proteins: Unveiling the secrets of a crucial regulatory mechanism in mammalian cells
    • F Koch-Nolte, S Adriouch, P Bannas, C Krebs, F Scheuplein, M Seman, F Haag: ADP-ribosylation of membrane proteins: unveiling the secrets of a crucial regulatory mechanism in mammalian cells. Ann Med 38, 188-199 (2006)
    • (2006) Ann Med , vol.38 , pp. 188-199
    • Koch-Nolte, F.1    Adriouch, S.2    Bannas, P.3    Krebs, C.4    Scheuplein, F.5    Seman, M.6    Haag, F.7
  • 91
    • 67349283054 scopus 로고    scopus 로고
    • The evolving understanding of COPI vesicle formation
    • VW Hsu, SY Lee, JS Yang: The evolving understanding of COPI vesicle formation. Nat Rev Mol Cell Biol 10, 360-364 (2009)
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 360-364
    • Hsu, V.W.1    Lee, S.Y.2    Yang, J.S.3
  • 94
    • 84867877340 scopus 로고    scopus 로고
    • The NAD metabolome - A key determinant of cancer cell biology
    • A Chiarugi, C Dolle, R Felici, M Ziegler: The NAD metabolome - a key determinant of cancer cell biology. Nat Rev Cancer 12, 741-752 (2012)
    • (2012) Nat Rev Cancer , vol.12 , pp. 741-752
    • Chiarugi, A.1    Dolle, C.2    Felici, R.3    Ziegler, M.4
  • 95
    • 84881460276 scopus 로고    scopus 로고
    • How metabolism generates signals during innate immunity and inflammation
    • AF McGettrick, LA O'Neill: How metabolism generates signals during innate immunity and inflammation. J Biol Chem 288, 22893-22898 (2013)
    • (2013) J Biol Chem , vol.288 , pp. 22893-22898
    • McGettrick, A.F.1    O'Neill, L.A.2
  • 98
    • 84864463147 scopus 로고    scopus 로고
    • Seq2Logo: A method for construction and visualization of amino acid binding motifs and sequence profiles including sequence weighting, pseudo counts and two-sided representation of amino acid enrichment and depletion
    • MC Thomsen, M Nielsen: Seq2Logo: a method for construction and visualization of amino acid binding motifs and sequence profiles including sequence weighting, pseudo counts and two-sided representation of amino acid enrichment and depletion. Nucleic Acids Res 40, W281-287 (2012)
    • (2012) Nucleic Acids Res , vol.40
    • Thomsen, M.C.1    Nielsen, M.2
  • 103
    • 84864772007 scopus 로고    scopus 로고
    • The CD19/CD81 complex physically interacts with CD38 but is not required to induce proliferation in mouse B lymphocytes
    • F Vences-Catalan, R Rajapaksa, S Levy, L Santos-Argumedo: The CD19/CD81 complex physically interacts with CD38 but is not required to induce proliferation in mouse B lymphocytes. Immunology 137, 48-55 (2012)
    • (2012) Immunology , vol.137 , pp. 48-55
    • Vences-Catalan, F.1    Rajapaksa, R.2    Levy, S.3    Santos-Argumedo, L.4
  • 104
    • 84860364617 scopus 로고    scopus 로고
    • The role of CD38 in Fcgamma receptor (FcgammaR)-mediated phagocytosis in murine macrophages
    • J Kang, KH Park, JJ Kim, EK Jo, MK Han, UH Kim: The role of CD38 in Fcgamma receptor (FcgammaR)-mediated phagocytosis in murine macrophages. J Biol Chem 287, 14502-14514 (2012)
    • (2012) J Biol Chem , vol.287 , pp. 14502-14514
    • Kang, J.1    Park, K.H.2    Kim, J.J.3    Jo, E.K.4    Han, M.K.5    Kim, U.H.6
  • 107
    • 84881527948 scopus 로고    scopus 로고
    • Potential role of the CD38/cADPR signaling pathway as an underlying mechanism of the effects of medetomidine on insulin and glucose homeostasis
    • AG Guedes, EP Rude, MS Kannan: Potential role of the CD38/cADPR signaling pathway as an underlying mechanism of the effects of medetomidine on insulin and glucose homeostasis. Vet Anaesth Analg 40, 512-516 (2013)
    • (2013) Vet Anaesth Analg , vol.40 , pp. 512-516
    • Guedes, A.G.1    Rude, E.P.2    Kannan, M.S.3
  • 110
    • 84855459605 scopus 로고    scopus 로고
    • NAD(P)H oxidase-dependent intracellular and extracellular O2&z.Ast;- production in coronary arterial myocytes from CD38 knockout mice
    • M Xu, Y Zhang, M Xia, XX Li, JK Ritter, F Zhang, PL Li: NAD(P)H oxidase-dependent intracellular and extracellular O2&z.ast;- production in coronary arterial myocytes from CD38 knockout mice. Free Radic Biol Med 52, 357-365 (2012)
    • (2012) Free Radic Biol Med , vol.52 , pp. 357-365
    • Xu, M.1    Zhang, Y.2    Xia, M.3    Li, X.X.4    Ritter, J.K.5    Zhang, F.6    Li, P.L.7
  • 112
    • 84455180597 scopus 로고    scopus 로고
    • Altered behavioral and metabolic circadian rhythms in mice with disrupted NAD+ oscillation
    • S Sahar, V Nin, MT Barbosa, EN Chini, P Sassone-Corsi: Altered behavioral and metabolic circadian rhythms in mice with disrupted NAD+ oscillation. Aging 3, 794-802 (2011)
    • (2011) Aging , vol.3 , pp. 794-802
    • Sahar, S.1    Nin, V.2    Barbosa, M.T.3    Chini, E.N.4    Sassone-Corsi, P.5
  • 113
    • 84860422561 scopus 로고    scopus 로고
    • Disruption of CD38 gene enhances cardiac functions by elevating serum testosterone in the male null mice
    • L Gan, W Jiang, YF Xiao, L Deng, LD Gu, ZY Guo, ZC Zhou, D Wu, HB Xin: Disruption of CD38 gene enhances cardiac functions by elevating serum testosterone in the male null mice. Life Sci 89, 491-497 (2011)
    • (2011) Life Sci , vol.89 , pp. 491-497
    • Gan, L.1    Jiang, W.2    Xiao, Y.F.3    Deng, L.4    Gu, L.D.5    Guo, Z.Y.6    Zhou, Z.C.7    Wu, D.8    Xin, H.B.9
  • 114
    • 84860395796 scopus 로고    scopus 로고
    • Cyclic ADP-ribose requires CD38 to regulate the release of ATP in visceral smooth muscle
    • L Durnin, VN Mutafova-Yambolieva: Cyclic ADP-ribose requires CD38 to regulate the release of ATP in visceral smooth muscle. FEBS J 278, 3095-3108 (2011)
    • (2011) FEBS J , vol.278 , pp. 3095-3108
    • Durnin, L.1    Mutafova-Yambolieva, V.N.2
  • 115
    • 84872790450 scopus 로고    scopus 로고
    • Regulation of renin release via cyclic ADP-ribose-mediated signaling: Evidence from mice lacking CD38 gene
    • J Xiong, M Xia, F Yi, JM Abais, N Li, KM Boini, PL Li: Regulation of renin release via cyclic ADP-ribose-mediated signaling: evidence from mice lacking CD38 gene. Cell Physiol Biochem 31, 44-55 (2013)
    • (2013) Cell Physiol Biochem , vol.31 , pp. 44-55
    • Xiong, J.1    Xia, M.2    Yi, F.3    Abais, J.M.4    Li, N.5    Boini, K.M.6    Li, P.L.7
  • 117
    • 84864699888 scopus 로고    scopus 로고
    • CD38 deficiency in the tumor microenvironment attenuates glioma progression and modulates features of tumor-associated microglia/macrophages
    • A Levy, E Blacher, H Vaknine, FE Lund, R Stein, L Mayo: CD38 deficiency in the tumor microenvironment attenuates glioma progression and modulates features of tumor-associated microglia/macrophages. Neuro Oncol 14, 1037-1049 (2012)
    • (2012) Neuro Oncol , vol.14 , pp. 1037-1049
    • Levy, A.1    Blacher, E.2    Vaknine, H.3    Lund, F.E.4    Stein, R.5    Mayo, L.6
  • 119
    • 79953886283 scopus 로고    scopus 로고
    • Critical role for CD38-mediated Ca2+ signaling in thrombin-induced procoagulant activity of mouse platelets and hemostasis
    • M Mushtaq, TS Nam, UH Kim: Critical role for CD38-mediated Ca2+ signaling in thrombin-induced procoagulant activity of mouse platelets and hemostasis. J Biol Chem 286, 12952-12958 (2011)
    • (2011) J Biol Chem , vol.286 , pp. 12952-12958
    • Mushtaq, M.1    Nam, T.S.2    Kim, U.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.