메뉴 건너뛰기




Volumn 287, Issue 38, 2012, Pages 31633-31640

Cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate (NAADP) as messengers for calcium mobilization

Author keywords

[No Author keywords available]

Indexed keywords

ADP-RIBOSE; CALCIUM MOBILIZATION; CATALYTIC MECHANISMS; ENDOPLASMIC RETICULUM; NICOTINIC ACID ADENINE DINUCLEOTIDE PHOSPHATE; RYANODINE RECEPTORS; SECOND MESSENGER;

EID: 84866361328     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.R112.349464     Document Type: Short Survey
Times cited : (170)

References (101)
  • 1
    • 0020643801 scopus 로고
    • 2+from a non-mitochondrial intracellular store in pancreatic acinar cells by inositol 1,4,5-trisphosphate
    • 2+ from a non-mitochondrial intracellular store in pancreatic acinar cells by inositol 1,4,5-trisphosphate. Nature 306, 67-69
    • (1983) Nature , vol.306 , pp. 67-69
    • Streb, H.1    Irvine, R.F.2    Berridge, M.J.3    Schulz, I.4
  • 2
    • 0028950282 scopus 로고
    • A derivative of NADP mobilizes calcium stores insensitive to inositol trisphosphate and cyclic ADP-ribose
    • Lee, H. C., and Aarhus, R. (1995) A derivative of NADP mobilizes calcium stores insensitive to inositol trisphosphate and cyclic ADP-ribose. J. Biol. Chem. 270, 2152-2157
    • (1995) J. Biol. Chem. , vol.270 , pp. 2152-2157
    • Lee, H.C.1    Aarhus, R.2
  • 3
    • 0028402138 scopus 로고
    • The crystal structure of cyclic ADP-ribose
    • Lee, H. C., Aarhus, R., and Levitt, D. (1994) The crystal structure of cyclic ADP-ribose. Nat. Struct. Biol. 1, 143-144
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 143-144
    • Lee, H.C.1    Aarhus, R.2    Levitt, D.3
  • 5
    • 0031444350 scopus 로고    scopus 로고
    • Abscisic acid signaling through cyclic ADP-ribose in plants
    • DOI 10.1126/science.278.5346.2126
    • Wu, Y., Kuzma, J., Maréchal, E., Graeff, R., Lee, H. C., Foster, R., and Chua, N. H. (1997) Abscisic acid signaling through cyclic ADP-ribose in plants. Science 278, 2126-2130 (Pubitemid 28028323)
    • (1997) Science , vol.278 , Issue.5346 , pp. 2126-2130
    • Wu, Y.1    Kuzma, J.2    Marechal, E.3    Graeff, R.4    Lee, H.C.5    Foster, R.6    Chua, N.-H.7
  • 7
    • 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., and Wong, J. T. (2009) Cyclic ADP-ribose links metabolism to multiple fission in the dinoflagellate Crypthecodinium cohnii. Cell Calcium 45, 346-357
    • (2009) Cell Calcium , vol.45 , pp. 346-357
    • Lam, C.M.1    Yeung, P.K.2    Lee, H.C.3    Wong, J.T.4
  • 11
    • 79960629413 scopus 로고    scopus 로고
    • Cyclic ADP-ribose and NAADP: Fraternal twin messengers for calcium signaling
    • Lee, H. C. (2011) Cyclic ADP-ribose and NAADP: fraternal twin messengers for calcium signaling. Sci. China Life Sci. 54, 699-711
    • (2011) Sci. China Life Sci. , vol.54 , pp. 699-711
    • Lee, H.C.1
  • 12
    • 0345609814 scopus 로고    scopus 로고
    • Mechanisms of calcium signaling by cyclic ADP-ribose and NAADP
    • Lee, H. C. (1997) Mechanisms of calcium signaling by cyclic ADP-ribose and NAADP. Physiol. Rev. 77, 1133-1164
    • (1997) Physiol. Rev. , vol.77 , pp. 1133-1164
    • Lee, H.C.1
  • 13
    • 0019881742 scopus 로고
    • Structure of the active ternary complex of pig heart lactate dehydrogenase with S-lac-NAD at 2.7 Å resolution
    • Grau, U. M., Trommer, W. E., and Rossmann, M. G. (1981) Structure of the active ternary complex of pig heart lactate dehydrogenase with S-lac-NAD at 2.7 Å resolution. J. Mole. Biol. 151, 289-307
    • (1981) J. Mole. Biol. , vol.151 , pp. 289-307
    • Grau, U.M.1    Trommer, W.E.2    Rossmann, M.G.3
  • 14
    • 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., and Lee, H. C. (1987) Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate. J. Biol. Chem. 262, 9561-9568 (Pubitemid 17102610)
    • (1987) Journal of Biological Chemistry , vol.262 , Issue.20 , pp. 9561-9568
    • Clapper, D.L.1    Walseth, T.F.2    Dargie, P.J.3    Hon, C.L.4
  • 15
    • 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. 1, 279-290
    • (1990) Cell Regul. , vol.1 , pp. 279-290
    • Dargie, P.J.1    Agre, M.C.2    Lee, H.C.3
  • 16
    • 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 253, 1143-1146
    • (1991) Science , vol.253 , pp. 1143-1146
    • Galione, A.1    Lee, H.C.2    Busa, W.B.3
  • 17
    • 0027518440 scopus 로고
    • Potentiation of calcium- And caffeine-induced calcium release by cyclic ADP-ribose
    • Lee, H. C. (1993) Potentiation of calcium- and caffeine-induced calcium release by cyclic ADP-ribose. J. Biol. Chem. 268, 293-299
    • (1993) J. Biol. Chem. , vol.268 , pp. 293-299
    • Lee, H.C.1
  • 18
    • 0035033022 scopus 로고    scopus 로고
    • Physiological functions of cyclic ADP-ribose and NAADP as calcium messengers
    • Lee, H. C. (2001) Physiological functions of cyclic ADP-ribose and NAADP as calcium messengers. Annu. Rev. Pharmacol. Toxicol. 41, 317-345
    • (2001) Annu. Rev. Pharmacol. Toxicol. , vol.41 , pp. 317-345
    • Lee, H.C.1
  • 19
    • 0028131433 scopus 로고
    • Cyclic ADP ribose activation of the ryanodine receptor is mediated by calmodulin
    • DOI 10.1038/370307a0
    • Lee, H. C., Aarhus, R., Graeff, R., Gurnack, M. E., and Walseth, T. F. (1994) Cyclic ADP ribose activation of the ryanodine receptor is mediated by calmodulin. Nature 370, 307-309 (Pubitemid 24250128)
    • (1994) Nature , vol.370 , Issue.6487 , pp. 307-309
    • Lee, H.C.1    Aarhus, R.2    Graeff, R.3    Gurnack, M.E.4    Walseth, T.F.5
  • 20
    • 0028961777 scopus 로고
    • Sensitization of calcium-induced calcium release by cyclic ADP-ribose and calmodulin
    • Lee, H. C., Aarhus, R., and Graeff, R. M. (1995) Sensitization of calcium-induced calcium release by cyclic ADP-ribose and calmodulin. J. Biol. Chem. 270, 9060-9066
    • (1995) J. Biol. Chem. , vol.270 , pp. 9060-9066
    • Lee, H.C.1    Aarhus, R.2    Graeff, R.M.3
  • 26
    • 55349126396 scopus 로고    scopus 로고
    • Synergistic regulation of endogenous TRPM2 channels by adenine dinucleotides in primary human neutrophils
    • Lange, I., Penner, R., Fleig, A., and Beck, A. (2008) Synergistic regulation of endogenous TRPM2 channels by adenine dinucleotides in primary human neutrophils. Cell Calcium 44, 604-615
    • (2008) Cell Calcium , vol.44 , pp. 604-615
    • Lange, I.1    Penner, R.2    Fleig, A.3    Beck, A.4
  • 27
    • 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., Higashi, T., Konishi, Y., Mori, Y., and Tominaga, M. (2006) TRPM2 activation by cyclic ADP-ribose at body temperature is involved in insulin secretion. EMBO J. 25, 1804-1815
    • (2006) EMBO J. , vol.25 , pp. 1804-1815
    • Togashi, K.1    Hara, Y.2    Tominaga, T.3    Higashi, T.4    Konishi, Y.5    Mori, Y.6    Tominaga, M.7
  • 28
    • 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., Walseth, T. F., and Lee, H. C. (1995) ADP-ribosyl cyclase and CD38 catalyze the synthesis of a calcium-mobilizing metabolite from NADP. J. Biol. Chem. 270, 30327-30333
    • (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
  • 31
    • 0029706922 scopus 로고    scopus 로고
    • Modulator and messenger functions of cyclic ADP-ribose in calcium signaling
    • discussion 389
    • Lee, H. C. (1996) Modulator and messenger functions of cyclic ADP-ribose in calcium signaling. Recent Prog. Horm. Res. 51, 355-388; discussion 389
    • (1996) Recent Prog. Horm. Res. , vol.51 , pp. 355-388
    • Lee, H.C.1
  • 32
    • 0034496224 scopus 로고    scopus 로고
    • Functional visualization of the separate but interacting calcium stores sensitive to NAADP and cyclic ADP-ribose
    • Lee, H. C., and Aarhus, R. (2000) Functional visualization of the separate but interacting calcium stores sensitive to NAADP and cyclic ADP-ribose. J. Cell Sci. 113, 4413-4420 (Pubitemid 32117901)
    • (2000) Journal of Cell Science , vol.113 , Issue.24 , pp. 4413-4420
    • Lee, H.C.1    Aarhus, R.2
  • 38
    • 77955291039 scopus 로고    scopus 로고
    • TPC2 proteins mediate nicotinic acid adenine dinucleotide phosphate (NAADP)- And agonist-evoked contractions of smooth muscle
    • Tugba Durlu-Kandilci, N., Ruas, M., Chuang, K. T., Brading, A., Parrington, J., and Galione, A. (2010) TPC2 proteins mediate nicotinic acid adenine dinucleotide phosphate (NAADP)- and agonist-evoked contractions of smooth muscle. J. Biol. Chem. 285, 24925-24932
    • (2010) J. Biol. Chem. , vol.285 , pp. 24925-24932
    • Tugba Durlu-Kandilci, N.1    Ruas, M.2    Chuang, K.T.3    Brading, A.4    Parrington, J.5    Galione, A.6
  • 39
    • 78650525751 scopus 로고    scopus 로고
    • Nicotinic acid adenine dinucleotide phosphate regulates skeletal muscle differentiation via action at two-pore channels
    • Aley, P. K., Mikolajczyk, A. M., Munz, B., Churchill, G. C., Galione, A., and Berger, F. (2010) Nicotinic acid adenine dinucleotide phosphate regulates skeletal muscle differentiation via action at two-pore channels. Proc. Natl. Acad. Sci. U.S.A. 107, 19927-19932
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 19927-19932
    • Aley, P.K.1    Mikolajczyk, A.M.2    Munz, B.3    Churchill, G.C.4    Galione, A.5    Berger, F.6
  • 44
    • 80053942483 scopus 로고    scopus 로고
    • NAADP influences excitation-contraction coupling by releasing calcium from lysosomes in atrial myocytes
    • Collins, T. P., Bayliss, R., Churchill, G. C., Galione, A., and Terrar, D. A. (2011) NAADP influences excitation-contraction coupling by releasing calcium from lysosomes in atrial myocytes. Cell Calcium 50, 449-458
    • (2011) Cell Calcium , vol.50 , pp. 449-458
    • Collins, T.P.1    Bayliss, R.2    Churchill, G.C.3    Galione, A.4    Terrar, D.A.5
  • 48
    • 33745217366 scopus 로고    scopus 로고
    • Second messenger function of nicotinic acid adenine dinucleotide phosphate revealed by an improved enzymatic cycling assay
    • Gasser, A., Bruhn, S., and Guse, A. H. (2006) Second messenger function of nicotinic acid adenine dinucleotide phosphate revealed by an improved enzymatic cycling assay. J. Biol. Chem. 281, 16906-16913
    • (2006) J. Biol. Chem. , vol.281 , pp. 16906-16913
    • Gasser, A.1    Bruhn, S.2    Guse, A.H.3
  • 53
    • 0025831860 scopus 로고
    • Determination of endogenous levels of cyclic ADP-ribose in rat tissues
    • Walseth, T. F., Aarhus, R., Zeleznikar, R. J., Jr., and Lee, H. C. (1991) Determination of endogenous levels of cyclic ADP-ribose in rat tissues. Biochim. Biophys. Acta 1094, 113-120
    • (1991) Biochim. Biophys. Acta , vol.1094 , pp. 113-120
    • Walseth, T.F.1    Aarhus, R.2    Zeleznikar Jr., R.J.3    Lee, H.C.4
  • 54
    • 0037081860 scopus 로고    scopus 로고
    • A novel cycling assay for cellular cADP-ribose with nanomolar sensitivity
    • DOI 10.1042/0264-6021:3610379
    • Graeff, R., and Lee, H. C. (2002) A novel cycling assay for cellular cADP-ribose with nanomolar sensitivity. Biochem. J. 361, 379-384 (Pubitemid 34174505)
    • (2002) Biochemical Journal , vol.361 , Issue.2 , pp. 379-384
    • Graeff, R.1    Lee, H.C.2
  • 56
    • 0036795474 scopus 로고    scopus 로고
    • Nicotinic acid adenine dinucleotide phosphate (NAADP) is present at micromolar concentrations in sea urchin spermatozoa
    • DOI 10.1113/jphysiol.2002.030098
    • Billington, R. A., Ho, A., and Genazzani, A. A. (2002) Nicotinic acid adenine dinucleotide phosphate (NAADP) is present at micromolar concentrations in sea urchin spermatozoa. J. Physiol. 544, 107-112 (Pubitemid 35153817)
    • (2002) Journal of Physiology , vol.544 , Issue.1 , pp. 107-112
    • Billington, R.A.1    Ho, A.2    Genazzani, A.A.3
  • 57
    • 0036798917 scopus 로고    scopus 로고
    • A novel cycling assay for nicotinic acid-adenine dinucleotide phosphate with nanomolar sensitivity
    • DOI 10.1042/BJ20020644
    • Graeff, R., and Lee, H. C. (2002) A novel cycling assay for nicotinic acid-adenine dinucleotide phosphate with nanomolar sensitivity. Biochem. J. 367, 163-168 (Pubitemid 35176902)
    • (2002) Biochemical Journal , vol.367 , Issue.1 , pp. 163-168
    • Graeff, R.1    Lee, H.C.2
  • 59
    • 79953886283 scopus 로고    scopus 로고
    • 2+ signaling in thrombin-induced procoagulant activity of mouse platelets and hemostasis
    • 2+ signaling in thrombin-induced procoagulant activity of mouse platelets and hemostasis. J. Biol. Chem. 286, 12952-12958
    • (2011) J. Biol. Chem. , vol.286 , pp. 12952-12958
    • Mushtaq, M.1    Nam, T.S.2    Kim, U.H.3
  • 61
    • 14844354701 scopus 로고
    • +into a calcium-mobilizing metabolite
    • + into a calcium-mobilizing metabolite. Cell Regul. 2, 203-209
    • (1991) Cell Regul. , vol.2 , pp. 203-209
    • Lee, H.C.1    Aarhus, R.2
  • 62
    • 0026468136 scopus 로고
    • Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase and human lymphocyte antigen CD38
    • States, D. J., Walseth, T. F., and Lee, H. C. (1992) Similarities in amino acid sequences of Aplysia ADP-ribosyl cyclase and human lymphocyte antigen CD38. Trends Biochem. Sci. 17, 495
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 495
    • States, D.J.1    Walseth, T.F.2    Lee, H.C.3
  • 64
    • 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., Koguma, T., Nata, K., Sugimoto, T., Yonekura, H., and Okamoto, H. (1993) Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen CD38 and inhibition of the hydrolysis by ATP. J. Biol. Chem. 268, 26052-26054 (Pubitemid 23361662)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.35 , pp. 26052-26054
    • Takasawa, S.1    Tohgo, A.2    Noguchi, N.3    Koguma, T.4    Nata, K.5    Sugimoto, T.6    Yonekura, H.7    Okamoto, H.8
  • 65
    • 0027892021 scopus 로고
    • Synthesis and degradation of cyclic ADP-ribose by NAD glycohydrolases
    • Kim, H., Jacobson, E. L., and Jacobson, M. K. (1993) Synthesis and degradation of cyclic ADP-ribose by NAD glycohydrolases. Science 261, 1330-1333 (Pubitemid 24081171)
    • (1993) Science , vol.261 , Issue.5126 , pp. 1330-1333
    • Kim, H.1    Jacobson, E.L.2    Jacobson, M.K.3
  • 66
    • 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
    • Jackson, D. G., and Bell, J. I. (1990) 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 (Pubitemid 20136694)
    • (1990) Journal of Immunology , vol.144 , Issue.7 , pp. 2811-2815
    • Jackson, D.G.1    Bell, J.I.2
  • 67
    • 24344490302 scopus 로고    scopus 로고
    • Crystal structure of human CD38 extracellular domain
    • DOI 10.1016/j.str.2005.05.012, PII S0969212605002388
    • Liu, Q., Kriksunov, I. A., Graeff, R., Munshi, C., Lee, H. C., and Hao, Q. (2005) Crystal structure of human CD38 extracellular domain. Structure 13, 1331-1339 (Pubitemid 41262100)
    • (2005) Structure , vol.13 , Issue.9 , pp. 1331-1339
    • Liu, Q.1    Kriksunov, I.A.2    Graeff, R.3    Munshi, C.4    Hon, C.L.5    Hao, Q.6
  • 68
    • 0029858306 scopus 로고    scopus 로고
    • Crystal structure of Aplysia ADP ribosyl cyclase, a homologue of the bifunctional ectozyme CD38
    • DOI 10.1038/nsb1196-957
    • Prasad, G. S., McRee, D. E., Stura, E. A., Levitt, D. G., Lee, H. C., and Stout, C. D. (1996) Crystal structure of Aplysia ADP ribosyl cyclase, a homolog of the bifunctional ectozyme CD38. Nat. Struct. Biol. 3, 957-964 (Pubitemid 26398330)
    • (1996) Nature Structural Biology , vol.3 , Issue.11 , pp. 957-964
    • Prasad, G.S.1    McRee, D.E.2    Stura, E.A.3    Levitt, D.G.4    Lee, H.C.5    Stout, C.D.6
  • 70
    • 0034647497 scopus 로고    scopus 로고
    • Identification of the enzymatic active site of CD38 by site-directed mutagenesis
    • DOI 10.1074/jbc.M909365199
    • Munshi, C., Aarhus, R., Graeff, R., Walseth, T. F., Levitt, D., and Lee, H. C. (2000) Identification of the enzymatic active site of CD38 by site-directed mutagenesis. J. Biol. Chem. 275, 21566-21571 (Pubitemid 30481862)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.28 , pp. 21566-21571
    • Munshi, C.1    Aarhus, R.2    Graeff, R.3    Walseth, T.F.4    Levitt, D.5    Lee, H.C.6
  • 71
  • 72
    • 0033961770 scopus 로고    scopus 로고
    • Enzymatic functions and structures of CD38 and homologs
    • Lee, H. C. (2000) Enzymatic functions and structures of CD38 and homologs. Chem. Immunol. 75, 39-59
    • (2000) Chem. Immunol. , vol.75 , pp. 39-59
    • Lee, H.C.1
  • 73
    • 33749409972 scopus 로고    scopus 로고
    • Acidic residues at the active sites of CD38 and ADP-ribosylt cyclase determine nicotinic acid adenine dinucleotide phosphate (NAADP) synthesis and hydrolysis activities
    • DOI 10.1074/jbc.M604370200
    • Graeff, R., Liu, Q., Kriksunov, I. A., Hao, Q., and Lee, H. C. (2006) Acidic residues at the active sites of CD38 and ADP-ribosyl cyclase determine nicotinic acid adenine dinucleotide phosphate (NAADP) synthesis and hydrolysis activities. J. Biol. Chem. 281, 28951-28957 (Pubitemid 44507038)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.39 , pp. 28951-28957
    • Graeff, R.1    Liu, Q.2    Kriksunov, I.A.3    Hao, Q.4    Hon, C.L.5
  • 75
    • 34047231298 scopus 로고    scopus 로고
    • Structural basis for formation and hydrolysis of the calcium messenger cyclic ADP-ribose by human CD38
    • DOI 10.1074/jbc.M609093200
    • Liu, Q., Kriksunov, I. A., Graeff, R., Lee, H. C., and Hao, Q. (2007) Structural basis for formation and hydrolysis of the calcium messenger cyclic ADP-ribose by human CD38. J. Biol. Chem. 282, 5853-5861 (Pubitemid 47093739)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.8 , pp. 5853-5861
    • Liu, Q.1    Kriksunov, I.A.2    Graeff, R.3    Hon, C.L.4    Hao, Q.5
  • 76
    • 33845936792 scopus 로고    scopus 로고
    • Structural basis for the mechanistic understanding of human CD38-controlled multiple catalysis
    • DOI 10.1074/jbc.M606365200
    • Liu, Q., Kriksunov, I. A., Graeff, R., Munshi, C., Lee, H. C., and Hao, Q. (2006) Structural basis for the mechanistic understanding of human CD38-controlled multiple catalysis. J. Biol. Chem. 281, 32861-32869 (Pubitemid 46036841)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.43 , pp. 32861-32869
    • Liu, Q.1    Kriksunov, I.A.2    Graeff, R.3    Munshi, C.4    Hon, C.L.5    Hao, Q.6
  • 77
    • 53849148622 scopus 로고    scopus 로고
    • Covalent and noncovalent intermediates of an NAD utilizing enzyme, human CD38
    • Liu, Q., Kriksunov, I. A., Jiang, H., Graeff, R., Lin, H., Lee, H. C., and Hao, Q. (2008) Covalent and noncovalent intermediates of an NAD utilizing enzyme, human CD38. Chem. Biol. 15, 1068-1078
    • (2008) Chem. Biol. , vol.15 , pp. 1068-1078
    • Liu, Q.1    Kriksunov, I.A.2    Jiang, H.3    Graeff, R.4    Lin, H.5    Lee, H.C.6    Hao, Q.7
  • 78
    • 34548317513 scopus 로고    scopus 로고
    • Catalysis-associated conformational changes revealed by human CD38 complexed with a non-hydrolyzable substrate analog
    • DOI 10.1074/jbc.M701653200
    • Liu, Q., Kriksunov, I. A., Moreau, C., Graeff, R., Potter, B. V., Lee, H. C., and Hao, Q. (2007) Catalysis-associated conformational changes revealed by human CD38 complexed with a non-hydrolyzable substrate analog. J. Biol. Chem. 282, 24825-24832 (Pubitemid 47347511)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.34 , pp. 24825-24832
    • Liu, Q.1    Kriksunov, I.A.2    Moreau, C.3    Graeff, R.4    Potter, B.V.L.5    Hon, C.L.6    Hao, Q.7
  • 79
    • 84855828493 scopus 로고    scopus 로고
    • Structural studies of intermediates along the cyclization pathway of Aplysia ADP-ribosyl cyclase
    • Kotaka, M., Graeff, R., Chen, Z., Zhang, L. H., Lee, H. C., and Hao, Q. (2012) Structural studies of intermediates along the cyclization pathway of Aplysia ADP-ribosyl cyclase. J. Mol. Biol. 415, 514-526
    • (2012) J. Mol. Biol. , vol.415 , pp. 514-526
    • Kotaka, M.1    Graeff, R.2    Chen, Z.3    Zhang, L.H.4    Lee, H.C.5    Hao, Q.6
  • 80
    • 79251593960 scopus 로고    scopus 로고
    • Dynamic conformations of the CD38-mediated NAD cyclization captured in a single crystal
    • Zhang, H., Graeff, R., Chen, Z., Zhang, L., Zhang, L., Lee, H., and Hao, Q. (2011) Dynamic conformations of the CD38-mediated NAD cyclization captured in a single crystal. J. Mol. Biol. 405, 1070-1078
    • (2011) J. Mol. Biol. , vol.405 , pp. 1070-1078
    • Zhang, H.1    Graeff, R.2    Chen, Z.3    Zhang, L.4    Zhang, L.5    Lee, H.6    Hao, Q.7
  • 82
    • 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. 285, 576-582
    • (2010) J. Biol. Chem. , vol.285 , pp. 576-582
    • Kim, S.Y.1    Cho, B.H.2    Kim, U.H.3
  • 84
    • 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
    • DOI 10.1038/nm1101-1209
    • Partida-Sánchez, S., Cockayne, D. A., Monard, S., Jacobson, E. L., Oppenheimer, N., Garvy, B., Kusser, K., Goodrich, S., Howard, M., Harmsen, A., Randall, T. D., and Lund, F. E. (2001) 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. Nat. Med. 7, 1209-1216 (Pubitemid 33063776)
    • (2001) Nature Medicine , vol.7 , Issue.11 , pp. 1209-1216
    • Partida-Sanchez, S.1    Cockayne, D.A.2    Monard, S.3    Jacobson, E.L.4    Oppenheimer, N.5    Garvy, B.6    Kusser, K.7    Goodrich, S.8    Howard, M.9    Harmsen, A.10    Randall, T.D.11    Lund, F.E.12
  • 93
    • 0037033120 scopus 로고    scopus 로고
    • Equilibrative and concentrative nucleoside transporters mediate influx of extracellular cyclic ADP-ribose into 3T3 murine fibroblasts
    • DOI 10.1074/jbc.M207793200
    • Guida, L., Bruzzone, S., Sturla, L., Franco, L., Zocchi, E., and De Flora, A. (2002) Equilibrative and concentrative nucleoside transporters mediate influx of extracellular cyclic ADP-ribose into 3T3 murine fibroblasts. J. Biol. Chem. 277, 47097-47105 (Pubitemid 36159218)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.49 , pp. 47097-47105
    • Guida, L.1    Bruzzone, S.2    Sturla, L.3    Franco, L.4    Zocchi, E.5    De Flora, A.6
  • 96
    • 0242412541 scopus 로고    scopus 로고
    • Mutational Analysis of Topological Determinants in Prion Protein (PrP) and Measurement of Transmembrane and Cytosolic PrP during Prion Infection
    • DOI 10.1074/jbc.M307833200
    • Stewart, R. S., and Harris, D. A. (2003) Mutational analysis of topological determinants in prion protein (PrP) and measurement of transmembrane and cytosolic PrP during prion infection. J. Biol. Chem. 278, 45960-45968 (Pubitemid 37432743)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.46 , pp. 45960-45968
    • Stewart, R.S.1    Harris, D.A.2
  • 97
    • 77954070546 scopus 로고    scopus 로고
    • Control of membrane protein topology by a single C-terminal residue
    • Seppälä, S., Slusky, J. S., Lloris-Garcerá, P., Rapp, M., and von Heijne, G. (2010) Control of membrane protein topology by a single C-terminal residue. Science 328, 1698-1700
    • (2010) Science , vol.328 , pp. 1698-1700
    • Seppälä, S.1    Slusky, J.S.2    Lloris-Garcerá, P.3    Rapp, M.4    Von Heijne, G.5
  • 98
    • 79959264613 scopus 로고    scopus 로고
    • Expression of CD38 with intracellular enzymatic activity: A possible explanation for the insulin release induced by intracellular cADPR
    • Ohta, Y., Kitanaka, A., Mihara, K., Imataki, O., Ohnishi, H., Tanaka, T., Taminato, T., and Kubota, Y. (2011) Expression of CD38 with intracellular enzymatic activity: a possible explanation for the insulin release induced by intracellular cADPR. Mol. Cell. Biochem. 352, 293-299
    • (2011) Mol. Cell. Biochem. , vol.352 , pp. 293-299
    • Ohta, Y.1    Kitanaka, A.2    Mihara, K.3    Imataki, O.4    Ohnishi, H.5    Tanaka, T.6    Taminato, T.7    Kubota, Y.8
  • 99
    • 79959365485 scopus 로고    scopus 로고
    • Cytosolic CD38 protein forms intact disulfides and is active in elevating intracellular cyclic ADP-ribose
    • Zhao, Y. J., Zhang, H. M., Lam, C. M., Hao, Q., and Lee, H. C. (2011) Cytosolic CD38 protein forms intact disulfides and is active in elevating intracellular cyclic ADP-ribose. J. Biol. Chem. 286, 22170-22177
    • (2011) J. Biol. Chem. , vol.286 , pp. 22170-22177
    • Zhao, Y.J.1    Zhang, H.M.2    Lam, C.M.3    Hao, Q.4    Lee, H.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.