메뉴 건너뛰기




Volumn 40, Issue 12, 1997, Pages 1485-1491

The CD38-cyclic ADP-ribose signalling system in insulin secretion: Molecular basis and clinical implications

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE DIPHOSPHATE RIBOSE; CD38 ANTIGEN; INSULIN; POTASSIUM CHANNEL;

EID: 0031437662     PISSN: 0012186X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s001250050854     Document Type: Review
Times cited : (48)

References (70)
  • 1
    • 0018831212 scopus 로고
    • Translational control of proinsulin synthesis by glucose
    • Itoh N, Okamoto H (1980) Translational control of proinsulin synthesis by glucose. Nature 283: 100-102
    • (1980) Nature , vol.283 , pp. 100-102
    • Itoh, N.1    Okamoto, H.2
  • 2
    • 0019443677 scopus 로고
    • Regulation of proinsulin synthesis in pancreatic islets and a new aspect to insulin-dependent diabetes
    • Okamoto H (1981) Regulation of proinsulin synthesis in pancreatic islets and a new aspect to insulin-dependent diabetes. Mol Cell Biochem 37: 43-61
    • (1981) Mol Cell Biochem , vol.37 , pp. 43-61
    • Okamoto, H.1
  • 3
    • 0019222406 scopus 로고
    • Mechanism of glucose-induced insulin secretion
    • Hedeskov CJ (1980) Mechanism of glucose-induced insulin secretion. Physiol Rev 60: 442-509
    • (1980) Physiol Rev , vol.60 , pp. 442-509
    • Hedeskov, C.J.1
  • 4
    • 0028294981 scopus 로고
    • Control of cytosolic free calcium in cultured human pancreatic β-cells occurs by external calcium-dependent and independent mechanisms
    • Rojas E, Carroll PB, Ricordi C, Boschero AC et al. (1994) Control of cytosolic free calcium in cultured human pancreatic β-cells occurs by external calcium-dependent and independent mechanisms. Endocrinology 134: 1771-1781
    • (1994) Endocrinology , vol.134 , pp. 1771-1781
    • Rojas, E.1    Carroll, P.B.2    Ricordi, C.3    Boschero, A.C.4
  • 5
    • 0021741559 scopus 로고
    • Glucose induced closure of single potassium channels in isolated rat pancreatic β-cells
    • Ashcroft FM, Harrison DE, Ashcroft SJH (1984) Glucose induced closure of single potassium channels in isolated rat pancreatic β-cells. Nature 312: 446-448
    • (1984) Nature , vol.312 , pp. 446-448
    • Ashcroft, F.M.1    Harrison, D.E.2    Ashcroft, S.J.H.3
  • 6
    • 0024453294 scopus 로고
    • Inositol phosphate and cell signalling
    • Berridge MJ, Irvine RF (1989) Inositol phosphate and cell signalling. Nature 341: 197-201
    • (1989) Nature , vol.341 , pp. 197-201
    • Berridge, M.J.1    Irvine, R.F.2
  • 7
    • 0019812690 scopus 로고
    • Streptozotocin and alloxan induce DNA strand breaks and poly(ADP-ribose) synthetase in pancreatic islets
    • Yamamoto H, Uchigata Y, Okamoto H (1981) Streptozotocin and alloxan induce DNA strand breaks and poly(ADP-ribose) synthetase in pancreatic islets. Nature 294: 284-286
    • (1981) Nature , vol.294 , pp. 284-286
    • Yamamoto, H.1    Uchigata, Y.2    Okamoto, H.3
  • 8
    • 0020315923 scopus 로고
    • Protection by superoxide dismutase, catalase, and poly(ADP-ribose) synthetase inhibitors against alloxan- and streptozotocin-induced islet DNA strand breaks and against the inhibition of proinsulin synthesis
    • Uchigata Y, Yamamoto H, Kawamura A, Okamoto H (1982) Protection by superoxide dismutase, catalase, and poly(ADP-ribose) synthetase inhibitors against alloxan- and streptozotocin-induced islet DNA strand breaks and against the inhibition of proinsulin synthesis. J Biol Chem 257: 6084-6088
    • (1982) J Biol Chem , vol.257 , pp. 6084-6088
    • Uchigata, Y.1    Yamamoto, H.2    Kawamura, A.3    Okamoto, H.4
  • 9
    • 0020679246 scopus 로고
    • Effect of poly(ADP-ribose) synthetase inhibitor administration to rats before and after injection of alloxan and streptozotocin on islet proinsulin synthesis
    • Uchigata Y, Yamamoto H, Nagai H, Okamoto H (1983) Effect of poly(ADP-ribose) synthetase inhibitor administration to rats before and after injection of alloxan and streptozotocin on islet proinsulin synthesis. Diabetes 32: 316-318
    • (1983) Diabetes , vol.32 , pp. 316-318
    • Uchigata, Y.1    Yamamoto, H.2    Nagai, H.3    Okamoto, H.4
  • 10
    • 84977305049 scopus 로고
    • Molecular basis of experimental diabetes: Degradation, oncogenesis, and regeneration of pancreatic B-cells of islets of Langerhans
    • Okamoto H (1985) Molecular basis of experimental diabetes: degradation, oncogenesis, and regeneration of pancreatic B-cells of islets of Langerhans. BioEssays 2: 15-21
    • (1985) BioEssays , vol.2 , pp. 15-21
    • Okamoto, H.1
  • 11
    • 0002423940 scopus 로고
    • The molecular basis of experimental diabetes
    • Okamoto H (ed) Cambridge University Press, Cambridge
    • Okamoto H (1990) The molecular basis of experimental diabetes. In: Okamoto H (ed) Molecular biology of the islets of Langerhans. Cambridge University Press, Cambridge pp 209-231
    • (1990) Molecular Biology of the Islets of Langerhans , pp. 209-231
    • Okamoto, H.1
  • 12
    • 0002292206 scopus 로고    scopus 로고
    • Okamoto model for B-cell damage: Recent advances
    • Shafrir E (ed) Birkhäuser, Boston
    • Okamolo H (1996) Okamoto model for B-cell damage: recent advances. In: Shafrir E (ed) Lessons from animal diabetes VI. Birkhäuser, Boston pp 97-111
    • (1996) Lessons from Animal Diabetes VI , pp. 97-111
    • Okamolo, H.1
  • 13
    • 0023219685 scopus 로고
    • Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate
    • Clapper DL, Walseth TF, Dargie PJ, Lee HC (1987) Pyridine nucleotide metabolites stimulate calcium release from sea urchin egg microsomes desensitized to inositol trisphosphate. J Biol Chem 262: 9561-9568
    • (1987) J Biol Chem , vol.262 , pp. 9561-9568
    • Clapper, D.L.1    Walseth, T.F.2    Dargie, P.J.3    Lee, H.C.4
  • 15
    • 0027393833 scopus 로고
    • Cyclic ADP-ribose in insulin secretion from pancreatic β cells
    • Takasawa S, Nata K, Yonekura H, Okamoto H (1993) Cyclic ADP-ribose in insulin secretion from pancreatic β cells. Science 259: 370-373
    • (1993) Science , vol.259 , pp. 370-373
    • Takasawa, S.1    Nata, K.2    Yonekura, H.3    Okamoto, H.4
  • 16
    • 0027452685 scopus 로고
    • Cyclic ADP-ribose: A new way to control calcium
    • Galione A (1993) Cyclic ADP-ribose: a new way to control calcium. Science 259: 325-326
    • (1993) Science , vol.259 , pp. 325-326
    • Galione, A.1
  • 20
    • 0028131433 scopus 로고
    • Cyclic ADP ribose activation of the ryanodine receptor is mediated by calmodulin
    • Lee HC, Aarhus R, Graeff R, Gurnack ME, Walseth TF (1994) Cyclic ADP ribose activation of the ryanodine receptor is mediated by calmodulin. Nature 370: 307-309
    • (1994) Nature , vol.370 , pp. 307-309
    • Lee, H.C.1    Aarhus, R.2    Graeff, R.3    Gurnack, M.E.4    Walseth, T.F.5
  • 25
    • 0028875421 scopus 로고
    • 2+ release in intestinal longitudinal muscle
    • 2+ release in intestinal longitudinal muscle. J Biol Chem 270: 25488-25494
    • (1995) J Biol Chem , vol.270 , pp. 25488-25494
    • Kuemmerle, J.F.1    Makhlouf, G.M.2
  • 26
    • 0028919947 scopus 로고
    • 2+ from distinct intracellular pools in permeabilized lacrimal acinar cells
    • 2+ from distinct intracellular pools in permeabilized lacrimal acinar cells. FEBS Lett 360: 303-306
    • (1995) FEBS Lett , vol.360 , pp. 303-306
    • Gromada, J.1    Jørgensen, T.D.2    Dissing, S.3
  • 28
    • 0030221463 scopus 로고    scopus 로고
    • A specific cyclic ADP-ribose antagonist inhibits cardiac excitation-contraction coupling
    • Rakovic S, Galione A, Ashamu GA, Potter BVL, Terrar DA (1996) A specific cyclic ADP-ribose antagonist inhibits cardiac excitation-contraction coupling. Curr Biol 6: 989-996
    • (1996) Curr Biol , vol.6 , pp. 989-996
    • Rakovic, S.1    Galione, A.2    Ashamu, G.A.3    Potter, B.V.L.4    Terrar, D.A.5
  • 29
    • 0030916182 scopus 로고    scopus 로고
    • Role of cyclic ADP-ribose in ATP-activated potassium currents in alveolar macrophages
    • Ebihara S, Sasaki T, Hida W et al. (1997) Role of cyclic ADP-ribose in ATP-activated potassium currents in alveolar macrophages. J Biol Chem 272: 16023-16029
    • (1997) J Biol Chem , vol.272 , pp. 16023-16029
    • Ebihara, S.1    Sasaki, T.2    Hida, W.3
  • 30
    • 0029129832 scopus 로고
    • New aspects of the physiological significance of NAD, poly ADP-rihose and cyclic ADP-ribose
    • Okamoto H, Takasawa S, Tohgo A (1995) New aspects of the physiological significance of NAD, poly ADP-rihose and cyclic ADP-ribose. Biochimie 77: 356-363
    • (1995) Biochimie , vol.77 , pp. 356-363
    • Okamoto, H.1    Takasawa, S.2    Tohgo, A.3
  • 31
    • 0031420602 scopus 로고    scopus 로고
    • Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen CD38: Inhibition of hydrolysis by ATP and the physiological significance
    • Okamoto H, Takasawa S, Tohgo A, Nata K, Kato I, Noguchi N (1997) Synthesis and hydrolysis of cyclic ADP-ribose by human leukocyte antigen CD38: inhibition of hydrolysis by ATP and the physiological significance. Meth Enzymol 280: 306-318
    • (1997) Meth Enzymol , vol.280 , pp. 306-318
    • Okamoto, H.1    Takasawa, S.2    Tohgo, A.3    Nata, K.4    Kato, I.5    Noguchi, N.6
  • 32
    • 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. (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
    • (1993) J Biol Chem , vol.268 , pp. 26052-26054
    • Takasawa, S.1    Tohgo, A.2    Noguchi, N.3
  • 33
    • 0029589269 scopus 로고
    • Regulatory role of CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase) in insulin secretion by glucose in pancreatic β cells. Enhanced insulin secretion in CD38-expressing transgenic mice
    • Kato I, Takasawa S, Akabane A et al. (1995) Regulatory role of CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase) in insulin secretion by glucose in pancreatic β cells. Enhanced insulin secretion in CD38-expressing transgenic mice. J Biol Chem 270: 30045-30050
    • (1995) J Biol Chem , vol.270 , pp. 30045-30050
    • Kato, I.1    Takasawa, S.2    Akabane, A.3
  • 34
    • 0031051548 scopus 로고    scopus 로고
    • Lysine 129 of CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase) participates in the binding of ATP to inhibit the cyclic ADP-ribose hydrolase
    • Tohgo A, Munakata H, Takasawa S et al. (1997) Lysine 129 of CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase) participates in the binding of ATP to inhibit the cyclic ADP-ribose hydrolase. J Biol Chem 272: 3879-3882
    • (1997) J Biol Chem , vol.272 , pp. 3879-3882
    • Tohgo, A.1    Munakata, H.2    Takasawa, S.3
  • 36
    • 6844265160 scopus 로고    scopus 로고
    • The CD38-cyclic ADP-ribose signaling system in insulin secretion
    • in press
    • Okamoto H (1997) The CD38-cyclic ADP-ribose signaling system in insulin secretion. Mol Cell Biochem (in press)
    • (1997) Mol Cell Biochem
    • Okamoto, H.1
  • 39
    • 0029739796 scopus 로고    scopus 로고
    • 2+ concentration in the pancreatic β-cell are independent of cyclic ADP-ribose
    • 2+ concentration in the pancreatic β-cell are independent of cyclic ADP-ribose. J Biol Chem 271: 19074-19079
    • (1996) J Biol Chem , vol.271 , pp. 19074-19079
    • Webb, D.-L.1    Islam, M.S.2    Efanov, A.M.3
  • 42
    • 0027318996 scopus 로고
    • Sequence and functional characterization of a third inositol trisphosphate receptor subtype, IP3R-3, expressed in pancreatic islets, kidney, gastrointestinal tract, and other tissues
    • Blondel O, Takeda J, Janssen H, Seino S, Bell GI (1993) Sequence and functional characterization of a third inositol trisphosphate receptor subtype, IP3R-3, expressed in pancreatic islets, kidney, gastrointestinal tract, and other tissues. J Biol Chem 268: 11356-11363
    • (1993) J Biol Chem , vol.268 , pp. 11356-11363
    • Blondel, O.1    Takeda, J.2    Janssen, H.3    Seino, S.4    Bell, G.I.5
  • 43
    • 0029143465 scopus 로고
    • Accumulation of cyclic ADP-ribose measured by a specific radioimmunoassay in differentiated human leukemic HL-60 cells with all-trans-retinoic acid
    • Takahashi K, Kukimoto I, Tokita KI et al. (1995) Accumulation of cyclic ADP-ribose measured by a specific radioimmunoassay in differentiated human leukemic HL-60 cells with all-trans-retinoic acid. FEBS Lett 371: 204-208
    • (1995) FEBS Lett , vol.371 , pp. 204-208
    • Takahashi, K.1    Kukimoto, I.2    Tokita, K.I.3
  • 45
    • 0027497231 scopus 로고
    • + glycohydrolase, ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase activities at the outer surface of human erythrocytes
    • + glycohydrolase, ADP-ribosyl cyclase and cyclic ADP-ribose hydrolase activities at the outer surface of human erythrocytes. Biochem Biophys Res Commun 196: 1459-1465
    • (1993) Biochem Biophys Res Commun , vol.196 , pp. 1459-1465
    • Zocchi, E.1    Frano, L.2    Guida, L.3
  • 46
    • 0027763586 scopus 로고
    • Formation and hydrolysis of cyclic ADP-ribose catalyzed by lymphocyte antigen CD38
    • Howard M, Grimaldi JC, Bazan JF et al. (1993) Formation and hydrolysis of cyclic ADP-ribose catalyzed by lymphocyte antigen CD38. Science 262: 1056-1059
    • (1993) Science , vol.262 , pp. 1056-1059
    • Howard, M.1    Grimaldi, J.C.2    Bazan, J.F.3
  • 47
    • 0028085717 scopus 로고
    • Cloning and characterization of cDNA encoding rat ADP-ribosyl cyclase/ cyclic ADP-ribose hydrolase (homologue of human CD38) from islets of Langerhans
    • Koguma T, Takasawa S, Tohgo A et al. (1994) Cloning and characterization of cDNA encoding rat ADP-ribosyl cyclase/ cyclic ADP-ribose hydrolase (homologue of human CD38) from islets of Langerhans. Biochim Biophys Acta 1223: 160-162
    • (1994) Biochim Biophys Acta , vol.1223 , pp. 160-162
    • Koguma, T.1    Takasawa, S.2    Tohgo, A.3
  • 48
    • 0028301332 scopus 로고
    • BST-1, a surface molecule of bone marrow stromal cell lines that facilitates pre B-cell growth
    • Kaisho T, Ishikawa J, Oritani K et al. (1994) BST-1, a surface molecule of bone marrow stromal cell lines that facilitates pre B-cell growth. Proc Natl Acad Sci USA 91: 5325-5329
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5325-5329
    • Kaisho, T.1    Ishikawa, J.2    Oritani, K.3
  • 49
    • 0028046026 scopus 로고
    • ADP ribosyl cyclase activity of a novel bone marrow stromal cell surface molecule, BST-1
    • Hirata Y, Kimura N, Sato K et al. (1994) ADP ribosyl cyclase activity of a novel bone marrow stromal cell surface molecule, BST-1. FEBS Lett 356: 244-248
    • (1994) FEBS Lett , vol.356 , pp. 244-248
    • Hirata, Y.1    Kimura, N.2    Sato, K.3
  • 50
    • 0028818365 scopus 로고
    • Cloning of a cDNA encoding rat bone marrow stromal cell antigen 1 (BST-1) from the islets of Langerhans
    • Furuya Y, Takasawa S, Yonekura H et al. (1995) Cloning of a cDNA encoding rat bone marrow stromal cell antigen 1 (BST-1) from the islets of Langerhans. Gene 165: 329-330
    • (1995) Gene , vol.165 , pp. 329-330
    • Furuya, Y.1    Takasawa, S.2    Yonekura, H.3
  • 51
    • 0029120736 scopus 로고
    • Expression of CD38 gene, but not of mitochondrial glycerol-3-phosphate dehydrogenase gene, is impaired in pancreatic islets of GK rats
    • Matsuoka T, Kajimoto Y, Watada H et al. (1995) Expression of CD38 gene, but not of mitochondrial glycerol-3-phosphate dehydrogenase gene, is impaired in pancreatic islets of GK rats. Biochem Biophys Res Commun 214: 239-246
    • (1995) Biochem Biophys Res Commun , vol.214 , pp. 239-246
    • Matsuoka, T.1    Kajimoto, Y.2    Watada, H.3
  • 52
    • 0003151519 scopus 로고
    • Spontaneous diabetes produced by selective breeding of normal Wistar rats
    • Goto Y, Kakizaki M, Masaki N (1975) Spontaneous diabetes produced by selective breeding of normal Wistar rats. Proc Jpn Acad 51: 80-85
    • (1975) Proc Jpn Acad , vol.51 , pp. 80-85
    • Goto, Y.1    Kakizaki, M.2    Masaki, N.3
  • 54
    • 0029055014 scopus 로고
    • The structure of the Aplysia kurodai gene encoding ADP-ribosyl cyclase, a second-messenger enzyme
    • Nata K, Sugimoto T, Tohgo A et al. (1995) The structure of the Aplysia kurodai gene encoding ADP-ribosyl cyclase, a second-messenger enzyme. Gene 158: 213-218
    • (1995) Gene , vol.158 , pp. 213-218
    • Nata, K.1    Sugimoto, T.2    Tohgo, A.3
  • 55
    • 18844471424 scopus 로고    scopus 로고
    • Human gene encoding CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase): Organization, nucleotide sequence and alternative splicing
    • Nata K, Takamura T, Karasawa T et al. (1997) Human gene encoding CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase): organization, nucleotide sequence and alternative splicing. Gene 186: 285-292
    • (1997) Gene , vol.186 , pp. 285-292
    • Nata, K.1    Takamura, T.2    Karasawa, T.3
  • 56
    • 0028817072 scopus 로고
    • Assignment of CD38, the gene encoding human leukocyte antigen CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase), to chromosome 4p15
    • Nakagawara K, Mori M, Takasawa S et al. (1995) Assignment of CD38, the gene encoding human leukocyte antigen CD38 (ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase), to chromosome 4p15. Cytogenet Cell Genet 69: 38-39
    • (1995) Cytogenet Cell Genet , vol.69 , pp. 38-39
    • Nakagawara, K.1    Mori, M.2    Takasawa, S.3
  • 57
    • 0028006715 scopus 로고
    • Essential cysteine residues for cyclic ADP-ribose synthesis and hydrolysis by CD38
    • Tohgo A, Takasawa S, Noguchi N et al. (1994) Essential cysteine residues for cyclic ADP-ribose synthesis and hydrolysis by CD38. J Biol Chem 269: 28555-28557
    • (1994) J Biol Chem , vol.269 , pp. 28555-28557
    • Tohgo, A.1    Takasawa, S.2    Noguchi, N.3
  • 58
    • 6844244529 scopus 로고    scopus 로고
    • CD38 gene Arg140Trp mutation in Japanese subjects with NIDDM
    • Abstract
    • Yagui K, Shimada F, Miura M et al. (1997) CD38 gene Arg140Trp mutation in Japanese subjects with NIDDM. Diabetes 46: 174A (Abstract)
    • (1997) Diabetes , vol.46
    • Yagui, K.1    Shimada, F.2    Miura, M.3
  • 59
    • 0023644484 scopus 로고
    • Purification of the ryanodine receptor and identity with feet structures of junctional terminal cisternae of sarcoplasmic reticulum from fast skeletal muscle
    • Inui M, Saito A, Fleischer S (1987) Purification of the ryanodine receptor and identity with feet structures of junctional terminal cisternae of sarcoplasmic reticulum from fast skeletal muscle. J Biol Chem 262: 1740-1747
    • (1987) J Biol Chem , vol.262 , pp. 1740-1747
    • Inui, M.1    Saito, A.2    Fleischer, S.3
  • 60
    • 0023241909 scopus 로고
    • Isolation of the ryanodine receptor from cardiac sarcoplasmic reticulum and identity with the feet structures
    • Inui M, Saito A, Fleischer S (1987) Isolation of the ryanodine receptor from cardiac sarcoplasmic reticulum and identity with the feet structures. J Biol Chem 262: 15637-15642
    • (1987) J Biol Chem , vol.262 , pp. 15637-15642
    • Inui, M.1    Saito, A.2    Fleischer, S.3
  • 61
    • 0026738916 scopus 로고
    • FK506 binding protein associated with the calcium release channel (ryanodine receptor)
    • Jayaraman T, Brillantes A-M, Timerman AP et al. (1992) FK506 binding protein associated with the calcium release channel (ryanodine receptor). J Biol Chem 267: 9474-9477
    • (1992) J Biol Chem , vol.267 , pp. 9474-9477
    • Jayaraman, T.1    Brillantes, A.-M.2    Timerman, A.P.3
  • 62
    • 0028206051 scopus 로고
    • The ryanodine receptor from canine heart sarcoplasmic reticulum is associated with a novel FK-506 binding protein
    • Timerman AP, Jayaraman T, Wiederrecht G et al. (1994) The ryanodine receptor from canine heart sarcoplasmic reticulum is associated with a novel FK-506 binding protein. Biochem Biophys Res Commun 198: 701-706
    • (1994) Biochem Biophys Res Commun , vol.198 , pp. 701-706
    • Timerman, A.P.1    Jayaraman, T.2    Wiederrecht, G.3
  • 63
    • 0029810883 scopus 로고    scopus 로고
    • Selective binding of FKBP12.6 by the cardiac ryanodine receptor
    • Timerman AP, Onoue H, Xin H-B et al. (1996) Selective binding of FKBP12.6 by the cardiac ryanodine receptor. J Biol Chem 271: 20385-20391
    • (1996) J Biol Chem , vol.271 , pp. 20385-20391
    • Timerman, A.P.1    Onoue, H.2    Xin, H.-B.3
  • 64
    • 0028358901 scopus 로고
    • Stabilization of calcium release channel (ryanodine receptor) function by FK506-binding protein
    • Brillantes A-MB, Ondrias K, Scott A et al. (1994) Stabilization of calcium release channel (ryanodine receptor) function by FK506-binding protein. Cell 77: 513-523
    • (1994) Cell , vol.77 , pp. 513-523
    • Brillantes, A.-M.B.1    Ondrias, K.2    Scott, A.3
  • 65
    • 14444273436 scopus 로고    scopus 로고
    • Muscarinic receptor-mediated dual regulation of ADP-ribosyl cyclase in NG108-15 neuronal cell membranes analyzed by thin layer chromatography
    • in press
    • Higashida H, Yokoyama S, Hashii M et al. (1997) Muscarinic receptor-mediated dual regulation of ADP-ribosyl cyclase in NG108-15 neuronal cell membranes analyzed by thin layer chromatography. J Biol Chem (in press)
    • (1997) J Biol Chem
    • Higashida, H.1    Yokoyama, S.2    Hashii, M.3
  • 66
    • 6844266664 scopus 로고
    • Calcium induced release of calcium from the sarcoplasmic reticulum of skinned muscle fibre
    • Endo M, Tanaka M, Ogawa Y (1970) Calcium induced release of calcium from the sarcoplasmic reticulum of skinned muscle fibre. Nature 249: 469-475
    • (1970) Nature , vol.249 , pp. 469-475
    • Endo, M.1    Tanaka, M.2    Ogawa, Y.3
  • 67
    • 0014929598 scopus 로고
    • Regenerative calcium release within muscle cells
    • Ford LE, Podolsky RJ (1970) Regenerative calcium release within muscle cells. Science 167: 58-59
    • (1970) Science , vol.167 , pp. 58-59
    • Ford, L.E.1    Podolsky, R.J.2
  • 68
    • 6844262172 scopus 로고
    • Antitumor activity of streptolysin S-forming streptococci
    • Bernheimer AW (ed). John Wiley & Sons, New York
    • Okamoto H Sr (1976) Antitumor activity of streptolysin S-forming streptococci. In: Bernheimer AW (ed). Mechanisms in bacterial toxinology. John Wiley & Sons, New York pp 237-257
    • (1976) Mechanisms in Bacterial Toxinology , pp. 237-257
    • Okamoto Sr., H.1
  • 69
    • 0022523112 scopus 로고
    • Streptococcal preparation (OK-432) inhibits development of type I diabetes in NOD mice
    • Toyota T, Satoh J, Oya K, Shintani S, Okano T (1986) Streptococcal preparation (OK-432) inhibits development of type I diabetes in NOD mice. Diabetes 35: 496-499
    • (1986) Diabetes , vol.35 , pp. 496-499
    • Toyota, T.1    Satoh, J.2    Oya, K.3    Shintani, S.4    Okano, T.5
  • 70
    • 0028972501 scopus 로고
    • KATP: An inward rectifier subunit plus the sulfonylurea receptor
    • KATP: an inward rectifier subunit plus the sulfonylurea receptor. Science 270: 1166-1170
    • (1995) Science , vol.270 , pp. 1166-1170
    • Inagaki, N.1    Gonoi, T.2    Clement IV, J.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.