메뉴 건너뛰기




Volumn 50, Issue 4, 2003, Pages 947-972

Analogs of diadenosine tetraphosphate (Ap4A) Circled white star

Author keywords

Ap4A; Ap4A analogs; Biological effects of Ap4A analogs; Diadenosine tetraphosphate; Dinucleoside polyphosphates

Indexed keywords

CHROMOGENIC SUBSTRATE; DIADENOSINE TETRAPHOSPHATE; DINUCLEOSIDE PHOSPHATE; ENZYME; LIGAND; POLYPHOSPHATE;

EID: 2442582635     PISSN: 0001527X     EISSN: None     Source Type: Journal    
DOI: 10.18388/abp.2003_3626     Document Type: Review
Times cited : (14)

References (135)
  • 2
    • 0036217818 scopus 로고    scopus 로고
    • The crystal structure of diadenosine tetraphosphate hydrolase from Caenorhabditis elegans in free and binary complex forms
    • Bailey S, Sedelnikova S, Blackburn GM, Abdelghany HM, Baker PJ, McLennan AG, Rafferty JB. (2002) The crystal structure of diadenosine tetraphosphate hydrolase from Caenorhabditis elegans in free and binary complex forms. Structure.; 10: 589-600.
    • (2002) Structure , vol.10 , pp. 589-600
    • Bailey, S.1    Sedelnikova, S.2    Blackburn, G.M.3    Abdelghany, H.M.4    Baker, P.J.5    McLennan, A.G.6    Rafferty, J.B.7
  • 3
    • 0033521161 scopus 로고    scopus 로고
    • Diadenylated polyols as new non-isopolar analogues of diadenosine triand tetraphosphates
    • Baraniak J, Wasilewska E, Korczyński D, Stec WJ. (1999) Diadenylated polyols as new non-isopolar analogues of diadenosine triand tetraphosphates. Tetrahedron Lett.; 40: 8603-6.
    • (1999) Tetrahedron Lett , vol.40 , pp. 8603-8606
    • Baraniak, J.1    Wasilewska, E.2    Korczyński, D.3    Stec, W.J.4
  • 6
    • 0021754332 scopus 로고
    • Nucleotide pyrophosphatase from potato tubers; purification and properties
    • Bartkiewicz M, Sierakowska H, Shugar D. (1984) Nucleotide pyrophosphatase from potato tubers; purification and properties. Eur J Biochem.; 143: 419-26.
    • (1984) Eur J Biochem , vol.143 , pp. 419-426
    • Bartkiewicz, M.1    Sierakowska, H.2    Shugar, D.3
  • 8
    • 0029835350 scopus 로고    scopus 로고
    • The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes
    • Bessman MJ, Frick DN, O'Handley SF. (1996) The MutT proteins or "Nudix" hydrolases, a family of versatile, widely distributed, "housecleaning" enzymes. J Biol Chem.; 271: 25059-62.
    • (1996) J Biol Chem , vol.271 , pp. 25059-25062
    • Bessman, M.J.1    Frick, D.N.2    O'Handley, S.F.3
  • 15
    • 0022878104 scopus 로고
    • Inhibition of adenosine and thymidylate kinases by bisubstrate analogs
    • Bone R, Cheng Y-C, Wolfenden R. (1986b) Inhibition of adenosine and thymidylate kinases by bisubstrate analogs. J Biol Chem.; 261: 16410-3.
    • (1986) J Biol Chem , vol.261 , pp. 16410-16413
    • Bone, R.1    Cheng, Y.-C.2    Wolfenden, R.3
  • 17
    • 0026095603 scopus 로고
    • Isolation and characterization of a dinucleoside triphosphatase from Saccharomyces cerevisiae
    • Brevet A, Chen J, Fromant M, Blanquet S, Plateau P. (1991) Isolation and characterization of a dinucleoside triphosphatase from Saccharomyces cerevisiae. J Bacteriol.; 173: 5275-9.
    • (1991) J Bacteriol , vol.173 , pp. 5275-5279
    • Brevet, A.1    Chen, J.2    Fromant, M.3    Blanquet, S.4    Plateau, P.5
  • 20
    • 0033605754 scopus 로고    scopus 로고
    • 6A) hydrolase member of the MutT motif (Nudix hydrolase) family
    • 6A) hydrolase member of the MutT motif (Nudix hydrolase) family. J Biol Chem.; 274: 8604-10.
    • (1999) J Biol Chem , vol.274 , pp. 8604-8610
    • Cartwright, J.L.1    McLennan, A.G.2
  • 21
    • 0033599487 scopus 로고    scopus 로고
    • The ialA invasion gene of Bartonella bacilliformis encodes a (di)nucleoside polyphosphate hydrolase of the MutT motif family and has homologs in other invasive bacteria
    • Cartwright JL, Britton P, Minnick MF, McLennan AG. (1999) The ialA invasion gene of Bartonella bacilliformis encodes a (di)nucleoside polyphosphate hydrolase of the MutT motif family and has homologs in other invasive bacteria. Biochem Biophys Res Commun.; 256: 474-9.
    • (1999) Biochem Biophys Res Commun , vol.256 , pp. 474-479
    • Cartwright, J.L.1    Britton, P.2    Minnick, M.F.3    McLennan, A.G.4
  • 23
    • 0020110870 scopus 로고
    • +, ADP-ribose and adenosine(5′)tetraphospho(5′)adenosine
    • +, ADP-ribose and adenosine(5′)tetraphospho(5′)adenosine. Eur J Biochem.; 122: 601-8.
    • (1982) Eur J Biochem , vol.122 , pp. 601-608
    • Cayley, P.J.1    Kerr, I.M.2
  • 25
    • 0022499324 scopus 로고
    • Homogeneous uridine kinase from Ehrlich ascites tumor: Substrate specificity and inhibition by bisubstrate analogs
    • Cheng N, Payne RC, Kemp Jr. WE, Traut ThW. (1986) Homogeneous uridine kinase from Ehrlich ascites tumor: substrate specificity and inhibition by bisubstrate analogs. Mol Pharmacol.; 30: 159-63.
    • (1986) Mol Pharmacol , vol.30 , pp. 159-163
    • Cheng, N.1    Payne, R.C.2    Kemp Jr., W.E.3    Traut, Th.W.4
  • 26
    • 0033555520 scopus 로고    scopus 로고
    • The gene, ialA, associated with the invasion of human erythrocytes by Bartonella bacilliformis, designates a Nudix hydrolase active on dinucleoside 5′-polyphosphates
    • Conyers GB, Bessman MJ. (1999) The gene, ialA, associated with the invasion of human erythrocytes by Bartonella bacilliformis, designates a Nudix hydrolase active on dinucleoside 5′-polyphosphates. J Biol Chem.; 274: 1203-6.
    • (1999) J Biol Chem , vol.274 , pp. 1203-1206
    • Conyers, G.B.1    Bessman, M.J.2
  • 27
    • 0023645493 scopus 로고
    • Nonadenylylated bis(5′-nucleosidyl) tetraphosphates occur in Saccharomyces cerevisiae and in Escherichia coli and accumulate upon temperature shift or exposure to cadmium
    • Coste H, Brevet A, Plateau P, Blanquet S. (1987) Nonadenylylated bis(5′-nucleosidyl) tetraphosphates occur in Saccharomyces cerevisiae and in Escherichia coli and accumulate upon temperature shift or exposure to cadmium. J Biol Chem.; 262: 12096-103.
    • (1987) J Biol Chem , vol.262 , pp. 12096-12103
    • Coste, H.1    Brevet, A.2    Plateau, P.3    Blanquet, S.4
  • 28
    • 0023676388 scopus 로고
    • Dinucleotide analogues as inhibitors of thymidine kinase, thymidylate kinase, and ribonucleotide reductase
    • Davies LC, Stock JA, Barrie SE, Orr RM, Harrap KR. (1988) Dinucleotide analogues as inhibitors of thymidine kinase, thymidylate kinase, and ribonucleotide reductase. J Med Chem.; 31: 1305-8.
    • (1988) J Med Chem , vol.31 , pp. 1305-1308
    • Davies, L.C.1    Stock, J.A.2    Barrie, S.E.3    Orr, R.M.4    Harrap, K.R.5
  • 29
    • 0030849928 scopus 로고    scopus 로고
    • Diadenosine polyphosphates inhibit adenosine kinase activity but decrease levels of endogenous adenosine in rat brain
    • Delaney SM, Blackburn GM, Geiger JD. (1997) Diadenosine polyphosphates inhibit adenosine kinase activity but decrease levels of endogenous adenosine in rat brain. Eur J Pharmacol.; 332: 35-42.
    • (1997) Eur J Pharmacol , vol.332 , pp. 35-42
    • Delaney, S.M.1    Blackburn, G.M.2    Geiger, J.D.3
  • 30
    • 0035831299 scopus 로고    scopus 로고
    • Synthesis of (di)adenosine polyphosphates by non-ribosomal peptide synthetases (NRPS)
    • Dieckmann R, Pavela-Vrancic M, von Döhren H. (2001) Synthesis of (di)adenosine polyphosphates by non-ribosomal peptide synthetases (NRPS). Biochim Biophys Acta.; 1546: 234-41.
    • (2001) Biochim Biophys Acta , vol.1546 , pp. 234-241
    • Dieckmann, R.1    Pavela-Vrancic, M.2    Von Döhren, H.3
  • 31
    • 0024961699 scopus 로고
    • Synthesis of (Rp,Rp)-P1,P4-bis(5′-adenosyl)-1[17O,18O 2],4 [17O,18 O2]tetraphosphate from (Sp,Sp)-P1,P4-bis(5′-adenosyl)-1 [thio-18 O2],4[thio-18 O2]
    • 4A phosphodiesterase from lupin seeds
    • 4A phosphodiesterase from lupin seeds. J Biol Chem.; 264: 2069-74.
    • (1989) J Biol Chem , vol.264 , pp. 2069-2074
    • Dixon, R.M.1    Lowe, G.2
  • 32
    • 0023737213 scopus 로고
    • Affinity labeling of pyridoxal kinase with adenosine polyphosphopyridoxal
    • Dominici P, Scholz G, Kwok F, Churchich JE. (1988) Affinity labeling of pyridoxal kinase with adenosine polyphosphopyridoxal. J Biol Chem.; 263: 14712-6.
    • (1988) J Biol Chem , vol.263 , pp. 14712-14716
    • Dominici, P.1    Scholz, G.2    Kwok, F.3    Churchich, J.E.4
  • 33
    • 0030944841 scopus 로고    scopus 로고
    • Diadenosine polyphosphate-stimulated gluconeogenesis in isolated rat proximal tubules
    • Edgecombe M, Craddock HS, Smith DC, McLennan AG, Fisher MJ. (1997) Diadenosine polyphosphate-stimulated gluconeogenesis in isolated rat proximal tubules. Biochem J.; 323: 451-6.
    • (1997) Biochem J , vol.323 , pp. 451-456
    • Edgecombe, M.1    Craddock, H.S.2    Smith, D.C.3    McLennan, A.G.4    Fisher, M.J.5
  • 34
  • 35
    • 0016794104 scopus 로고
    • Synthetic inhibitors of adenylate kinases in the assays for ATPases and phosphokinases
    • Feldhaus P, Fröhlich T, Goody RS, Isakov M, Schirmer RH. (1975) Synthetic inhibitors of adenylate kinases in the assays for ATPases and phosphokinases. Eur J Biochem.; 57: 197-204.
    • (1975) Eur J Biochem , vol.57 , pp. 197-204
    • Feldhaus, P.1    Fröhlich, T.2    Goody, R.S.3    Isakov, M.4    Schirmer, R.H.5
  • 36
    • 15144357478 scopus 로고    scopus 로고
    • Acyl-CoA synthetase from Pseudomonas fragi catalyzes the synthesis of adenosine 5′-polyphosphates and dinucleoside polyphosphates
    • Fontes R, Günther Sillero MA, Sillero A. (1998) Acyl-CoA synthetase from Pseudomonas fragi catalyzes the synthesis of adenosine 5′- polyphosphates and dinucleoside polyphosphates. J Bacteriol.; 180: 3152-8.
    • (1998) J Bacteriol , vol.180 , pp. 3152-3158
    • Fontes, R.1    Günther Sillero, M.A.2    Sillero, A.3
  • 40
    • 0031732134 scopus 로고    scopus 로고
    • The hydrolytic activity of bovine adrenal medullary plasma membranes towards diadenosine polyphosphates is due to alkaline phosphodiesterase-I
    • Gasmi L, Cartwright JL, McLennan AG. (1998) The hydrolytic activity of bovine adrenal medullary plasma membranes towards diadenosine polyphosphates is due to alkaline phosphodiesterase-I. Biochim Biophys Acta.; 1405: 121-7.
    • (1998) Biochim Biophys Acta , vol.1405 , pp. 121-127
    • Gasmi, L.1    Cartwright, J.L.2    McLennan, A.G.3
  • 41
    • 0013261044 scopus 로고
    • 4-tetraphosphate triggers initiation of in vitro DNA replication in baby hamster kidney cells
    • 4-tetraphosphate triggers initiation of in vitro DNA replication in baby hamster kidney cells. Proc Natl Acad Sci U S A.; 75: 371-4.
    • (1978) Proc Natl Acad Sci U S A , vol.75 , pp. 371-374
    • Grummt, F.1
  • 43
    • 0026066590 scopus 로고
    • Synthesis of dinucleoside polyphosphates catalyzed by firefly luciferase
    • Günther Sillero MA, Guranowski A, Sillero A. (1991) Synthesis of dinucleoside polyphosphates catalyzed by firefly luciferase. Eur J Biochem.; 202: 507-13.
    • (1991) Eur J Biochem , vol.202 , pp. 507-513
    • Günther Sillero, M.A.1    Guranowski, A.2    Sillero, A.3
  • 44
    • 0343765844 scopus 로고    scopus 로고
    • 4N counterparts as substrates of firefly luciferase, dinucleoside tetraphosphatase and phosphodiesterases
    • 4N counterparts as substrates of firefly luciferase, dinucleoside tetraphosphatase and phosphodiesterases. Biochim Biophys Acta.; 1334: 191-9.
    • (1997) Biochim Biophys Acta , vol.1334 , pp. 191-199
    • Günther Sillero, M.A.1    Madrid, O.2    Zaera, E.3    Sillero, A.4
  • 47
    • 0033796736 scopus 로고    scopus 로고
    • Specific and nonspecific enzymes involved in the catabolism of mononucleoside and dinucleoside polyphosphates
    • Guranowski A. (2000) Specific and nonspecific enzymes involved in the catabolism of mononucleoside and dinucleoside polyphosphates. Pharmacol Ther.; 87: 117-39.
    • (2000) Pharmacol Ther , vol.87 , pp. 117-139
    • Guranowski, A.1
  • 48
    • 0021991642 scopus 로고
    • 4-tetraphosphate α,β-phosphorylase from Saccharomyces cerevisiae
    • 4- tetraphosphate α,β-phosphorylase from Saccharomyces cerevisiae. J Biol Chem.; 260: 3542-7.
    • (1985) J Biol Chem , vol.260 , pp. 3542-3547
    • Guranowski, A.1    Blanquet, S.2
  • 49
    • 0021112845 scopus 로고
    • 4-tetraphosphate (symmetrical) pyrophosphohydrolase from Escherichia coli K12
    • 4-tetraphosphate (symmetrical) pyrophosphohydrolase from Escherichia coli K12. J Biol Chem.; 258: 14784-9.
    • (1983) J Biol Chem , vol.258 , pp. 14784-14789
    • Guranowski, A.1    Jakubowski, H.2    Holler, H.3
  • 51
    • 0024291658 scopus 로고
    • 4-tetraphosphate (AppppA) from adenosine 5′-phosphosulfate and adenosine 5′-triphosphate catalyzed by yeast AppppA phosphorylase
    • 4-tetraphosphate (AppppA) from adenosine 5′-phosphosulfate and adenosine 5′-triphosphate catalyzed by yeast AppppA phosphorylase. Biochemistry.; 27: 2959-64.
    • (1988) Biochemistry , vol.27 , pp. 2959-2964
    • Guranowski, A.1    Just, G.2    Holler, E.3    Jakubowski, H.4
  • 53
    • 0028117144 scopus 로고
    • Regiospecificity of the hydrolysis of diadenosine polyphosphates catalyzed by three specific pyrophosphohydrolases
    • Guranowski A, Brown P, Ashton PA, Blackburn GM. (1994) Regiospecificity of the hydrolysis of diadenosine polyphosphates catalyzed by three specific pyrophosphohydrolases. Biochemistry.; 33: 235-40.
    • (1994) Biochemistry , vol.33 , pp. 235-240
    • Guranowski, A.1    Brown, P.2    Ashton, P.A.3    Blackburn, G.M.4
  • 55
    • 0028857534 scopus 로고
    • Conversion of adenosine (5′)oligophospho(5′)adenosines into inosine(5′)oligophospho(5′)inosines by non-specific adenylate deaminase from the snail Helix pomatia
    • Guranowski A, Starzyńska E, Günther Sillero MA, Sillero A. (1995) Conversion of adenosine (5′)oligophospho(5′)adenosines into inosine(5′)oligophospho(5′)inosines by non-specific adenylate deaminase from the snail Helix pomatia. Biochim Biophys Acta.; 1243: 78-84.
    • (1995) Biochim Biophys Acta , vol.1243 , pp. 78-84
    • Guranowski, A.1    Starzyńska, E.2    Günther Sillero, M.A.3    Sillero, A.4
  • 58
    • 0042889174 scopus 로고    scopus 로고
    • Selective splitting of 3′-adenylated dinucleoside polyphosphates by specific enzymes degrading dinucleoside polyphosphates
    • Guranowski A, Sillero A, Günther Sillero MA. (2003a) Selective splitting of 3′-adenylated dinucleoside polyphosphates by specific enzymes degrading dinucleoside polyphosphates. Acta Biochim Polon.; 50: 123-30.
    • (2003) Acta Biochim Polon , vol.50 , pp. 123-130
    • Guranowski, A.1    Sillero, A.2    Günther Sillero, M.A.3
  • 59
    • 0041370059 scopus 로고    scopus 로고
    • Adenosine-5′-O-phosphorylated and adenosine-5′-O- phosphorothioylated polyols as strong inhibitors of symmetrical and asymmetrical dinucleoside tetraphosphatases
    • Guranowski A, Starzyńska E, McLennan AG, Baraniak J, Stec W. (2003b) Adenosine-5′-O-phosphorylated and adenosine-5′-O- phosphorothioylated polyols as strong inhibitors of symmetrical and asymmetrical dinucleoside tetraphosphatases. Biochem J.; 373: 635-40.
    • (2003) Biochem J , vol.373 , pp. 635-640
    • Guranowski, A.1    Starzyńska, E.2    McLennan, A.G.3    Baraniak, J.4    Stec, W.5
  • 62
    • 0034701056 scopus 로고    scopus 로고
    • Mutational, kinetic, and NMR studies of the roles of conserved glutamate residues and of lysine-39 in the mechanism of the MutT pyrophosphohydrolase
    • Harris TK, Wu G, Massiah MA, Mildvan AS. (2000) Mutational, kinetic, and NMR studies of the roles of conserved glutamate residues and of lysine-39 in the mechanism of the MutT pyrophosphohydrolase. Biochemistry.; 39: 1655-74.
    • (2000) Biochemistry , vol.39 , pp. 1655-1674
    • Harris, T.K.1    Wu, G.2    Massiah, M.A.3    Mildvan, A.S.4
  • 63
    • 0016768428 scopus 로고
    • Inhibition of platelet aggregation and the platelet release reaction by α,ω diadenosine polyphosphates
    • Harrison MJ, Brossmer R, Goody RS. (1975) Inhibition of platelet aggregation and the platelet release reaction by α,ω diadenosine polyphosphates. FEBS Lett.; 54: 57-60.
    • (1975) FEBS Lett , vol.54 , pp. 57-60
    • Harrison, M.J.1    Brossmer, R.2    Goody, R.S.3
  • 64
    • 0027526626 scopus 로고
    • Use of adenosine(5′)polyphospho(5′)pyridoxals to study the substrate-binding region of glutathione synthetase from Escherichia coli B
    • Hibi T, Kato H, Nishioka T, Oda J, Yamaguchi H, Katsube Y, Tanizawa K, Fukui T. (1993) Use of adenosine(5′)polyphospho(5′)pyridoxals to study the substrate-binding region of glutathione synthetase from Escherichia coli B. Biochemistry.; 32: 1548-54.
    • (1993) Biochemistry , vol.32 , pp. 1548-1554
    • Hibi, T.1    Kato, H.2    Nishioka, T.3    Oda, J.4    Yamaguchi, H.5    Katsube, Y.6    Tanizawa, K.7    Fukui, T.8
  • 66
    • 0022971279 scopus 로고
    • Multisubstrate analogs for deoxynucleoside kinases; triphosphate end products and synthetic bisubstrate analogs exhibit identical modes of binding and are useful probes for distinguishing kinetic mechanisms
    • Ikeda S, Chakravarty R, Ives DH. (1986) Multisubstrate analogs for deoxynucleoside kinases; triphosphate end products and synthetic bisubstrate analogs exhibit identical modes of binding and are useful probes for distinguishing kinetic mechanisms. J Biol Chem.; 261: 15836-43.
    • (1986) J Biol Chem , vol.261 , pp. 15836-15843
    • Ikeda, S.1    Chakravarty, R.2    Ives, D.H.3
  • 67
    • 0033596871 scopus 로고    scopus 로고
    • 6-hexaphosphate hydrolase that is a member of the Nudix (MutT) family of hydrolases: Cloning of the gene and characterization of the purified enzyme
    • 6-hexaphosphate hydrolase that is a member of the Nudix (MutT) family of hydrolases: cloning of the gene and characterization of the purified enzyme. Biochemistry.; 38: 3649-55.
    • (1999) Biochemistry , vol.38 , pp. 3649-3655
    • Ingram, S.W.1    Stratemann, S.A.2    Barnes, L.D.3
  • 68
    • 0020667868 scopus 로고
    • 4-tetraphosphate and related compounds by plant (Lupinus luteus) seryl-tRNA and phenylalanyl-tRNA synthetases
    • 4-tetraphosphate and related compounds by plant (Lupinus luteus) seryl-tRNA and phenylalanyl-tRNA synthetases. Acta Biochim Polon.; 30: 51-69.
    • (1983) Acta Biochim Polon , vol.30 , pp. 51-69
    • Jakubowski, H.1
  • 69
    • 0021112456 scopus 로고
    • Enzymes hydrolyzing ApppA and/or AppppA in higher plants; purification and some properties of diadenosine triphosphatase, diadenosine tetraphosphatase, and phosphodiesterase from yellow lupin (Lupinus luteus) seeds
    • Jakubowski H, Guranowski A. (1983) Enzymes hydrolyzing ApppA and/or AppppA in higher plants; purification and some properties of diadenosine triphosphatase, diadenosine tetraphosphatase, and phosphodiesterase from yellow lupin (Lupinus luteus) seeds. J Biol Chem.; 258: 9982-9.
    • (1983) J Biol Chem , vol.258 , pp. 9982-9989
    • Jakubowski, H.1    Guranowski, A.2
  • 72
    • 0032564339 scopus 로고    scopus 로고
    • Structural basis for efficient phosphorylation of 3′-azidothymidine monophosphate by Escherichia coli thymidylate kinase
    • Lavie A, Ostermann N, Brundiers R, Goody RS, Reinstein J, Konrad M, Schlichting I. (1998b) Structural basis for efficient phosphorylation of 3′-azidothymidine monophosphate by Escherichia coli thymidylate kinase. Proc Natl Acad Sci USA.; 95: 14045-50.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14045-14050
    • Lavie, A.1    Ostermann, N.2    Brundiers, R.3    Goody, R.S.4    Reinstein, J.5    Konrad, M.6    Schlichting, I.7
  • 73
    • 0021099614 scopus 로고
    • 4-tetraphosphate and related adenylylated nucleotides in Salmonella typhimurium
    • 4-tetraphosphate and related adenylylated nucleotides in Salmonella typhimurium. J Biol Chem.; 258: 6827-34.
    • (1983) J Biol Chem , vol.258 , pp. 6827-6834
    • Phc, L.1    Bochner, B.R.2    Ames, B.N.3
  • 74
    • 0015918941 scopus 로고
    • 5-Di(adenosine-5′) pentaphosphate, a potent multisubstrate inhibitor of adenylate kinase
    • 5- Di(adenosine-5′) pentaphosphate, a potent multisubstrate inhibitor of adenylate kinase. J Biol Chem.; 248: 1121-3.
    • (1973) J Biol Chem , vol.248 , pp. 1121-1123
    • Lienhard, G.E.1    Secemski, I.I.2
  • 75
    • 0028341136 scopus 로고
    • Purification and properties of GTP:GTP guanylyltransferase from encysted embryos of the brine shrimp Artemia
    • Liu JJ, McLennan AG. (1994) Purification and properties of GTP:GTP guanylyltransferase from encysted embryos of the brine shrimp Artemia. J Biol Chem.; 269: 11787-94.
    • (1994) J Biol Chem , vol.269 , pp. 11787-11794
    • Liu, J.J.1    McLennan, A.G.2
  • 78
    • 0037809252 scopus 로고    scopus 로고
    • The NudA protein in the gastric pathogen Helicobacter pylori is an ubiquitous and constitutively expressed dinucleoside polyphosphate hydrolase
    • Lundin A, Nilsson Ch, Gerhard M, Andersson DI, Krabbe M, Engstrand L. (2003) The NudA protein in the gastric pathogen Helicobacter pylori is an ubiquitous and constitutively expressed dinucleoside polyphosphate hydrolase. J Biol Chem.; 278: 12574-8.
    • (2003) J Biol Chem , vol.278 , pp. 12574-12578
    • Lundin, A.1    Nilsson, Ch.2    Gerhard, M.3    Andersson, D.I.4    Krabbe, M.5    Engstrand, L.6
  • 80
    • 0023818447 scopus 로고
    • 3A in whole blood. The dinucleotides are long-lived signal molecules in the blood ending up as intracellular ATP in the erythrocytes
    • 3A in whole blood. The dinucleotides are long-lived signal molecules in the blood ending up as intracellular ATP in the erythrocytes. Eur J Biochem.: 173: 241-5.
    • (1988) Eur J Biochem , vol.173 , pp. 241-245
    • Lüthje, J.1    Ogilvie, A.2
  • 83
    • 0009881698 scopus 로고    scopus 로고
    • Methanetrisphosphonate and its adenine nucleotide derivatives as inhibitors of human and plant diadenosine tetraphosphate hydrolases
    • Maksel D, Gayler K, Liu X, Blackburn M, McLennan AG, Guranowski A. (1999) Methanetrisphosphonate and its adenine nucleotide derivatives as inhibitors of human and plant diadenosine tetraphosphate hydrolases. Cell Mol Biol Lett.; 4: 418.
    • (1999) Cell Mol Biol Lett , vol.4 , pp. 418
    • Maksel, D.1    Gayler, K.2    Liu, X.3    Blackburn, M.4    McLennan, A.G.5    Guranowski, A.6
  • 85
    • 0033796851 scopus 로고    scopus 로고
    • Dinucleoside polyphosphates - Friend or foe?
    • McLennan AG. (2000) Dinucleoside polyphosphates - friend or foe? Pharmacol Ther.; 87: 73-89.
    • (2000) Pharmacol Ther , vol.87 , pp. 73-89
    • McLennan, A.G.1
  • 86
    • 0024563895 scopus 로고
    • Recognition of ββ-substituted and αβ, α′β′-disubstituted phosphonate analogues of bis(5′-adenosyl) tetraphosphate by the bis(5′-nucleosidyl)- tetraphosphate pyrophosphohydrolases from Artemia embryos and Escherichia coli
    • McLennan AG, Taylor GE, Prescott M, Blackburn GM. (1989) Recognition of ββ-substituted and αβ,α′β′- disubstituted phosphonate analogues of bis(5′-adenosyl) tetraphosphate by the bis(5′-nucleosidyl)-tetraphosphate pyrophosphohydrolases from Artemia embryos and Escherichia coli. Biochemistry.; 28: 3868-75.
    • (1989) Biochemistry , vol.28 , pp. 3868-3875
    • McLennan, A.G.1    Taylor, G.E.2    Prescott, M.3    Blackburn, G.M.4
  • 87
    • 0032506228 scopus 로고    scopus 로고
    • Unblocking of chain-terminated primer by HIV-1 reverse transcriptase through a nucleotide-dependent mechanism
    • Meyer PR, Matsuura SE, So AG, Scott WA. (1998) Unblocking of chain-terminated primer by HIV-1 reverse transcriptase through a nucleotide-dependent mechanism. Proc Natl Acad Sci U S A.; 95: 13471-6.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 13471-13476
    • Meyer, P.R.1    Matsuura, S.E.2    So, A.G.3    Scott, W.A.4
  • 90
    • 0023663476 scopus 로고
    • The action of a water-soluble carbodiimide on adenosine-5′- polyphosphates
    • Ng KE, Orgel LE. (1987) The action of a water-soluble carbodiimide on adenosine-5′-polyphosphates. Nucleic Acids Res.; 15: 3573-80.
    • (1987) Nucleic Acids Res , vol.15 , pp. 3573-3580
    • Ng, K.E.1    Orgel, L.E.2
  • 92
    • 0027397016 scopus 로고
    • Specific synthesis of adenosine(5′)tetraphospho(5′)nucleoside and adenosine (5′)oligophospho(5′)adenosine (n>4) catalyzed by firefly luciferase
    • Ortiz B, Sillero A, Günther Sillero MA. (1993) Specific synthesis of adenosine(5′)tetraphospho(5′)nucleoside and adenosine (5′)oligophospho(5′)adenosine (n>4) catalyzed by firefly luciferase. Eur J Biochem.; 212: 263-70.
    • (1993) Eur J Biochem , vol.212 , pp. 263-270
    • Ortiz, B.1    Sillero, A.2    Günther Sillero, M.A.3
  • 93
    • 0017381166 scopus 로고
    • Substrate positions and induced-fit in crystalline adenylate kinase
    • Pai EF, Sachsenheimer W, Schirmer RH, Schulz GE. (1977) Substrate positions and induced-fit in crystalline adenylate kinase. J Mol Biol.; 114: 37-45.
    • (1977) J Mol Biol , vol.114 , pp. 37-45
    • Pai, E.F.1    Sachsenheimer, W.2    Schirmer, R.H.3    Schulz, G.E.4
  • 94
    • 0025848075 scopus 로고
    • Alteration in the accumulation of adenylylated nucleotides in heavy-metal-ion-stressed and heat-stressed Synechococcus sp. strain PCC 6301, cyanobacterium, in light and dark
    • Pálfi Z, Surányi G, Borbély G. (1991) Alteration in the accumulation of adenylylated nucleotides in heavy-metal-ion-stressed and heat-stressed Synechococcus sp. strain PCC 6301, cyanobacterium, in light and dark. Biochem J.; 276: 487-91.
    • (1991) Biochem J , vol.276 , pp. 487-491
    • Pálfi, Z.1    Surányi, G.2    Borbély, G.3
  • 95
    • 0023257046 scopus 로고
    • 5-bis(5′-adenosyl) pentaphosphate
    • 5-bis(5′-adenosyl) pentaphosphate. Biochemistry.; 26: 2033-8.
    • (1987) Biochemistry , vol.26 , pp. 2033-2038
    • Pandey, V.1    Modak, M.J.2
  • 97
    • 0346034526 scopus 로고    scopus 로고
    • 4-Coumarate:coenzyme a ligase has the catalytic capacity to synthesize and reutilize various (di)adenosine polyphosphates
    • Pietrowska-Borek M, Stuible H-P, Kombrink E, Guranowski A. (2003) 4-Coumarate:coenzyme A ligase has the catalytic capacity to synthesize and reutilize various (di)adenosine polyphosphates. Plant Physiol.; 131: 1401-10.
    • (2003) Plant Physiol , vol.131 , pp. 1401-1410
    • Pietrowska-Borek, M.1    Stuible, H.-P.2    Kombrink, E.3    Guranowski, A.4
  • 99
    • 0031017168 scopus 로고    scopus 로고
    • Diinosine polyphosphates, a group of dinucleotides with antagonistic effects on diadenosine polyphosphate receptor
    • Pintor J, Gualix J, Miras-Portugal MT. (1997) Diinosine polyphosphates, a group of dinucleotides with antagonistic effects on diadenosine polyphosphate receptor. Mol Pharmacol.; 51: 277-84.
    • (1997) Mol Pharmacol , vol.51 , pp. 277-284
    • Pintor, J.1    Gualix, J.2    Miras-Portugal, M.T.3
  • 100
    • 0026542177 scopus 로고
    • Characterization and quantification of diadenosine hexaphosphate in chromaffin cells: Granular storage and secretagogue-induced release
    • Pintor J, Rotllán P, Torres M, Miras Portugal M T. (1992b) Characterization and quantification of diadenosine hexaphosphate in chromaffin cells: Granular storage and secretagogue-induced release. Anal Biochem.; 200: 296-300.
    • (1992) Anal Biochem , vol.200 , pp. 296-300
    • Pintor, J.1    Rotllán, P.2    Torres, M.3    Miras Portugal, M.T.4
  • 102
    • 0020361375 scopus 로고
    • 4-tetraphosphates by Escherichia coli lysyl-tRNA synthetase
    • 4-tetraphosphates by Escherichia coli lysyl-tRNA synthetase. Biochemistry.; 21: 5273-9.
    • (1982) Biochemistry , vol.21 , pp. 5273-5279
    • Plateau, P.1    Blanquet, S.2
  • 104
    • 0017404154 scopus 로고
    • 5-di(adenosine 5′) pentaphosphate; evidence for two ATP binding sites
    • 5-di(adenosine 5′) pentaphosphate; evidence for two ATP binding sites. J Biol Chem.; 252: 3558-60.
    • (1977) J Biol Chem , vol.252 , pp. 3558-3560
    • Powers, S.G.1    Griffith, O.W.2    Meister, A.3
  • 106
    • 0024673008 scopus 로고
    • Characterization of the bis(5′-nucleosidyl) tetraphosphate pyrophosphohydrolase from encysted embryos of the brine shrimp Artemia
    • Prescott M, Milne AD, McLennan AG. (1989) Characterization of the bis(5′-nucleosidyl) tetraphosphate pyrophosphohydrolase from encysted embryos of the brine shrimp Artemia. Biochem J.; 259: 831-8.
    • (1989) Biochem J , vol.259 , pp. 831-838
    • Prescott, M.1    Milne, A.D.2    McLennan, A.G.3
  • 107
    • 0026511334 scopus 로고
    • Characterisation of a bis(5′-nucleosidyl)triphosphate pyrophosphohydrolase from encysted embryos of the brine shrimp Artemia
    • Prescott M, Thorne MH, Milne AD, McLennan AG. (1992) Characterisation of a bis(5′-nucleosidyl)triphosphate pyrophosphohydrolase from encysted embryos of the brine shrimp Artemia. Int J Biochem.; 24: 565-71.
    • (1992) Int J Biochem , vol.24 , pp. 565-571
    • Prescott, M.1    Thorne, M.H.2    Milne, A.D.3    McLennan, A.G.4
  • 108
    • 0028881662 scopus 로고
    • The synthesis and reactivity of new 2-(N,N-diisopropylamino)-3- methylsulfonyl-1,3,2-benzoxazaphosph oles. The utility of the 5-chloro analogue in the one-pot synthesis of oligothiophosphates: [ApsppA, ApspppA, ppp5′ A2′ ps5′ A, m7GpsppA, Apspppp, Apspp]
    • spp]. Tetrahedron.; 51: 2991-3014.
    • (1995) Tetrahedron , vol.51 , pp. 2991-3014
    • Puri, N.1    Hünsch, S.2    Sund, Ch.3    Ugi, I.4    Chattopadhyaya, J.5
  • 109
    • 0027368946 scopus 로고
    • Inhibition of casein kinase II by dinucleoside polyphosphates
    • Pype S, Siegers H. (1993) Inhibition of casein kinase II by dinucleoside polyphosphates. Enzyme Protein.; 47: 14-21.
    • (1993) Enzyme Protein , vol.47 , pp. 14-21
    • Pype, S.1    Siegers, H.2
  • 110
    • 0014007454 scopus 로고
    • Isolation and characterization of dinucleoside tetra- And triphosphates formed in the presence of lysyl-sRNA synthetase
    • Randerath K, Janeway CM, Stephenson ML, Zamecnik PC. (1966) Isolation and characterization of dinucleoside tetra- and triphosphates formed in the presence of lysyl-sRNA synthetase. Biochem Biophys Res Commun.; 24: 98-105.
    • (1966) Biochem Biophys Res Commun , vol.24 , pp. 98-105
    • Randerath, K.1    Janeway, C.M.2    Stephenson, M.L.3    Zamecnik, P.C.4
  • 112
    • 0142025153 scopus 로고    scopus 로고
    • ATP N-glycosidase a novel ATP-converting activity from a marine sponge Axinella polypoides
    • Reintamm T, Lopp A, Kuusksalu A, Pehk T, Kelve M. (2003) ATP N-glycosidase a novel ATP-converting activity from a marine sponge Axinella polypoides. Eur J Biochem.; 270: 4122-32.
    • (2003) Eur J Biochem , vol.270 , pp. 4122-4132
    • Reintamm, T.1    Lopp, A.2    Kuusksalu, A.3    Pehk, T.4    Kelve, M.5
  • 113
    • 0013805471 scopus 로고
    • Dismutation reactions of nucleoside polyphosphates. III. The synthesis of α,ω-dinucleoside 5′-polyphosphates
    • Reiss JR, Moffatt JG. (1965) Dismutation reactions of nucleoside polyphosphates. III. The synthesis of α,ω-dinucleoside 5′-polyphosphates. J Org Chem.; 30: 3381-7.
    • (1965) J Org Chem , vol.30 , pp. 3381-3387
    • Reiss, J.R.1    Moffatt, J.G.2
  • 115
    • 0022371088 scopus 로고
    • Adenosine kinase from bovine adrenal medulla
    • Rotllan P, Miras Portugal MT. (1985) Adenosine kinase from bovine adrenal medulla. Eur J Biochem.; 151: 365-71.
    • (1985) Eur J Biochem , vol.151 , pp. 365-371
    • Rotllan, P.1    Miras Portugal, M.T.2
  • 117
    • 0033618424 scopus 로고    scopus 로고
    • The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase: Overlapping substrate specificities in a MutT motif
    • Safrany ST, Ingram SW, Cartwright JL, Falck JR, McLennan AG, Barnes LD, Shears SB. (1999) The diadenosine hexaphosphate hydrolases from Schizosaccharomyces pombe and Saccharomyces cerevisiae are homologues of the human diphosphoinositol polyphosphate phosphohydrolase: overlapping substrate specificities in a MutT motif. J Biol Chem.; 274: 21735-40.
    • (1999) J Biol Chem , vol.274 , pp. 21735-21740
    • Safrany, S.T.1    Ingram, S.W.2    Cartwright, J.L.3    Falck, J.R.4    McLennan, A.G.5    Barnes, L.D.6    Shears, S.B.7
  • 119
    • 2442578434 scopus 로고
    • Fluorescent and imido-analogues of diadenosine tetraphosphate
    • Shumiyanzeva W, Poletaev AI. (1984) Fluorescent and imido-analogues of diadenosine tetraphosphate. Nucleic Acids Res Symp Ser.; 14: 289-90.
    • (1984) Nucleic Acids Res Symp Ser , vol.14 , pp. 289-290
    • Shumiyanzeva, W.1    Poletaev, A.I.2
  • 121
    • 0034613019 scopus 로고    scopus 로고
    • The three-dimensional structure of the nudix enzyme diadenosine tetraphosphate hydrolase from Lupinus angustifolius L.
    • Swarbrick JD, Bashtannyk T, Maksel D, Zhang X-R, Blackburn GM, Gayler KR, Gooley PR. (2000) The three-dimensional structure of the nudix enzyme diadenosine tetraphosphate hydrolase from Lupinus angustifolius L. J Mol Biol.; 302: 1165-77.
    • (2000) J Mol Biol , vol.302 , pp. 1165-1177
    • Swarbrick, J.D.1    Bashtannyk, T.2    Maksel, D.3    Zhang, X.-R.4    Blackburn, G.M.5    Gayler, K.R.6    Gooley, P.R.7
  • 122
    • 0022472345 scopus 로고
    • Modification of lactate dehydrogenase by pyridoxal phosphate and adenosine polyphosphopyridoxal
    • Tagaya M, Fukui T. (1986) Modification of lactate dehydrogenase by pyridoxal phosphate and adenosine polyphosphopyridoxal. Biochemistry.; 25: 2958-64.
    • (1986) Biochemistry , vol.25 , pp. 2958-2964
    • Tagaya, M.1    Fukui, T.2
  • 123
    • 0001246918 scopus 로고
    • 4-bis(5′-adenosyl) tetraphosphate and its phosphonate analogue with the use of carbonyl derivatives of nitrogen-containing heterocycles
    • in Russian, abstract in English
    • 4-bis(5′-adenosyl)tetraphosphate and its phosphonate analogue with the use of carbonyl derivatives of nitrogen-containing heterocycles. Bioorg Khim.; 12: 404-7. (in Russian, abstract in English).
    • (1986) Bioorg Khim , vol.12 , pp. 404-407
    • Tarussova, N.B.1    Osipova, T.I.2    Purygin, P.P.3    Yakimova, I.A.4
  • 124
    • 0342294661 scopus 로고
    • Organophosphorous analogs of biologically active compounds. XII. Synthesis and properties of diadenosine tetraphosphate and its phosphonate analogs
    • in Russian, abstract in English
    • Tarussova NB, Shumiyanzeva VV, Krylov AC, Karpeisky MYa, Khomutov RM. (1983) Organophosphorous analogs of biologically active compounds. XII. Synthesis and properties of diadenosine tetraphosphate and its phosphonate analogs. Bioorg Khim.; 9: 838-43. (in Russian, abstract in English).
    • (1983) Bioorg Khim , vol.9 , pp. 838-843
    • Tarussova, N.B.1    Shumiyanzeva, V.V.2    Krylov, A.C.3    Karpeisky, M.Ya.4    Khomutov, R.M.5
  • 127
    • 0242669288 scopus 로고    scopus 로고
    • Synthetic, nondegradable diadenosine polyphosphates and diinosine polyphosphates: Their effects on insulin-secreting cells and cultured vascular smooth muscle cells
    • Verspohl EJ, Blackburn GM, Hohmeier N, Hagemann J, Lempka M. (2003) Synthetic, nondegradable diadenosine polyphosphates and diinosine polyphosphates: their effects on insulin-secreting cells and cultured vascular smooth muscle cells. J Med Chem.; 46: 1554-62.
    • (2003) J Med Chem , vol.46 , pp. 1554-1562
    • Verspohl, E.J.1    Blackburn, G.M.2    Hohmeier, N.3    Hagemann, J.4    Lempka, M.5
  • 129
    • 0025911363 scopus 로고
    • 1-ATPase; evidence for an adenylate kinase-like orientation of catalytic and noncatalytic sites
    • 1-ATPase; evidence for an adenylate kinase-like orientation of catalytic and noncatalytic sites. J Biol Chem.; 256: 6101-5.
    • (1991) J Biol Chem , vol.256 , pp. 6101-6105
    • Vogel, P.D.1    Cross, R.L.2
  • 130
    • 0038713657 scopus 로고    scopus 로고
    • Hydrolysis of diadenosine polyphosphates by nucleotide pyrophosphatases/phosphodiesterases
    • Vollmayer P, Clair T, Goding JW, Sano K, Servos J, Zimmermann H. (2003) Hydrolysis of diadenosine polyphosphates by nucleotide pyrophosphatases/ phosphodiesterases. Eur J Biochem.; 270: 2971-8.
    • (2003) Eur J Biochem , vol.270 , pp. 2971-2978
    • Vollmayer, P.1    Clair, T.2    Goding, J.W.3    Sano, K.4    Servos, J.5    Zimmermann, H.6
  • 131
    • 0037025450 scopus 로고    scopus 로고
    • Inhibition of ADP-triggered blood platelet aggregation by diadenosine polyphosphate analogues
    • Walkowiak B, Baraniak J, Cierniewski CzS, Stec W. (2002) Inhibition of ADP-triggered blood platelet aggregation by diadenosine polyphosphate analogues. Bioorg Med Chem Lett.; 12: 1959-62.
    • (2002) Bioorg Med Chem Lett , vol.12 , pp. 1959-1962
    • Walkowiak, B.1    Baraniak, J.2    Cierniewski, Cz.S.3    Stec, W.4
  • 132
    • 0021760889 scopus 로고
    • 3N compounds by guanylyltransferase from encysted embryos of the brine shrimp Artemia
    • 3N compounds by guanylyltransferase from encysted embryos of the brine shrimp Artemia. Nucleic Acids Res.; 12: 2303-15.
    • (1984) Nucleic Acids Res , vol.12 , pp. 2303-2315
    • Wang, D.1    Shatkin, A.J.2
  • 133
    • 0021991704 scopus 로고
    • Continuous fluorimetric assay of nucleotide pyrophosphatase. Kinetics, inhibitors, and extension to dinucleoside oligophosphatases
    • Wierzchowski J, Sierakowska H, Shugar D. (1985) Continuous fluorimetric assay of nucleotide pyrophosphatase. Kinetics, inhibitors, and extension to dinucleoside oligophosphatases. Biochim Biophys Acta.; 828: 109-15.
    • (1985) Biochim Biophys Acta , vol.828 , pp. 109-115
    • Wierzchowski, J.1    Sierakowska, H.2    Shugar, D.3
  • 134
    • 0023928585 scopus 로고
    • Adenosine di-, tri- And tetraphosphopyridoxals modify the same lysyl residue at the ATP-binding site in adenylate kinase
    • Yagami T, Tagaya M, Fukui T. (1988) Adenosine di-, tri- and tetraphosphopyridoxals modify the same lysyl residue at the ATP-binding site in adenylate kinase. FEBS Lett.; 229: 261-4.
    • (1988) FEBS Lett , vol.229 , pp. 261-264
    • Yagami, T.1    Tagaya, M.2    Fukui, T.3
  • 135
    • 0014007431 scopus 로고
    • Enzymatic synthesis of diadenosine tetraphosphate and diadenosine triphosphate with a purified lysyl-sRNA synthetase
    • Zamecnik PC, Stephenson ML, Janeway CM, Randerath K. (1966) Enzymatic synthesis of diadenosine tetraphosphate and diadenosine triphosphate with a purified lysyl-sRNA synthetase. Biochem Biophys Res Commun.; 24: 91-7.
    • (1966) Biochem Biophys Res Commun , vol.24 , pp. 91-97
    • Zamecnik, P.C.1    Stephenson, M.L.2    Janeway, C.M.3    Randerath, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.