메뉴 건너뛰기




Volumn 44, Issue 11, 2005, Pages 4416-4425

Ricin A-chain activity on stem-loop and unstructured DNA substrates

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CHEMICAL BONDS; RNA; SUBSTRATES; TOXIC MATERIALS;

EID: 15544388341     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0474362     Document Type: Article
Times cited : (22)

References (46)
  • 1
    • 0017142394 scopus 로고
    • Toxicity, distribution and elimination of the cancerostatic lectins abrin and ricin after parenteral injection into mice
    • Fodstad, O., Olsnes, S., and Pihl, A. (1976) Toxicity, distribution and elimination of the cancerostatic lectins abrin and ricin after parenteral injection into mice, Br. J. Cancer 34, 418-425.
    • (1976) Br. J. Cancer , vol.34 , pp. 418-425
    • Fodstad, O.1    Olsnes, S.2    Pihl, A.3
  • 2
    • 0030147202 scopus 로고    scopus 로고
    • Lesions of acute inhaled lethal ricin intoxication in rhesus monkeys
    • Wilhelmsen, C. L., and Pitt, M. L. (1996) Lesions of acute inhaled lethal ricin intoxication in rhesus monkeys. Vet. Pathol. 33, 296-302.
    • (1996) Vet. Pathol. , vol.33 , pp. 296-302
    • Wilhelmsen, C.L.1    Pitt, M.L.2
  • 3
    • 0037011902 scopus 로고    scopus 로고
    • Structure-based design and characterization of novel platforms for ricin and shiga toxin inhibition
    • Miller, D. J., Ravikumar, K., Shen, H., Suh, J. K., Kerwin, S. M., and Robertas, J. D. (2002) Structure-based design and characterization of novel platforms for ricin and shiga toxin inhibition, J. Med. Chem. 45, 90-98.
    • (2002) J. Med. Chem. , vol.45 , pp. 90-98
    • Miller, D.J.1    Ravikumar, K.2    Shen, H.3    Suh, J.K.4    Kerwin, S.M.5    Robertas, J.D.6
  • 4
    • 0019158721 scopus 로고
    • Georgi Markov: Death in a pellet
    • Crompton, R., and Gall, D. (1980) Georgi Markov: Death in a pellet, Med.-Leg. J. 48, 51-62.
    • (1980) Med.-Leg. J. , vol.48 , pp. 51-62
    • Crompton, R.1    Gall, D.2
  • 5
    • 0034935042 scopus 로고    scopus 로고
    • Chemical construction of immunotoxins
    • Ghetie, V., and Vitetta, E. S. (2001) Chemical construction of immunotoxins, Mol. Biotechnol. 18, 251-268.
    • (2001) Mol. Biotechnol. , vol.18 , pp. 251-268
    • Ghetie, V.1    Vitetta, E.S.2
  • 6
    • 0025615069 scopus 로고
    • Immunotoxins: New therapeutic reagents for autoimmunity, cancer, and AIDS
    • Vitetta, E. S. (1990) Immunotoxins: New therapeutic reagents for autoimmunity, cancer, and AIDS, J. Clin. Immunol. 10, 15S-18S.
    • (1990) J. Clin. Immunol. , vol.10
    • Vitetta, E.S.1
  • 7
    • 0034255636 scopus 로고    scopus 로고
    • The effect of a monoclonal antibody coupled to ricin a chain-derived peptides on endothelial cells in vitro: Insights into toxin-mediated vascular damage
    • Baluna, R., Coleman, E., Jones, C., Ghetie, V., and Vitetta, E. S. (2000) The effect of a monoclonal antibody coupled to ricin A chain-derived peptides on endothelial cells in vitro: Insights into toxin-mediated vascular damage, Exp. Cell Res. 258, 417-424.
    • (2000) Exp. Cell Res. , vol.258 , pp. 417-424
    • Baluna, R.1    Coleman, E.2    Jones, C.3    Ghetie, V.4    Vitetta, E.S.5
  • 8
    • 0030862195 scopus 로고    scopus 로고
    • Vascular leak syndrome: A side effect of immunotherapy
    • Baluna, R., and Vitetta, E. S. (1997) Vascular leak syndrome: A side effect of immunotherapy, Immimopharmacology 37, 117-132.
    • (1997) Immimopharmacology , vol.37 , pp. 117-132
    • Baluna, R.1    Vitetta, E.S.2
  • 11
    • 0032544216 scopus 로고    scopus 로고
    • Ricin A-chain: Kinetics, mechanism, and RNA stem-loop inhibitors
    • Chen, X. Y., Link, T. M., and Schramm, V. L. (1998) Ricin A-chain: Kinetics, mechanism, and RNA stem-loop inhibitors, Biochemistry 37, 11605-11613.
    • (1998) Biochemistry , vol.37 , pp. 11605-11613
    • Chen, X.Y.1    Link, T.M.2    Schramm, V.L.3
  • 13
    • 0035289779 scopus 로고    scopus 로고
    • Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings
    • Lipinski, C. A., Lombardo, F., Dominy, B. W., and Feeney, P. J. (2001) Experimental and computational approaches to estimate solubility and permeability in drug discovery and development settings, Adv. Drug Delivery Rev. 46, 3-26.
    • (2001) Adv. Drug Delivery Rev. , vol.46 , pp. 3-26
    • Lipinski, C.A.1    Lombardo, F.2    Dominy, B.W.3    Feeney, P.J.4
  • 14
    • 0029960070 scopus 로고    scopus 로고
    • High-resolution NMR study of a GdAGA tetranucleotide loop that is an improved substrate for ricin, a cytotoxic plant protein
    • Orita, M., Mishikawa, F., Kohno, T., Senda, T., Mitsui, Y., Endo, Y., Taira, K., and Nishikawa, S. (1996) High-resolution NMR study of a GdAGA tetranucleotide loop that is an improved substrate for ricin, a cytotoxic plant protein, Nucleic Acids Res. 24, 611-618.
    • (1996) Nucleic Acids Res. , vol.24 , pp. 611-618
    • Orita, M.1    Mishikawa, F.2    Kohno, T.3    Senda, T.4    Mitsui, Y.5    Endo, Y.6    Taira, K.7    Nishikawa, S.8
  • 15
    • 0023664263 scopus 로고
    • The mechanism of action of ricin and telated toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28S ribosomal RNA caused by the toxins
    • Endo, Y., Mitsui, K., Motizuki, M., and Tsurge, K. (1987) The mechanism of action of ricin and telated toxic lectins on eukaryotic ribosomes. The site and the characteristics of the modification in 28S ribosomal RNA caused by the toxins, J. Biol. Chem. 262, 5908-5912.
    • (1987) J. Biol. Chem. , vol.262 , pp. 5908-5912
    • Endo, Y.1    Mitsui, K.2    Motizuki, M.3    Tsurge, K.4
  • 16
    • 0016441396 scopus 로고
    • Inhibition by ricin of protein synthesis in vitro. Inhibition of the binding of elongation factor 2 and of adenosine diphosphate-ribosylated elongation factor 2 to ribosomes
    • Montanaro, L., Sperti, S., Mattioli, A., Testoni, G., and Stirpe, F. (1975) Inhibition by ricin of protein synthesis in vitro. Inhibition of the binding of elongation factor 2 and of adenosine diphosphate-ribosylated elongation factor 2 to ribosomes, Biochem. J. 146, 127-131.
    • (1975) Biochem. J. , vol.146 , pp. 127-131
    • Montanaro, L.1    Sperti, S.2    Mattioli, A.3    Testoni, G.4    Stirpe, F.5
  • 17
    • 0026704534 scopus 로고
    • Ribosomal RNA identity elements for ricin A-chain recognition and catalysis. Analysis with tetraloop mutants
    • Gluck, A., Endo, Y., and Wool, I. G. (1992) Ribosomal RNA identity elements for ricin A-chain recognition and catalysis. Analysis with tetraloop mutants, J. MoI. Biol. 226, 411-424.
    • (1992) J. MoI. Biol. , vol.226 , pp. 411-424
    • Gluck, A.1    Endo, Y.2    Wool, I.G.3
  • 18
    • 0029379566 scopus 로고
    • Synthesis and biochemical evaluation of RNA containing an intrahelical disulfide cross-link
    • Allerson, C. R., and Verdine, G. L. (1995) Synthesis and biochemical evaluation of RNA containing an intrahelical disulfide cross-link, Chem. Biol. 2, 667-675.
    • (1995) Chem. Biol. , vol.2 , pp. 667-675
    • Allerson, C.R.1    Verdine, G.L.2
  • 19
    • 0034686760 scopus 로고    scopus 로고
    • Transition-state analysis for depurination of DNA by ricin A-chain
    • Xiang-Yang, C., Berti, P. J., and Schramm, V. L. (2000) Transition-State Analysis for Depurination of DNA by Ricin A-Chain, J. Am. Chem. Soc. 122, 6527-6534.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 6527-6534
    • Xiang-Yang, C.1    Berti, P.J.2    Schramm, V.L.3
  • 20
    • 0034088859 scopus 로고    scopus 로고
    • Ricin A-chain: Kinetic isotope effects and transition state structure with stem-loop RNA
    • Xiang-Yang, C., Berti, P. J., and Schramm, V. L. (2000) Ricin A-Chain: Kinetic Isotope Effects and Transition State Structure with Stem-Loop RNA, J. Am. Chem. Soc. 122, 1609-1617.
    • (2000) J. Am. Chem. Soc. , vol.122 , pp. 1609-1617
    • Xiang-Yang, C.1    Berti, P.J.2    Schramm, V.L.3
  • 21
    • 0034471698 scopus 로고    scopus 로고
    • Polynucleotide: Adenosine glycosidase activity of immunotoxins containing ribosome-inactivating proteins
    • Barbieri, L., Bolognesi, A., Valbonesi, P., Polito, L., Olivieri, F., and Stirpe, F. (2000) Polynucleotide: Adenosine glycosidase activity of immunotoxins containing ribosome-inactivating proteins, J. Drug Targeting 8, 281-288.
    • (2000) J. Drug Targeting , vol.8 , pp. 281-288
    • Barbieri, L.1    Bolognesi, A.2    Valbonesi, P.3    Polito, L.4    Olivieri, F.5    Stirpe, F.6
  • 22
    • 0032530844 scopus 로고    scopus 로고
    • A rapid and sensitive method to measure the enzymatic activity of ribosome-inactivating proteins
    • Brigotti, M., Barbieri, L., Valbonesi, P., Stirpe, F., Montanaro, L., and Sperti, S. (1998) A rapid and sensitive method to measure the enzymatic activity of ribosome-inactivating proteins. Nucleic Acids Res. 26, 4306-4307.
    • (1998) Nucleic Acids Res. , vol.26 , pp. 4306-4307
    • Brigotti, M.1    Barbieri, L.2    Valbonesi, P.3    Stirpe, F.4    Montanaro, L.5    Sperti, S.6
  • 23
    • 0035997348 scopus 로고    scopus 로고
    • V(D)J recombination: RAG proteins, repair factors, and regulation
    • Gellert, M. (2002) V(D)J recombination: RAG proteins, repair factors, and regulation, Annu. Rev. Biochem. 71, 101-132.
    • (2002) Annu. Rev. Biochem. , vol.71 , pp. 101-132
    • Gellert, M.1
  • 24
    • 0242718930 scopus 로고    scopus 로고
    • Trinucleotide repeat instability: A hairpin curve at the crossroads of replication, recombination, and repair
    • Lenzmeier, B. A., and Freudenreich, C. H. (2003) Trinucleotide repeat instability: A hairpin curve at the crossroads of replication, recombination, and repair, Cytogenet. Genome Res. 100, 7-24.
    • (2003) Cytogenet. Genome Res. , vol.100 , pp. 7-24
    • Lenzmeier, B.A.1    Freudenreich, C.H.2
  • 25
    • 0034045279 scopus 로고    scopus 로고
    • Targeting DNA secondary structures
    • Wadkins, R. M. (2000) Targeting DNA secondary structures, Curr. Med. Chem. 7, 1-15.
    • (2000) Curr. Med. Chem. , vol.7 , pp. 1-15
    • Wadkins, R.M.1
  • 27
    • 0025942059 scopus 로고
    • A thermodynamic study of unusually stable RNA and DNA hairpins
    • Antao, V. P., Lai, S. Y., and Tinoco, I., Jr. (1991) A thermodynamic study of unusually stable RNA and DNA hairpins, Nucleic Acids Res. 19, 5901-5905.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 5901-5905
    • Antao, V.P.1    Lai, S.Y.2    Tinoco Jr., I.3
  • 28
    • 0037015994 scopus 로고    scopus 로고
    • Selection for thermodynamically stable DNA tetraloops using temperature gradient gel electrophoresis reveals four motifs: D(cGNNAg), d(cGNABg), d(cCNNGg), and d(gCNNGc)
    • Nakano, M., Moody, E. M., Liang, J., and Bevilacqua, P. C. (2002) Selection for thermodynamically stable DNA tetraloops using temperature gradient gel electrophoresis reveals four motifs: d(cGNNAg), d(cGNABg), d(cCNNGg), and d(gCNNGc), Biochemistry 41, 14281-14292.
    • (2002) Biochemistry , vol.41 , pp. 14281-14292
    • Nakano, M.1    Moody, E.M.2    Liang, J.3    Bevilacqua, P.C.4
  • 29
    • 0026593806 scopus 로고
    • Thermodynamic parameters for loop formation in RNA and DNA hairpin tetraloops
    • Antao, V. P., and Tinoco, I., Jr. (1992) Thermodynamic parameters for loop formation in RNA and DNA hairpin tetraloops, Nucleic Acids Res. 20, 819-824.
    • (1992) Nucleic Acids Res. , vol.20 , pp. 819-824
    • Antao, V.P.1    Tinoco Jr., I.2
  • 30
    • 0347064295 scopus 로고    scopus 로고
    • Folding of a stable DNA motif involves a highly cooperative network of interactions
    • Moody, E. M., and Bevilacqua, P. C. (2003) Folding of a stable DNA motif involves a highly cooperative network of interactions, J. Am. Chem. Soc. 125, 16285-16293.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 16285-16293
    • Moody, E.M.1    Bevilacqua, P.C.2
  • 31
    • 0037467110 scopus 로고    scopus 로고
    • Thermodynamic coupling of the loop and stem in unusually stable DNA hairpins closed by CG base pairs
    • Moody, E. M., and Bevilacqua, P. C. (2003) Thermodynamic coupling of the loop and stem in unusually stable DNA hairpins closed by CG base pairs, J. Am. Chem. Soc. 725, 2032-2033.
    • (2003) J. Am. Chem. Soc. , vol.725 , pp. 2032-2033
    • Moody, E.M.1    Bevilacqua, P.C.2
  • 32
    • 5144233105 scopus 로고
    • MLEV-17-based two-dimensional homonuclear magnetization transfer spectroscopy
    • Bax, A., and Davis, D. G. (1985) MLEV-17-Based Two-Dimensional Homonuclear Magnetization Transfer Spectroscopy, J. Magn. Reson. 65, 355.
    • (1985) J. Magn. Reson. , vol.65 , pp. 355
    • Bax, A.1    Davis, D.G.2
  • 33
    • 0018339645 scopus 로고
    • The translational friction coefficient of proteins
    • Teller, D. C., Swanson, E., and de Haen, C. (1979) The translational friction coefficient of proteins, Methods Enzymol. 61, 103-124.
    • (1979) Methods Enzymol. , vol.61 , pp. 103-124
    • Teller, D.C.1    Swanson, E.2    De Haen, C.3
  • 34
    • 58149362694 scopus 로고
    • An improved diffusion-ordered spectroscopy experiment incorporating bipolar-gradient pulses
    • Wu, D., Chen, A., and Johnson, C. S. (1995) An Improved Diffusion-Ordered Spectroscopy Experiment Incorporating Bipolar-Gradient Pulses, J. Magn. Reson., Ser. A 115, 260-264.
    • (1995) J. Magn. Reson., Ser. A , vol.115 , pp. 260-264
    • Wu, D.1    Chen, A.2    Johnson, C.S.3
  • 35
    • 0032795253 scopus 로고    scopus 로고
    • J-coupling restraints in RNA stucture determination
    • Marino, J. P., Schwalbe, H., and Griesinger, C. (1999) J-Coupling Restraints in RNA Stucture Determination, Acc. Chem. Res. 32, 614-623.
    • (1999) Acc. Chem. Res. , vol.32 , pp. 614-623
    • Marino, J.P.1    Schwalbe, H.2    Griesinger, C.3
  • 36
    • 0028247062 scopus 로고
    • Most compact hairpin-turn structure exerted by a short DNA fragment, d(GCGAAGC) in solution: An extraordinarily stable structure resistant to nucleases and heat
    • Hirao, I., Kawai, G., Yoshizawa, S., Nishimura, Y., Ishido, Y., Watanabe, K., and Miura, K. (1994) Most compact hairpin-turn structure exerted by a short DNA fragment, d(GCGAAGC) in solution: An extraordinarily stable structure resistant to nucleases and heat, Nucleic Acids Res. 22, 576-582.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 576-582
    • Hirao, I.1    Kawai, G.2    Yoshizawa, S.3    Nishimura, Y.4    Ishido, Y.5    Watanabe, K.6    Miura, K.7
  • 37
    • 0015528973 scopus 로고
    • Solvolysis of adenine nucleosides. I. Effects of sugars and adenine substituents on acid solvolyses
    • Garrett, E. R., and Mehta, P. J. (1972) Solvolysis of adenine nucleosides. I. Effects of sugars and adenine substituents on acid solvolyses, J. Am. Chem. Soc. 94, 8532-8541.
    • (1972) J. Am. Chem. Soc. , vol.94 , pp. 8532-8541
    • Garrett, E.R.1    Mehta, P.J.2
  • 38
    • 2142824196 scopus 로고    scopus 로고
    • Ricin A-chain substrate specificity in RNA, DNA and hybrid stem-loop structures
    • Amukele, T. K., and Schramm, V. L. (2004) Ricin A-chain substrate specificity in RNA, DNA and hybrid stem-loop structures. Biochemistry 43, 4913-4922.
    • (2004) Biochemistry , vol.43 , pp. 4913-4922
    • Amukele, T.K.1    Schramm, V.L.2
  • 39
    • 0018788372 scopus 로고
    • Conformations of dinucleoside phosphates in aqueous solution
    • Lee, C. H., Charney, E., and Tinoco, I., Jr. (1979) Conformations of dinucleoside phosphates in aqueous solution, Biochemistry 18, 5636-5641.
    • (1979) Biochemistry , vol.18 , pp. 5636-5641
    • Lee, C.H.1    Charney, E.2    Tinoco Jr., I.3
  • 41
    • 0033578939 scopus 로고    scopus 로고
    • The two faces of the Escherichia coli 23 S rRNA sarcin/ricin domain: The structure at 1.11 Å resolution
    • Correll, C. C., Wool, I. G., and Munishkin, A. (1999) The two faces of the Escherichia coli 23 S rRNA sarcin/ricin domain: The structure at 1.11 Å resolution, J. Mol. Biol. 292, 275-287.
    • (1999) J. Mol. Biol. , vol.292 , pp. 275-287
    • Correll, C.C.1    Wool, I.G.2    Munishkin, A.3
  • 42
    • 0030596092 scopus 로고    scopus 로고
    • A network of heterogeneous hydrogen bonds in GNRA tetraloops
    • Jucker, F. M., Heus, H. A., Yip, P. F., Moors, E. H., and Pardi, A. (1996) A network of heterogeneous hydrogen bonds in GNRA tetraloops, J. Mol. Biol. 264, 968-980.
    • (1996) J. Mol. Biol. , vol.264 , pp. 968-980
    • Jucker, F.M.1    Heus, H.A.2    Yip, P.F.3    Moors, E.H.4    Pardi, A.5
  • 43
    • 0344442882 scopus 로고    scopus 로고
    • Crystal structure of Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase complexed with an analogue of 1,3-bisphospho-D-glyceric acid
    • Ladame, S., Castilho, M. S., Silva, C. H., Denier, C., Hannaert, V., Perie, J., Oliva, G., and Willson, M. (2003) Crystal structure of Trypanosoma cruzi glyceraldehyde-3-phosphate dehydrogenase complexed with an analogue of 1,3-bisphospho-D-glyceric acid, Eur. J. Biochem. 270, 4574-4586.
    • (2003) Eur. J. Biochem. , vol.270 , pp. 4574-4586
    • Ladame, S.1    Castilho, M.S.2    Silva, C.H.3    Denier, C.4    Hannaert, V.5    Perie, J.6    Oliva, G.7    Willson, M.8
  • 44
    • 0014939710 scopus 로고
    • Studies of the binding of phosphoribosyl pyrophosphate to adenine phosphoribosyltrans-ferase
    • Gadd, R. E., and Henderson, J. F. (1970) Studies of the binding of phosphoribosyl pyrophosphate to adenine phosphoribosyltrans-ferase, J. Biol. Chem. 245, 2979-2984.
    • (1970) J. Biol. Chem. , vol.245 , pp. 2979-2984
    • Gadd, R.E.1    Henderson, J.F.2
  • 45
    • 0027405824 scopus 로고
    • Stabilization of mRNA in an Escherichia coli cell-free translation system
    • Hirao, I., Yoshizawa, S., and Miura, K. (1993) Stabilization of mRNA in an Escherichia coli cell-free translation system, FEBS Lett. 321, 169-172.
    • (1993) FEBS Lett. , vol.321 , pp. 169-172
    • Hirao, I.1    Yoshizawa, S.2    Miura, K.3
  • 46
    • 0025096450 scopus 로고
    • Unique hairpin structures occurring at the replication origin of phage G4 DNA
    • Hirao, I., Ishida, M., Watanabe, K., and Miura, K. (1990) Unique hairpin structures occurring at the replication origin of phage G4 DNA, Biochim. Biophys. Acta 1087, 199-204.
    • (1990) Biochim. Biophys. Acta , vol.1087 , pp. 199-204
    • Hirao, I.1    Ishida, M.2    Watanabe, K.3    Miura, K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.