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Volumn 30, Issue 8, 2008, Pages 781-790

Binase and other microbial RNases as potential anticancer agents

Author keywords

[No Author keywords available]

Indexed keywords

ALEMTUZUMAB; ALPHA SARCIN; ANTINEOPLASTIC AGENT; BARNASE; BINASE; BLEOMYCIN; CETUXIMAB; GEMTUZUMAB OZOGAMICIN; IBRITUMOMAB TIUXETAN; PANITUMUMAB; RANPIRNASE; RIBONUCLEASE; RITUXIMAB; TOSITUMOMAB; TRASTUZUMAB;

EID: 48949094215     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.20789     Document Type: Article
Times cited : (83)

References (78)
  • 2
    • 0018938880 scopus 로고
    • In vitro studies on selective inhibition of tumor cell growth by seminal ribonuclease
    • Vescia S, Tramontano D, Augusti-Tocco G, D'Alessio G. 1980. In vitro studies on selective inhibition of tumor cell growth by seminal ribonuclease. Cancer Res 40:3740-3744.
    • (1980) Cancer Res , vol.40 , pp. 3740-3744
    • Vescia, S.1    Tramontano, D.2    Augusti-Tocco, G.3    D'Alessio, G.4
  • 4
    • 38549168927 scopus 로고    scopus 로고
    • Ribonuclealses as novel chemotherapeutics: The ranpirnase example
    • Lee JE, Raines RT, 2008. Ribonuclealses as novel chemotherapeutics: the ranpirnase example. BioDrugs 22:63-58.
    • (2008) BioDrugs , vol.22 , pp. 63-58
    • Lee, J.E.1    Raines, R.T.2
  • 5
    • 0036137925 scopus 로고    scopus 로고
    • Phase II trial of a single weekly intravenous dose of rapimase in patient with unresectable malignant mesothelioma
    • Mikulski SM, Costanzi JJ, Vogelzang NJ, McCachren S, Taub RN et at, 2002. Phase II trial of a single weekly intravenous dose of rapimase in patient with unresectable malignant mesothelioma. J. Clin Oncol 20: 274-281.
    • (2002) J. Clin Oncol , vol.20 , pp. 274-281
    • Mikulski, S.M.1    Costanzi, J.J.2    Vogelzang, N.J.3    McCachren, S.4    Taub, R.N.5    et at6
  • 6
    • 48949100668 scopus 로고    scopus 로고
    • Alfacell Provides Update on ONCONASE Phase IIIb Confirmatory Registration Trial
    • Alfacell Corporation, Media Release: 27 April 2006. Available from URL Accessed April 27, 2007
    • Alfacell Corporation. Alfacell Provides Update on ONCONASE Phase IIIb Confirmatory Registration Trial; Releases First Interim Analysis Data. Media Release: 27 April 2006. Available from URL http://www.alfacell.com Accessed April 27, 2007.
    • Releases First Interim Analysis Data
  • 7
    • 33847391138 scopus 로고    scopus 로고
    • Ranpirnase amphibian ribanuclease A. P-30 protein - Alfacell 2007. Drugs R and D 8:120-124.
    • Ranpirnase amphibian ribanuclease A. P-30 protein - Alfacell 2007. Drugs R and D 8:120-124.
  • 8
    • 48949084396 scopus 로고
    • Effect of bacterial deoxyribonuclease on Ehrlich's ascites carcinoma cells in vitro
    • Belyaeva MI, Kyune MF, Nuzhina AM. 1964. Effect of bacterial deoxyribonuclease on Ehrlich's ascites carcinoma cells in vitro. Fed Proc Transl Suppl 23:345-348.
    • (1964) Fed Proc Transl , Issue.SUPPL. 23 , pp. 345-348
    • Belyaeva, M.I.1    Kyune, M.F.2    Nuzhina, A.M.3
  • 11
    • 0036014773 scopus 로고    scopus 로고
    • The structure of substrate-free microbial ribanuclease binase and of its complexes with 3'GMP and sulfate ions
    • Polyakov KM, Lebedev AA, Okorokov AL, Panov KI, Schulga AA et al. 2002. The structure of substrate-free microbial ribanuclease binase and of its complexes with 3'GMP and sulfate ions, Acta Cryst Section D 58: 744-750.
    • (2002) Acta Cryst Section D , vol.58 , pp. 744-750
    • Polyakov, K.M.1    Lebedev, A.A.2    Okorokov, A.L.3    Panov, K.I.4    Schulga, A.A.5
  • 12
    • 36048943980 scopus 로고    scopus 로고
    • Intraspecies regulation of ribonucleolytic activity
    • Johnson RJ, Lavis LD, Raines RT, 2007. Intraspecies regulation of ribonucleolytic activity. Biochemistry 46:13131-13140.
    • (2007) Biochemistry , vol.46 , pp. 13131-13140
    • Johnson, R.J.1    Lavis, L.D.2    Raines, R.T.3
  • 13
    • 0024293097 scopus 로고    scopus 로고
    • Hartley RW. 1988. Bamase and barstar. Exp~ession of its cloned inhibitor permits expression of a cloned ribonuclease. J. Mol Biol 202:913-915.
    • Hartley RW. 1988. Bamase and barstar. Exp~ession of its cloned inhibitor permits expression of a cloned ribonuclease. J. Mol Biol 202:913-915.
  • 14
    • 0029032298 scopus 로고
    • Dissociation constants and thermal stability of complexes of Bacillus intermedius RNase and the protein inhibitor of Bacillus amyloliquefaciens RNase
    • Yakovlev GI, Moiseyev GP, Protasevich II, Ranjbar B, Bocharov AL et al. 1995. Dissociation constants and thermal stability of complexes of Bacillus intermedius RNase and the protein inhibitor of Bacillus amyloliquefaciens RNase. FEBS Letters 366:156-158.
    • (1995) FEBS Letters , vol.366 , pp. 156-158
    • Yakovlev, G.I.1    Moiseyev, G.P.2    Protasevich, I.I.3    Ranjbar, B.4    Bocharov, A.L.5
  • 15
    • 0037033001 scopus 로고    scopus 로고
    • X-Ray structure of two crystalline forms of a streptomycete ribonuclease with cytotoxic activity
    • Sevcik J, Urbanikova L, Leland PA, Raines RT. 2002. X-Ray structure of two crystalline forms of a streptomycete ribonuclease with cytotoxic activity. J. Biol Chem 277:47325-47330.
    • (2002) J. Biol Chem , vol.277 , pp. 47325-47330
    • Sevcik, J.1    Urbanikova, L.2    Leland, P.A.3    Raines, R.T.4
  • 16
    • 0024585923 scopus 로고
    • Ribonuclease inhibitor from pig brain: Purification, characterization, and direct spectrophotometric assay
    • Cho S, Joshi JG, 1989. Ribonuclease inhibitor from pig brain: Purification, characterization, and direct spectrophotometric assay. Anal Biochem 176:175-179.
    • (1989) Anal Biochem , vol.176 , pp. 175-179
    • Cho, S.1    Joshi, J.G.2
  • 17
    • 0027570389 scopus 로고
    • The action of Oxogenous RNAse on the cells of lower eukaryotes]
    • II'inskaia ON, Krylova NI. 1993. [The action of Oxogenous RNAse on the cells of lower eukaryotes] Prikl Biokhim Mikrobiol 29:280-285.
    • (1993) Prikl Biokhim Mikrobiol , vol.29 , pp. 280-285
    • II'inskaia, O.N.1    Krylova, N.I.2
  • 18
    • 0034218193 scopus 로고    scopus 로고
    • Dependence of the effect of RNAase from Bacillus intermedius on the growth of baker's yeast on the concentration of the exogenous enzyme]
    • Kolpakov Al, Kupriianova-Ashina FG, Leshchinskaia IB. 2000. [Dependence of the effect of RNAase from Bacillus intermedius on the growth of baker's yeast on the concentration of the exogenous enzyme]. Mikrobiologiia 69:478-482.
    • (2000) Mikrobiologiia , vol.69 , pp. 478-482
    • Kolpakov, A.1    Kupriianova-Ashina, F.G.2    Leshchinskaia, I.B.3
  • 19
    • 0029071573 scopus 로고
    • Bacterial ribonuclease: Mutagenic effect in microbial test-systems
    • Ilinskaya ON, Ivanchenko OB, Karamova NS. 1995. Bacterial ribonuclease: mutagenic effect in microbial test-systems. Mutagenesis 10:165-170.
    • (1995) Mutagenesis , vol.10 , pp. 165-170
    • Ilinskaya, O.N.1    Ivanchenko, O.B.2    Karamova, N.S.3
  • 23
    • 0035793124 scopus 로고    scopus 로고
    • Bacillus intermedius ribonuclease as inhibitor of cell proliferation and membrane current
    • Ilinskaya O, Decker K, Koschinski A, Dreyer F, Repp H. 2001. Bacillus intermedius ribonuclease as inhibitor of cell proliferation and membrane current. Toxicology 156:101-107.
    • (2001) Toxicology , vol.156 , pp. 101-107
    • Ilinskaya, O.1    Decker, K.2    Koschinski, A.3    Dreyer, F.4    Repp, H.5
  • 26
    • 0037259429 scopus 로고    scopus 로고
    • RNA cleavage and inhibition of protein synthesis by bleomycin
    • Abraham AT, Lin J, Newton DL, Rybak S, Hecht S. 2003. RNA cleavage and inhibition of protein synthesis by bleomycin. Chem Biol 10:45-52.
    • (2003) Chem Biol , vol.10 , pp. 45-52
    • Abraham, A.T.1    Lin, J.2    Newton, D.L.3    Rybak, S.4    Hecht, S.5
  • 27
    • 0037430969 scopus 로고    scopus 로고
    • Cytotoxic ribonucleases: Molecular weapons and their targets
    • Makarov AA. Ilinskaya ON. 2003. Cytotoxic ribonucleases: molecular weapons and their targets. FEBS Lett 540:15-20.
    • (2003) FEBS Lett , vol.540 , pp. 15-20
    • Makarov, A.A.1    Ilinskaya, O.N.2
  • 28
    • 0036829110 scopus 로고    scopus 로고
    • Increased exposure of anionic phospholipids on the surface of tumor blood vessels
    • Ran S, Downes A, Thorpe PE. 2002. Increased exposure of anionic phospholipids on the surface of tumor blood vessels. Cancer Res 62: 6132-6140.
    • (2002) Cancer Res , vol.62 , pp. 6132-6140
    • Ran, S.1    Downes, A.2    Thorpe, P.E.3
  • 29
    • 0036784623 scopus 로고    scopus 로고
    • Changing the net charge from negative to positive makes ribonuclease Sa cytotoxic
    • Ilinskaya ON, Dreyer F, Mitkevich VA, Shaw KL, Pace CN et al. 2002. Changing the net charge from negative to positive makes ribonuclease Sa cytotoxic. Protein Sci 11:2522-2525.
    • (2002) Protein Sci , vol.11 , pp. 2522-2525
    • Ilinskaya, O.N.1    Dreyer, F.2    Mitkevich, V.A.3    Shaw, K.L.4    Pace, C.N.5
  • 30
    • 0035954402 scopus 로고    scopus 로고
    • Preparation of potent cytotoxic ribonucleases by cationization: Enhanced cellular uptake and decreased interaction with ribonuclease inhibitor by chemical modification of carboxyl groups
    • Futami J, Maeda T, Kitazoe M, Nukui E, Tada H et al. 2001. Preparation of potent cytotoxic ribonucleases by cationization: enhanced cellular uptake and decreased interaction with ribonuclease inhibitor by chemical modification of carboxyl groups. Biochemistry 40:7518-7524.
    • (2001) Biochemistry , vol.40 , pp. 7518-7524
    • Futami, J.1    Maeda, T.2    Kitazoe, M.3    Nukui, E.4    Tada, H.5
  • 31
    • 35148841124 scopus 로고    scopus 로고
    • Cytotoxic ribonucleases: The dichotomy of Coulombic forces
    • Johnson RJ, Chao TY, Lavis LD, Raines RT. 2007. Cytotoxic ribonucleases: the dichotomy of Coulombic forces. Biochemistry 46:10308-10316.
    • (2007) Biochemistry , vol.46 , pp. 10308-10316
    • Johnson, R.J.1    Chao, T.Y.2    Lavis, L.D.3    Raines, R.T.4
  • 32
    • 34948877694 scopus 로고    scopus 로고
    • Endocytotic internalization as a crucial factor for the cytotoxicity of ribonucleases
    • Leich F, Stöhr N, Rietz A, Ulbrich-Hofmann R, Arnold U. 2007. Endocytotic internalization as a crucial factor for the cytotoxicity of ribonucleases. J. Biol Chem 282:27640-27646.
    • (2007) J. Biol Chem , vol.282 , pp. 27640-27646
    • Leich, F.1    Stöhr, N.2    Rietz, A.3    Ulbrich-Hofmann, R.4    Arnold, U.5
  • 33
    • 38549179303 scopus 로고    scopus 로고
    • The cytotoxicity of eosinophil cationic protein/ribonuclease 3 on eukaryotic cell lines takes place through its aggregation on the cell membrane
    • Navarro S, Aleu J, Jiménez M, Boix E, Cuchillo CM et al. 2008. The cytotoxicity of eosinophil cationic protein/ribonuclease 3 on eukaryotic cell lines takes place through its aggregation on the cell membrane. Cell Mol Life Sci 65:324-337.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 324-337
    • Navarro, S.1    Aleu, J.2    Jiménez, M.3    Boix, E.4    Cuchillo, C.M.5
  • 34
    • 0026725327 scopus 로고
    • Translocation mediated by domain II of Pseudomonas exotoxin A: Transport of bamase into the cytosol
    • Prior TI, FitzGerald DJ, Pastan I. 1992. Translocation mediated by domain II of Pseudomonas exotoxin A: transport of bamase into the cytosol. Biochemistry 31:3555-3559.
    • (1992) Biochemistry , vol.31 , pp. 3555-3559
    • Prior, T.I.1    FitzGerald, D.J.2    Pastan, I.3
  • 35
    • 0033572942 scopus 로고    scopus 로고
    • Natural and engineered cytotoxic ribonucleases: Therapeutic potential
    • Rybak SM, Newton DL. 1999. Natural and engineered cytotoxic ribonucleases: therapeutic potential. Exp Cell Res 253:325-335.
    • (1999) Exp Cell Res , vol.253 , pp. 325-335
    • Rybak, S.M.1    Newton, D.L.2
  • 36
    • 32044474915 scopus 로고    scopus 로고
    • A new vector for controllable expression of an anti-HER2/neu mini-antibody-bamase fusion protein in HEK 293T cells
    • Glinka EM, Edelweiss EF, Sapozhnikov AM, Deyev SM. 2006. A new vector for controllable expression of an anti-HER2/neu mini-antibody-bamase fusion protein in HEK 293T cells. Gene 366:97-103.
    • (2006) Gene , vol.366 , pp. 97-103
    • Glinka, E.M.1    Edelweiss, E.F.2    Sapozhnikov, A.M.3    Deyev, S.M.4
  • 37
    • 33846216043 scopus 로고    scopus 로고
    • Intracellular route and mechanism of action of ERB-hRNase, a human anti-ErbB2 anticancer immunoagent
    • De Lorenzo C, Di Malta C, Cali G, Troise F, Nitsch L et al. 2007. Intracellular route and mechanism of action of ERB-hRNase, a human anti-ErbB2 anticancer immunoagent. FEBS Lett 581:296-300.
    • (2007) FEBS Lett , vol.581 , pp. 296-300
    • De Lorenzo, C.1    Di Malta, C.2    Cali, G.3    Troise, F.4    Nitsch, L.5
  • 38
    • 33645825444 scopus 로고    scopus 로고
    • Mechanisms of the growth-inhibitory effect of the RNase-EGF fused protein against EGFR-overexpressing cells
    • Hoshimoto S, Ueda M, Jinno H, Kitajima M, Futami J et al. 2006. Mechanisms of the growth-inhibitory effect of the RNase-EGF fused protein against EGFR-overexpressing cells. Anticancer Res 26:857-863.
    • (2006) Anticancer Res , vol.26 , pp. 857-863
    • Hoshimoto, S.1    Ueda, M.2    Jinno, H.3    Kitajima, M.4    Futami, J.5
  • 39
    • 18144419692 scopus 로고    scopus 로고
    • Efficient killing of CD22+ tumor cells by a humanized diabody-RNase fusion protein
    • Krauss J, Arndt MA, Vu BK, Newton DL, Seeber S et al. 2005. Efficient killing of CD22+ tumor cells by a humanized diabody-RNase fusion protein. Biochem Biophys Res Commun 331:595-602.
    • (2005) Biochem Biophys Res Commun , vol.331 , pp. 595-602
    • Krauss, J.1    Arndt, M.A.2    Vu, B.K.3    Newton, D.L.4    Seeber, S.5
  • 40
    • 29444443508 scopus 로고    scopus 로고
    • Cytotoxicity of human RNase-based immunotoxins requires cytosolic access and resistance to ribonuclease inhibition
    • Erickson HA, Jund MD, Pennell CA. 2006. Cytotoxicity of human RNase-based immunotoxins requires cytosolic access and resistance to ribonuclease inhibition. Protein Eng Des Sel 19:37-45.
    • (2006) Protein Eng Des Sel , vol.19 , pp. 37-45
    • Erickson, H.A.1    Jund, M.D.2    Pennell, C.A.3
  • 41
    • 43549115973 scopus 로고    scopus 로고
    • Human antibody RNase fusion protein targeting CD30+ lymphomas
    • Menzel C, Schirrmann T, Konthur Z, Jostock T, Dubel S. 2008. Human antibody RNase fusion protein targeting CD30+ lymphomas. Blood 111: 3830-3837.
    • (2008) Blood , vol.111 , pp. 3830-3837
    • Menzel, C.1    Schirrmann, T.2    Konthur, Z.3    Jostock, T.4    Dubel, S.5
  • 42
    • 33748536073 scopus 로고    scopus 로고
    • Natural and engineered ribonucleases as potential cancer therapeutics
    • Arnold U, Ulbrich-Hofmann R. 2006. Natural and engineered ribonucleases as potential cancer therapeutics. Biotechnol Lett 28:1615-1622.
    • (2006) Biotechnol Lett , vol.28 , pp. 1615-1622
    • Arnold, U.1    Ulbrich-Hofmann, R.2
  • 43
    • 0037177808 scopus 로고    scopus 로고
    • Entry into cells and selec!tive degradation of tRNAs by a cytotoxic member of the RNase A family
    • Saxena SK, Sirdeshmukh R, Ardelt W, Mikulski SM, Shogen K et al. 2003. Entry into cells and selec!tive degradation of tRNAs by a cytotoxic member of the RNase A family. J. Biol Chem 277:15142-15146.
    • (2003) J. Biol Chem , vol.277 , pp. 15142-15146
    • Saxena, S.K.1    Sirdeshmukh, R.2    Ardelt, W.3    Mikulski, S.M.4    Shogen, K.5
  • 44
    • 0037407561 scopus 로고    scopus 로고
    • Onconase and its therapeutic potential
    • Saxena SK, Shogen K, Ardelt W. 2003. Onconase and its therapeutic potential. Lab Med 34:380-387.
    • (2003) Lab Med , vol.34 , pp. 380-387
    • Saxena, S.K.1    Shogen, K.2    Ardelt, W.3
  • 45
    • 0034072727 scopus 로고    scopus 로고
    • Molecular determinants of apoptosis induced by the cytotoxic ribonuclease onconase: Evidence for cytotoxic mechanisms different from inhibition of protein synthesis
    • Iordanov MS, Ryabinina OP, Wong J, Newton DL, Rybak SM et al. 2000. Molecular determinants of apoptosis induced by the cytotoxic ribonuclease onconase: Evidence for cytotoxic mechanisms different from inhibition of protein synthesis. Cancer Res 60:1983-1994.
    • (2000) Cancer Res , vol.60 , pp. 1983-1994
    • Iordanov, M.S.1    Ryabinina, O.P.2    Wong, J.3    Newton, D.L.4    Rybak, S.M.5
  • 46
    • 0041696477 scopus 로고    scopus 로고
    • Cytotoxic ribonucleases and RNA interference (RNAi)
    • Ardelt B, Ardelt W, Darzynkiewicz Z. 2003. Cytotoxic ribonucleases and RNA interference (RNAi). Cell Cycle 2:22-24.
    • (2003) Cell Cycle , vol.2 , pp. 22-24
    • Ardelt, B.1    Ardelt, W.2    Darzynkiewicz, Z.3
  • 48
    • 0041823566 scopus 로고    scopus 로고
    • Degradation of double-stranded RNA by human pancreatic ribonuclease: Crucial role of noncatalytic basic amino acid residues
    • Sorrentino S, Naddeo M, Russo A, D'Alessio G. 2003. Degradation of double-stranded RNA by human pancreatic ribonuclease: Crucial role of noncatalytic basic amino acid residues. Biochemistry 42:10182-19190.
    • (2003) Biochemistry , vol.42 , pp. 10182-19190
    • Sorrentino, S.1    Naddeo, M.2    Russo, A.3    D'Alessio, G.4
  • 49
    • 1542581581 scopus 로고    scopus 로고
    • Noncatalytic assembly of ribonuclease III with double-stranded RNA
    • Blaszczyk J, Gan J, Tropea JE, Court DL, Waugh DS et al. 2004. Noncatalytic assembly of ribonuclease III with double-stranded RNA. Structure 12:457-466.
    • (2004) Structure , vol.12 , pp. 457-466
    • Blaszczyk, J.1    Gan, J.2    Tropea, J.E.3    Court, D.L.4    Waugh, D.S.5
  • 50
    • 0028931427 scopus 로고
    • Recombinant human eosinophil cationic protein. Ribonuclease activity is not essential for cytotoxicity
    • Rosenberg HF. 1995. Recombinant human eosinophil cationic protein. Ribonuclease activity is not essential for cytotoxicity. J. Biol Chem 270: 7876-7881.
    • (1995) J. Biol Chem , vol.270 , pp. 7876-7881
    • Rosenberg, H.F.1
  • 52
    • 0037086474 scopus 로고    scopus 로고
    • Essential stations in the intracellular pathway of cytotoxic bovine seminal ribonuclease
    • Bracale A, Spalletti-Cernia D, Mastronicola M, Castaldi F, Mannucci R et al. 2002. Essential stations in the intracellular pathway of cytotoxic bovine seminal ribonuclease. Biochem J 362:553-560.
    • (2002) Biochem J , vol.362 , pp. 553-560
    • Bracale, A.1    Spalletti-Cernia, D.2    Mastronicola, M.3    Castaldi, F.4    Mannucci, R.5
  • 53
    • 0030933277 scopus 로고    scopus 로고
    • Oncoprotein networks review
    • Hunter T. 1997 Oncoprotein networks review. Cell 88:333-346.
    • (1997) Cell , vol.88 , pp. 333-346
    • Hunter, T.1
  • 54
    • 35948990925 scopus 로고    scopus 로고
    • c-KIT is frequently mutated in bilateral germ cell tumors and down-regulated during progression from intratubular germ cell neoplasia to seminoma
    • Biermann K, Göke F, Nettersheim D, Eckert D, Zhou H et al. 2007. c-KIT is frequently mutated in bilateral germ cell tumors and down-regulated during progression from intratubular germ cell neoplasia to seminoma. J. Pathol 213:311-318.
    • (2007) J. Pathol , vol.213 , pp. 311-318
    • Biermann, K.1    Göke, F.2    Nettersheim, D.3    Eckert, D.4    Zhou, H.5
  • 57
    • 33750560668 scopus 로고    scopus 로고
    • Ion channels and cell volume in regulation of cell proliferation and apoptotic cell death
    • Lang F, Shumilina E, Ritter M, Gulbins E, Vereninov A et al. 2006. Ion channels and cell volume in regulation of cell proliferation and apoptotic cell death. Contrib Nephrol 152:142-160.
    • (2006) Contrib Nephrol , vol.152 , pp. 142-160
    • Lang, F.1    Shumilina, E.2    Ritter, M.3    Gulbins, E.4    Vereninov, A.5
  • 58
    • 48949105847 scopus 로고    scopus 로고
    • 2+ current. Biochim Biophys Acta 1269:57-63.
    • 2+ current. Biochim Biophys Acta 1269:57-63.
  • 59
    • 34249064186 scopus 로고    scopus 로고
    • Cell-cycle-dependent regulation of Ca2+-activated K+ channel in Jurkat T-lymphocyte
    • Morimoto T, Ohya S, Hayashi H, Onozaki K, Imaizumi Y. 2007. Cell-cycle-dependent regulation of Ca2+-activated K+ channel in Jurkat T-lymphocyte. J. Pharmacol Sci 104:94-98.
    • (2007) J. Pharmacol Sci , vol.104 , pp. 94-98
    • Morimoto, T.1    Ohya, S.2    Hayashi, H.3    Onozaki, K.4    Imaizumi, Y.5
  • 60
    • 0842329860 scopus 로고    scopus 로고
    • Highly selective toxic and proapoptotic effects of two dimeric ribonucleases on thyroid cancer cells compared to the effects of doxorubicin
    • Spalletti-Cernia D, Sorrentino R, Di Gaetano S, Piccoli R, Santoro V et al. 2004. Highly selective toxic and proapoptotic effects of two dimeric ribonucleases on thyroid cancer cells compared to the effects of doxorubicin. Brit J Cancer Res 90:270-277.
    • (2004) Brit J Cancer Res , vol.90 , pp. 270-277
    • Spalletti-Cernia, D.1    Sorrentino, R.2    Di Gaetano, S.3    Piccoli, R.4    Santoro, V.5
  • 61
    • 33847616665 scopus 로고    scopus 로고
    • Antitumor efficacy of the cytotoxic RNase, ranpirnase, on A549 human lung cancer xenografts of nude mice
    • Lee I, Kalota A, Gewirtz AM, Shogen K. 2007. Antitumor efficacy of the cytotoxic RNase, ranpirnase, on A549 human lung cancer xenografts of nude mice. Anticancer Res 27:299-307.
    • (2007) Anticancer Res , vol.27 , pp. 299-307
    • Lee, I.1    Kalota, A.2    Gewirtz, A.M.3    Shogen, K.4
  • 62
    • 33845338765 scopus 로고    scopus 로고
    • Cellular senescence and cancer treatment
    • Schmitt CA. 2007. Cellular senescence and cancer treatment. Biochim Biophys Acta 1775:5-20.
    • (2007) Biochim Biophys Acta , vol.1775 , pp. 5-20
    • Schmitt, C.A.1
  • 63
    • 33750521563 scopus 로고    scopus 로고
    • The discovery of mRNA interferases: Implication in bacterial physiology and application to biotechnology
    • Inouye M. 2006. The discovery of mRNA interferases: implication in bacterial physiology and application to biotechnology. Cell Physiol 209: 670-676.
    • (2006) Cell Physiol , vol.209 , pp. 670-676
    • Inouye, M.1
  • 65
    • 34248348654 scopus 로고    scopus 로고
    • Role of 2-5A-dependent RNase-L in senescence and longevity
    • Andersen JB, Li XL, Judge CS, Zhou A, Jha BK et al. 2007. Role of 2-5A-dependent RNase-L in senescence and longevity. Oncogene 26: 3081-3088.
    • (2007) Oncogene , vol.26 , pp. 3081-3088
    • Andersen, J.B.1    Li, X.L.2    Judge, C.S.3    Zhou, A.4    Jha, B.K.5
  • 66
    • 34347338785 scopus 로고    scopus 로고
    • Diverse functions of RNase L and implications in pathology
    • Bisbal C, Silverman RH. 2007. Diverse functions of RNase L and implications in pathology. Biochimie 89:789-798.
    • (2007) Biochimie , vol.89 , pp. 789-798
    • Bisbal, C.1    Silverman, R.H.2
  • 67
    • 0242499270 scopus 로고    scopus 로고
    • Enhancement of activation-induced apoptosis of lymphocytes by the cytotoxic ribonuclease (ranpirnase)
    • Halicka DH, Pozarowski P, Ita M, Ardelt WJ, Mikulski SM et al. 2002. Enhancement of activation-induced apoptosis of lymphocytes by the cytotoxic ribonuclease (ranpirnase). Int J Oncol 21:1245-1250.
    • (2002) Int J Oncol , vol.21 , pp. 1245-1250
    • Halicka, D.H.1    Pozarowski, P.2    Ita, M.3    Ardelt, W.J.4    Mikulski, S.M.5
  • 69
    • 0027256672 scopus 로고
    • A cytotoxic ribonuclease. Study of the mechanism of onconase cytotoxicity
    • Wu Y, Mikulski SM, Ardelt W, Rybak SM, Youle RJ. 1993. A cytotoxic ribonuclease. Study of the mechanism of onconase cytotoxicity. J. Biol Chem 268:10686-10693.
    • (1993) J. Biol Chem , vol.268 , pp. 10686-10693
    • Wu, Y.1    Mikulski, S.M.2    Ardelt, W.3    Rybak, S.M.4    Youle, R.J.5
  • 70
    • 33749011163 scopus 로고    scopus 로고
    • The NC160 human tumour cell line anticancer drug screen
    • Shoemaker RH. 2006. The NC160 human tumour cell line anticancer drug screen. Nat Rev Cancer 6:813-823.
    • (2006) Nat Rev Cancer , vol.6 , pp. 813-823
    • Shoemaker, R.H.1
  • 71
    • 0033118475 scopus 로고    scopus 로고
    • Apoptosis, p53, and tumor cell Sensitivity to anticancer agents
    • Brown JM, Wouters, BG. 1999. Apoptosis, p53, and tumor cell Sensitivity to anticancer agents. Cancer Res 59:1391-1399.
    • (1999) Cancer Res , vol.59 , pp. 1391-1399
    • Brown, J.M.1    Wouters, B.G.2
  • 72
    • 0037324378 scopus 로고    scopus 로고
    • Ribonuclease inhibitor as an intracellular sentry
    • Haigis MC, Kurten EL, Raines RT. 2003. Ribonuclease inhibitor as an intracellular sentry. Nucleic Acids Res 31:1024-1032.
    • (2003) Nucleic Acids Res , vol.31 , pp. 1024-1032
    • Haigis, M.C.1    Kurten, E.L.2    Raines, R.T.3
  • 73
    • 0035018435 scopus 로고    scopus 로고
    • Cancer chemotherapy: Ribonucleases to the rescue
    • Leland P., Raines R. 2001. Cancer chemotherapy: Ribonucleases to the rescue. Chem. Biol 8:405-413.
    • (2001) Chem. Biol , vol.8 , pp. 405-413
    • Leland, P.1    Raines, R.2
  • 74
    • 0035863726 scopus 로고    scopus 로고
    • Potent and specific antitumor effects of an anti-CD22-targeted cytotoxic ribonuclease: Potential for the treatment of non-Hodgkin lymphoma
    • Newton DL, Hansen HJ, Mikulski SM, Goldenberg DM, Rybak SM. 2001. Potent and specific antitumor effects of an anti-CD22-targeted cytotoxic ribonuclease: potential for the treatment of non-Hodgkin lymphoma. Blood 97:528-535.
    • (2001) Blood , vol.97 , pp. 528-535
    • Newton, D.L.1    Hansen, H.J.2    Mikulski, S.M.3    Goldenberg, D.M.4    Rybak, S.M.5
  • 75
    • 34249093093 scopus 로고    scopus 로고
    • Intracellular pathway of onconase that enables its delivery to the cytosol
    • Rodríguez M, Torrent G, Bosch M, Rayne F, Dubremetz JF et al. 2007. Intracellular pathway of onconase that enables its delivery to the cytosol. J. Cell Sci 120:1405-1411.
    • (2007) J. Cell Sci , vol.120 , pp. 1405-1411
    • Rodríguez, M.1    Torrent, G.2    Bosch, M.3    Rayne, F.4    Dubremetz, J.F.5
  • 76
    • 1342281681 scopus 로고    scopus 로고
    • Glycosylation of onconase increases its conformational stability and toxicity for cancer cells
    • Kim BM, Kim H, Raines RT, Lee Y. 2004. Glycosylation of onconase increases its conformational stability and toxicity for cancer cells. Biochem Biophys Res Commun 315:976-983.
    • (2004) Biochem Biophys Res Commun , vol.315 , pp. 976-983
    • Kim, B.M.1    Kim, H.2    Raines, R.T.3    Lee, Y.4
  • 77
    • 0035900671 scopus 로고    scopus 로고
    • Endowing human pancreatic ribonuclease with toxicity for cancer cells
    • Leland PA, Staniszewski KE, Kim SM, Raines RT. 2001. Endowing human pancreatic ribonuclease with toxicity for cancer cells. J. Biol Chem 276:43095-43102.
    • (2001) J. Biol Chem , vol.276 , pp. 43095-43102
    • Leland, P.A.1    Staniszewski, K.E.2    Kim, S.M.3    Raines, R.T.4
  • 78
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis PJ. 1991. MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl Crystallogr 24:7768-7773.
    • (1991) J. Appl Crystallogr , vol.24 , pp. 7768-7773
    • Kraulis, P.J.1


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