메뉴 건너뛰기




Volumn 39, Issue 1, 2005, Pages 1-10

Why ribonucleases induce tumor cell death

Author keywords

Antitumor activity; Catalytic activity; Charge; Cytotoxicity; KCa channels; Ras; Ribonucleases; RNA interference; Stability; Structure

Indexed keywords

ANTINEOPLASTIC AGENT; ANTINEOPLASTIC ANTIBIOTIC; CYANAMIDE; CYTOTOXIC AGENT; DIGITONIN; DOUBLE STRANDED RNA; DOXORUBICIN; ETHYLENEDIAMINE; GLYCINE METHYL ESTER; HYALURONIDASE; HYBRID PROTEIN; INTERLEUKIN 2; IODINE 125; LECTIN; MACROGOL; MESSENGER RNA; MICRORNA; PANCREATIC RIBONUCLEASE; PROTEIN INHIBITOR; RANPIRNASE; RAS PROTEIN; RECEPTOR PROTEIN; RIBONUCLEASE; RIBONUCLEASE A; RIBONUCLEASE III; SIALIC ACID; TAURINE;

EID: 21744445959     PISSN: 00268933     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11008-005-0001-4     Document Type: Review
Times cited : (14)

References (76)
  • 1
    • 0035193362 scopus 로고    scopus 로고
    • Exoribonucleases and their multiple roles in RNA metabolism
    • Deutscher M.P., Li Z. 2001. Exoribonucleases and their multiple roles in RNA metabolism. Prog. Nucleic Acid Res. Mol. Biol. 66, 67-105.
    • (2001) Prog. Nucleic Acid Res. Mol. Biol. , vol.66 , pp. 67-105
    • Deutscher, M.P.1    Li, Z.2
  • 2
    • 0037195896 scopus 로고    scopus 로고
    • RNase 7, a novel innate immune defense antimicrobial protein of healthy human skin
    • Harder J., Schroder J.M. 2002. RNase 7, a novel innate immune defense antimicrobial protein of healthy human skin. J. Biol. Chem. 277, 46784-16799.
    • (2002) J. Biol. Chem. , vol.277 , pp. 46784-116799
    • Harder, J.1    Schroder, J.M.2
  • 3
    • 0035212431 scopus 로고    scopus 로고
    • Eosinophils, eosinophil ribonucleases, and their role in host defense against respiratory virus pathogens
    • Rosenberg H.F., Domachowske J.B. 2001. Eosinophils, eosinophil ribonucleases, and their role in host defense against respiratory virus pathogens. J. Leukoc. Biol. 70, 691-698.
    • (2001) J. Leukoc. Biol. , vol.70 , pp. 691-698
    • Rosenberg, H.F.1    Domachowske, J.B.2
  • 4
    • 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
  • 7
    • 0036594060 scopus 로고    scopus 로고
    • Effect of replacing the aspartic acid/glutamic acid residues of bullfrog sialic acid binding lectin with asparagine/glutamine and arginine on the inhibition of cell proliferation in murine leukemia P388 cells
    • Ogawa Y., Iwama M., Ohgi K., Tsuji T., Irie M., Itagaki T., Kobajashi H., Inokushi N. 2002. Effect of replacing the aspartic acid/glutamic acid residues of bullfrog sialic acid binding lectin with asparagine/glutamine and arginine on the inhibition of cell proliferation in murine leukemia P388 cells. Biol. Pharm. Bull. 25, 722-727.
    • (2002) Biol. Pharm. Bull. , vol.25 , pp. 722-727
    • Ogawa, Y.1    Iwama, M.2    Ohgi, K.3    Tsuji, T.4    Irie, M.5    Itagaki, T.6    Kobajashi, H.7    Inokushi, N.8
  • 8
    • 0035957231 scopus 로고    scopus 로고
    • Antitumor action of seminal ribonuclease, its dimeric structure, and its resistance to the ribonuclease inhibitor
    • Antignani A., Naddo M., Cubellis M.V., Russo A., D'Alessio G. 2001. Antitumor action of seminal ribonuclease, its dimeric structure, and its resistance to the ribonuclease inhibitor. Biochemistry. 40, 3492-3496.
    • (2001) Biochemistry , vol.40 , pp. 3492-3496
    • Antignani, A.1    Naddo, M.2    Cubellis, M.V.3    Russo, A.4    D'Alessio, G.5
  • 9
    • 0035219058 scopus 로고    scopus 로고
    • RNA damage and inhibition of neoplastic endothelial cells growth: Effects of human and amphibian ribonucleases
    • Newton D.L., Kaur G., Rhim J.S., Sausville E.A., Rybak S.M. 2001. RNA damage and inhibition of neoplastic endothelial cells growth: Effects of human and amphibian ribonucleases. Radiat. Res. 155, 171-174.
    • (2001) Radiat. Res. , vol.155 , pp. 171-174
    • Newton, D.L.1    Kaur, G.2    Rhim, J.S.3    Sausville, E.A.4    Rybak, S.M.5
  • 12
    • 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
  • 13
    • 0037033001 scopus 로고    scopus 로고
    • X-Ray structure of two crystalline forms of a streptomycete ribonuclease with cytotoxic activity
    • Sevcik J., Urbanikova L., Leland P.A., Raines R.T. 2002. X-Ray structure of two crystalline forms of a streptomycete ribonuclease with cytotoxic activity. J. Biol. Chem. 277, 47325-17330.
    • (2002) J. Biol. Chem. , vol.277 , pp. 47325-117330
    • Sevcik, J.1    Urbanikova, L.2    Leland, P.A.3    Raines, R.T.4
  • 15
    • 0024585923 scopus 로고
    • Ribonuclease inhibitor from pig brain: Purification, characterization, and direct spectrophotometric assay
    • Cho S., Joshi J.G. 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
  • 16
    • 0037259429 scopus 로고    scopus 로고
    • RNA cleavage and inhibition of protein synthesis by bleomycin
    • Abraham A.T., Lin J., Newton D.L., 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
  • 17
    • 0036786231 scopus 로고    scopus 로고
    • Structural and energetic analysis of metal ions essential to SRP signal recognition domain assembly
    • Batey R.T., Doudna J.A. 2002. Structural and energetic analysis of metal ions essential to SRP signal recognition domain assembly. Biochemistry. 41, 11703-11710.
    • (2002) Biochemistry , vol.41 , pp. 11703-11710
    • Batey, R.T.1    Doudna, J.A.2
  • 18
    • 0345818258 scopus 로고    scopus 로고
    • MicroRNAs and cancer
    • McManus M.T. 2003. MicroRNAs and cancer. Semin. Cancer Biol. 13, 253-258.
    • (2003) Semin. Cancer Biol. , vol.13 , pp. 253-258
    • McManus, M.T.1
  • 19
    • 0037146606 scopus 로고    scopus 로고
    • Small RNAs make big splash
    • Couzin J. 2002. Small RNAs make big splash. Science. 298, 2296-2297.
    • (2002) Science , vol.298 , pp. 2296-2297
    • Couzin, J.1
  • 20
    • 0037407561 scopus 로고    scopus 로고
    • Onconase and its therapeutic potential
    • Saxena S.K., 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
  • 21
    • 0037177808 scopus 로고    scopus 로고
    • Entry into cells and selective degradation of tRNAs by a cytotoxic member of the RNase A family
    • Saxena S.K., Sirdeshmukh R., Ardelt W., Mikulski S.M., Shogen K., Youle R.J. 2003. Entry into cells and selective degradation of tRNAs by a cytotoxic member of the RNase A family. J. Biol. Chem. 277, 15 142-15146.
    • (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    Youle, R.J.6
  • 22
    • 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, A10-F12.
    • (2003) Cell Cycle , vol.2
    • Ardelt, B.1    Ardelt, W.2    Darzynkiewicz, Z.3
  • 23
    • 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
  • 24
    • 1542581581 scopus 로고    scopus 로고
    • Noncatalytic assembly of ribonuclease III with double-stranded RNA
    • Cambridge
    • Blaszczyk J., Gan J., Tropea J.E., Court D.L., Waugh D.S., Ji X. 2004. Noncatalytic assembly of ribonuclease III with double-stranded RNA. Structure (Cambridge). 12, 457-166.
    • (2004) Structure , vol.12 , pp. 457-1166
    • Blaszczyk, J.1    Gan, J.2    Tropea, J.E.3    Court, D.L.4    Waugh, D.S.5    Ji, X.6
  • 25
    • 0036829110 scopus 로고    scopus 로고
    • Increased exposure of anionic phospholipids on the surface of tumor blood vessels
    • Ran S., Downes A., Thorpe P.E. 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
  • 26
    • 0036891466 scopus 로고    scopus 로고
    • Phosphatidylserine is a marker of tumor vasculature and potential target for cancer imaging and therapy
    • Ran S., Thorpe RE. 2002. Phosphatidylserine is a marker of tumor vasculature and potential target for cancer imaging and therapy. Int. J. Radiat. Oncol. Biol. Phys. 54, 1479-1484.
    • (2002) Int. J. Radiat. Oncol. Biol. Phys. , vol.54 , pp. 1479-1484
    • Ran, S.1    Thorpe, R.E.2
  • 27
    • 0037439769 scopus 로고    scopus 로고
    • Secretory ribonucleases are internalized by a dynamin-independent endocytic pathway
    • Haigis M.C., Raines R.T. 2002. Secretory ribonucleases are internalized by a dynamin-independent endocytic pathway. J. Cell Sci. 116, 313-324.
    • (2002) J. Cell Sci. , vol.116 , pp. 313-324
    • Haigis, M.C.1    Raines, R.T.2
  • 29
    • 0037155852 scopus 로고    scopus 로고
    • Antiplasmin activity of a peptide that binds to the receptor-binding site of angiogenin
    • Gho Y.S., Yoon W.H., Chae C.B. 2002. Antiplasmin activity of a peptide that binds to the receptor-binding site of angiogenin. J. Biol. Chem. 277, 9690-9694.
    • (2002) J. Biol. Chem. , vol.277 , pp. 9690-9694
    • Gho, Y.S.1    Yoon, W.H.2    Chae, C.B.3
  • 30
    • 0036381074 scopus 로고    scopus 로고
    • Ion channel formation and membrane-linked pathologies of misfolded hydrophobic proteins: The role of dangerous unchaperoned molecules
    • Kourie J.I., Henry C.L. 2002. Ion channel formation and membrane-linked pathologies of misfolded hydrophobic proteins: The role of dangerous unchaperoned molecules. Clin. Exp. Pharmacol. Physiol. 29, 741-753.
    • (2002) Clin. Exp. Pharmacol. Physiol. , vol.29 , pp. 741-753
    • Kourie, J.I.1    Henry, C.L.2
  • 31
    • 0029716036 scopus 로고    scopus 로고
    • An immunochemical study of Bacillus intermedius ribonuclease entry into Candida tropicalis cells and effects of the enzyme on yeast growth
    • Egorov S.Yu., Dmitriev I.I., Naumova E.S., Kupriyanova-Ashina F.G. 1996. An immunochemical study of Bacillus intermedius ribonuclease entry into Candida tropicalis cells and effects of the enzyme on yeast growth. Tsitologiya. 38, 66-69.
    • (1996) Tsitologiya , vol.38 , pp. 66-69
    • Egorov, S.Yu.1    Dmitriev, I.I.2    Naumova, E.S.3    Kupriyanova-Ashina, F.G.4
  • 32
    • 0030018987 scopus 로고    scopus 로고
    • Studies on the activity of barnase toxins in vitro and in vivo
    • Prior T.I., Kunwar S., Pastan I. 1996. Studies on the activity of barnase toxins in vitro and in vivo. Bioconjug. Chem. 7, 23-29.
    • (1996) Bioconjug. Chem. , vol.7 , pp. 23-29
    • Prior, T.I.1    Kunwar, S.2    Pastan, I.3
  • 33
    • 0036902921 scopus 로고    scopus 로고
    • Biological role of alpha-fetoprotein in cancer: Prospects for anticancer therapy
    • Mizejewski G.T. 2002. Biological role of alpha-fetoprotein in cancer: Prospects for anticancer therapy. Expert Rev. Anticancer Ther. 2, 709-735.
    • (2002) Expert Rev. Anticancer Ther. , vol.2 , pp. 709-735
    • Mizejewski, G.T.1
  • 34
    • 0036237495 scopus 로고    scopus 로고
    • Specifically targeting the CD22 receptor of human B-cell lymphomas with RNA damaging agents: A new generation of therapeutics
    • Hursey M., Newton D.L., Hansen H.J., Ruby D., Goldenberg D.M., Rybak S.M. 2002. Specifically targeting the CD22 receptor of human B-cell lymphomas with RNA damaging agents: A new generation of therapeutics. Leuk. Lymphoma. 43, 953-959.
    • (2002) Leuk. Lymphoma , vol.43 , pp. 953-959
    • Hursey, M.1    Newton, D.L.2    Hansen, H.J.3    Ruby, D.4    Goldenberg, D.M.5    Rybak, S.M.6
  • 35
    • 0035893923 scopus 로고    scopus 로고
    • Human angiogenin fused to human CD30 ligand (Ang-CD30L) exhibits specific cytotoxicity against CD30-positive lymphoma
    • Huhn M., Sasse S., Tur M.K., Matthey B., Scinkothe T., Rybak S.M., Barth S., Engert A. 2001. Human angiogenin fused to human CD30 ligand (Ang-CD30L) exhibits specific cytotoxicity against CD30-positive lymphoma. Cancer Res. 61, 8737-8742.
    • (2001) Cancer Res. , vol.61 , pp. 8737-8742
    • Huhn, M.1    Sasse, S.2    Tur, M.K.3    Matthey, B.4    Scinkothe, T.5    Rybak, S.M.6    Barth, S.7    Engert, A.8
  • 36
    • 0037051903 scopus 로고    scopus 로고
    • A new RNase-based immunoconjugate selectively cytotoxic for ErbB2-overexpressing cells
    • Di Lorenzo C., Nigro A., Piccoli R., D'Alessio G. 2002. A new RNase-based immunoconjugate selectively cytotoxic for ErbB2-overexpressing cells. FEBS Lett. 516, 208-212.
    • (2002) FEBS Lett. , vol.516 , pp. 208-212
    • Di Lorenzo, C.1    Nigro, A.2    Piccoli, R.3    D'Alessio, G.4
  • 37
    • 0033939774 scopus 로고    scopus 로고
    • Targeting activated lymphocytes with an antirelay human immunotoxin analogue: Human pancreatic RNase1-human IL-2 fusion
    • Psarras K., Ueda M., Tanabe M., Kitajima M., Aiso S., Komatsu S., Seno M. 2000. Targeting activated lymphocytes with an antirelay human immunotoxin analogue: Human pancreatic RNase1-human IL-2 fusion. Cytokine. 12, 786-790.
    • (2000) Cytokine , vol.12 , pp. 786-790
    • Psarras, K.1    Ueda, M.2    Tanabe, M.3    Kitajima, M.4    Aiso, S.5    Komatsu, S.6    Seno, M.7
  • 39
    • 0033602045 scopus 로고    scopus 로고
    • Cell cycle-related differences in susceptibility of NIH/3T3 cells to ribonucleases
    • Smith M.R., Newton D.L., Mikulski S.M., Rybak S.M. 1999. Cell cycle-related differences in susceptibility of NIH/3T3 cells to ribonucleases. Exp. Cell. Res. 247, 220-232.
    • (1999) Exp. Cell. Res. , vol.247 , pp. 220-232
    • Smith, M.R.1    Newton, D.L.2    Mikulski, S.M.3    Rybak, S.M.4
  • 41
  • 43
    • 0034683225 scopus 로고    scopus 로고
    • Potassium channel openers prevent beta-amyloid toxicity in bovine vascular endothelial cells
    • Chi X., Sutton E.T., Hellermenn G., Price J.M. 2000. Potassium channel openers prevent beta-amyloid toxicity in bovine vascular endothelial cells. Neurosci. Lett. 290, 9-12.
    • (2000) Neurosci. Lett. , vol.290 , pp. 9-12
    • Chi, X.1    Sutton, E.T.2    Hellermenn, G.3    Price, J.M.4
  • 45
    • 0141746349 scopus 로고    scopus 로고
    • The role of protein stability, solubility, and net charge in amyloid fibril formation
    • Schmittschmitt J.P., Scholtz M. 2003. The role of protein stability, solubility, and net charge in amyloid fibril formation. Protein Sci. 12, 2374-2378.
    • (2003) Protein Sci. , vol.12 , pp. 2374-2378
    • Schmittschmitt, J.P.1    Scholtz, M.2
  • 46
    • 0031593435 scopus 로고    scopus 로고
    • + current in mouse fibroblasts by lysophosphatidic acid requires a pertussis toxin-sensitive G protein and Ras
    • + current in mouse fibroblasts by lysophosphatidic acid requires a pertussis toxin-sensitive G protein and Ras. Naunyn-Schmiedeberg's Arch. Pharmacol. 358, 509-517.
    • (1998) Naunyn-Schmiedeberg's Arch. Pharmacol. , vol.358 , pp. 509-517
    • Repp, H.1    Koshinski, A.2    Decker, K.3    Dreyer, F.4
  • 48
    • 21744455815 scopus 로고    scopus 로고
    • Cell targets for the antitumor action of microbial endonucleases
    • Ilinskaya O.N., Kolpakov A.I. Cell targets for the antitumor action of microbial endonucleases. Naukoemk. Tekhnol. 4, 61-67.
    • Naukoemk. Tekhnol. , vol.4 , pp. 61-67
    • Ilinskaya, O.N.1    Kolpakov, A.I.2
  • 51
    • 0029071573 scopus 로고
    • Bacterial ribonuclease: Mutagenic effect in microbial test-systems
    • Ilinskaya O.N., Ivanchenko O.B., Karamova N.S. 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
  • 52
    • 0030914745 scopus 로고    scopus 로고
    • Nephrotoxic effects of bacterial ribonucleases in the isolated perfused rat kidney
    • Ilinskaya O.N., Vamvakas S. 1997. Nephrotoxic effects of bacterial ribonucleases in the isolated perfused rat kidney. Toxicology. 120, 55-63.
    • (1997) Toxicology , vol.120 , pp. 55-63
    • Ilinskaya, O.N.1    Vamvakas, S.2
  • 53
    • 21744439715 scopus 로고    scopus 로고
    • Genotoxic effects of ribonuclease in vivo
    • Ilinskaya O.N., Frai H. 2000. Genotoxic effects of ribonuclease in vivo. Biopolim. Kletka. 4, 270-274.
    • (2000) Biopolim. Kletka. , vol.4 , pp. 270-274
    • Ilinskaya, O.N.1    Frai, H.2
  • 54
    • 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 M.S., Ryabinina O.P., Wong J., Newton D.L., Rybak S.M., Magun B.E. 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    Magun, B.E.6
  • 55
    • 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., Seno M., Kosaka M., Yamada H. 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    Seno, M.6    Kosaka, M.7    Yamada, H.8
  • 56
    • 0028931427 scopus 로고
    • Recombinant human eosinophil cationic protein. Ribonuclease activity is not essential for cytotoxicity
    • Rosenberg H.F. 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
  • 58
    • 0034625439 scopus 로고    scopus 로고
    • Conformational stability is a determinant of ribonuclease A cytotoxicity
    • Klink T.A., Raines R.T. 2000. Conformational stability is a determinant of ribonuclease A cytotoxicity. J. Biol Chem. 275, 17463-17467.
    • (2000) J. Biol Chem. , vol.275 , pp. 17463-17467
    • Klink, T.A.1    Raines, R.T.2
  • 59
    • 0034698264 scopus 로고    scopus 로고
    • A synamorphic disulfide bond is critical for the conformational stability and cytotoxicity of an amphibian ribonuclease
    • Leland P.A., Staniszewski K.E., Kim B.M., Raines R. 2000. A synamorphic disulfide bond is critical for the conformational stability and cytotoxicity of an amphibian ribonuclease. FEBS Lett. 477, 203-207.
    • (2000) FEBS Lett. , vol.477 , pp. 203-207
    • Leland, P.A.1    Staniszewski, K.E.2    Kim, B.M.3    Raines, R.4
  • 60
    • 0035822616 scopus 로고    scopus 로고
    • Contribution of chain termini to the conformational stability and biological activity of onconase
    • Notomista E., Catanzano F., Graziano G., Di Gaetano S., Barone G., Di Donate A. 2001. Contribution of chain termini to the conformational stability and biological activity of onconase. Biochemistry. 40, 9097-9103.
    • (2001) Biochemistry , vol.40 , pp. 9097-9103
    • Notomista, E.1    Catanzano, F.2    Graziano, G.3    Di Gaetano, S.4    Barone, G.5    Di Donate, A.6
  • 61
    • 1642441835 scopus 로고    scopus 로고
    • Effect of hyaluronidase and PEG chain conjugation on the biologic and antitumor activity of RNase A
    • Matousek J., Pouckova P., Hlouskova D., Zadvinova M., Soucek J., Skvor J. 2004. Effect of hyaluronidase and PEG chain conjugation on the biologic and antitumor activity of RNase A. J. Contr. Release. 94, 401-410.
    • (2004) J. Contr. Release. , vol.94 , pp. 401-410
    • Matousek, J.1    Pouckova, P.2    Hlouskova, D.3    Zadvinova, M.4    Soucek, J.5    Skvor, J.6
  • 62
    • 1342281681 scopus 로고    scopus 로고
    • Glycosylation of onconase increases its conformational stability and toxicity for cancer cells
    • Kim B.M., Kim H., Raines R., 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.3    Lee, Y.4
  • 66
    • 0036684790 scopus 로고    scopus 로고
    • Optimum modification for the highest cytotoxicity of cationized ribonuclease
    • Tokyo
    • Futami J., Nukui E., Maeda T., Kosaka M., Tada H., Sano M., Yamada H. 2002. Optimum modification for the highest cytotoxicity of cationized ribonuclease. J. Biochem. (Tokyo). 132, 223-228.
    • (2002) J. Biochem. , vol.132 , pp. 223-228
    • Futami, J.1    Nukui, E.2    Maeda, T.3    Kosaka, M.4    Tada, H.5    Sano, M.6    Yamada, H.7
  • 67
    • 0037430969 scopus 로고    scopus 로고
    • Cytotoxic ribonucleases: Molecular weapons and their targets
    • Makarov A.A., Ilinskaya O.N. 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
  • 68
    • 1442300945 scopus 로고    scopus 로고
    • A nuclear localization sequence endows human pancreatic ribonuclease with cytotoxic activity
    • Bosch M., Benito A., Ribo M., Puig T., Beaumelle B., Vilanova M. 2004. A nuclear localization sequence endows human pancreatic ribonuclease with cytotoxic activity. Biochemistry. 43, 2167-2177.
    • (2004) Biochemistry , vol.43 , pp. 2167-2177
    • Bosch, M.1    Benito, A.2    Ribo, M.3    Puig, T.4    Beaumelle, B.5    Vilanova, M.6
  • 69
    • 0034827077 scopus 로고    scopus 로고
    • Effect of modification of the carboxyl groups of sialic acid binding lectin from bullfrog (Rana catesbiana) oocyte on anti-tumor activity
    • Iwama M., Ogawa Y., Sasaki N., Nitta K., Takajanagi Y., Ohgi K., Tsuji T., Irie M. 2001. Effect of modification of the carboxyl groups of sialic acid binding lectin from bullfrog (Rana catesbiana) oocyte on anti-tumor activity. Biol. Pharm. Bull. 24, 978-981.
    • (2001) Biol. Pharm. Bull. , vol.24 , pp. 978-981
    • Iwama, M.1    Ogawa, Y.2    Sasaki, N.3    Nitta, K.4    Takajanagi, Y.5    Ohgi, K.6    Tsuji, T.7    Irie, M.8
  • 70
    • 2642567595 scopus 로고    scopus 로고
    • A novel ribotoxin with ribonuclease activity that specifically cleaves a single phosphodiester bond in rat 28S ribosomal RNA and inactivates ribosome
    • Xu H., He W.J., Liu W.Y. 2004. A novel ribotoxin with ribonuclease activity that specifically cleaves a single phosphodiester bond in rat 28S ribosomal RNA and inactivates ribosome. Arch. Biochem. Biophys. 427, 30-40.
    • (2004) Arch. Biochem. Biophys. , vol.427 , pp. 30-40
    • Xu, H.1    He, W.J.2    Liu, W.Y.3
  • 71
    • 4043112821 scopus 로고    scopus 로고
    • Purification and characterization of Moschatin, a novel type I ribosome-inactivated protein from the mature seeds of pumpkin (Cucurbita moschata), and preparation of its immunotoxin against human melanoma cells
    • Xia H.C., Li F., Zhang Z.C. 2003. Purification and characterization of Moschatin, a novel type I ribosome-inactivated protein from the mature seeds of pumpkin (Cucurbita moschata), and preparation of its immunotoxin against human melanoma cells. Cell Res. 13, 369-374.
    • (2003) Cell Res. , vol.13 , pp. 369-374
    • Xia, H.C.1    Li, F.2    Zhang, Z.C.3
  • 72
    • 0036589213 scopus 로고    scopus 로고
    • The modes of action of colicins E5 and D, and related cytotoxic tRNases
    • Masaki H., Ogawa T. 2002. The modes of action of colicins E5 and D, and related cytotoxic tRNases. Biochimie. 84, 433-138.
    • (2002) Biochimie , vol.84 , pp. 433-1138
    • Masaki, H.1    Ogawa, T.2
  • 73
    • 0036402981 scopus 로고    scopus 로고
    • Glycine 38 is crucial for the ribonucleolytic activity of human pancreatic ribonuclease on double-stranded RNA
    • Gaur D., Seth D., Batra J.K. 2002. Glycine 38 is crucial for the ribonucleolytic activity of human pancreatic ribonuclease on double-stranded RNA. Biochem. Biophys. Res. Commun. 297, 390-395.
    • (2002) Biochem. Biophys. Res. Commun. , vol.297 , pp. 390-395
    • Gaur, D.1    Seth, D.2    Batra, J.K.3
  • 74
    • 0031596225 scopus 로고    scopus 로고
    • G1 arrest of U-937 cells by onconase is associated with suppression of cyclin D3 expression, induction of p16INK4A, p21WAF1/CIP1 and p27KIP and decreased pRb phosphorylation
    • Juan G., Ardelt B., Li X., Mikulski S.M., Shogen K., Ardelt W., Mittelman A., Darzynkiewicz Z. 1998. G1 arrest of U-937 cells by onconase is associated with suppression of cyclin D3 expression, induction of p16INK4A, p21WAF1/CIP1 and p27KIP and decreased pRb phosphorylation. Leukemia. 12, 1241-1248.
    • (1998) Leukemia , vol.12 , pp. 1241-1248
    • Juan, G.1    Ardelt, B.2    Li, X.3    Mikulski, S.M.4    Shogen, K.5    Ardelt, W.6    Mittelman, A.7    Darzynkiewicz, Z.8
  • 75
    • 2942670774 scopus 로고    scopus 로고
    • Oligonucleotides as a basis for gene-directed therapeutics
    • Vlasov V.V. 2004. Oligonucleotides as a basis for gene-directed therapeutics. Vestn. Ross. Akad. Nauk. 74, 419-423.
    • (2004) Vestn. Ross. Akad. Nauk. , vol.74 , pp. 419-423
    • Vlasov, V.V.1
  • 76
    • 1642603947 scopus 로고    scopus 로고
    • A small modulatory dsRNA specifies the fate of adult neural stem cells
    • Kuwabara T., Hsieh J., Nakashima K., Taira K., Gage F.H. 2004. A small modulatory dsRNA specifies the fate of adult neural stem cells. Cell. 116, 779-793.
    • (2004) Cell , vol.116 , pp. 779-793
    • Kuwabara, T.1    Hsieh, J.2    Nakashima, K.3    Taira, K.4    Gage, F.H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.