메뉴 건너뛰기




Volumn 48, Issue 23, 2009, Pages 5051-5053

Silencing an inhibitor unleashes a cytotoxic enzyme

Author keywords

[No Author keywords available]

Indexed keywords

BOVINE PANCREATIC RIBONUCLEASE; CYTOSOLIC PROTEINS; CYTOTOXIC; MOLECULAR EVOLUTION; POTENT INHIBITOR; RNA INTERFERENCE; RNASE A;

EID: 67049170817     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi900489y     Document Type: Article
Times cited : (4)

References (32)
  • 3
    • 0024496381 scopus 로고
    • Tight-binding inhibition of angiogenin and ribonuclease a by placental ribonuclease inhibitor
    • DOI 10.1021/bi00427a031
    • Lee, F. S., Shapiro, R., and Vallee, B. L. (1989) Tight-binding inhibition of angiogenin and ribonucleaseAby placental ribonuclease inhibitor. Biochemistry28, 225-230. (Pubitemid 19046737)
    • (1989) Biochemistry , vol.28 , Issue.1 , pp. 225-230
    • Lee, F.S.1    Shapiro, R.2    Vallee, B.L.3
  • 4
    • 0025006582 scopus 로고
    • Protein chemical and kinetic characterization of recombinant porcine ribonuclease inhibitor expressed in Saccharomyces cerevisiae
    • DOI 10.1021/bi00489a046
    • Vicentini, A. M., Kieffer, B., Matthies, R., Meyhack, B., Hemmings, B. A., Stone, S. R., and Hofsteenge, J. (1990) Protein chemical and kinetic characterization of recombinant porcine ribonuclease inhibitor expressed in Saccharomyces cerevisiae. Biochemistry29, 8827-8834. (Pubitemid 20302782)
    • (1990) Biochemistry , vol.29 , Issue.37 , pp. 8827-8834
    • Vicentini, A.M.1    Kieffer, B.2    Matthies, R.3    Meyhack, B.4    Hemmings, B.A.5    Stone, S.R.6    Hofsteenge, J.7
  • 5
    • 33947598165 scopus 로고    scopus 로고
    • Inhibition of human pancreatic ribonuclease by the human ribonuclease inhibitor protein
    • Johnson, R. J., McCoy, J. G., Bingman, C. A., Phillips, G. N.Jr., and Raines, R. T. (2007) Inhibition of human pancreatic ribonuclease by the human ribonuclease inhibitor protein. J. Mol. Biol.367, 434-449.
    • (2007) J. Mol. Biol. , vol.367 , pp. 434-449
    • Johnson, R.J.1    McCoy, J.G.2    Bingman, C.A.3    Phillips Jr., G.N.4    Raines, R.T.5
  • 6
    • 36048943980 scopus 로고    scopus 로고
    • Intraspecies regulation of ribonucleolytic activity
    • DOI 10.1021/bi701521q
    • Johnson, R. J., Lavis, L. D., and Raines, R. T. (2007) Intraspecies regulation of ribonucleolytic activity. Biochemistry46, 13131-13140. (Pubitemid 350086231)
    • (2007) Biochemistry , vol.46 , Issue.45 , pp. 13131-13140
    • Johnson, R.J.1    Lavis, L.D.2    Raines, R.T.3
  • 7
    • 54049094773 scopus 로고    scopus 로고
    • Cytotoxic ribonuclease onconase targets RNA interference (siRNA)
    • Zhao, H., Ardelt, B., Ardelt, W., Shogen, K., and Darzynkiewicz, Z. (2008) Cytotoxic ribonuclease onconase targets RNA interference (siRNA). Cell Cycle7, 3258-3261.
    • (2008) Cell Cycle , vol.7 , pp. 3258-3261
    • Zhao, H.1    Ardelt, B.2    Ardelt, W.3    Shogen, K.4    Darzynkiewicz, Z.5
  • 8
    • 0029006175 scopus 로고
    • Catalytic activity of bovine seminal ribonuclease is essential for its immunosuppressive and other biological activities
    • Kim, J.-S., Souček, J., Matoušek, J., and Raines, R. T. (1995) Catalytic activity of bovine seminal ribonuclease is essential for its immunosuppressive and other biological activities. Biochem. J.308, 547-550.
    • (1995) Biochem. J. , vol.308 , pp. 547-550
    • Kim, J.-S.1    Souček, J.2    Matoušek, J.3    Raines, R.T.4
  • 9
    • 0028911034 scopus 로고
    • A structural basis of the interactions between leucine-rich repeats and protein ligands
    • Kobe, B., and Deisenhofer, J. (1995) A structural basis of the interactions between leucine-rich repeats and protein ligands. Nature374, 183-186.
    • (1995) Nature , vol.374 , pp. 183-186
    • Kobe, B.1    Deisenhofer, J.2
  • 10
    • 0027256672 scopus 로고
    • A cytotoxic ribonuclease. Study of the mechanism of onconase cytotoxicity
    • Wu, Y., Mikulski, S. M., Ardelt, W., Rybak, S. M., and Youle, R. J. (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
  • 11
    • 55549133584 scopus 로고    scopus 로고
    • Interaction of onconase with the human ribonuclease inhibitor protein
    • Turcotte, R. F., and Raines, R. T. (2008) Interaction of onconase with the human ribonuclease inhibitor protein. Biochem. Biophys. Res. Commun.377, 512-514.
    • (2008) Biochem. Biophys. Res. Commun. , vol.377 , pp. 512-514
    • Turcotte, R.F.1    Raines, R.T.2
  • 12
    • 38549168927 scopus 로고    scopus 로고
    • Ribonucleases as novel chemotherapeutics: The ranpirnase example
    • Lee, J. E., and Raines, R. T. (2008) Ribonucleases as novel chemotherapeutics: The ranpirnase example. BioDrugs22, 53-58. (Pubitemid 351158535)
    • (2008) BioDrugs , vol.22 , Issue.1 , pp. 53-58
    • Lee, J.E.1    Raines, R.T.2
  • 13
    • 47749087053 scopus 로고    scopus 로고
    • Onconase and Amphinase, the antitumor ribonucleases from Rana pipiens oocytes
    • Ardelt, W., Shogen, K., and Darzynkiewicz, Z. (2008) Onconase and Amphinase, the antitumor ribonucleases from Rana pipiens oocytes. Curr. Pharm. Biotechnol.9, 215-225.
    • (2008) Curr. Pharm. Biotechnol. , vol.9 , pp. 215-225
    • Ardelt, W.1    Shogen, K.2    Darzynkiewicz, Z.3
  • 15
    • 27344441004 scopus 로고    scopus 로고
    • Disruption of shape-complementarity markers to create cytotoxic variants of ribonuclease A
    • Rutkoski, T. J., Kurten, E. L., Mitchell, J. C., and Raines, R. T. (2005) Disruption of shape-complementarity markers to create cytotoxic variants of ribonuclease A. J. Mol. Biol.354, 41-54.
    • (2005) J. Mol. Biol. , vol.354 , pp. 41-54
    • Rutkoski, T.J.1    Kurten, E.L.2    Mitchell, J.C.3    Raines, R.T.4
  • 16
    • 0035900671 scopus 로고    scopus 로고
    • Endowing human pancreatic ribonuclease with toxicity for cancer cells
    • Leland, P. A., Staniszewski, K. E., Kim, B.-M., and Raines, R. T. (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, B.-M.3    Raines, R.T.4
  • 17
    • 47749114193 scopus 로고    scopus 로고
    • Evasion of ribonuclease inhibitor as a determinant of ribonuclease cytotoxicity
    • Rutkoski, T. J., and Raines, R. T. (2008) Evasion of ribonuclease inhibitor as a determinant of ribonuclease cytotoxicity. Curr. Pharm. Biotechnol.9, 185-189.
    • (2008) Curr. Pharm. Biotechnol. , vol.9 , pp. 185-189
    • Rutkoski, T.J.1    Raines, R.T.2
  • 18
    • 0034615926 scopus 로고    scopus 로고
    • A ribonuclease A variant with low catalytic activity but high cytotoxicity
    • Bretscher, L. E., Abel, R. L., and Raines, R. T. (2000) A ribonuclease A variant with low catalytic activity but high cytotoxicity. J. Biol. Chem.275, 9893-9896.
    • (2000) J. Biol. Chem. , vol.275 , pp. 9893-9896
    • Bretscher, L.E.1    Abel, R.L.2    Raines, R.T.3
  • 19
    • 0038723718 scopus 로고    scopus 로고
    • Compensating effects on the cytotoxicity of ribonuclease A variants
    • Dickson, K. A., Dahlberg, C. L., and Raines, R. T. (2003) Compensating effects on the cytotoxicity of ribonuclease A variants. Arch. Biochem. Biophys.415, 172-177.
    • (2003) Arch. Biochem. Biophys. , vol.415 , pp. 172-177
    • Dickson, K.A.1    Dahlberg, C.L.2    Raines, R.T.3
  • 20
    • 4544330800 scopus 로고    scopus 로고
    • Cytosolic RNase inhibitor only affects RNases with intrinsic cytotoxicity
    • Monti, D. M., and D'Alessio, G. (2004) Cytosolic RNase inhibitor only affects RNases with intrinsic cytotoxicity. J. Biol. Chem.279, 39195-39198.
    • (2004) J. Biol. Chem. , vol.279 , pp. 39195-39198
    • Monti, D.M.1    D'Alessio, G.2
  • 21
    • 0035942736 scopus 로고    scopus 로고
    • Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells
    • DOI 10.1038/35078107
    • Elbashir, S. M., Harborth, J., Lendeckel, W., Yalcin, A., Weber, K., and Tuschl, T. (2001) Duplexes of 21-nucleotide RNAs mediate RNA interference in cultured mammalian cells. Nature411, 494-498. (Pubitemid 32494397)
    • (2001) Nature , vol.411 , Issue.6836 , pp. 494-498
    • Elbashir, S.M.1    Harborth, J.2    Lendeckel, W.3    Yalcin, A.4    Weber, K.5    Tuschl, T.6
  • 22
    • 0035859929 scopus 로고    scopus 로고
    • Specific inhibition of gene expression by small double-stranded RNAs in invertebrate and vertebrate systems
    • Caplen, N. J., Parrish, S., Imani, F., Fire, A., and Morgan, R. A. (2001) Specific inhibition of gene expression by small double-stranded RNAs in invertebrate and vertebrate systems. Proc. Natl. Acad. Sci. U.S.A.98, 9742-9747.
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 9742-9747
    • Caplen, N.J.1    Parrish, S.2    Imani, F.3    Fire, A.4    Morgan, R.A.5
  • 24
    • 0037324378 scopus 로고    scopus 로고
    • Ribonuclease inhibitor as an intracellular sentry
    • DOI 10.1093/nar/gkg163
    • Haigis, M. C., Kurten, E. L., and Raines, R. T. (2003) Ribonuclease inhibitor as an intracellular sentry. Nucleic Acids Res.31, 1024-1032. (Pubitemid 36240441)
    • (2003) Nucleic Acids Research , vol.31 , Issue.3 , pp. 1024-1032
    • Haigis, M.C.1    Kurten, E.L.2    Raines, R.T.3
  • 25
    • 0035478585 scopus 로고    scopus 로고
    • Macromolecular crowding: Obvious but unappreciated
    • Ellis, R. J. (2001) Macromolecular crowding: Obvious but unappreciated. Trends Biochem. Sci.26, 597-604.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 597-604
    • Ellis, R.J.1
  • 26
    • 41049090929 scopus 로고    scopus 로고
    • Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences
    • Zhou, H. X., Rivas, G., and Minton, A. P. (2008) Macromolecular crowding and confinement: Biochemical, biophysical, and potential physiological consequences. Annu. Rev. Biophys.37, 375-397.
    • (2008) Annu. Rev. Biophys. , vol.37 , pp. 375-397
    • Zhou, H.X.1    Rivas, G.2    Minton, A.P.3
  • 27
    • 47749124982 scopus 로고    scopus 로고
    • Aspects of the cytotoxic action of ribonucleases
    • Arnold, U. (2008) Aspects of the cytotoxic action of ribonucleases. Curr. Pharm. Biotechnol.9, 161-168.
    • (2008) Curr. Pharm. Biotechnol. , vol.9 , pp. 161-168
    • Arnold, U.1
  • 28
    • 47749138585 scopus 로고    scopus 로고
    • Intracellular routing of cytotoxic pancreatic-type ribonucleases
    • Benito, A., Vilanova, M., and Ribó, M. (2008) Intracellular routing of cytotoxic pancreatic-type ribonucleases. Curr. Pharm. Biotechnol.9, 169-179.
    • (2008) Curr. Pharm. Biotechnol. , vol.9 , pp. 169-179
    • Benito, A.1    Vilanova, M.2    Ribó, M.3
  • 30
    • 0035630691 scopus 로고    scopus 로고
    • Protein-protein interfaces: Mimics and inhibitors
    • Cochran, A. G. (2001) Protein-protein interfaces: Mimics and inhibitors. Curr. Opin. Chem. Biol.5, 654-659.
    • (2001) Curr. Opin. Chem. Biol. , vol.5 , pp. 654-659
    • Cochran, A.G.1
  • 31
    • 33646567148 scopus 로고    scopus 로고
    • Between a rock and a hard place
    • Whitty, A., and Kumaravel, G. (2006) Between a rock and a hard place. Nat. Chem. Biol.2, 112-118.
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 112-118
    • Whitty, A.1    Kumaravel, G.2
  • 32
    • 37249004920 scopus 로고    scopus 로고
    • Reaching for high-hanging fruit in drug discovery at protein-protein interfaces
    • DOI 10.1038/nature06526, PII NATURE06526
    • Wells, J. A., and McClendon, C. L. (2007) Reaching for high-hanging fruit in drug discovery at protein-protein interfaces. Nature450, 1001-1009. (Pubitemid 350273630)
    • (2007) Nature , vol.450 , Issue.7172 , pp. 1001-1009
    • Wells, J.A.1    McClendon, C.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.