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Volumn 278, Issue 19, 2011, Pages 3633-3643

Barnase and binase: Twins with distinct fates

Author keywords

Bacillus; bacterial RNases; barnase; binase; biosynthesis; cancer therapy; cytotoxicity; physiological role; practical application; RNase inhibitor

Indexed keywords

ANTINEOPLASTIC AGENT; BARNASE; BINASE; CARBON NANOTUBE; HYBRID PROTEIN; NANOPARTICLE; PHOSPHATE; QUANTUM DOT; RIBONUCLEASE; SINGLE CHAIN FRAGMENT VARIABLE ANTIBODY BARNASE FUSION PROTEIN; UNCLASSIFIED DRUG;

EID: 80052965616     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2011.08294.x     Document Type: Article
Times cited : (76)

References (84)
  • 2
    • 77956034926 scopus 로고    scopus 로고
    • Novel endoribonucleases as central players in various pathways of eukaryotic RNA metabolism
    • Tomecki R, &, Dziembowski A, (2010) Novel endoribonucleases as central players in various pathways of eukaryotic RNA metabolism. RNA 9, 1692-1724.
    • (2010) RNA , vol.9 , pp. 1692-1724
    • Tomecki, R.1    Dziembowski, A.2
  • 4
    • 44649149642 scopus 로고    scopus 로고
    • RNase A ribonucleases and host defense: An evolving story
    • DOI 10.1189/jlb.1107725
    • Rosenberg HF, (2008) RNase A ribonucleases and host defense: an evolving story. J Leukoc Biol 83, 1079-1087. (Pubitemid 351960339)
    • (2008) Journal of Leukocyte Biology , vol.83 , Issue.5 , pp. 1079-1087
    • Rosenberg, H.F.1
  • 5
    • 48949094215 scopus 로고    scopus 로고
    • Binase and other microbial RNases as potential anticancer agents
    • Makarov AA, Kolchinsky A, &, Ilinskaya ON, (2008) Binase and other microbial RNases as potential anticancer agents. Bioessays 30, 781-790.
    • (2008) Bioessays , vol.30 , pp. 781-790
    • Makarov, A.A.1    Kolchinsky, A.2    Ilinskaya, O.N.3
  • 6
    • 71749083324 scopus 로고    scopus 로고
    • Ribonucleases as potential modalities in anticancer therapy
    • Ardelt W, Ardelt B, &, Darzynkiewicz Z, (2009) Ribonucleases as potential modalities in anticancer therapy. Eur J Pharmacol 625, 181-189.
    • (2009) Eur J Pharmacol , vol.625 , pp. 181-189
    • Ardelt, W.1    Ardelt, B.2    Darzynkiewicz, Z.3
  • 7
    • 78650539904 scopus 로고    scopus 로고
    • Ribonucleases of different origins with a wide spectrum of medicinal applications
    • Fang EF, &, Ng TB, (2011) Ribonucleases of different origins with a wide spectrum of medicinal applications. Biochim Biophys Acta 1815, 65-74.
    • (2011) Biochim Biophys Acta , vol.1815 , pp. 65-74
    • Fang, E.F.1    Ng, T.B.2
  • 8
    • 47749087053 scopus 로고    scopus 로고
    • Onconase and amphinase, the antitumor ribonucleases from Rana pipiens oocytes
    • DOI 10.2174/138920108784567245
    • Ardelt W, Shogen K, &, Darzynkiewicz Z, (2008) Onconase and amphinase, the antitumor ribonucleases from Rana pipiens oocytes. Curr Pharm Biotechnol 9, 215-225. (Pubitemid 352024698)
    • (2008) Current Pharmaceutical Biotechnology , vol.9 , Issue.3 , pp. 215-225
    • Ardelt, W.1    Shogen, K.2    Darzynkiewicz, Z.3
  • 9
    • 54249139787 scopus 로고    scopus 로고
    • Agents from amphibians with anticancer properties
    • Lu CX, Nan KJ, &, Lei Y, (2008) Agents from amphibians with anticancer properties. Anticancer Drugs 19, 931-939.
    • (2008) Anticancer Drugs , vol.19 , pp. 931-939
    • Lu, C.X.1    Nan, K.J.2    Lei, Y.3
  • 10
    • 0035957231 scopus 로고    scopus 로고
    • Antitumor action of seminal ribonuclease, its dimeric structure, and its resistance to the cytosolic ribonuclease inhibitor
    • DOI 10.1021/bi002781m
    • Antignani A, Naddeo M, Cubellis MV, Russo A, &, D'Alessio G, (2001) Antitumor action of seminal ribonuclease, its dimeric structure, and its resistance to the cytosolic ribonuclease inhibitor. Biochemistry 40, 3492-3496. (Pubitemid 32242806)
    • (2001) Biochemistry , vol.40 , Issue.12 , pp. 3492-3496
    • Antignani, A.1    Naddeo, M.2    Cubellis, M.V.3    Russo, A.4    D'Alessio, G.5
  • 11
    • 47749113698 scopus 로고    scopus 로고
    • Eosinophil-derived neurotoxin/RNase 2: Connecting the past, the present and the future
    • DOI 10.2174/138920108784567236
    • Rosenberg HF, (2008) Eosinophil-derived neurotoxin/RNase 2: connecting the past, the present and the future. Curr Pharm Biotechnol 9, 135-140. (Pubitemid 352024689)
    • (2008) Current Pharmaceutical Biotechnology , vol.9 , Issue.3 , pp. 135-140
    • Rosenberg, H.F.1
  • 12
    • 20944447573 scopus 로고    scopus 로고
    • Surface-exposed amino acids of eosinophil cationic protein play a critical role in the inhibition of mammalian cell proliferation
    • DOI 10.1007/s11010-005-4777-2
    • Carreras E, Boix E, Navarro S, Rosenberg HF, Cuchillo CM, &, Nogués MV, (2005) Surface-exposed amino acids of eosinophil cationic protein play a critical role in the inhibition of mammalian cell proliferation. Mol Cell Biochem 272, 1-7. (Pubitemid 40867359)
    • (2005) Molecular and Cellular Biochemistry , vol.272 , Issue.1-2 , pp. 1-7
    • Carreras, E.1    Boix, E.2    Navarro, S.3    Rosenberg, H.F.4    Cuchillo, C.M.5    Nogues, M.V.6
  • 13
    • 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 Suppl , vol.23 , pp. 345-348
    • Belyaeva, M.I.1    Kyune, M.F.2    Nuzhina, A.M.3
  • 14
    • 0034809187 scopus 로고    scopus 로고
    • The ribonuclease T1 family
    • DOI 10.1016/S0076-6879(01)41143-8
    • Yoshida H, (2001) The ribonuclease T1 family. Methods Enzymol 341, 28-41. (Pubitemid 32928517)
    • (2001) Methods in Enzymology , vol.341 , pp. 28-41
    • Yoshida, H.1
  • 15
    • 34547781750 scopus 로고    scopus 로고
    • MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) software version 4.0
    • DOI 10.1093/molbev/msm092
    • Tamura K, Dudley J, Nei M, &, Kumar S, (2007) MEGA4: Molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol Biol Evol 24, 1596-1599. (Pubitemid 47236692)
    • (2007) Molecular Biology and Evolution , vol.24 , Issue.8 , pp. 1596-1599
    • Tamura, K.1    Dudley, J.2    Nei, M.3    Kumar, S.4
  • 16
    • 47749114193 scopus 로고    scopus 로고
    • Evasion of ribonuclease inhibitor as a determinant of ribonuclease cytotoxicity
    • Rutkoski TJ, &, Raines RT, (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
  • 17
    • 84886615942 scopus 로고
    • Primary structure of ribonuclease from Bacillus intermedius 7P
    • DOI 10.1016/0014-5793(79)80056-3
    • Aphanasenko GA, Dudkin SM, Kaminir LB, Leshchinskaya IB, &, Severin ES, (1979) Primary structure of ribonuclease from Bacillus intermedius 7P. FEBS Lett 97, 77-80. (Pubitemid 9108524)
    • (1979) FEBS Letters , vol.97 , Issue.1 , pp. 77-80
    • Aphanasenko, G.A.1    Dudkin, S.M.2    Kaminir, L.B.3
  • 18
    • 0015494427 scopus 로고
    • Amino-acid sequence of extracellular ribonuclease (barnase) of Bacillus amyloliquefaciens
    • Hartley RW, &, Barker EA, (1972) Amino-acid sequence of extracellular ribonuclease (barnase) of Bacillus amyloliquefaciens. Nature 235, 15-16.
    • (1972) Nature , vol.235 , pp. 15-16
    • Hartley, R.W.1    Barker, E.A.2
  • 19
    • 0026044754 scopus 로고
    • Determination of the three-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy
    • Bycroft M, Ludvigsen S, Fersht AR, &, Poulsen FM, (1991) Determination of the three-dimensional solution structure of barnase using nuclear magnetic resonance spectroscopy. Biochemistry 30, 8697-8701.
    • (1991) Biochemistry , vol.30 , pp. 8697-8701
    • Bycroft, M.1    Ludvigsen, S.2    Fersht, A.R.3    Poulsen, F.M.4
  • 23
    • 0024453699 scopus 로고
    • Barnase and barstar: Two small proteins to fold and fit together
    • Hartley RW, (1989) Barnase and barstar: two small proteins to fold and fit together. Trends Biochem Sci 14, 450-454. (Pubitemid 19273210)
    • (1989) Trends in Biochemical Sciences , vol.14 , Issue.11 , pp. 450-454
    • Hartley, R.W.1
  • 24
    • 0024293097 scopus 로고
    • Barnase and barstar. Expression of its cloned inhibitor permits expression of a cloned ribonuclease
    • Hartley RW, (1988) Barnase and barstar. Expression of its cloned inhibitor permits expression of a cloned ribonuclease. J Mol Biol 202, 913-915.
    • (1988) J Mol Biol , vol.202 , pp. 913-915
    • Hartley, R.W.1
  • 25
    • 0035228058 scopus 로고    scopus 로고
    • Methods for studying the interaction of barnase with its inhibitor barstar
    • Schreiber G, (2001) Methods for studying the interaction of barnase with its inhibitor barstar. Methods Mol Biol 160, 213-226.
    • (2001) Methods Mol Biol , vol.160 , pp. 213-226
    • Schreiber, G.1
  • 26
    • 0028074974 scopus 로고
    • Protein-protein recognition: Crystal structural analysis of a barnase- barstar complex at 2.0-A resolution
    • DOI 10.1021/bi00196a004
    • Buckle AM, Schreiber G, &, Fersht AR, (1994) Protein-protein recognition: crystal structural analysis of a barnase-barstar complex at 2.0-Å resolution. Biochemistry 33, 8878-8889. (Pubitemid 24257995)
    • (1994) Biochemistry , vol.33 , Issue.30 , pp. 8878-8889
    • Buckle, A.M.1    Schreiber, G.2    Fersht, A.R.3
  • 27
    • 77956154559 scopus 로고    scopus 로고
    • Downhill binding energy surface of the barnase-barstar complex
    • Wang L, Siu SW, Gu W, &, Helms V, (2010) Downhill binding energy surface of the barnase-barstar complex. Biopolymers 93, 977-985.
    • (2010) Biopolymers , vol.93 , pp. 977-985
    • Wang, L.1    Siu, S.W.2    Gu, W.3    Helms, V.4
  • 30
    • 69949150299 scopus 로고    scopus 로고
    • Interactions of Bacillus spp. and plants with special reference to induced systemic resistance (ISR)
    • Choudhary DK, &, Johri BN, (2009) Interactions of Bacillus spp. and plants with special reference to induced systemic resistance (ISR). Microbiol Res 164, 493-513.
    • (2009) Microbiol Res , vol.164 , pp. 493-513
    • Choudhary, D.K.1    Johri, B.N.2
  • 31
    • 0027230257 scopus 로고
    • The roles of signal peptide and mature protein in RNase (barnase) export from Bacillus subtilis
    • Chen M, &, Nagarajan V, (1993) The roles of signal peptide and mature protein in RNase (barnase) export from Bacillus subtilis. Mol Gen Genet 239, 409-415. (Pubitemid 23194805)
    • (1993) Molecular and General Genetics , vol.239 , Issue.3 , pp. 409-415
    • Chen, M.1    Nagarajan, V.2
  • 32
    • 17444365846 scopus 로고    scopus 로고
    • Some secretion characteristics of bacterial ribonuclease
    • DOI 10.1007/s11021-005-0024-9
    • Sharipova MR, Lopukhov LV, Vershinina OA, &, Leshchinskaya IB, (2005) Some secretion characteristics of bacterial ribonucleases. Microbiology (Moscow, Russ. Fed.) 74, 27-31. (Pubitemid 40534088)
    • (2005) Microbiology , vol.74 , Issue.1 , pp. 27-31
    • Sharipova, M.R.1    Lopukhov, L.V.2    Vershinina, O.A.3    Leshchinskaya, I.B.4
  • 33
    • 77954065271 scopus 로고    scopus 로고
    • I-TASSER: A unified platform for automated protein structure and function prediction
    • Roy A, Kucukural A, &, Zhang Y, (2010) I-TASSER: a unified platform for automated protein structure and function prediction. Nat Protoc 5, 725-738.
    • (2010) Nat Protoc , vol.5 , pp. 725-738
    • Roy, A.1    Kucukural, A.2    Zhang, Y.3
  • 34
    • 0027177102 scopus 로고
    • Interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering
    • DOI 10.1021/bi00070a025
    • Schreiber G, &, Fersht AR, (1993) The interaction of barnase with its polypeptide inhibitor barstar studied by protein engineering. Biochemistry 32, 5145-5150. (Pubitemid 23162083)
    • (1993) Biochemistry , vol.32 , Issue.19 , pp. 5145-5150
    • Schreiber, G.1    Fersht, A.R.2
  • 35
  • 36
    • 0033804284 scopus 로고    scopus 로고
    • A novel secreted ribonuclease from Bacillus intermedius: Gene structure and regulatory control
    • Hahnen E, Znamenskaya L, Koczan D, Leshchinskaya I, &, Hobom G, (2000) A novel secreted ribonuclease from Bacillus intermedius: gene structure and regulatory control. Mol Gen Genet 263, 571-580.
    • (2000) Mol Gen Genet , vol.263 , pp. 571-580
    • Hahnen, E.1    Znamenskaya, L.2    Koczan, D.3    Leshchinskaya, I.4    Hobom, G.5
  • 38
    • 0029976302 scopus 로고    scopus 로고
    • The signal-transduction network for Pho regulation in Bacillus subtilis
    • Hulett FM, (1996) The signal transduction network for PHO regulation in Bacillus subtilis. Mol Microbiol 19, 933-939. (Pubitemid 26083423)
    • (1996) Molecular Microbiology , vol.19 , Issue.5 , pp. 933-939
    • Hulett, F.M.1
  • 40
    • 28044440054 scopus 로고    scopus 로고
    • Genome-wide transcriptional analysis of the phosphate starvation stimulon of Bacillus subtilis
    • DOI 10.1128/JB.187.23.8063-8080.2005
    • Allenby NE, O'Connor N, Prágai Z, Ward AC, Wipat A, &, Harwood CR, (2005) Genome-wide transcriptional analysis of the phosphate starvation stimulon of Bacillus subtilis. J Bacteriol 187, 8063-8080. (Pubitemid 41691700)
    • (2005) Journal of Bacteriology , vol.187 , Issue.23 , pp. 8063-8080
    • Allenby, N.E.E.1    O'Connor, N.2    Pragai, Z.3    Ward, A.C.4    Wipat, A.5    Harwood, C.R.6
  • 41
    • 0344197082 scopus 로고    scopus 로고
    • Expression of the genes for guanyl-specific ribonucleases from Bacillus intermedius and Bacillus pumilus is regulated by the two component signal transduction system PhoP-PhoR in B. subtilis
    • DOI 10.1016/S0378-1097(99)00077-4, PII S0378109799000774
    • Znamenskaya LV, Vershinina OA, Vershinina VI, Leshchinskaya IB, &, Hartley RW, (1999) Expression of the genes for guanyl-specific ribonucleases from Bacillus intermedius and Bacillus pumilis is regulated by the two-component signal-transduction system PhoP-PhoR in B. subtilis. FEMS Microbiol Lett 173, 217-222. (Pubitemid 29132794)
    • (1999) FEMS Microbiology Letters , vol.173 , Issue.1 , pp. 217-222
    • Znamenskaya, L.V.1    Vershinina, O.A.2    Vershinina, V.I.3    Leshchinskaya, I.B.4    Hartley, R.W.5
  • 42
    • 35349006283 scopus 로고    scopus 로고
    • The effect of Spo0A and AbrB proteins on expression of the genes of guanyl-specific ribonucleases from Bacillus intermedius and Bacillus pumilus in Bacillus subtilis recombinant strains
    • DOI 10.1134/S0026261707050086
    • Ul'ianova VV, Vershinina VI, Kharitonova MA, &, Sharipova MR, (2007) The effect of Spo0A and AbrB proteins on expression of the genes of guanyl-specific ribonucleases from Bacillus intermedius and Bacillus pumilus in Bacillus subtilis recombinant strains. Microbiology (Moscow, Russ. Fed.) 76, 563-568. (Pubitemid 47609314)
    • (2007) Microbiology , vol.76 , Issue.5 , pp. 563-568
    • Ul'yanova, V.V.1    Vershinina, V.I.2    Kharitonova, M.A.3    Sharipova, M.R.4
  • 43
    • 24944483644 scopus 로고    scopus 로고
    • Evidence that entry into sporulation in Bacillus subtilis is governed by a gradual increase in the level and activity of the master regulator Spo0A
    • DOI 10.1101/gad.1335705
    • Fujita M, &, Losick R, (2005) Evidence that entry into sporulation in Bacillus subtilis is governed by a gradual increase in the level and activity of the master regulator Spo0A. Genes Dev 19, 2236-2244. (Pubitemid 41330324)
    • (2005) Genes and Development , vol.19 , Issue.18 , pp. 2236-2244
    • Fujita, M.1    Losick, R.2
  • 44
    • 0042366189 scopus 로고    scopus 로고
    • Cannibalism by sporulating bacteria
    • DOI 10.1126/science.1086462
    • Gonzalez-Pastor JE, Hobbs EC, &, Losick R, (2003) Cannibalism by sporulating bacteria. Science 301, 510-513. (Pubitemid 36900307)
    • (2003) Science , vol.301 , Issue.5632 , pp. 510-513
    • Gonzalez-Pastor, J.E.1    Hobbs, E.C.2    Losick, R.3
  • 45
  • 46
    • 58149483378 scopus 로고    scopus 로고
    • DegU and Spo0A jointly control transcription of two loci required for complex colony development by Bacillus subtilis
    • Verhamme DT, Murray EJ, &, Stanley-Wall NR, (2009) DegU and Spo0A jointly control transcription of two loci required for complex colony development by Bacillus subtilis. J Bacteriol 191, 100-108.
    • (2009) J Bacteriol , vol.191 , pp. 100-108
    • Verhamme, D.T.1    Murray, E.J.2    Stanley-Wall, N.R.3
  • 47
    • 67650604265 scopus 로고    scopus 로고
    • Stressing out over tRNA cleavage
    • Thompson DM, &, Parker R, (2009) Stressing out over tRNA cleavage. Cell 138, 215-219.
    • (2009) Cell , vol.138 , pp. 215-219
    • Thompson, D.M.1    Parker, R.2
  • 48
    • 33749506727 scopus 로고    scopus 로고
    • Antibiosis by Bacillus amyloliquefaciens ribonuclease barnase expressed in Escherichia coli against symbiotic and endophytic nitrogen-fixing bacteria
    • DOI 10.1016/j.jbiotec.2006.04.020, PII S0168165606003464
    • Ramos HJO, Souza EM, Soares-Ramos JRL, &, Pedrosa FO, (2006) Antibiosis by Bacillus amyloliquefaciens ribonuclease barnase expressed in Escherichia coli against symbiotic and endophytic nitrogen-fixing bacteria. J Biotechnol 126, 291-294. (Pubitemid 44528786)
    • (2006) Journal of Biotechnology , vol.126 , Issue.3 , pp. 291-294
    • Ramos, H.J.O.1    Souza, E.M.2    Soares-Ramos, J.R.L.3    Pedrosa, F.O.4
  • 49
    • 33746088411 scopus 로고    scopus 로고
    • Evidence for a novel protease governing regulated intramembrane proteolysis and resistance to antimicrobial peptides in Bacillus subtilis
    • DOI 10.1101/gad.1440606
    • Ellermeier CD, &, Losick R, (2006) Evidence for a novel protease governing regulated intramembrane proteolysis and resistance to antimicrobial peptides in Bacillus subtilis. Genes Dev 20, 1911-1922. (Pubitemid 44079328)
    • (2006) Genes and Development , vol.20 , Issue.14 , pp. 1911-1922
    • Ellermeier, C.D.1    Losick, R.2
  • 50
    • 0035917323 scopus 로고    scopus 로고
    • Experimental assignment of the structure of the transition state for the association of barnase and barstar
    • DOI 10.1006/jmbi.2001.4577
    • Frisch C, Fersht AR, &, Schreiber G, (2001) Experimental assignment of the structure of the transition state for the association of barnase and barstar. J Mol Biol 308, 69-77. (Pubitemid 33027628)
    • (2001) Journal of Molecular Biology , vol.308 , Issue.1 , pp. 69-77
    • Frisch, C.1    Fersht, A.R.2    Schreiber, G.3
  • 51
    • 0028272419 scopus 로고
    • Female sterile tobacco plants are produced by stigma-specific cell ablation
    • Goldman MH, Goldberg RB, &, Mariani C, (1994) Female sterile tobacco plants are produced by stigma-specific cell ablation. EMBO J 13, 2976-2984. (Pubitemid 24213449)
    • (1994) EMBO Journal , vol.13 , Issue.13 , pp. 2976-2984
    • Goldman, M.H.S.1    Goldberg, R.B.2    Mariani, C.3
  • 52
    • 0028822097 scopus 로고
    • Inhibition of fungal disease development in plants by engineering controlled cell death
    • Strittmatter G, Jansses J, Opsomer C, &, Botterma J, (1995) Inhibition of fungal disease development in plants by engineering controlled cell death. Nat Biotechnol 13, 1085-1089.
    • (1995) Nat Biotechnol , vol.13 , pp. 1085-1089
    • Strittmatter, G.1    Jansses, J.2    Opsomer, C.3    Botterma, J.4
  • 54
    • 65249094239 scopus 로고    scopus 로고
    • Structural and thermodynamic analysis of a conformationally-strained circular permutant of barnase
    • Butler JS, Mitrea DM, Mitrousis G, Cingolani G, &, Loh SN, (2009) Structural and thermodynamic analysis of a conformationally-strained circular permutant of barnase. Biochemistry 48, 3497-3507.
    • (2009) Biochemistry , vol.48 , pp. 3497-3507
    • Butler, J.S.1    Mitrea, D.M.2    Mitrousis, G.3    Cingolani, G.4    Loh, S.N.5
  • 55
    • 79151480850 scopus 로고    scopus 로고
    • Antitumor activity and toxicity of anti-HER2 immunoRNase scFv 4D5-dibarnase in mice bearing human breast cancer xenografts
    • Balandin TG, Edelweiss E, Andronova NV, Treshalina EM, Sapozhnikov AM, &, Deyev SM, (2011) Antitumor activity and toxicity of anti-HER2 immunoRNase scFv 4D5-dibarnase in mice bearing human breast cancer xenografts. Invest New Drugs 29, 22-32.
    • (2011) Invest New Drugs , vol.29 , pp. 22-32
    • Balandin, T.G.1    Edelweiss, E.2    Andronova, N.V.3    Treshalina, E.M.4    Sapozhnikov, A.M.5    Deyev, S.M.6
  • 57
    • 0030914745 scopus 로고    scopus 로고
    • Nephrotoxic effects of bacterial ribonucleases in the isolated perfused rat kidney
    • DOI 10.1016/S0300-483X(97)03639-1, PII S0300483X97036391
    • Ilinskaya ON, &, Vamvakas S, (1997) Nephrotoxic effects of bacterial ribonucleases in the isolated perfused rat kidney. Toxicology 120, 55-63. (Pubitemid 27199433)
    • (1997) Toxicology , vol.120 , Issue.1 , pp. 55-63
    • Ilinskaya, O.N.1    Vamvakas, S.2
  • 58
    • 77953621551 scopus 로고    scopus 로고
    • Barnase-barstar: From first encounter to final complex
    • Hoefling M, &, Gottschalk KE, (2010) Barnase-barstar: from first encounter to final complex. J Struct Biol 171, 52-63.
    • (2010) J Struct Biol , vol.171 , pp. 52-63
    • Hoefling, M.1    Gottschalk, K.E.2
  • 59
    • 30344454390 scopus 로고    scopus 로고
    • Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI
    • DOI 10.1016/j.jmb.2005.11.005, PII S0022283605013720
    • Niemann HH, Schmoldt HU, Wentzel A, Kolmar H, &, Heinz DW, (2006) Barnase fusion as a tool to determine the crystal structure of the small disulfide-rich protein McoEeTI. J Mol Biol 356, 1-8. (Pubitemid 43069722)
    • (2006) Journal of Molecular Biology , vol.356 , Issue.1 , pp. 1-8
    • Niemann, H.H.1    Schmoldt, H.-U.2    Wentzel, A.3    Kolmar, H.4    Heinz, D.W.5
  • 61
    • 33745025718 scopus 로고    scopus 로고
    • Production of recombinant RNase Ba and its application in downstream processing of plasmid DNA for pharmaceutical use
    • DOI 10.1021/bp050417e
    • Voss C, Lindau D, &, Flasche E, (2006) Production of recombinant RNase Ba and its application in downstream processing of plasmid DNA for pharmaceutical use. Biotechnol Prog 22, 737-744. (Pubitemid 43877442)
    • (2006) Biotechnology Progress , vol.22 , Issue.3 , pp. 737-744
    • Voss, C.1    Lindau, D.2    Flaschel, E.3
  • 62
    • 68149126127 scopus 로고    scopus 로고
    • A novel vector for direct cloning PCR fragments by positive selection based on the lethal barnase
    • You L, Weng H, Chen Z, Wang A, Xu W, Wang M, &, Dong Z, (2009) A novel vector for direct cloning PCR fragments by positive selection based on the lethal barnase. Mol Biol Rep 36, 1793-1798.
    • (2009) Mol Biol Rep , vol.36 , pp. 1793-1798
    • You, L.1    Weng, H.2    Chen, Z.3    Wang, A.4    Xu, W.5    Wang, M.6    Dong, Z.7
  • 64
    • 65049089717 scopus 로고    scopus 로고
    • Production of male- and female-sterile plants through reproductive tissue ablation
    • Gardner N, Felsheim R, &, Smith AG, (2009) Production of male- and female-sterile plants through reproductive tissue ablation. J Plant Physiol 166, 871-881.
    • (2009) J Plant Physiol , vol.166 , pp. 871-881
    • Gardner, N.1    Felsheim, R.2    Smith, A.G.3
  • 65
    • 0242461279 scopus 로고    scopus 로고
    • Genetically engineered self-destruction: An alternative to herbicides for cover crop systems
    • DOI 10.1614/0043-1745(2002)050[0794:GESDAA]2.0.CO;2
    • Stanislaus MA, &, Cheng CL, (2002) Genetically engineered self-destruction: an alternative to herbicides for cover crop systems. Weed Sci 50, 794-801. (Pubitemid 43670300)
    • (2002) Weed Science , vol.50 , Issue.6 , pp. 794-801
    • Stanislaus, M.A.1    Cheng, C.-L.2
  • 66
    • 77951120498 scopus 로고    scopus 로고
    • Removing the mustard oil bomb from seeds: Transgenic ablation of myrosin cells in oilseed rape (Brassica napus) produces MINELESS seeds
    • Borgen BH, Thangstad OP, Ahuja I, Rossiter JT, &, Bones AM, (2010) Removing the mustard oil bomb from seeds: transgenic ablation of myrosin cells in oilseed rape (Brassica napus) produces MINELESS seeds. J Exp Bot 61, 1683-1697.
    • (2010) J Exp Bot , vol.61 , pp. 1683-1697
    • Borgen, B.H.1    Thangstad, O.P.2    Ahuja, I.3    Rossiter, J.T.4    Bones, A.M.5
  • 70
    • 78650394311 scopus 로고    scopus 로고
    • Cellular uptake of ribonuclease A relies on anionic glycans
    • Chao TY, Lavis LD, &, Raines RT, (2010) Cellular uptake of ribonuclease A relies on anionic glycans. Biochemistry 49, 10666-10673.
    • (2010) Biochemistry , vol.49 , pp. 10666-10673
    • Chao, T.Y.1    Lavis, L.D.2    Raines, R.T.3
  • 71
    • 67650688135 scopus 로고    scopus 로고
    • Onconase cytotoxicity relies on the distribution of its positive charge
    • Turcotte RF, Lavis LD, &, Raines RT, (2009) Onconase cytotoxicity relies on the distribution of its positive charge. FEBS J 276, 3846-3857.
    • (2009) FEBS J , vol.276 , pp. 3846-3857
    • Turcotte, R.F.1    Lavis, L.D.2    Raines, R.T.3
  • 73
    • 47749131189 scopus 로고    scopus 로고
    • Design of cytotoxic ribonucleases by cationization to enhance intracellular protein delivery
    • DOI 10.2174/138920108784567326
    • Futami J, &, Yamada H, (2008) Design of cytotoxic ribonucleases by cationization to enhance intracellular protein delivery. Curr Pharm Biotechnol 9, 180-184. (Pubitemid 352024694)
    • (2008) Current Pharmaceutical Biotechnology , vol.9 , Issue.3 , pp. 180-184
    • Futami, J.1    Yamada, H.2
  • 74
    • 57049128294 scopus 로고    scopus 로고
    • Design and characterization of an HIV-specific ribonuclease zymogen
    • Turcotte RF, &, Raines RT, (2008) Design and characterization of an HIV-specific ribonuclease zymogen. AIDS Res Hum Retroviruses 24, 1357-1363.
    • (2008) AIDS Res Hum Retroviruses , vol.24 , pp. 1357-1363
    • Turcotte, R.F.1    Raines, R.T.2
  • 76
    • 78049457039 scopus 로고    scopus 로고
    • Intracellular delivery and anti-cancer effect of self-assembled heparin-Pluronic nanogels with RNase A
    • Choi JH, Jang JY, Joung YK, Kwon MH, &, Park KD, (2010) Intracellular delivery and anti-cancer effect of self-assembled heparin-Pluronic nanogels with RNase A. J Control Release 147, 420-427.
    • (2010) J Control Release , vol.147 , pp. 420-427
    • Choi, J.H.1    Jang, J.Y.2    Joung, Y.K.3    Kwon, M.H.4    Park, K.D.5
  • 77
    • 77950142741 scopus 로고    scopus 로고
    • Nanoparticle-mediated cytoplasmic delivery of proteins to target cellular machinery
    • Bale SS, Kwon SJ, Shah DA, Banerjee A, Dordick JS, &, Kane RS, (2010) Nanoparticle-mediated cytoplasmic delivery of proteins to target cellular machinery. ACS Nano 4, 1493-1500.
    • (2010) ACS Nano , vol.4 , pp. 1493-1500
    • Bale, S.S.1    Kwon, S.J.2    Shah, D.A.3    Banerjee, A.4    Dordick, J.S.5    Kane, R.S.6
  • 79
    • 0035793124 scopus 로고    scopus 로고
    • Bacillus intermedius ribonuclease as inhibitor of cell proliferation and membrane current
    • DOI 10.1016/S0300-483X(00)00335-8, PII S0300483X00003358
    • 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. (Pubitemid 32119482)
    • (2001) Toxicology , vol.156 , Issue.2-3 , pp. 101-107
    • Ilinskaya, O.1    Decker, K.2    Koschinski, A.3    Dreyer, F.4    Repp, H.5
  • 82
    • 64949132552 scopus 로고    scopus 로고
    • Effect of Onconase on double-stranded RNA in vitro
    • Saxena A, Saxena SK, &, Shogen K, (2009) Effect of Onconase on double-stranded RNA in vitro. Anticancer Res 29, 1067-1071.
    • (2009) Anticancer Res , vol.29 , pp. 1067-1071
    • Saxena, A.1    Saxena, S.K.2    Shogen, K.3
  • 83
    • 54049094773 scopus 로고    scopus 로고
    • The cytotoxic ribonuclease onconase targets RNA interference (siRNA)
    • Zhao H, Ardelt B, Ardelt W, Shogen K, &, Darzynkiewicz Z, (2008) The cytotoxic ribonuclease onconase targets RNA interference (siRNA). Cell Cycle 7, 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
  • 84
    • 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. (Pubitemid 35244462)
    • (2002) Cancer Research , vol.62 , Issue.21 , pp. 6132-6140
    • Ran, S.1    Downes, A.2    Thorpe, P.E.3


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