메뉴 건너뛰기




Volumn 83, Issue 5, 2008, Pages 1079-1087

RNase A ribonucleases and host defense: An evolving story

Author keywords

Bactericidal; Cationic; Eosinophil; Evolution; Leukocyte; Virus

Indexed keywords

CYTOTOXIC FACTOR; EOSINOPHIL CATIONIC PROTEIN; G PROTEIN COUPLED RECEPTOR; NEUROTOXIN; RIBONUCLEASE; RIBONUCLEASE 7; RIBONUCLEASE A; RIBONUCLEASE A2; TOLL LIKE RECEPTOR 2;

EID: 44649149642     PISSN: 07415400     EISSN: None     Source Type: Journal    
DOI: 10.1189/jlb.1107725     Document Type: Review
Times cited : (164)

References (78)
  • 1
    • 0031697202 scopus 로고    scopus 로고
    • The ribonuclease A superfamily: General discussion
    • Beintema, J. J., Kleineidam, R. G. (1998) The ribonuclease A superfamily: general discussion. Cell. Mol. Life Sci. 54, 825-832.
    • (1998) Cell. Mol. Life Sci , vol.54 , pp. 825-832
    • Beintema, J.J.1    Kleineidam, R.G.2
  • 2
    • 0142151785 scopus 로고    scopus 로고
    • Eosinophil-derived neurotoxin (EDN), an antimicrobial protein with chemotactic activities for dendritic cells
    • Yang, D., Rosenberg, H. F., Chen, Q., Dyer, K. D., Kurosaka, K., Oppenheim, J. J. (2003) Eosinophil-derived neurotoxin (EDN), an antimicrobial protein with chemotactic activities for dendritic cells. Blood 102, 3396-3403.
    • (2003) Blood , vol.102 , pp. 3396-3403
    • Yang, D.1    Rosenberg, H.F.2    Chen, Q.3    Dyer, K.D.4    Kurosaka, K.5    Oppenheim, J.J.6
  • 3
    • 8444222667 scopus 로고    scopus 로고
    • Human ribonuclease A superfamily members, eosinophil-derived neurotoxin and pancreatic ribonuclease, induce dendritic cell maturation and activation
    • Yang, D., Chen, Q., Rosenberg, H. F., Rybak, S. M., Newton, D. L., Wang, Z. Y., Fu, Q., Tchernev, V. T., Wang, M., Schweitzer, B., et al. (2004) Human ribonuclease A superfamily members, eosinophil-derived neurotoxin and pancreatic ribonuclease, induce dendritic cell maturation and activation. J. Immunol. 173, 6134-6142.
    • (2004) J. Immunol , vol.173 , pp. 6134-6142
    • Yang, D.1    Chen, Q.2    Rosenberg, H.F.3    Rybak, S.M.4    Newton, D.L.5    Wang, Z.Y.6    Fu, Q.7    Tchernev, V.T.8    Wang, M.9    Schweitzer, B.10
  • 4
    • 0031596883 scopus 로고    scopus 로고
    • Recombinant human eosinophil-derived neurotoxin/RNase 2 functions as an effective antiviral agent against respiratory syncytial virus
    • Domachowske, J. B., Dyer, K. D., Bonville, C. A., Rosenberg, H. F. (1998) Recombinant human eosinophil-derived neurotoxin/RNase 2 functions as an effective antiviral agent against respiratory syncytial virus. J. Infect. Dis. 177, 1458-1464.
    • (1998) J. Infect. Dis , vol.177 , pp. 1458-1464
    • Domachowske, J.B.1    Dyer, K.D.2    Bonville, C.A.3    Rosenberg, H.F.4
  • 6
    • 0345505219 scopus 로고    scopus 로고
    • Ribonuclease is partly responsible for the HIV-1 inhibitory effect activated by HLA alloantigen recognition
    • Rugeles, M. T., Trubey, C. M., Bedoya, V. I., Pinto, L. A., Oppenheim, J. J., Rybak, S. M., Shearer, G. M. (2003) Ribonuclease is partly responsible for the HIV-1 inhibitory effect activated by HLA alloantigen recognition. AIDS 17, 481-486.
    • (2003) AIDS , vol.17 , pp. 481-486
    • Rugeles, M.T.1    Trubey, C.M.2    Bedoya, V.I.3    Pinto, L.A.4    Oppenheim, J.J.5    Rybak, S.M.6    Shearer, G.M.7
  • 7
    • 38749088662 scopus 로고    scopus 로고
    • Eosinophil-derived neurotoxin acts as an alarmin to activate TLR2-MyD88 signal pathway in dendritic cells and enhances Th2 immune responses
    • Yang, D., Chen, Q. Su, S. B., Zhang, P., Kurosaka, K., Caspi, R. R., Michalek, S. M., Rosenberg, H. F., Zhang, N., Oppenheim, J. J. (2008) Eosinophil-derived neurotoxin acts as an alarmin to activate TLR2-MyD88 signal pathway in dendritic cells and enhances Th2 immune responses. J. Exp. Med., 205, 79-90.
    • (2008) J. Exp. Med , vol.205 , pp. 79-90
    • Yang, D.1    Chen, Q.2    Su, S.B.3    Zhang, P.4    Kurosaka, K.5    Caspi, R.R.6    Michalek, S.M.7    Rosenberg, H.F.8    Zhang, N.9    Oppenheim, J.J.10
  • 8
    • 0021016603 scopus 로고
    • Distinctive cationic proteins of the human eosinophil granule: Major basic protein, eosinophil cationic protein, and eosinophil-derived neurotoxin
    • Ackerman, S. J., Loegering, D. A., Venge, P., Olsson, I., Harley, J. B., Fauci, A. S., Gleich, G. J. (1983) Distinctive cationic proteins of the human eosinophil granule: major basic protein, eosinophil cationic protein, and eosinophil-derived neurotoxin. J. Immunol. 131, 2977-2982.
    • (1983) J. Immunol , vol.131 , pp. 2977-2982
    • Ackerman, S.J.1    Loegering, D.A.2    Venge, P.3    Olsson, I.4    Harley, J.B.5    Fauci, A.S.6    Gleich, G.J.7
  • 9
    • 0025274658 scopus 로고
    • In vitro killing of microfilariae of Brugia pahangi and Brugia malayi by eosinophil granule proteins
    • Hamann, K. J., Gleich, G. J., Checkel, J. L., Loegering, D. A., McCall, J. W., Barker, R. L. (1990) In vitro killing of microfilariae of Brugia pahangi and Brugia malayi by eosinophil granule proteins. J. Immunol. 144, 3166-3173.
    • (1990) J. Immunol , vol.144 , pp. 3166-3173
    • Hamann, K.J.1    Gleich, G.J.2    Checkel, J.L.3    Loegering, D.A.4    McCall, J.W.5    Barker, R.L.6
  • 10
    • 0023846221 scopus 로고
    • Toxic effects produced or mediated by human eosinophil granule components on Trypanosoma cruzi
    • Molina, H. A., Kierszenbaum, F., Hamann, K. J., Gleich, G. J. (1988) Toxic effects produced or mediated by human eosinophil granule components on Trypanosoma cruzi. Am. J. Trop. Med. Hyg. 38, 327-334.
    • (1988) Am. J. Trop. Med. Hyg , vol.38 , pp. 327-334
    • Molina, H.A.1    Kierszenbaum, F.2    Hamann, K.J.3    Gleich, G.J.4
  • 11
    • 0023358395 scopus 로고
    • Comparative toxicity of purified human eosinophil granule proteins for newborn larvae of Trichinella spiralis
    • Hamann, K. J., Barker, R. L., Loegering, D. A., Gleich, G. J. (1987) Comparative toxicity of purified human eosinophil granule proteins for newborn larvae of Trichinella spiralis. J. Parasitol. 73, 523-529.
    • (1987) J. Parasitol , vol.73 , pp. 523-529
    • Hamann, K.J.1    Barker, R.L.2    Loegering, D.A.3    Gleich, G.J.4
  • 12
    • 0022403203 scopus 로고
    • Comparative toxicity of purified human eosinophil granule cationic proteins for schistosomula of Schistosoma mansoni
    • Ackerman, S. J., Gleich, G. J., Loegering, D. A., Richardson, B. A., Butterworth, A. E. (1985) Comparative toxicity of purified human eosinophil granule cationic proteins for schistosomula of Schistosoma mansoni. Am. J. Trop. Med. Hyg. 34, 735-745.
    • (1985) Am. J. Trop. Med. Hyg , vol.34 , pp. 735-745
    • Ackerman, S.J.1    Gleich, G.J.2    Loegering, D.A.3    Richardson, B.A.4    Butterworth, A.E.5
  • 13
    • 0023358395 scopus 로고
    • Comparative toxicity of purified human eosinophil granule proteins for newborn larvae of Trichinella spiralis
    • Hamann, K. J., Barker, R. L., Loegering, D. A., Gleich, G. J. (1987) Comparative toxicity of purified human eosinophil granule proteins for newborn larvae of Trichinella spiralis. J. Parasitol. 73, 523-529.
    • (1987) J. Parasitol , vol.73 , pp. 523-529
    • Hamann, K.J.1    Barker, R.L.2    Loegering, D.A.3    Gleich, G.J.4
  • 14
    • 0024385410 scopus 로고
    • Antibacterial properties of eosinophil major basic protein and eosinophil cationic protein
    • Lehrer, R. I., Szklarek, D., Barton, A., Ganz, T., Hamann, K. J., Gleich, G. J. (1989) Antibacterial properties of eosinophil major basic protein and eosinophil cationic protein. J. Immunol. 142, 4428-4434.
    • (1989) J. Immunol , vol.142 , pp. 4428-4434
    • Lehrer, R.I.1    Szklarek, D.2    Barton, A.3    Ganz, T.4    Hamann, K.J.5    Gleich, G.J.6
  • 15
    • 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
  • 18
    • 0034895072 scopus 로고    scopus 로고
    • Expression and purification of recombinant rat eosinophil-associated ribonucleases, homologues of human eosinophil cationic protein and eosinophil-derived neurotoxin, and their characterization
    • Nakajima, M., Hirakata, M., Nittoh, T., Ishihara, K., Ohuchi, K. (2001) Expression and purification of recombinant rat eosinophil-associated ribonucleases, homologues of human eosinophil cationic protein and eosinophil-derived neurotoxin, and their characterization. Int. Arch. Allergy Immunol. 125, 241-249.
    • (2001) Int. Arch. Allergy Immunol , vol.125 , pp. 241-249
    • Nakajima, M.1    Hirakata, M.2    Nittoh, T.3    Ishihara, K.4    Ohuchi, K.5
  • 19
    • 0038645277 scopus 로고    scopus 로고
    • Preparation of recombinant rat eosinophil-associated ribonuclease-1 and -2 and analysis of their biological activities
    • Ishihara, K., Asai, K., Nakajima, M., Mue, S., Ohuchi, K. (2003) Preparation of recombinant rat eosinophil-associated ribonuclease-1 and -2 and analysis of their biological activities. Biochim. Biophys. Acta 1638, 164-172.
    • (2003) Biochim. Biophys. Acta , vol.1638 , pp. 164-172
    • Ishihara, K.1    Asai, K.2    Nakajima, M.3    Mue, S.4    Ohuchi, K.5
  • 20
    • 0037340434 scopus 로고    scopus 로고
    • Angiogenins: A new class of microbicidal proteins involved in innate immunity
    • Hooper, L. V., Stappenbeck, T. S., Hong, C. V., Gordon, J. I. (2003) Angiogenins: a new class of microbicidal proteins involved in innate immunity. Nat. Immunol. 4, 269-273.
    • (2003) Nat. Immunol , vol.4 , pp. 269-273
    • Hooper, L.V.1    Stappenbeck, T.S.2    Hong, C.V.3    Gordon, J.I.4
  • 22
    • 0037195896 scopus 로고    scopus 로고
    • RNase 7, a novel innate immune defense antimicrobial protein of healthy human skin
    • Harder, J., Schröder, J. M. (2002) RNase 7, a novel innate immune defense antimicrobial protein of healthy human skin. J. Biol. Chem. 277, 46779-46784.
    • (2002) J. Biol. Chem , vol.277 , pp. 46779-46784
    • Harder, J.1    Schröder, J.M.2
  • 24
    • 33748742183 scopus 로고    scopus 로고
    • Evolution and function of leukocyte RNase A ribonucleases of the avian species, Gallus gallus
    • Nitto, T., Dyer, K. D., Czapiga, M., Rosenberg, H. F. (2006) Evolution and function of leukocyte RNase A ribonucleases of the avian species, Gallus gallus. J. Biol. Chem. 281, 25622-25634.
    • (2006) J. Biol. Chem , vol.281 , pp. 25622-25634
    • Nitto, T.1    Dyer, K.D.2    Czapiga, M.3    Rosenberg, H.F.4
  • 25
    • 34548305002 scopus 로고    scopus 로고
    • Zebrafish ribonucleases are bactericidal: Implications for the origin of vertebrate RNase A superfamily
    • Cho, S., Zhang, J. (2007) Zebrafish ribonucleases are bactericidal: implications for the origin of vertebrate RNase A superfamily. Mol. Biol. Evol. 24, 1259-1268.
    • (2007) Mol. Biol. Evol , vol.24 , pp. 1259-1268
    • Cho, S.1    Zhang, J.2
  • 26
    • 46949091102 scopus 로고
    • Studies on structure of ribonuclease
    • Hirs, C. H., Moore, S., Stein, W. H. (1956) Studies on structure of ribonuclease. Fed. Proc. 15, 840-848.
    • (1956) Fed. Proc , vol.15 , pp. 840-848
    • Hirs, C.H.1    Moore, S.2    Stein, W.H.3
  • 27
    • 0000106940 scopus 로고
    • The amino acid composition of ribonuclease
    • Hirs, C. H., Stein, W. H., Moore, S. (1954) The amino acid composition of ribonuclease. J. Biol. Chem. 211, 941-950.
    • (1954) J. Biol. Chem , vol.211 , pp. 941-950
    • Hirs, C.H.1    Stein, W.H.2    Moore, S.3
  • 28
    • 1642502542 scopus 로고
    • The isolation and characterization of ribonucleases from sheep pancreas
    • Aqvist, S. E., Anfinsen, C. B. (1959) The isolation and characterization of ribonucleases from sheep pancreas. J. Biol. Chem. 234, 1112-1117.
    • (1959) J. Biol. Chem , vol.234 , pp. 1112-1117
    • Aqvist, S.E.1    Anfinsen, C.B.2
  • 29
    • 0022372327 scopus 로고
    • Sequence of the cDNA and gene for angiogenin, a human angiogenesis factor
    • Kurachi, K., Davie, E. W., Strydom, D. J., Riordan, J. F., Vallee, B. L. (1985) Sequence of the cDNA and gene for angiogenin, a human angiogenesis factor. Biochemistry 24, 5494-5499.
    • (1985) Biochemistry , vol.24 , pp. 5494-5499
    • Kurachi, K.1    Davie, E.W.2    Strydom, D.J.3    Riordan, J.F.4    Vallee, B.L.5
  • 30
    • 0003458175 scopus 로고
    • Molecular cloning of the human eosinophil-derived neurotoxin: A member of the ribonuclease gene family
    • Rosenberg, H. F., Tenen, D. G., Ackerman, S. J. (1989) Molecular cloning of the human eosinophil-derived neurotoxin: a member of the ribonuclease gene family. Proc. Natl. Acad. Sci. USA 86, 4460-4464.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 4460-4464
    • Rosenberg, H.F.1    Tenen, D.G.2    Ackerman, S.J.3
  • 31
    • 0024436758 scopus 로고
    • Sequence of human eosinophil-derived neurotoxin cDNA: Identity of deduced amino acid sequence with human nonsecretory ribonucleases
    • Hamann, K. J., Barker, R. L., Loegering, D. A., Pease, L. R., Gleich, G. J. (1989) Sequence of human eosinophil-derived neurotoxin cDNA: identity of deduced amino acid sequence with human nonsecretory ribonucleases. Gene 83, 161-167.
    • (1989) Gene , vol.83 , pp. 161-167
    • Hamann, K.J.1    Barker, R.L.2    Loegering, D.A.3    Pease, L.R.4    Gleich, G.J.5
  • 32
    • 0024365717 scopus 로고
    • Eosinophil cationic protein cDNA. Comparison with other toxic cationic proteins and ribonucleases
    • Barker, R. L., Loegering, D. A., Ten, R. M., Hamann, K. J., Pease, L. R., Gleich, G. J. (1989) Eosinophil cationic protein cDNA. Comparison with other toxic cationic proteins and ribonucleases. J. Immunol. 143, 952-955.
    • (1989) J. Immunol , vol.143 , pp. 952-955
    • Barker, R.L.1    Loegering, D.A.2    Ten, R.M.3    Hamann, K.J.4    Pease, L.R.5    Gleich, G.J.6
  • 33
    • 0024308934 scopus 로고
    • Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity
    • Rosenberg, H. F., Ackerman, S. J., Tenen, D. G. (1989) Human eosinophil cationic protein. Molecular cloning of a cytotoxin and helminthotoxin with ribonuclease activity. J. Exp. Med. 170, 163-176.
    • (1989) J. Exp. Med , vol.170 , pp. 163-176
    • Rosenberg, H.F.1    Ackerman, S.J.2    Tenen, D.G.3
  • 35
    • 0025960523 scopus 로고
    • Amino acid sequence of an anti-tumor protein from Rana pipiens oocytes and early embryos. Homology to pancreatic ribonucleases
    • Ardelt, W., Mikulski, S. M., Shogen, K. (1991) Amino acid sequence of an anti-tumor protein from Rana pipiens oocytes and early embryos. Homology to pancreatic ribonucleases. J. Biol. Chem. 266, 245-251.
    • (1991) J. Biol. Chem , vol.266 , pp. 245-251
    • Ardelt, W.1    Mikulski, S.M.2    Shogen, K.3
  • 36
    • 0031691978 scopus 로고    scopus 로고
    • Introduction: The ribonuclease A superfamily
    • Beintema, J. J. (1998) Introduction: the ribonuclease A superfamily. Cell. Mol. Life Sci. 54, 763-765.
    • (1998) Cell. Mol. Life Sci , vol.54 , pp. 763-765
    • Beintema, J.J.1
  • 37
    • 33845351359 scopus 로고    scopus 로고
    • The RNase A superfamily: Generation of diversity and innate host defense
    • Dyer, K. D., Rosenberg, H. F. (2006) The RNase A superfamily: generation of diversity and innate host defense. Mol. Divers. 10, 585-597.
    • (2006) Mol. Divers , vol.10 , pp. 585-597
    • Dyer, K.D.1    Rosenberg, H.F.2
  • 38
    • 34547781750 scopus 로고    scopus 로고
    • Tamura, K, Dudley, J, Nei, M, Kumar, S, 2007 MEGA 4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24, 1596-1599
    • Tamura, K., Dudley, J., Nei, M., Kumar, S. (2007) MEGA 4: molecular evolutionary genetics analysis (MEGA) software version 4.0. Mol. Biol. Evol. 24, 1596-1599.
  • 39
    • 0242361715 scopus 로고    scopus 로고
    • Discovery in silico and characterization in vitro of novel genes exclusively expressed in the mouse epididymis
    • Penttinen, J., Pujianto, D. A., Sipila, P., Huhtaniemi, I., Poutanen, M. (2003) Discovery in silico and characterization in vitro of novel genes exclusively expressed in the mouse epididymis. Mol. Endocrinol. 17, 2138-2151.
    • (2003) Mol. Endocrinol , vol.17 , pp. 2138-2151
    • Penttinen, J.1    Pujianto, D.A.2    Sipila, P.3    Huhtaniemi, I.4    Poutanen, M.5
  • 41
    • 12844257490 scopus 로고    scopus 로고
    • The ribonuclease A superfamily of mammals and birds: Identifying new members and tracing evolutionary histories
    • Cho, S., Beintema, J. J., Zhang, J. (2005) The ribonuclease A superfamily of mammals and birds: identifying new members and tracing evolutionary histories. Genomics 85, 208-220.
    • (2005) Genomics , vol.85 , pp. 208-220
    • Cho, S.1    Beintema, J.J.2    Zhang, J.3
  • 43
    • 34249780819 scopus 로고    scopus 로고
    • Eosinophils: Singularly destructive effector cells or purveyors of immunoregulation?
    • Jacobsen, E. A., Taranova, A. G., Lee, N. A., Lee, J. J. (2007) Eosinophils: singularly destructive effector cells or purveyors of immunoregulation? J. Allergy Clin. Immunol. 119, 1313-1320.
    • (2007) J. Allergy Clin. Immunol , vol.119 , pp. 1313-1320
    • Jacobsen, E.A.1    Taranova, A.G.2    Lee, N.A.3    Lee, J.J.4
  • 44
    • 0347499617 scopus 로고    scopus 로고
    • The role of eosinophils in host defense against helminth parasites
    • Klion, A. D., Nutman, T. B. (2004) The role of eosinophils in host defense against helminth parasites. J. Allergy Clin. Immunol. 113, 30-37.
    • (2004) J. Allergy Clin. Immunol , vol.113 , pp. 30-37
    • Klion, A.D.1    Nutman, T.B.2
  • 45
    • 27744464663 scopus 로고    scopus 로고
    • Eosinophil degranulation: An evolutionary vestige or a universally destructive effector function?
    • Lee, J. J., Lee, N. A. (2005) Eosinophil degranulation: an evolutionary vestige or a universally destructive effector function? Clin. Exp. Allergy 35, 986-994.
    • (2005) Clin. Exp. Allergy , vol.35 , pp. 986-994
    • Lee, J.J.1    Lee, N.A.2
  • 46
    • 0022646701 scopus 로고
    • Biochemical properties of the eosinophil cationic protein and demonstration of its biosynthesis in vitro in marrow cells from patients with an eosinophilia
    • Olsson, I., Persson, A. M., Winqvist, I. (1986) Biochemical properties of the eosinophil cationic protein and demonstration of its biosynthesis in vitro in marrow cells from patients with an eosinophilia. Blood 67, 498-503.
    • (1986) Blood , vol.67 , pp. 498-503
    • Olsson, I.1    Persson, A.M.2    Winqvist, I.3
  • 48
    • 0001633426 scopus 로고
    • Biochemical and functional similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein: Homology with ribonuclease
    • Gleich, G. J., Loegering, D. A., Bell, M. P., Checkel, J. L., Ackerman, S. J., McKean, D. J. (1986) Biochemical and functional similarities between human eosinophil-derived neurotoxin and eosinophil cationic protein: homology with ribonuclease. Proc. Natl. Acad. Sci. USA 83, 3146-3150.
    • (1986) Proc. Natl. Acad. Sci. USA , vol.83 , pp. 3146-3150
    • Gleich, G.J.1    Loegering, D.A.2    Bell, M.P.3    Checkel, J.L.4    Ackerman, S.J.5    McKean, D.J.6
  • 49
    • 0023003622 scopus 로고
    • Ribonuclease activity associated with human eosinophil-derived neurotoxin and eosinophil cationic protein
    • Slifman, N. R., Loegering, D. A., McKean, D. J., Gleich, G. J. (1986) Ribonuclease activity associated with human eosinophil-derived neurotoxin and eosinophil cationic protein. J. Immunol. 137, 2913-2917.
    • (1986) J. Immunol , vol.137 , pp. 2913-2917
    • Slifman, N.R.1    Loegering, D.A.2    McKean, D.J.3    Gleich, G.J.4
  • 50
    • 0029041577 scopus 로고
    • Rapid evolution of a unique family of primate ribonuclease genes
    • Rosenberg, H. F., Dyer, K. D., Tiffany, H. L., Gonzalez, M. (1995) Rapid evolution of a unique family of primate ribonuclease genes. Nat. Genet. 10, 219-223.
    • (1995) Nat. Genet , vol.10 , pp. 219-223
    • Rosenberg, H.F.1    Dyer, K.D.2    Tiffany, H.L.3    Gonzalez, M.4
  • 51
    • 0033507441 scopus 로고    scopus 로고
    • Eosinophils, ribonucleases and host defense: Solving the puzzle
    • Rosenberg, H. F., Domachowske, J. B. (1999) Eosinophils, ribonucleases and host defense: solving the puzzle. Immunol. Res. 20, 261-274.
    • (1999) Immunol. Res , vol.20 , pp. 261-274
    • Rosenberg, H.F.1    Domachowske, J.B.2
  • 52
    • 0029120329 scopus 로고
    • Eosinophil cationic protein and eosinophil-derived neurotoxin. Evolution of novel function in a primate ribonuclease gene family
    • Rosenberg, H. F., Dyer, K. D. (1995) Eosinophil cationic protein and eosinophil-derived neurotoxin. Evolution of novel function in a primate ribonuclease gene family. J. Biol. Chem. 270, 21539-21544.
    • (1995) J. Biol. Chem , vol.270 , pp. 21539-21544
    • Rosenberg, H.F.1    Dyer, K.D.2
  • 53
    • 0029965581 scopus 로고    scopus 로고
    • Two highly homologous ribonuclease genes expressed in mouse eosinophils identify a larger subgroup of the mammalian ribonuclease superfamily
    • Larson, K. A., Olson, E. V., Madden, B. J., Gleich, G. J., Lee, N. A., Lee, J. J. (1996) Two highly homologous ribonuclease genes expressed in mouse eosinophils identify a larger subgroup of the mammalian ribonuclease superfamily. Proc. Natl. Acad. Sci. USA 93, 12370-12375.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 12370-12375
    • Larson, K.A.1    Olson, E.V.2    Madden, B.J.3    Gleich, G.J.4    Lee, N.A.5    Lee, J.J.6
  • 54
    • 0034712830 scopus 로고    scopus 로고
    • Evolution of the rodent eosinophil-associated RNase gene family by rapid gene sorting and positive selection
    • Zhang, J., Dyer, K. D., Rosenberg, H. F. (2000) Evolution of the rodent eosinophil-associated RNase gene family by rapid gene sorting and positive selection. Proc. Natl. Acad. Sci. USA 97, 4701-4706.
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4701-4706
    • Zhang, J.1    Dyer, K.D.2    Rosenberg, H.F.3
  • 55
    • 34548010262 scopus 로고    scopus 로고
    • The 434(G>C) polymorphism within the coding sequence of eosinophil cationic protein (ECP) correlates with the natural course of Schistosoma mansoni infection
    • Eriksson, J., Reimert, C. M., Kabatereine, N. B., Kazibwe, F., Ireri, E., Kadzo, H., Eltahir, H. B., Mohamed, A. O., Vennervald, B. J., Venge, P. (2007) The 434(G>C) polymorphism within the coding sequence of eosinophil cationic protein (ECP) correlates with the natural course of Schistosoma mansoni infection. Int. J. Parasitol. 37, 1359-1366.
    • (2007) Int. J. Parasitol , vol.37 , pp. 1359-1366
    • Eriksson, J.1    Reimert, C.M.2    Kabatereine, N.B.3    Kazibwe, F.4    Ireri, E.5    Kadzo, H.6    Eltahir, H.B.7    Mohamed, A.O.8    Vennervald, B.J.9    Venge, P.10
  • 56
    • 0034528906 scopus 로고    scopus 로고
    • Sequence variation at two eosinophil-associated ribonuclease loci in humans
    • Zhang, J., Rosenberg, H. F. (2000) Sequence variation at two eosinophil-associated ribonuclease loci in humans. Genetics 156, 1949-1958.
    • (2000) Genetics , vol.156 , pp. 1949-1958
    • Zhang, J.1    Rosenberg, H.F.2
  • 57
    • 33846423842 scopus 로고    scopus 로고
    • The functional heterogeneity of eosinophil cationic protein is determined by a gene polymorphism and post-translational modifications
    • Trulson, A., Byström, J., Engstrom, A., Larsson, R., Venge, P. (2007) The functional heterogeneity of eosinophil cationic protein is determined by a gene polymorphism and post-translational modifications. Clin. Exp. Allergy 37, 208-218.
    • (2007) Clin. Exp. Allergy , vol.37 , pp. 208-218
    • Trulson, A.1    Byström, J.2    Engstrom, A.3    Larsson, R.4    Venge, P.5
  • 58
    • 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
  • 59
    • 0022558797 scopus 로고
    • Mechanism of membrane damage mediated by human eosinophil cationic protein
    • Young, J. D., Peterson, C. G., Venge, P., Cohn, Z. A. (1986) Mechanism of membrane damage mediated by human eosinophil cationic protein. Nature 321, 613-616.
    • (1986) Nature , vol.321 , pp. 613-616
    • Young, J.D.1    Peterson, C.G.2    Venge, P.3    Cohn, Z.A.4
  • 60
    • 0038661343 scopus 로고    scopus 로고
    • Both aromatic and cationic residues contribute to the membrane-lytic and bactericidal activity of eosinophil cationic protein
    • Carreras, E., Boix, E., Rosenberg, H. F., Cuchillo, C. M., Nogués, M. V. (2003) Both aromatic and cationic residues contribute to the membrane-lytic and bactericidal activity of eosinophil cationic protein. Biochemistry 42, 6636-6644.
    • (2003) Biochemistry , vol.42 , pp. 6636-6644
    • Carreras, E.1    Boix, E.2    Rosenberg, H.F.3    Cuchillo, C.M.4    Nogués, M.V.5
  • 62
    • 1642284891 scopus 로고    scopus 로고
    • Bactericidal cationic peptides can also function as bacteriolysis-inducing agents mimicking β-lactam antibiotics? it is enigmatic why this concept is consistently disregarded
    • Ginsburg, I. (2004) Bactericidal cationic peptides can also function as bacteriolysis-inducing agents mimicking β-lactam antibiotics? it is enigmatic why this concept is consistently disregarded. Med. Hypotheses 62, 367-374.
    • (2004) Med. Hypotheses , vol.62 , pp. 367-374
    • Ginsburg, I.1
  • 63
    • 34247645414 scopus 로고    scopus 로고
    • Mammalian antimicrobial proteins and peptides: Overview on the RNase A superfamily members involved in innate host defense
    • Boix, E., Nogués, M. V. (2007) Mammalian antimicrobial proteins and peptides: overview on the RNase A superfamily members involved in innate host defense. Mol. Biosyst. 3, 317-335.
    • (2007) Mol. Biosyst , vol.3 , pp. 317-335
    • Boix, E.1    Nogués, M.V.2
  • 64
    • 34548409182 scopus 로고    scopus 로고
    • Eosinophils contribute to innate antiviral immunity and promote clearance of respiratory syncytial virus
    • Phipps, S., Lam, C. E., Mahalingam, S., Newhouse, M., Ramirez, R., Rosenberg, H. F., Foster, P. S., Matthaei, K. I. (2007) Eosinophils contribute to innate antiviral immunity and promote clearance of respiratory syncytial virus. Blood 110, 1578-1586.
    • (2007) Blood , vol.110 , pp. 1578-1586
    • Phipps, S.1    Lam, C.E.2    Mahalingam, S.3    Newhouse, M.4    Ramirez, R.5    Rosenberg, H.F.6    Foster, P.S.7    Matthaei, K.I.8
  • 65
    • 11144332894 scopus 로고    scopus 로고
    • The pneumonia virus of mice infection model for severe respiratory syncytial virus infection: Identifying novel targets for therapeutic intervention
    • Rosenberg, H. F., Bonville, C. A., Easton, A. J., Domachowske, J. B. (2005) The pneumonia virus of mice infection model for severe respiratory syncytial virus infection: identifying novel targets for therapeutic intervention. Pharmacol. Ther. 105, 1-6.
    • (2005) Pharmacol. Ther , vol.105 , pp. 1-6
    • Rosenberg, H.F.1    Bonville, C.A.2    Easton, A.J.3    Domachowske, J.B.4
  • 67
    • 33747188606 scopus 로고    scopus 로고
    • Angiogenin: A review of the pathophysiology and potential clinical applications
    • Tello-Montoliu, A., Patel, J. V., Lip, G. Y. (2006) Angiogenin: a review of the pathophysiology and potential clinical applications. J. Thromb. Haemost. 4, 1864-1874.
    • (2006) J. Thromb. Haemost , vol.4 , pp. 1864-1874
    • Tello-Montoliu, A.1    Patel, J.V.2    Lip, G.Y.3
  • 68
    • 0036213175 scopus 로고    scopus 로고
    • Diversifying selection of the tumor-growth promoter angiogenin in primate evolution
    • Zhang, J., Rosenberg, H. F. (2002) Diversifying selection of the tumor-growth promoter angiogenin in primate evolution. Mol. Biol. Evol. 19, 438-445.
    • (2002) Mol. Biol. Evol , vol.19 , pp. 438-445
    • Zhang, J.1    Rosenberg, H.F.2
  • 69
    • 0037440095 scopus 로고    scopus 로고
    • Human RNase 7: A new cationic ribonuclease of the RNase A superfamily
    • Zhang, J., Dyer, K. D., Rosenberg, H. F. (2003) Human RNase 7: a new cationic ribonuclease of the RNase A superfamily. Nucleic Acids Res. 31, 602-607.
    • (2003) Nucleic Acids Res , vol.31 , pp. 602-607
    • Zhang, J.1    Dyer, K.D.2    Rosenberg, H.F.3
  • 70
    • 33947513637 scopus 로고    scopus 로고
    • The flexible and clustered lysine residues of human ribonuclease 7 are critical for membrane permeability and antimicrobial activity
    • Huang, Y. C., Lin, Y. M., Chang, T. W., Wu, S. J., Lee, Y. S., Chang, M. D., Chen, C., Wu, S. H., Liao, Y. D. (2007) The flexible and clustered lysine residues of human ribonuclease 7 are critical for membrane permeability and antimicrobial activity. J. Biol. Chem. 282, 4626-4633.
    • (2007) J. Biol. Chem , vol.282 , pp. 4626-4633
    • Huang, Y.C.1    Lin, Y.M.2    Chang, T.W.3    Wu, S.J.4    Lee, Y.S.5    Chang, M.D.6    Chen, C.7    Wu, S.H.8    Liao, Y.D.9
  • 71
    • 0036493226 scopus 로고    scopus 로고
    • RNase 8, a novel RNase A superfamily ribonuclease expressed uniquely in placenta
    • Zhang, J., Dyer, K. D., Rosenberg, H. F. (2002) RNase 8, a novel RNase A superfamily ribonuclease expressed uniquely in placenta. Nucleic Acids Res. 30, 1169-1175.
    • (2002) Nucleic Acids Res , vol.30 , pp. 1169-1175
    • Zhang, J.1    Dyer, K.D.2    Rosenberg, H.F.3
  • 73
    • 36749100831 scopus 로고    scopus 로고
    • The success of the RNase scaffold in the advance of biosciences and in evolution
    • Pizzo, E., D'Alessio, G. (2007) The success of the RNase scaffold in the advance of biosciences and in evolution. Gene 406, 8-12.
    • (2007) Gene , vol.406 , pp. 8-12
    • Pizzo, E.1    D'Alessio, G.2
  • 74
    • 33645761337 scopus 로고    scopus 로고
    • Ranpirnase - an antitumor ribonuclease: Its potential role in malignant mesothelioma
    • Pavlakis, N., Vogelzang, N. J. (2006) Ranpirnase - an antitumor ribonuclease: its potential role in malignant mesothelioma. Expert Opin. Biol. Ther. 6, 391-399.
    • (2006) Expert Opin. Biol. Ther , vol.6 , pp. 391-399
    • Pavlakis, N.1    Vogelzang, N.J.2
  • 75
    • 33344475705 scopus 로고    scopus 로고
    • Ribonucleases as a novel pro-apoptotic anticancer strategy: Review of the preclinical and clinical data for ranpirnase
    • Costanzi, J., Sidransky, D., Navon, A., Goldsweig, H. (2005) Ribonucleases as a novel pro-apoptotic anticancer strategy: review of the preclinical and clinical data for ranpirnase. Cancer Invest. 23, 643-650.
    • (2005) Cancer Invest , vol.23 , pp. 643-650
    • Costanzi, J.1    Sidransky, D.2    Navon, A.3    Goldsweig, H.4
  • 77
    • 0035006458 scopus 로고    scopus 로고
    • Rapid diversification of RNase A superfamily ribonucleases from the bullfrog, Rana catesbeiana
    • Rosenberg, H. F., Zhang, J., Liao, Y. D., Dyer, K. D. (2001) Rapid diversification of RNase A superfamily ribonucleases from the bullfrog, Rana catesbeiana. J. Mol. Evol. 53, 31-38.
    • (2001) J. Mol. Evol , vol.53 , pp. 31-38
    • Rosenberg, H.F.1    Zhang, J.2    Liao, Y.D.3    Dyer, K.D.4
  • 78


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.