메뉴 건너뛰기




Volumn 280, Issue 22, 2013, Pages 5841-5852

Towards the rational design of antimicrobial proteins: Single point mutations can switch on bactericidal and agglutinating activities on the RNase A superfamily lineage

Author keywords

antimicrobial peptides; eosinophil cationic protein; eosinophil derived neurotoxin; protein evolution; ribonuclease

Indexed keywords

BACTERIUM LIPOPOLYSACCHARIDE; EOSINOPHIL CATIONIC PROTEIN; EOSINOPHIL PROTEIN X; POLYPEPTIDE ANTIBIOTIC AGENT; RIBONUCLEASE A;

EID: 84886597087     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/febs.12506     Document Type: Article
Times cited : (19)

References (67)
  • 1
    • 0031697202 scopus 로고    scopus 로고
    • The ribonuclease A superfamily: General discussion
    • Beintema JJ, &, Kleineidam RG, (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
    • 80052710778 scopus 로고    scopus 로고
    • Bovine pancreatic ribonuclease: Fifty years of the first enzymatic reaction mechanism
    • Cuchillo CM, Nogues MV, &, Raines RT, (2011) Bovine pancreatic ribonuclease: fifty years of the first enzymatic reaction mechanism. Biochemistry 50, 7835-7841.
    • (2011) Biochemistry , vol.50 , pp. 7835-7841
    • Cuchillo, C.M.1    Nogues, M.V.2    Raines, R.T.3
  • 3
    • 77952950532 scopus 로고    scopus 로고
    • The eight human 'canonical' ribonucleases: Molecular diversity, catalytic properties, and special biological actions of the enzyme proteins
    • Sorrentino S, (2010) The eight human 'canonical' ribonucleases: molecular diversity, catalytic properties, and special biological actions of the enzyme proteins. FEBS Lett 584, 2194-2200.
    • (2010) FEBS Lett , vol.584 , pp. 2194-2200
    • Sorrentino, S.1
  • 4
    • 0001005285 scopus 로고    scopus 로고
    • Ribonuclease A
    • Raines RT, (1998) Ribonuclease A. Chem Rev 98, 1045-1066.
    • (1998) Chem Rev , vol.98 , pp. 1045-1066
    • Raines, R.T.1
  • 5
    • 34247645414 scopus 로고    scopus 로고
    • Mammalian antimicrobial proteins and peptides: Overview on the RNase A superfamily members involved in innate host defence
    • Boix E, &, Nogues MV, (2007) Mammalian antimicrobial proteins and peptides: overview on the RNase A superfamily members involved in innate host defence. Mol BioSyst 3, 317-335.
    • (2007) Mol BioSyst , vol.3 , pp. 317-335
    • Boix, E.1    Nogues, M.V.2
  • 6
    • 34548305002 scopus 로고    scopus 로고
    • Zebrafish ribonucleases are bactericidal: Implications for the origin of the vertebrate RNase A superfamily
    • Cho S, &, Zhang J, (2007) Zebrafish ribonucleases are bactericidal: implications for the origin of the 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
  • 7
    • 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
  • 8
    • 44649149642 scopus 로고    scopus 로고
    • RNase A ribonucleases and host defense: An evolving story
    • Rosenberg HF, (2008) RNase A ribonucleases and host defense: an evolving story. J Leukoc Biol 83, 1079-1087.
    • (2008) J Leukoc Biol , vol.83 , pp. 1079-1087
    • Rosenberg, H.F.1
  • 10
    • 84859706326 scopus 로고    scopus 로고
    • Antimicrobial activity of human eosinophil granule proteins: Involvement in host defence against pathogens
    • Malik A, &, Batra JK, (2012) Antimicrobial activity of human eosinophil granule proteins: involvement in host defence against pathogens. Crit Rev Microbiol 38, 168-181.
    • (2012) Crit Rev Microbiol , vol.38 , pp. 168-181
    • Malik, A.1    Batra, J.K.2
  • 11
    • 84869865730 scopus 로고    scopus 로고
    • Eosinophil extracellular DNA traps: Molecular mechanisms and potential roles in disease
    • Yousefi S, Simon D, &, Simon HU, (2012) Eosinophil extracellular DNA traps: molecular mechanisms and potential roles in disease. Curr Opin Immunol 24, 736-739.
    • (2012) Curr Opin Immunol , vol.24 , pp. 736-739
    • Yousefi, S.1    Simon, D.2    Simon, H.U.3
  • 12
    • 84874236075 scopus 로고    scopus 로고
    • The expanding world of extracellular traps: Not only neutrophils but much more
    • Goldmann O, &, Medina E, (2013) The expanding world of extracellular traps: not only neutrophils but much more. Front Immunol 3, 420.
    • (2013) Front Immunol , vol.3 , pp. 420
    • Goldmann, O.1    Medina, E.2
  • 13
    • 0029041577 scopus 로고
    • Rapid evolution of a unique family of primate ribonuclease genes
    • Rosenberg HF, Dyer KD, Tiffany HL, &, 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
  • 14
    • 0032584099 scopus 로고    scopus 로고
    • Positive Darwinian selection after gene duplication in primate ribonuclease genes
    • Zhang J, Rosenberg HF, &, Nei M, (1998) Positive Darwinian selection after gene duplication in primate ribonuclease genes. Proc Natl Acad Sci USA 95, 3708-3713.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 3708-3713
    • Zhang, J.1    Rosenberg, H.F.2    Nei, M.3
  • 15
    • 0025110837 scopus 로고
    • Structure and chromosome localization of the human eosinophil-derived neurotoxin and eosinophil cationic protein genes: Evidence for intronless coding sequences in the ribonuclease gene superfamily
    • Hamann KJ, Ten RM, Loegering DA, Jenkins RB, Heise MT, Schad CR, Pease LR, Gleich GJ, &, Barker RL, (1990) Structure and chromosome localization of the human eosinophil-derived neurotoxin and eosinophil cationic protein genes: evidence for intronless coding sequences in the ribonuclease gene superfamily. Genomics 7, 535-546.
    • (1990) Genomics , vol.7 , pp. 535-546
    • Hamann, K.J.1    Ten, R.M.2    Loegering, D.A.3    Jenkins, R.B.4    Heise, M.T.5    Schad, C.R.6    Pease, L.R.7    Gleich, G.J.8    Barker, R.L.9
  • 16
    • 0037117541 scopus 로고    scopus 로고
    • Complementary advantageous substitutions in the evolution of an antiviral RNase of higher primates
    • Zhang J, &, Rosenberg HF, (2002) Complementary advantageous substitutions in the evolution of an antiviral RNase of higher primates. Proc Natl Acad Sci USA 99, 5486-5491.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 5486-5491
    • Zhang, J.1    Rosenberg, H.F.2
  • 17
    • 33845351359 scopus 로고    scopus 로고
    • The RNase a superfamily: Generation of diversity and innate host defense
    • Dyer KD, &, Rosenberg HF, (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
  • 18
    • 84862259963 scopus 로고    scopus 로고
    • Structural determinants of the eosinophil cationic protein antimicrobial activity
    • Boix E, Salazar VA, Torrent M, Pulido D, Nogues MV, &, Moussaoui M, (2012) Structural determinants of the eosinophil cationic protein antimicrobial activity. Biol Chem 393, 801-815.
    • (2012) Biol Chem , vol.393 , pp. 801-815
    • Boix, E.1    Salazar, V.A.2    Torrent, M.3    Pulido, D.4    Nogues, M.V.5    Moussaoui, M.6
  • 19
    • 79955462769 scopus 로고    scopus 로고
    • Role of unique basic residues in cytotoxic, antibacterial and antiparasitic activities of human eosinophil cationic protein
    • Singh A, &, Batra JK, (2011) Role of unique basic residues in cytotoxic, antibacterial and antiparasitic activities of human eosinophil cationic protein. Biol Chem 392, 337-346.
    • (2011) Biol Chem , vol.392 , pp. 337-346
    • Singh, A.1    Batra, J.K.2
  • 21
    • 0031596883 scopus 로고    scopus 로고
    • Recombinant human eosinophil-derived neurotoxin/RNase 2 functions as an effective antiviral agent against respiratory syncytial virus
    • Domachowske JB, Dyer KD, Bonville CA, &, Rosenberg HF, (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
  • 22
    • 0026547094 scopus 로고
    • Eosinophil degranulation in the respiratory tract during naturally acquired respiratory syncytial virus infection
    • Garofalo R, Kimpen JL, Welliver RC, &, Ogra PL, (1992) Eosinophil degranulation in the respiratory tract during naturally acquired respiratory syncytial virus infection. J Pediatr 120, 28-32.
    • (1992) J Pediatr , vol.120 , pp. 28-32
    • Garofalo, R.1    Kimpen, J.L.2    Welliver, R.C.3    Ogra, P.L.4
  • 23
    • 0032989426 scopus 로고    scopus 로고
    • Respiratory syncytical virus-induced chemokine expression in the lower airways: Eosinophil recruitment and degranulation
    • Harrison AM, Bonville CA, Rosenberg HF, &, Domachowske JB, (1999) Respiratory syncytical virus-induced chemokine expression in the lower airways: eosinophil recruitment and degranulation. Am J Respir Crit Care Med 159, 1918-1924.
    • (1999) Am J Respir Crit Care Med , vol.159 , pp. 1918-1924
    • Harrison, A.M.1    Bonville, C.A.2    Rosenberg, H.F.3    Domachowske, J.B.4
  • 24
    • 84865001288 scopus 로고    scopus 로고
    • An insertion in loop L7 of human eosinophil-derived neurotoxin is crucial for its antiviral activity
    • Sikriwal D, Seth D, Parveen S, Malik A, Broor S, &, Batra JK, (2012) An insertion in loop L7 of human eosinophil-derived neurotoxin is crucial for its antiviral activity. J Cell Biochem 113, 3104-3112.
    • (2012) J Cell Biochem , vol.113 , pp. 3104-3112
    • Sikriwal, D.1    Seth, D.2    Parveen, S.3    Malik, A.4    Broor, S.5    Batra, J.K.6
  • 25
    • 0024385410 scopus 로고
    • Antibacterial properties of eosinophil major basic protein and eosinophil cationic protein
    • Lehrer RI, Szklarek D, Barton A, Ganz T, Hamann KJ, &, Gleich GJ, (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
  • 26
    • 0028931427 scopus 로고
    • Recombinant human eosinophil cationic protein. Ribonuclease activity is not essential for cytotoxicity
    • Rosenberg HF, (1995) Recombinant human eosinophil cationic protein. Ribonuclease activity is not essential for cytotoxicity. J Biol Chem 270, 7876-7881.
    • (1995) J Biol Chem , vol.270 , pp. 7876-7881
    • Rosenberg, H.F.1
  • 27
    • 0025274658 scopus 로고
    • In vitro killing of microfilariae of Brugia pahangi and Brugia malayi by eosinophil granule proteins
    • Hamann KJ, Gleich GJ, Checkel JL, Loegering DA, McCall JW, &, Barker RL, (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
  • 28
    • 0142151785 scopus 로고    scopus 로고
    • Eosinophil-derived neurotoxin (EDN), an antimicrobial protein with chemotactic activities for dendritic cells
    • Yang D, Rosenberg HF, Chen Q, Dyer KD, Kurosaka K, &, Oppenheim JJ, (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
  • 29
    • 47749113698 scopus 로고    scopus 로고
    • Eosinophil-derived neurotoxin/RNase 2: Connecting the past, the present and the future
    • Rosenberg HF, (2008) Eosinophil-derived neurotoxin/RNase 2: connecting the past, the present and the future. Curr Pharm Biotechnol 9, 135-140.
    • (2008) Curr Pharm Biotechnol , vol.9 , pp. 135-140
    • Rosenberg, H.F.1
  • 30
    • 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 HF, Rybak SM, Newton DL, Wang ZY, Fu Q, Tchernev VT, 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
  • 31
    • 38749088662 scopus 로고    scopus 로고
    • Eosinophil-derived neurotoxin acts as an alarmin to activate the TLR2-MyD88 signal pathway in dendritic cells and enhances Th2 immune responses
    • Yang D, Chen Q, Su SB, Zhang P, Kurosaka K, Caspi RR, Michalek SM, Rosenberg HF, Zhang N, &, Oppenheim JJ, (2008) Eosinophil-derived neurotoxin acts as an alarmin to activate the 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
  • 33
    • 0032865118 scopus 로고    scopus 로고
    • Eosinophil cationic protein (ECP): Molecular and biological properties and the use of ECP as a marker of eosinophil activation in disease
    • Venge P, Bystrom J, Carlson M, Hakansson L, Karawacjzyk M, Peterson C, Seveus L, &, Trulson A, (1999) Eosinophil cationic protein (ECP): molecular and biological properties and the use of ECP as a marker of eosinophil activation in disease. Clin Exp Allergy 29, 1172-1186.
    • (1999) Clin Exp Allergy , vol.29 , pp. 1172-1186
    • Venge, P.1    Bystrom, J.2    Carlson, M.3    Hakansson, L.4    Karawacjzyk, M.5    Peterson, C.6    Seveus, L.7    Trulson, A.8
  • 34
    • 78651349308 scopus 로고    scopus 로고
    • Analysing the eosinophil cationic protein - A clue to the function of the eosinophil granulocyte
    • Bystrom J, Amin K, &, Bishop-Bailey D, (2011) Analysing the eosinophil cationic protein-a clue to the function of the eosinophil granulocyte. Respir Res 12, 10.
    • (2011) Respir Res , vol.12 , pp. 10
    • Bystrom, J.1    Amin, K.2    Bishop-Bailey, D.3
  • 35
    • 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 HF, Cuchillo CM, &, Nogues MV, (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    Nogues, M.V.5
  • 36
    • 0021145733 scopus 로고
    • Schistosoma mansoni: Further studies of the interaction between schistosomula and granulocyte-derived cationic proteins in vitro
    • McLaren DJ, Peterson CG, &, Venge P, (1984) Schistosoma mansoni: further studies of the interaction between schistosomula and granulocyte-derived cationic proteins in vitro. Parasitology 88, 491-503.
    • (1984) Parasitology , vol.88 , pp. 491-503
    • McLaren, D.J.1    Peterson, C.G.2    Venge, P.3
  • 38
    • 0022636578 scopus 로고
    • Role of inflammatory cells in Chagas' disease. III. Kinetics of human eosinophil activation upon interaction with parasites (Trypanosoma cruzi)
    • Kierszenbaum F, Villalta F, &, Tai PC, (1986) Role of inflammatory cells in Chagas' disease. III. Kinetics of human eosinophil activation upon interaction with parasites (Trypanosoma cruzi). J Immunol 136, 662-666.
    • (1986) J Immunol , vol.136 , pp. 662-666
    • Kierszenbaum, F.1    Villalta, F.2    Tai, P.C.3
  • 40
    • 84880319676 scopus 로고    scopus 로고
    • Two human host defense ribonucleases against mycobacteria, the eosinophil cationic protein (RNase 3) and RNase 7
    • Pulido D, Torrent M, Andreu D, Nogués MV, &, Boix E, (2013) Two human host defense ribonucleases against mycobacteria, the eosinophil cationic protein (RNase 3) and RNase 7. Antimicrob Agents Chemother 57, 3797-3805.
    • (2013) Antimicrob Agents Chemother , vol.57 , pp. 3797-3805
    • Pulido, D.1    Torrent, M.2    Andreu, D.3    Nogués, M.V.4    Boix, E.5
  • 41
    • 69249227505 scopus 로고    scopus 로고
    • Bactericidal and membrane disruption activities of the eosinophil cationic protein are largely retained in an N-terminal fragment
    • Torrent M, de la Torre BG, Nogues VM, Andreu D, &, Boix E, (2009) Bactericidal and membrane disruption activities of the eosinophil cationic protein are largely retained in an N-terminal fragment. Biochem J 421, 425-434.
    • (2009) Biochem J , vol.421 , pp. 425-434
    • Torrent, M.1    De La Torre, B.G.2    Nogues, V.M.3    Andreu, D.4    Boix, E.5
  • 43
    • 20944447573 scopus 로고    scopus 로고
    • Surface-exposed amino acids of eosinophil cationic protein play a critical role in the inhibition of mammalian cell proliferation
    • Carreras E, Boix E, Navarro S, Rosenberg HF, Cuchillo CM, &, Nogues 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.
    • (2005) Mol Cell Biochem , vol.272 , pp. 1-7
    • Carreras, E.1    Boix, E.2    Navarro, S.3    Rosenberg, H.F.4    Cuchillo, C.M.5    Nogues, M.V.6
  • 44
    • 77955578891 scopus 로고    scopus 로고
    • Eosinophil cationic protein aggregation: Identification of an N-terminus amyloid prone region
    • Torrent M, Odorizzi F, Nogues MV, &, Boix E, (2010) Eosinophil cationic protein aggregation: identification of an N-terminus amyloid prone region. Biomacromolecules 11, 1983-1990.
    • (2010) Biomacromolecules , vol.11 , pp. 1983-1990
    • Torrent, M.1    Odorizzi, F.2    Nogues, M.V.3    Boix, E.4
  • 45
    • 84870827284 scopus 로고    scopus 로고
    • Exploring new biological functions of amyloids: Bacteria cell agglutination mediated by host protein aggregation
    • Torrent M, Pulido D, Nogues MV, &, Boix E, (2012) Exploring new biological functions of amyloids: bacteria cell agglutination mediated by host protein aggregation. PLoS Pathog 8, e1003005.
    • (2012) PLoS Pathog , vol.8
    • Torrent, M.1    Pulido, D.2    Nogues, M.V.3    Boix, E.4
  • 46
    • 40849124076 scopus 로고    scopus 로고
    • Eosinophil cationic protein high-affinity binding to bacteria-wall lipopolysaccharides and peptidoglycans
    • Torrent M, Navarro S, Moussaoui M, Nogues MV, &, Boix E, (2008) Eosinophil cationic protein high-affinity binding to bacteria-wall lipopolysaccharides and peptidoglycans. Biochemistry 47, 3544-3555.
    • (2008) Biochemistry , vol.47 , pp. 3544-3555
    • Torrent, M.1    Navarro, S.2    Moussaoui, M.3    Nogues, M.V.4    Boix, E.5
  • 47
    • 77956647384 scopus 로고    scopus 로고
    • Eosinophil-induced neurotoxicity: The role of eosinophil cationic protein/RNase 3
    • Navarro S, Boix E, Cuchillo CM, &, Nogues MV, (2010) Eosinophil-induced neurotoxicity: the role of eosinophil cationic protein/RNase 3. J Neuroimmunol 227, 60-70.
    • (2010) J Neuroimmunol , vol.227 , pp. 60-70
    • Navarro, S.1    Boix, E.2    Cuchillo, C.M.3    Nogues, M.V.4
  • 48
    • 0022558797 scopus 로고
    • Mechanism of membrane damage mediated by human eosinophil cationic protein
    • Young JD, Peterson CG, Venge P, &, Cohn ZA, (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
  • 49
    • 84860198236 scopus 로고    scopus 로고
    • Antimicrobial action and cell agglutination by the eosinophil cationic protein are modulated by the cell wall lipopolysaccharide structure
    • Pulido D, Moussaoui M, Andreu D, Nogues MV, Torrent M, &, Boix E, (2012) Antimicrobial action and cell agglutination by the eosinophil cationic protein are modulated by the cell wall lipopolysaccharide structure. Antimicrob Agents Chemother 56, 2378-2385.
    • (2012) Antimicrob Agents Chemother , vol.56 , pp. 2378-2385
    • Pulido, D.1    Moussaoui, M.2    Andreu, D.3    Nogues, M.V.4    Torrent, M.5    Boix, E.6
  • 51
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4.
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50, 760-763.
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 52
    • 0031717373 scopus 로고    scopus 로고
    • The eosinophil ribonucleases
    • Rosenberg HF, (1998) The eosinophil ribonucleases. Cell Mol Life Sci 54, 795-803.
    • (1998) Cell Mol Life Sci , vol.54 , pp. 795-803
    • Rosenberg, H.F.1
  • 55
    • 77958085274 scopus 로고    scopus 로고
    • Describing the mechanism of antimicrobial peptide action with the interfacial activity model
    • Wimley WC, (2010) Describing the mechanism of antimicrobial peptide action with the interfacial activity model. ACS Chem Biol 5, 905-917.
    • (2010) ACS Chem Biol , vol.5 , pp. 905-917
    • Wimley, W.C.1
  • 58
    • 80155128846 scopus 로고    scopus 로고
    • The generation of antimicrobial peptide activity: A trade-off between charge and aggregation?
    • Torrent M, Valle J, Nogués MV, Boix E, &, Andreu D, (2011) The generation of antimicrobial peptide activity: a trade-off between charge and aggregation? Angew Chem Int Ed Engl 50, 10686-10689.
    • (2011) Angew Chem Int Ed Engl , vol.50 , pp. 10686-10689
    • Torrent, M.1    Valle, J.2    Nogués, M.V.3    Boix, E.4    Andreu, D.5
  • 59
    • 79951801514 scopus 로고    scopus 로고
    • Connecting peptide physicochemical and antimicrobial properties by a rational prediction model
    • doi: 10.1371/journal.pone.0016968
    • Torrent M, Andreu D, Nogués VM, &, Boix E, (2011) Connecting peptide physicochemical and antimicrobial properties by a rational prediction model. PLoS One 6, e16968. doi: 10.1371/journal.pone.0016968
    • (2011) PLoS One , vol.6
    • Torrent, M.1    Andreu, D.2    Nogués, V.M.3    Boix, E.4
  • 60
    • 2642683177 scopus 로고    scopus 로고
    • Purification, primary structure, and antimicrobial activities of bovine apolipoprotein A-II
    • Motizuki M, Itoh T, Yamada M, Shimamura S, &, Tsurugi K, (1998) Purification, primary structure, and antimicrobial activities of bovine apolipoprotein A-II. J Biochem 123, 675-679.
    • (1998) J Biochem , vol.123 , pp. 675-679
    • Motizuki, M.1    Itoh, T.2    Yamada, M.3    Shimamura, S.4    Tsurugi, K.5
  • 62
    • 0033022636 scopus 로고    scopus 로고
    • Kinetic and product distribution analysis of human eosinophil cationic protein indicates a subsite arrangement that favors exonuclease-type activity
    • Boix E, Nikolovski Z, Moiseyev GP, Rosenberg HF, Cuchillo CM, &, Nogues MV, (1999) Kinetic and product distribution analysis of human eosinophil cationic protein indicates a subsite arrangement that favors exonuclease-type activity. J Biol Chem 274, 15605-15614.
    • (1999) J Biol Chem , vol.274 , pp. 15605-15614
    • Boix, E.1    Nikolovski, Z.2    Moiseyev, G.P.3    Rosenberg, H.F.4    Cuchillo, C.M.5    Nogues, M.V.6
  • 63
    • 0029871341 scopus 로고    scopus 로고
    • Role of the N-terminus in RNase A homologues: Differences in catalytic activity, ribonuclease inhibitor interaction and cytotoxicity
    • Boix E, Wu Y, Vasandani VM, Saxena SK, Ardelt W, Ladner J, &, Youle RJ, (1996) Role of the N-terminus in RNase A homologues: differences in catalytic activity, ribonuclease inhibitor interaction and cytotoxicity. J Mol Biol 257, 992-1007.
    • (1996) J Mol Biol , vol.257 , pp. 992-1007
    • Boix, E.1    Wu, Y.2    Vasandani, V.M.3    Saxena, S.K.4    Ardelt, W.5    Ladner, J.6    Youle, R.J.7
  • 64
    • 77949586101 scopus 로고    scopus 로고
    • Comparison of human RNase 3 and RNase 7 bactericidal action at the Gram-negative and Gram-positive bacterial cell wall
    • Torrent M, Badia M, Moussaoui M, Sanchez D, Nogues MV, &, Boix E, (2010) Comparison of human RNase 3 and RNase 7 bactericidal action at the Gram-negative and Gram-positive bacterial cell wall. FEBS J 277, 1713-1725.
    • (2010) FEBS J , vol.277 , pp. 1713-1725
    • Torrent, M.1    Badia, M.2    Moussaoui, M.3    Sanchez, D.4    Nogues, M.V.5    Boix, E.6
  • 65
    • 2942616397 scopus 로고    scopus 로고
    • Anti-endotoxin agents. 1. Development of a fluorescent probe displacement method optimized for the rapid identification of lipopolysaccharide-binding agents
    • Wood SJ, Miller KA, &, David SA, (2004) Anti-endotoxin agents. 1. Development of a fluorescent probe displacement method optimized for the rapid identification of lipopolysaccharide-binding agents. Comb Chem High Throughput Screen 7, 239-249.
    • (2004) Comb Chem High Throughput Screen , vol.7 , pp. 239-249
    • Wood, S.J.1    Miller, K.A.2    David, S.A.3
  • 67
    • 0037066104 scopus 로고    scopus 로고
    • Atomic resolution (0.98 Å) structure of eosinophil-derived neurotoxin
    • Swaminathan GJ, Holloway DE, Veluraja K, &, Acharya KR, (2002) Atomic resolution (0.98 Å) structure of eosinophil-derived neurotoxin. Biochemistry 41, 3341-3352.
    • (2002) Biochemistry , vol.41 , pp. 3341-3352
    • Swaminathan, G.J.1    Holloway, D.E.2    Veluraja, K.3    Acharya, K.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.