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Volumn 191, Issue 3, 2010, Pages 677-691

Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps

Author keywords

[No Author keywords available]

Indexed keywords

LEUKOCYTE ELASTASE; MYELOPEROXIDASE; SERINE PROTEINASE;

EID: 78049496216     PISSN: 00219525     EISSN: 00219525     Source Type: Journal    
DOI: 10.1083/jcb.201006052     Document Type: Article
Times cited : (1522)

References (70)
  • 1
    • 0035525791 scopus 로고    scopus 로고
    • Mutations in the ELA2 gene encoding neutrophil elastase are present in most patients with sporadic severe congenital neutropenia but only in some patients with the familial form of the disease
    • doi:10.1182/blood.V98.9.2645
    • Ancliff, P.J., R.E. Gale, R. Liesner, I.M. Hann, and D.C. Linch. 2001. Mutations in the ELA2 gene encoding neutrophil elastase are present in most patients with sporadic severe congenital neutropenia but only in some patients with the familial form of the disease. Blood. 98:2645-2650. doi:10.1182/blood. V98.9.2645
    • (2001) Blood , vol.98 , pp. 2645-2650
    • Ancliff, P.J.1    Gale, R.E.2    Liesner, R.3    Hann, I.M.4    Linch, D.C.5
  • 2
    • 0035479832 scopus 로고    scopus 로고
    • Mutations in the neutrophil elastase gene in cyclic and congenital neutropenia
    • doi:10.1016/S0952-7915(00)00254-5
    • Aprikyan, A.A., and D.C. Dale. 2001. Mutations in the neutrophil elastase gene in cyclic and congenital neutropenia. Curr. Opin. Immunol. 13:535-538. doi:10.1016/S0952-7915(00)00254-5
    • (2001) Curr. Opin. Immunol. , vol.13 , pp. 535-538
    • Aprikyan, A.A.1    Dale, D.C.2
  • 3
    • 0033041907 scopus 로고    scopus 로고
    • Severe impairment in early host defense against Candida albicans in mice deficient in myeloperoxidase
    • Aratani, Y., H. Koyama, S. Nyui, K. Suzuki, F. Kura, and N. Maeda. 1999. Severe impairment in early host defense against Candida albicans in mice deficient in myeloperoxidase. Infect. Immun. 67:1828-1836.
    • (1999) Infect. Immun. , vol.67 , pp. 1828-1836
    • Aratani, Y.1    Koyama, H.2    Nyui, S.3    Suzuki, K.4    Kura, F.5    Maeda, N.6
  • 4
    • 32944482526 scopus 로고    scopus 로고
    • An endonuclease allows Streptococcus pneumoniae to escape from neutrophil extracellular traps
    • doi:10.1016/j.cub.2006.01.056
    • Beiter, K., F. Wartha, B. Albiger, S. Normark, A. Zychlinsky, and B. Henriques- Normark. 2006. An endonuclease allows Streptococcus pneumoniae to escape from neutrophil extracellular traps. Curr. Biol. 16:401-407. doi:10.1016/j.cub.2006.01.056
    • (2006) Curr. Biol. , vol.16 , pp. 401-407
    • Beiter, K.1    Wartha, F.2    Albiger, B.3    Normark, S.4    Zychlinsky, A.5    Henriques- Normark, B.6
  • 5
    • 0036816820 scopus 로고    scopus 로고
    • Neutrophil elastase-mediated killing of bacteria: Lessons from targeted mutagenesis
    • DOI 10.1016/S1286-4579(02)01654-4, PII S1286457902016544
    • Belaaouaj, A. 2002. Neutrophil elastase-mediated killing of bacteria: lessons from targeted mutagenesis. Microbes Infect. 4:1259-1264. doi:10.1016/S1286-4579(02)01654-4 (Pubitemid 35435281)
    • (2002) Microbes and Infection , vol.4 , Issue.12 , pp. 1259-1264
    • Belaaouaj, A.1
  • 6
    • 0031836105 scopus 로고    scopus 로고
    • Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis
    • doi:10.1038/nm0598-615
    • Belaaouaj, A., R. McCarthy, M. Baumann, Z. Gao, T.J. Ley, S.N. Abraham, and S.D. Shapiro. 1998. Mice lacking neutrophil elastase reveal impaired host defense against gram negative bacterial sepsis. Nat. Med. 4:615-618. doi:10.1038/nm0598-615
    • (1998) Nat. Med. , vol.4 , pp. 615-618
    • Belaaouaj, A.1    McCarthy, R.2    Baumann, M.3    Gao, Z.4    Ley, T.J.5    Abraham, S.N.6    Shapiro, S.D.7
  • 7
    • 0034682860 scopus 로고    scopus 로고
    • Degradation of outer membrane protein a in Escherichia coli killing by neutrophil elastase
    • doi:10.1126/science.289.5482.1185
    • Belaaouaj, A., K.S. Kim, and S.D. Shapiro. 2000. Degradation of outer membrane protein A in Escherichia coli killing by neutrophil elastase. Science. 289:1185-1188. doi:10.1126/science.289.5482.1185
    • (2000) Science , vol.289 , pp. 1185-1188
    • Belaaouaj, A.1    Kim, K.S.2    Shapiro, S.D.3
  • 8
    • 0028964376 scopus 로고
    • DNA binds neutrophil elastase and mucus proteinase inhibitor and impairs their functional activity
    • doi:10.1016/0014-5793(95)00173-7
    • Belorgey, D., and J.G. Bieth. 1995. DNA binds neutrophil elastase and mucus proteinase inhibitor and impairs their functional activity. FEBS Lett. 361:265-268. doi:10.1016/0014-5793(95)00173-7
    • (1995) FEBS Lett. , vol.361 , pp. 265-268
    • Belorgey, D.1    Bieth, J.G.2
  • 11
    • 0030997435 scopus 로고    scopus 로고
    • Granules of the human neutrophilic polymorphonuclear leukocyte
    • Borregaard, N., and J.B. Cowland. 1997. Granules of the human neutrophilic polymorphonuclear leukocyte. Blood. 89:3503-3521.
    • (1997) Blood , vol.89 , pp. 3503-3521
    • Borregaard, N.1    Cowland, J.B.2
  • 12
    • 54949137644 scopus 로고    scopus 로고
    • Lysosomal membrane permeabilization in cell death
    • doi:10.1038/onc.2008.310
    • Boya, P., and G. Kroemer. 2008. Lysosomal membrane permeabilization in cell death. Oncogene. 27:6434-6451. doi:10.1038/onc.2008.310
    • (2008) Oncogene , vol.27 , pp. 6434-6451
    • Boya, P.1    Kroemer, G.2
  • 14
    • 32944465559 scopus 로고    scopus 로고
    • DNase expression allows the pathogen group a Streptococcus to escape killing in neutrophil extracellular traps
    • doi:10.1016/j.cub.2005.12.039
    • Buchanan, J.T., A.J. Simpson, R.K. Aziz, G.Y. Liu, S.A. Kristian, M. Kotb, J. Feramisco, and V. Nizet. 2006. DNase expression allows the pathogen group A Streptococcus to escape killing in neutrophil extracellular traps. Curr. Biol. 16:396-400. doi:10.1016/j.cub.2005.12.039
    • (2006) Curr. Biol. , vol.16 , pp. 396-400
    • Buchanan, J.T.1    Simpson, A.J.2    Aziz, R.K.3    Liu, G.Y.4    Kristian, S.A.5    Kotb, M.6    Feramisco, J.7    Nizet, V.8
  • 15
    • 14644388222 scopus 로고    scopus 로고
    • The dynamics of histone H1 function in chromatin
    • doi:10.1016/j.molcel.2005.02.019
    • Bustin, M., F. Catez, and J.H. Lim. 2005. The dynamics of histone H1 function in chromatin. Mol. Cell. 17:617-620. doi:10.1016/j.molcel.2005.02.019
    • (2005) Mol. Cell. , vol.17 , pp. 617-620
    • Bustin, M.1    Catez, F.2    Lim, J.H.3
  • 17
    • 0018255075 scopus 로고
    • Chronic granulomatous disease: Studies of a family with impaired neutrophil chemotactic, metabolic and bactericidal function
    • doi:10.1016/0002-9343(78)90745-3
    • Clark, F.A., and S.J. Klebanoff. 1978. Chronic granulomatous disease: studies of a family with impaired neutrophil chemotactic, metabolic and bactericidal function. Am. J. Med. 65:941-948. doi:10.1016/0002-9343(78)90745-3
    • (1978) Am. J. Med. , vol.65 , pp. 941-948
    • Clark, F.A.1    Klebanoff, S.J.2
  • 19
    • 0022503237 scopus 로고
    • The effect of the inhibitor diphenylene iodonium on the superoxide-generating system of neutrophils. Specific labelling of a component polypeptide of the oxidase
    • Cross, A.R., and O.T. Jones. 1986. The effect of the inhibitor diphenylene iodonium on the superoxide-generating system of neutrophils. Specific labelling of a component polypeptide of the oxidase. Biochem. J. 237:111-116.
    • (1986) Biochem. J. , vol.237 , pp. 111-116
    • Cross, A.R.1    Jones, O.T.2
  • 20
    • 0032556905 scopus 로고    scopus 로고
    • Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils
    • doi:10.1038/34923
    • Eiserich, J.P., M. Hristova, C.E. Cross, A.D. Jones, B.A. Freeman, B. Halliwell, and A. van der Vliet. 1998. Formation of nitric oxide-derived inflammatory oxidants by myeloperoxidase in neutrophils. Nature. 391:393-397. doi:10.1038/34923
    • (1998) Nature , vol.391 , pp. 393-397
    • Eiserich, J.P.1    Hristova, M.2    Cross, C.E.3    Jones, A.D.4    Freeman, B.A.5    Halliwell, B.6    Van Der Vliet, A.7
  • 25
    • 0002019504 scopus 로고    scopus 로고
    • Molecular chlorine generated by the myeloperoxidase-hydrogen peroxide-chloride system of phagocytes converts low density lipoprotein cholesterol into a family of chlorinated sterols
    • doi:10.1074/jbc.271.38.23080
    • Hazen, S.L., F.F. Hsu, K. Duffin, and J.W. Heinecke. 1996. Molecular chlorine generated by the myeloperoxidase-hydrogen peroxide-chloride system of phagocytes converts low density lipoprotein cholesterol into a family of chlorinated sterols. J. Biol. Chem. 271:23080-23088. doi:10.1074/jbc.271.38. 23080
    • (1996) J. Biol. Chem. , vol.271 , pp. 23080-23088
    • Hazen, S.L.1    Hsu, F.F.2    Duffin, K.3    Heinecke, J.W.4
  • 26
    • 0018399962 scopus 로고
    • Mast cell granule peroxidase: Location, secretion, and SRS-A inactivation
    • Henderson, W.R., and M. Kaliner. 1979. Mast cell granule peroxidase: location, secretion, and SRS-A inactivation. J. Immunol. 122:1322-1328.
    • (1979) J. Immunol. , vol.122 , pp. 1322-1328
    • Henderson, W.R.1    Kaliner, M.2
  • 27
    • 0023140258 scopus 로고
    • Tissue injury in inflammation. Oxidants, proteinases, and cationic proteins
    • doi:10.1172/JCI112869
    • Henson, P.M., and R.B. Johnston Jr. 1987. Tissue injury in inflammation. Oxidants, proteinases, and cationic proteins. J. Clin. Invest. 79:669-674. doi:10.1172/JCI112869
    • (1987) J. Clin. Invest. , vol.79 , pp. 669-674
    • Henson, P.M.1    Johnston Jr., R.B.2
  • 28
    • 1842556194 scopus 로고    scopus 로고
    • Deficiency in neutrophil elastase does not impair neutrophil recruitment to inflamed sites
    • doi:10.1165/rcmb.2003-0253OC
    • Hirche, T.O., J.J. Atkinson, S. Bahr, and A. Belaaouaj. 2004. Deficiency in neutrophil elastase does not impair neutrophil recruitment to inflamed sites. Am. J. Respir. Cell Mol. Biol. 30:576-584. doi:10.1165/rcmb.2003-0253OC
    • (2004) Am. J. Respir. Cell Mol. Biol. , vol.30 , pp. 576-584
    • Hirche, T.O.1    Atkinson, J.J.2    Bahr, S.3    Belaaouaj, A.4
  • 29
    • 0000220470 scopus 로고
    • Bactericidal action of histone
    • doi:10.1084/jem.108.6.925
    • Hirsch, J.G. 1958. Bactericidal action of histone. J. Exp. Med. 108:925-944. doi:10.1084/jem.108.6.925
    • (1958) J. Exp. Med. , vol.108 , pp. 925-944
    • Hirsch, J.G.1
  • 30
    • 33847395071 scopus 로고    scopus 로고
    • Neutrophil elastase in cyclic and severe congenital neutropenia
    • doi:10.1182/blood-2006-08-019166
    • Horwitz, M.S., Z. Duan, B. Korkmaz, H.H. Lee, M.E. Mealiffe, and S.J. Salipante. 2007. Neutrophil elastase in cyclic and severe congenital neutropenia. Blood. 109:1817-1824. doi:10.1182/blood-2006-08-019166
    • (2007) Blood , vol.109 , pp. 1817-1824
    • Horwitz, M.S.1    Duan, Z.2    Korkmaz, B.3    Lee, H.H.4    Mealiffe, M.E.5    Salipante, S.J.6
  • 31
    • 52449132868 scopus 로고    scopus 로고
    • Potential roles of histones in host defense as antimicrobial agents
    • Kawasaki, H., and S. Iwamuro. 2008. Potential roles of histones in host defense as antimicrobial agents. Infect. Disord. Drug Targets. 8:195-205.
    • (2008) Infect. Disord. Drug Targets , vol.8 , pp. 195-205
    • Kawasaki, H.1    Iwamuro, S.2
  • 33
    • 0031029267 scopus 로고    scopus 로고
    • Mechanism of inactivation of myeloperoxidase by 4-aminobenzoic acid hydrazide
    • Kettle, A.J., C.A. Gedye, and C.C. Winterbourn. 1997. Mechanism of inactivation of myeloperoxidase by 4-aminobenzoic acid hydrazide. Biochem. J. 321:503-508.
    • (1997) Biochem. J. , vol.321 , pp. 503-508
    • Kettle, A.J.1    Gedye, C.A.2    Winterbourn, C.C.3
  • 34
    • 0028265107 scopus 로고
    • Isolation and characterization of gelatinase granules from human neutrophils
    • Kjeldsen, L., H. Sengeløv, K. Lollike, M.H. Nielsen, and N. Borregaard. 1994. Isolation and characterization of gelatinase granules from human neutrophils. Blood. 83:1640-1649.
    • (1994) Blood , vol.83 , pp. 1640-1649
    • Kjeldsen, L.1    Sengeløv, H.2    Lollike, K.3    Nielsen, M.H.4    Borregaard, N.5
  • 37
    • 0025200926 scopus 로고
    • Antimicrobial polypeptides of human neutrophils
    • Lehrer, R.I., and T. Ganz. 1990. Antimicrobial polypeptides of human neutrophils. Blood. 76:2169-2181.
    • (1990) Blood , vol.76 , pp. 2169-2181
    • Lehrer, R.I.1    Ganz, T.2
  • 38
    • 0034619970 scopus 로고    scopus 로고
    • Immunodeficiency diseases caused by defects in phagocytes
    • doi:10.1056/NEJM200012073432307
    • Lekstrom-Himes, J.A., and J.I. Gallin. 2000. Immunodeficiency diseases caused by defects in phagocytes. N. Engl. J. Med. 343:1703-1714. doi:10.1056/NEJM200012073432307
    • (2000) N. Engl. J. Med. , vol.343 , pp. 1703-1714
    • Lekstrom-Himes, J.A.1    Gallin, J.I.2
  • 39
    • 0036775488 scopus 로고    scopus 로고
    • Role of mitochondrial inner membrane permeabilization in necrotic cell death, apoptosis, and autophagy
    • doi:10.1089/152308602760598918
    • Lemasters, J.J., T. Qian, L. He, J.S. Kim, S.P. Elmore, W.E. Cascio, and D.A. Brenner. 2002. Role of mitochondrial inner membrane permeabilization in necrotic cell death, apoptosis, and autophagy. Antioxid. Redox Signal. 4:769-781. doi:10.1089/152308602760598918
    • (2002) Antioxid. Redox Signal. , vol.4 , pp. 769-781
    • Lemasters, J.J.1    Qian, T.2    He, L.3    Kim, J.S.4    Elmore, S.P.5    Cascio, W.E.6    Brenner, D.A.7
  • 41
    • 0026564699 scopus 로고
    • Monoclonal autoantibodies to subnucleosomes from a MRL/Mp(-)+/+ mouse. Oligoclonality of the antibody response and recognition of a determinant composed of histones H2A, H2B, and DNA
    • Losman, M.J., T.M. Fasy, K.E. Novick, and M. Monestier. 1992. Monoclonal autoantibodies to subnucleosomes from a MRL/Mp(-)+/+ mouse. Oligoclonality of the antibody response and recognition of a determinant composed of histones H2A, H2B, and DNA. J. Immunol. 148:1561-1569.
    • (1992) J. Immunol. , vol.148 , pp. 1561-1569
    • Losman, M.J.1    Fasy, T.M.2    Novick, K.E.3    Monestier, M.4
  • 43
    • 0035832099 scopus 로고    scopus 로고
    • The discovery of a potent, intracellular, orally bioavailable, long duration inhibitor of human neutrophil elastase - GW311616A a development candidate
    • doi:10.1016/S0960-894X(01)00078-6
    • Macdonald, S.J., M.D. Dowle, L.A. Harrison, P. Shah, M.R. Johnson, G.G. Inglis, G.D. Clarke, R.A. Smith, D. Humphreys, C.R. Molloy, et al. 2001. The discovery of a potent, intracellular, orally bioavailable, long duration inhibitor of human neutrophil elastase - GW311616A a development candidate. Bioorg. Med. Chem. Lett. 11:895-898. doi:10.1016/S0960-894X(01)00078-6
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 895-898
    • Macdonald, S.J.1    Dowle, M.D.2    Harrison, L.A.3    Shah, P.4    Johnson, M.R.5    Inglis, G.G.6    Clarke, G.D.7    Smith, R.A.8    Humphreys, D.9    Molloy, C.R.10
  • 44
    • 33344468233 scopus 로고    scopus 로고
    • Neutrophils and immunity: Challenges and opportunities
    • doi:10.1038/nri1785
    • Nathan, C. 2006. Neutrophils and immunity: challenges and opportunities. Nat. Rev. Immunol. 6:173-182. doi:10.1038/nri1785
    • (2006) Nat. Rev. Immunol. , vol.6 , pp. 173-182
    • Nathan, C.1
  • 45
    • 34548588559 scopus 로고    scopus 로고
    • How human neutrophils kill and degrade microbes: An integrated view
    • doi:10.1111/j.1600-065X.2007.00550.x
    • Nauseef, W.M. 2007. How human neutrophils kill and degrade microbes: an integrated view. Immunol. Rev. 219:88-102. doi:10.1111/j.1600-065X.2007.00550.x
    • (2007) Immunol. Rev. , vol.219 , pp. 88-102
    • Nauseef, W.M.1
  • 46
    • 40749128547 scopus 로고    scopus 로고
    • Histone deimination as a response to inflammatory stimuli in neutrophils
    • Neeli, I., S.N. Khan, and M. Radic. 2008. Histone deimination as a response to inflammatory stimuli in neutrophils. J. Immunol. 180:1895-1902.
    • (2008) J. Immunol. , vol.180 , pp. 1895-1902
    • Neeli, I.1    Khan, S.N.2    Radic, M.3
  • 47
    • 3442892342 scopus 로고    scopus 로고
    • Localization of serglycin in human neutrophil granulocytes and their precursors
    • doi:10.1189/jlb.1003502
    • Niemann, C.U., J.B. Cowland, P. Klausen, J. Askaa, J. Calafat, and N. Borregaard. 2004. Localization of serglycin in human neutrophil granulocytes and their precursors. J. Leukoc. Biol. 76:406-415. doi:10.1189/jlb.1003502
    • (2004) J. Leukoc. Biol. , vol.76 , pp. 406-415
    • Niemann, C.U.1    Cowland, J.B.2    Klausen, P.3    Askaa, J.4    Calafat, J.5    Borregaard, N.6
  • 48
    • 70350029796 scopus 로고    scopus 로고
    • NETs: A new strategy for using old weapons
    • doi:10.1016/j.it.2009.07.011
    • Papayannopoulos, V., and A. Zychlinsky. 2009. NETs: a new strategy for using old weapons. Trends Immunol. 30:513-521. doi:10.1016/j.it.2009.07.011
    • (2009) Trends Immunol. , vol.30 , pp. 513-521
    • Papayannopoulos, V.1    Zychlinsky, A.2
  • 50
    • 0025776716 scopus 로고
    • Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase. Structural and functional properties
    • Rao, N.V., N.G. Wehner, B.C. Marshall, W.R. Gray, B.H. Gray, and J.R. Hoidal. 1991. Characterization of proteinase-3 (PR-3), a neutrophil serine proteinase. Structural and functional properties. J. Biol. Chem. 266:9540-9548.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9540-9548
    • Rao, N.V.1    Wehner, N.G.2    Marshall, B.C.3    Gray, W.R.4    Gray, B.H.5    Hoidal, J.R.6
  • 52
    • 0022432082 scopus 로고
    • The involvement of histone H1[0] in chromatin structure
    • doi:10.1093/nar/13.8.2843
    • Roche, J., J.L. Girardet, C. Gorka, and J.J. Lawrence. 1985. The involvement of histone H1[0] in chromatin structure. Nucleic Acids Res. 13:2843-2853. doi:10.1093/nar/13.8.2843
    • (1985) Nucleic Acids Res. , vol.13 , pp. 2843-2853
    • Roche, J.1    Girardet, J.L.2    Gorka, C.3    Lawrence, J.J.4
  • 53
    • 33745096897 scopus 로고    scopus 로고
    • The incidence of leukemia and mortality from sepsis in patients with severe congenital neutropenia receiving long-term G-CSF therapy
    • doi:10.1182/blood-2005-11-4370
    • Rosenberg, P.S., B.P. Alter, A.A. Bolyard, M.A. Bonilla, L.A. Boxer, B. Cham, C. Fier, M. Freedman, G. Kannourakis, S. Kinsey, et al. 2006. The incidence of leukemia and mortality from sepsis in patients with severe congenital neutropenia receiving long-term G-CSF therapy. Blood. 107:4628-4635. doi:10.1182/blood-2005-11-4370
    • (2006) Blood , vol.107 , pp. 4628-4635
    • Rosenberg, P.S.1    Alter, B.P.2    Bolyard, A.A.3    Bonilla, M.A.4    Boxer, L.A.5    Cham, B.6    Fier, C.7    Freedman, M.8    Kannourakis, G.9    Kinsey, S.10
  • 54
    • 17644377258 scopus 로고    scopus 로고
    • How neutrophils kill microbes
    • doi:10.1146/annurev.immunol.23.021704.115653
    • Segal, A.W. 2005. How neutrophils kill microbes. Annu. Rev. Immunol. 23:197-223. doi:10.1146/annurev.immunol.23.021704.115653
    • (2005) Annu. Rev. Immunol. , vol.23 , pp. 197-223
    • Segal, A.W.1
  • 55
    • 0023025461 scopus 로고
    • Complexes of heparin proteoglycans, chondroitin sulfate e proteoglycans, and [3H]diisopropyl fluorophosphate-binding proteins are exocytosed from activated mouse bone marrow-derived mast cells
    • Serafin, W.E., H.R. Katz, K.F. Austen, and R.L. Stevens. 1986. Complexes of heparin proteoglycans, chondroitin sulfate E proteoglycans, and [3H]diisopropyl fluorophosphate-binding proteins are exocytosed from activated mouse bone marrow-derived mast cells. J. Biol. Chem. 261:15017-15021.
    • (1986) J. Biol. Chem. , vol.261 , pp. 15017-15021
    • Serafin, W.E.1    Katz, H.R.2    Austen, K.F.3    Stevens, R.L.4
  • 56
    • 0024508002 scopus 로고
    • Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family
    • doi:10.1084/jem.169.5.1757
    • Ten, R.M., L.R. Pease, D.J. McKean, M.P. Bell, and G.J. Gleich. 1989. Molecular cloning of the human eosinophil peroxidase. Evidence for the existence of a peroxidase multigene family. J. Exp. Med. 169:1757-1769. doi:10.1084/jem.169.5.1757
    • (1989) J. Exp. Med. , vol.169 , pp. 1757-1769
    • Ten, R.M.1    Pease, L.R.2    McKean, D.J.3    Bell, M.P.4    Gleich, G.J.5
  • 57
    • 0034144636 scopus 로고    scopus 로고
    • Impaired immunity and enhanced resistance to endotoxin in the absence of neutrophil elastase and cathepsin G
    • doi:10.1016/S1074-7613(00)80173-9
    • Tkalcevic, J., M. Novelli, M. Phylactides, J.P. Iredale, A.W. Segal, and J. Roes. 2000. Impaired immunity and enhanced resistance to endotoxin in the absence of neutrophil elastase and cathepsin G. Immunity. 12:201-210. doi:10.1016/S1074-7613(00)80173-9
    • (2000) Immunity , vol.12 , pp. 201-210
    • Tkalcevic, J.1    Novelli, M.2    Phylactides, M.3    Iredale, J.P.4    Segal, A.W.5    Roes, J.6
  • 58
    • 32944463724 scopus 로고    scopus 로고
    • Neutrophil extracellular traps capture and kill Candida albicans yeast and hyphal forms
    • doi:10.1111/j.1462-5822.2005.00659.x
    • Urban, C.F., U. Reichard, V. Brinkmann, and A. Zychlinsky. 2006. Neutrophil extracellular traps capture and kill Candida albicans yeast and hyphal forms. Cell. Microbiol. 8:668-676. doi:10.1111/j.1462-5822.2005.00659.x
    • (2006) Cell. Microbiol. , vol.8 , pp. 668-676
    • Urban, C.F.1    Reichard, U.2    Brinkmann, V.3    Zychlinsky, A.4
  • 59
    • 73649099522 scopus 로고    scopus 로고
    • Neutrophil extracellular traps contain calprotectin, a cytosolic protein complex involved in host defense against Candida albicans
    • doi:10.1371/journal.ppat.1000639
    • Urban, C.F., D. Ermert, M. Schmid, U. Abu-Abed, C. Goosmann, W. Nacken, V. Brinkmann, P.R. Jungblut, and A. Zychlinsky. 2009. Neutrophil extracellular traps contain calprotectin, a cytosolic protein complex involved in host defense against Candida albicans. PLoS Pathog. 5:e1000639. doi:10.1371/journal.ppat. 1000639
    • (2009) PLoS Pathog. , vol.5
    • Urban, C.F.1    Ermert, D.2    Schmid, M.3    Abu-Abed, U.4    Goosmann, C.5    Nacken, W.6    Brinkmann, V.7    Jungblut, P.R.8    Zychlinsky, A.9
  • 60
    • 42449155517 scopus 로고    scopus 로고
    • Phagocytosis-independent antimicrobial activity of mast cells by means of extracellular trap formation
    • doi:10.1182/blood-2007-07-104018
    • von Köckritz-Blickwede, M., O. Goldmann, P. Thulin, K. Heinemann, A. Norrby- Teglund, M. Rohde, and E. Medina. 2008. Phagocytosis-independent antimicrobial activity of mast cells by means of extracellular trap formation. Blood. 111:3070-3080. doi:10.1182/blood-2007-07-104018
    • (2008) Blood , vol.111 , pp. 3070-3080
    • Von Köckritz-Blickwede, M.1    Goldmann, O.2    Thulin, P.3    Heinemann, K.4    Norrby- Teglund, A.5    Rohde, M.6    Medina, E.7
  • 63
    • 60849099332 scopus 로고    scopus 로고
    • Histone hypercitrullination mediates chromatin decondensation and neutrophil extracellular trap formation
    • doi:10.1083/jcb.200806072
    • Wang, Y., M. Li, S. Stadler, S. Correll, P. Li, D. Wang, R. Hayama, L. Leonelli, H. Han, S.A. Grigoryev, et al. 2009. Histone hypercitrullination mediates chromatin decondensation and neutrophil extracellular trap formation. J. Cell Biol. 184:205-213. doi:10.1083/jcb.200806072
    • (2009) J. Cell Biol. , vol.184 , pp. 205-213
    • Wang, Y.1    Li, M.2    Stadler, S.3    Correll, S.4    Li, P.5    Wang, D.6    Hayama, R.7    Leonelli, L.8    Han, H.9    Grigoryev, S.A.10
  • 64
    • 0037007656 scopus 로고    scopus 로고
    • Neutrophil elastase targets virulence factors of enterobacteria
    • doi:10.1038/417091a
    • Weinrauch, Y., D. Drujan, S.D. Shapiro, J. Weiss, and A. Zychlinsky. 2002. Neutrophil elastase targets virulence factors of enterobacteria. Nature. 417:91-94. doi:10.1038/417091a
    • (2002) Nature , vol.417 , pp. 91-94
    • Weinrauch, Y.1    Drujan, D.2    Shapiro, S.D.3    Weiss, J.4    Zychlinsky, A.5
  • 65
    • 0024602827 scopus 로고
    • Tissue destruction by neutrophils
    • doi:10.1056/NEJM198902093200606
    • Weiss, S.J. 1989. Tissue destruction by neutrophils. N. Engl. J. Med. 320:365-376. doi:10.1056/NEJM198902093200606
    • (1989) N. Engl. J. Med. , vol.320 , pp. 365-376
    • Weiss, S.J.1
  • 66
    • 70349643226 scopus 로고    scopus 로고
    • Extracellular DNA is required for root tip resistance to fungal infection
    • doi:10.1104/pp.109.142067
    • Wen, F., G.J. White, H.D. Van Etten, Z. Xiong, and M.C. Hawes. 2009. Extracellular DNA is required for root tip resistance to fungal infection. Plant Physiol. 151:820-829. doi:10.1104/pp.109.142067
    • (2009) Plant Physiol. , vol.151 , pp. 820-829
    • Wen, F.1    White, G.J.2    Van Etten, H.D.3    Xiong, Z.4    Hawes, M.C.5
  • 67
    • 0018085643 scopus 로고
    • A major serine protease in rat skeletal muscle: Evidence for its mast cell origin
    • doi:10.1073/pnas.75.11.5311
    • Woodbury, R.G., M. Everitt, Y. Sanada, N. Katunuma, D. Lagunoff, and H. Neurath. 1978. A major serine protease in rat skeletal muscle: evidence for its mast cell origin. Proc. Natl. Acad. Sci. USA. 75:5311-5313. doi:10.1073/pnas.75. 11.5311
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 5311-5313
    • Woodbury, R.G.1    Everitt, M.2    Sanada, Y.3    Katunuma, N.4    Lagunoff, D.5    Neurath, H.6
  • 68
    • 29244467484 scopus 로고    scopus 로고
    • Role of linker histone in chromatin structure and function: H1 stoichiometry and nucleosome repeat length
    • doi:10.1007/s10577-005-1024-3
    • Woodcock, C.L., A.I. Skoultchi, and Y. Fan. 2006. Role of linker histone in chromatin structure and function: H1 stoichiometry and nucleosome repeat length. Chromosome Res. 14:17-25. doi:10.1007/s10577-005-1024-3
    • (2006) Chromosome Res. , vol.14 , pp. 17-25
    • Woodcock, C.L.1    Skoultchi, A.I.2    Fan, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.