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Volumn 11, Issue 3, 2016, Pages 441-453

Histones as mediators of host defense, inflammation and thrombosis

Author keywords

antimicrobial peptides; histones; innate immunity; neutrophils; platelets

Indexed keywords

HISTONE; HISTONE H1; HISTONE H2A; HISTONE H2B; HISTONE H3; HISTONE H4; INFLAMMASOME; POLYPEPTIDE ANTIBIOTIC AGENT; SERINE PROTEINASE; THROMBIN; TOLL LIKE RECEPTOR; ANTIINFECTIVE AGENT;

EID: 84962434111     PISSN: 17460913     EISSN: 17460921     Source Type: Journal    
DOI: 10.2217/fmb.15.151     Document Type: Review
Times cited : (126)

References (109)
  • 1
    • 1842411320 scopus 로고    scopus 로고
    • Crystal structure of the nucleosome core particle at 2.8 A resolution
    • Luger K, Mader AW, Richmond RK, Sargent DF, Richmond TJ. Crystal structure of the nucleosome core particle at 2.8 A resolution. Nature 389(6648), 251-260 (1997).
    • (1997) Nature , vol.389 , Issue.6648 , pp. 251-260
    • Luger, K.1    Mader, A.W.2    Richmond, R.K.3    Sargent, D.F.4    Richmond, T.J.5
  • 2
    • 0019157001 scopus 로고
    • The structure of histone H1 and its location in chromatin
    • Allan J, Hartman PG, Crane-Robinson C, Aviles FX. The structure of histone H1 and its location in chromatin. Nature 288(5792), 675-679 (1980).
    • (1980) Nature , vol.288 , Issue.5792 , pp. 675-679
    • Allan, J.1    Hartman, P.G.2    Crane-Robinson, C.3    Aviles, F.X.4
  • 3
  • 4
    • 0025837183 scopus 로고
    • The nucleosomal core histone octamer at 3.1 A resolution: A tripartite protein assembly and a left-handed superhelix
    • Arents G, Burlingame RW, Wang BC, Love WE, Moudrianakis EN. The nucleosomal core histone octamer at 3.1 A resolution: a tripartite protein assembly and a left-handed superhelix. Proc. Natl Acad. Sci. USA 88(22), 10148-10152 (1991).
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , Issue.22 , pp. 10148-10152
    • Arents, G.1    Burlingame, R.W.2    Wang, B.C.3    Love, W.E.4    Moudrianakis, E.N.5
  • 5
    • 24744433805 scopus 로고    scopus 로고
    • Role of histone acetylation in the control of gene expression
    • Verdone L, Caserta M, Di Mauro E. Role of histone acetylation in the control of gene expression. Biochem. Cell Biol. 83(3), 344-353 (2005).
    • (2005) Biochem. Cell Biol , vol.83 , Issue.3 , pp. 344-353
    • Verdone, L.1    Caserta, M.2    Di Mauro, E.3
  • 6
    • 79952534189 scopus 로고    scopus 로고
    • Regulation of chromatin by histone modifications
    • Bannister AJ, Kouzarides T. Regulation of chromatin by histone modifications. Cell Res. 21(3), 381-395 (2011).
    • (2011) Cell Res , vol.21 , Issue.3 , pp. 381-395
    • Bannister, A.J.1    Kouzarides, T.2
  • 7
    • 84928130154 scopus 로고    scopus 로고
    • Epigenetics. Epigenetic inheritance uncoupled from sequence-specific recruitment
    • Ragunathan K, Jih G, Moazed D. Epigenetics. Epigenetic inheritance uncoupled from sequence-specific recruitment. Science 348(6230), 1258699 (2015).
    • (2015) Science , vol.348 , Issue.6230
    • Ragunathan, K.1    Jih, G.2    Moazed, D.3
  • 8
    • 10744233286 scopus 로고    scopus 로고
    • Involvement of histone H1.2 in apoptosis induced by DNA double-strand breaks
    • Konishi A, Shimizu S, Hirota J et al. Involvement of histone H1.2 in apoptosis induced by DNA double-strand breaks. Cell 114(6), 673-688 (2003).
    • (2003) Cell , vol.114 , Issue.6 , pp. 673-688
    • Konishi, A.1    Shimizu, S.2    Hirota, J.3
  • 9
    • 84896129831 scopus 로고    scopus 로고
    • The linker histone h1.2 is an intermediate in the apoptotic response to cytokine deprivation in T-effectors
    • Garg M, Perumalsamy LR, Shivashankar GV, Sarin A. The linker histone h1.2 is an intermediate in the apoptotic response to cytokine deprivation in T-effectors. Int. J. Cell. Biol. 2014, 674753 (2014).
    • (2014) Int. J. Cell. Biol , vol.2014
    • Garg, M.1    Perumalsamy, L.R.2    Shivashankar, G.V.3    Sarin, A.4
  • 10
    • 0034859839 scopus 로고    scopus 로고
    • Multiple pathways contribute to nuclear import of core histones
    • Muhlhausser P, Muller EC, Otto A, Kutay U. Multiple pathways contribute to nuclear import of core histones. EMBO J. 2(8), 690-696 (2001).
    • (2001) EMBO J , vol.2 , Issue.8 , pp. 690-696
    • Muhlhausser, P.1    Muller, E.C.2    Otto, A.3    Kutay, U.4
  • 12
    • 0029086911 scopus 로고
    • Extra-nuclear location of histones in activated human peripheral blood lymphocytes and cultured T-cells
    • Watson K, Edwards RJ, Shaunak S et al. Extra-nuclear location of histones in activated human peripheral blood lymphocytes and cultured T-cells. Biochem. Pharmacol. 50(3), 299-309 (1995).
    • (1995) Biochem. Pharmacol , vol.50 , Issue.3 , pp. 299-309
    • Watson, K.1    Edwards, R.J.2    Shaunak, S.3
  • 13
    • 84869508534 scopus 로고    scopus 로고
    • A novel role for lipid droplets in the organismal antibacterial response
    • Anand P, Cermelli S, Li Z et al. A novel role for lipid droplets in the organismal antibacterial response. eLife 1, e00003 (2012).
    • (2012) ELife , vol.1
    • Anand, P.1    Cermelli, S.2    Li, Z.3
  • 14
    • 34250220722 scopus 로고    scopus 로고
    • Isolation and characterization of antimicrobial proteins and peptide from chicken liver
    • Li GH, Mine Y, Hincke MT, Nys Y. Isolation and characterization of antimicrobial proteins and peptide from chicken liver. J. Pept. Sci. 13(6), 368-378 (2007).
    • (2007) J. Pept. Sci , vol.13 , Issue.6 , pp. 368-378
    • Li, G.H.1    Mine, Y.2    Hincke, M.T.3    Nys, Y.4
  • 15
    • 0030068934 scopus 로고    scopus 로고
    • A novel antimicrobial peptide from Bufo bufo gargarizans
    • Park CB, Kim MS, Kim SC. A novel antimicrobial peptide from Bufo bufo gargarizans. Biochem. Biophys. Res. Commun. 218(1), 408-413 (1996).
    • (1996) Biochem. Biophys. Res. Commun , vol.218 , Issue.1 , pp. 408-413
    • Park, C.B.1    Kim, M.S.2    Kim, S.C.3
  • 16
    • 0344495330 scopus 로고    scopus 로고
    • A protein with antimicrobial activity in the skin of Schlegel's green tree frog Rhacophorus schlegelii (Rhacophoridae) identified as histone H2B
    • Kawasaki H, Isaacson T, Iwamuro S, Conlon JM. A protein with antimicrobial activity in the skin of Schlegel's green tree frog Rhacophorus schlegelii (Rhacophoridae) identified as histone H2B. Biochem. Biophys. Res. Commun. 312(4), 1082-1086 (2003).
    • (2003) Biochem. Biophys. Res. Commun , vol.312 , Issue.4 , pp. 1082-1086
    • Kawasaki, H.1    Isaacson, T.2    Iwamuro, S.3    Conlon, J.M.4
  • 18
    • 0027191493 scopus 로고
    • Isolation and characterization of histogranin, a natural peptide with NMDA receptor antagonist activity
    • Lemaire S, Shukla VK, Rogers C et al. Isolation and characterization of histogranin, a natural peptide with NMDA receptor antagonist activity. Eur. J. Pharmacol. 245(3), 247-256 (1993).
    • (1993) Eur. J. Pharmacol , vol.245 , Issue.3 , pp. 247-256
    • Lemaire, S.1    Shukla, V.K.2    Rogers, C.3
  • 19
    • 70349158577 scopus 로고    scopus 로고
    • Histone H4 is a major component of the antimicrobial action of human sebocytes
    • Lee DY, Huang CM, Nakatsuji T et al. Histone H4 is a major component of the antimicrobial action of human sebocytes. J. Invest. Dermatol. 129(10), 2489-2496 (2009).
    • (2009) J. Invest. Dermatol , vol.129 , Issue.10 , pp. 2489-2496
    • Lee, D.Y.1    Huang, C.M.2    Nakatsuji, T.3
  • 20
    • 0031814274 scopus 로고    scopus 로고
    • Potential role of epithelial cell-derived histone H1 proteins in innate antimicrobial defense in the human gastrointestinal tract
    • Rose FR, Bailey K, Keyte JW, Chan WC, Greenwood D, Mahida YR. Potential role of epithelial cell-derived histone H1 proteins in innate antimicrobial defense in the human gastrointestinal tract. Infect. Immun. 66(7), 3255-3263 (1998).
    • (1998) Infect. Immun , vol.66 , Issue.7 , pp. 3255-3263
    • Rose, F.R.1    Bailey, K.2    Keyte, J.W.3    Chan, W.C.4    Greenwood, D.5    Mahida, Y.R.6
  • 22
    • 84872555329 scopus 로고    scopus 로고
    • Circulating histones are mediators of trauma-associated lung injury
    • Abrams ST, Zhang N, Manson J et al. Circulating histones are mediators of trauma-associated lung injury. Am. J. Respir. Crit. Care Med. 187(2), 160-169 (2013).
    • (2013) Am. J. Respir. Crit. Care Med , vol.187 , Issue.2 , pp. 160-169
    • Abrams, S.T.1    Zhang, N.2    Manson, J.3
  • 24
    • 0141563281 scopus 로고    scopus 로고
    • Inhibition of attachment of virions of Norwalk virus to mammalian cells by soluble histone molecules
    • Tamura M, Natori K, Kobayashi M, Miyamura T, Takeda N. Inhibition of attachment of virions of Norwalk virus to mammalian cells by soluble histone molecules. Arch. Virol. 148(9), 1659-1670 (2003).
    • (2003) Arch. Virol , vol.148 , Issue.9 , pp. 1659-1670
    • Tamura, M.1    Natori, K.2    Kobayashi, M.3    Miyamura, T.4    Takeda, N.5
  • 25
    • 0026357951 scopus 로고
    • H1 histones contribute to candidacidal activities of human epidermal extract
    • Kashima M. H1 histones contribute to candidacidal activities of human epidermal extract. J. Dermatol. 18(12), 695-706 (1991).
    • (1991) J. Dermatol , vol.18 , Issue.12 , pp. 695-706
    • Kashima, M.1
  • 26
    • 0042327762 scopus 로고    scopus 로고
    • Isolation and characterisation of oncorhyncin II, a histone H1-derived antimicrobial peptide from skin secretions of rainbow trout, Oncorhynchus mykiss
    • Fernandes JM, Molle G, Kemp GD, Smith VJ. Isolation and characterisation of oncorhyncin II, a histone H1-derived antimicrobial peptide from skin secretions of rainbow trout, Oncorhynchus mykiss. Dev. Comp. Immunol. 28(2), 127-138 (2004).
    • (2004) Dev. Comp. Immunol , vol.28 , Issue.2 , pp. 127-138
    • Fernandes, J.M.1    Molle, G.2    Kemp, G.D.3    Smith, V.J.4
  • 27
    • 19544375249 scopus 로고    scopus 로고
    • Proline conformationdependent antimicrobial activity of a proline-rich histone h1 N-terminal Peptide fragment isolated from the skin mucus of Atlantic salmon
    • Luders T, Birkemo GA, Nissen-Meyer J, Andersen O, Nes IF. Proline conformationdependent antimicrobial activity of a proline-rich histone h1 N-terminal Peptide fragment isolated from the skin mucus of Atlantic salmon. Antimicrob. Agents Chemother. 49(6), 2399-2406 (2005).
    • (2005) Antimicrob. Agents Chemother , vol.49 , Issue.6 , pp. 2399-2406
    • Luders, T.1    Birkemo, G.A.2    Nissen-Meyer, J.3    Andersen, O.4    Nes, I.F.5
  • 28
    • 0035038578 scopus 로고    scopus 로고
    • Synergy of histone-derived peptides of coho salmon with lysozyme and flounder pleurocidin
    • Patrzykat A, Zhang L, Mendoza V, Iwama GK, Hancock RE. Synergy of histone-derived peptides of coho salmon with lysozyme and flounder pleurocidin. Antimicrob. Agents Chemother. 45(5), 1337-1342 (2001).
    • (2001) Antimicrob. Agents Chemother , vol.45 , Issue.5 , pp. 1337-1342
    • Patrzykat, A.1    Zhang, L.2    Mendoza, V.3    Iwama, G.K.4    Hancock, R.E.5
  • 30
    • 1542287347 scopus 로고    scopus 로고
    • Neutrophil extracellular traps kill bacteria
    • Brinkmann V, Reichard U, Goosmann C et al. Neutrophil extracellular traps kill bacteria. Science 303(5663), 1532-1535 (2004).
    • (2004) Science , vol.303 , Issue.5663 , pp. 1532-1535
    • Brinkmann, V.1    Reichard, U.2    Goosmann, C.3
  • 31
    • 84942114244 scopus 로고    scopus 로고
    • Arginine-rich histones have strong antiviral activity for influenza A viruses
    • Hoeksema M, Tripathi S, White M et al. Arginine-rich histones have strong antiviral activity for influenza A viruses. Innate Immun. 21(7), 736-745 (2015).
    • (2015) Innate Immun , vol.21 , Issue.7 , pp. 736-745
    • Hoeksema, M.1    Tripathi, S.2    White, M.3
  • 32
    • 66149134072 scopus 로고    scopus 로고
    • Leishmania amazonensis promastigotes induce and are killed by neutrophil extracellular traps
    • Guimaraes-Costa AB, Nascimento MT, Froment GS et al. Leishmania amazonensis promastigotes induce and are killed by neutrophil extracellular traps. Proc. Natl Acad. Sci. USA 106(16), 6748-6753 (2009).
    • (2009) Proc. Natl Acad. Sci. USA , vol.106 , Issue.16 , pp. 6748-6753
    • Guimaraes-Costa, A.B.1    Nascimento, M.T.2    Froment, G.S.3
  • 33
    • 79952306488 scopus 로고    scopus 로고
    • Differential microbicidal effects of human histone proteins H2A and H2B on Leishmania promastigotes and amastigotes
    • Wang Y, Chen Y, Xin L et al. Differential microbicidal effects of human histone proteins H2A and H2B on Leishmania promastigotes and amastigotes. Infect. Immun. 79(3), 1124-1133 (2011).
    • (2011) Infect. Immun , vol.79 , Issue.3 , pp. 1124-1133
    • Wang, Y.1    Chen, Y.2    Xin, L.3
  • 34
    • 0042121501 scopus 로고    scopus 로고
    • Hipposin, a histone-derived antimicrobial peptide in Atlantic halibut (Hippoglossus hippoglossus L.)
    • Birkemo GA, Luders T, Andersen O, Nes IF, Nissen-Meyer J. Hipposin, a histone-derived antimicrobial peptide in Atlantic halibut (Hippoglossus hippoglossus L.). Biochim. Biophys. Acta 1646(1-2), 207-215 (2003).
    • (2003) Biochim. Biophys. Acta , vol.1646 , Issue.1-2 , pp. 207-215
    • Birkemo, G.A.1    Luders, T.2    Andersen, O.3    Nes, I.F.4    Nissen-Meyer, J.5
  • 35
    • 0032561422 scopus 로고    scopus 로고
    • Parasin i an antimicrobial peptide derived from histone H2A in the catfish Parasilurus asotus
    • Park IY, Park CB, Kim MS, Kim SC. Parasin I, an antimicrobial peptide derived from histone H2A in the catfish, Parasilurus asotus. FEBS Lett. 437(3), 258-262 (1998).
    • (1998) FEBS Lett , vol.437 , Issue.3 , pp. 258-262
    • Park, I.Y.1    Park, C.B.2    Kim, M.S.3    Kim, S.C.4
  • 36
    • 67649406168 scopus 로고    scopus 로고
    • Buforins: Histone H2A-derived antimicrobial peptides from toad stomach
    • Cho JH, Sung BH, Kim SC. Buforins: histone H2A-derived antimicrobial peptides from toad stomach. Biochim. Biophys. Acta 1788(8), 1564-1569 (2009).
    • (2009) Biochim. Biophys. Acta , vol.1788 , Issue.8 , pp. 1564-1569
    • Cho, J.H.1    Sung, B.H.2    Kim, S.C.3
  • 37
    • 0036514179 scopus 로고    scopus 로고
    • Cathepsin D produces antimicrobial peptide parasin i from histone H2A in the skin mucosa of fish
    • Cho JH, Park IY, Kim HS, Lee WT, Kim MS, Kim SC. Cathepsin D produces antimicrobial peptide parasin I from histone H2A in the skin mucosa of fish. FASEB J. 16(3), 429-431 (2002).
    • (2002) FASEB J , vol.16 , Issue.3 , pp. 429-431
    • Cho, J.H.1    Park, I.Y.2    Kim, H.S.3    Lee, W.T.4    Kim, M.S.5    Kim, S.C.6
  • 38
    • 0001439249 scopus 로고    scopus 로고
    • Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: The proline hinge is responsible for the cell-penetrating ability of buforin II
    • Park CB, Yi KS, Matsuzaki K, Kim MS, Kim SC. Structure-activity analysis of buforin II, a histone H2A-derived antimicrobial peptide: the proline hinge is responsible for the cell-penetrating ability of buforin II. Proc. Natl Acad. Sci. USA 97(15), 8245-8250 (2000).
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , Issue.15 , pp. 8245-8250
    • Park, C.B.1    Yi, K.S.2    Matsuzaki, K.3    Kim, M.S.4    Kim, S.C.5
  • 39
    • 80054064119 scopus 로고    scopus 로고
    • Antimicrobial properties of arginine- and lysine-rich histones and involvement of bacterial outer membrane protease T in their differential mode of actions
    • Tagai C, Morita S, Shiraishi T, Miyaji K, Iwamuro S. Antimicrobial properties of arginine- and lysine-rich histones and involvement of bacterial outer membrane protease T in their differential mode of actions. Peptides 32(10), 2003-2009 (2011).
    • (2011) Peptides , vol.32 , Issue.10 , pp. 2003-2009
    • Tagai, C.1    Morita, S.2    Shiraishi, T.3    Miyaji, K.4    Iwamuro, S.5
  • 40
    • 73849118671 scopus 로고    scopus 로고
    • Extrachromosomal histone H2B mediates innate antiviral immune responses induced by intracellular double-stranded DNA
    • Kobiyama K, Takeshita F, Jounai N et al. Extrachromosomal histone H2B mediates innate antiviral immune responses induced by intracellular double-stranded DNA. J. Virol. 84(2), 822-832 (2010).
    • (2010) J. Virol , vol.84 , Issue.2 , pp. 822-832
    • Kobiyama, K.1    Takeshita, F.2    Jounai, N.3
  • 41
    • 84883096593 scopus 로고    scopus 로고
    • Differential mode of antimicrobial actions of arginine-rich and lysine-rich histones against Gram-positive Staphylococcus aureus
    • Morita S, Tagai C, Shiraishi T, Miyaji K, Iwamuro S. Differential mode of antimicrobial actions of arginine-rich and lysine-rich histones against Gram-positive Staphylococcus aureus. Peptides 48, 75-82 (2013).
    • (2013) Peptides , vol.48 , pp. 75-82
    • Morita, S.1    Tagai, C.2    Shiraishi, T.3    Miyaji, K.4    Iwamuro, S.5
  • 42
    • 0028914936 scopus 로고
    • Histogranin, a modified histone H4 fragment endowed with N-methyl-d-aspartate antagonist and immunostimulatory activities
    • Lemaire S, Rogers C, Dumont M et al. Histogranin, a modified histone H4 fragment endowed with N-methyl-d-aspartate antagonist and immunostimulatory activities. Life Sci. 56(15), 1233-1241 (1995).
    • (1995) Life Sci , vol.56 , Issue.15 , pp. 1233-1241
    • Lemaire, S.1    Rogers, C.2    Dumont, M.3
  • 43
    • 53849108803 scopus 로고    scopus 로고
    • Antimicrobial effects of H4-(86-100), histogranin and related compounds-possible involvement of DNA gyrase
    • Lemaire S, Trinh TT, Le HT et al. Antimicrobial effects of H4-(86-100), histogranin and related compounds-possible involvement of DNA gyrase. FEBS J. 275(21), 5286-5297 (2008).
    • (2008) FEBS J , vol.275 , Issue.21 , pp. 5286-5297
    • Lemaire, S.1    Trinh Le, T.T.H.T.2
  • 44
    • 0001679690 scopus 로고
    • Antibacterial properties of protamine and histone
    • Miller BF, Abrams R, Dorfman A, Klein M. Antibacterial properties of protamine and histone. Science 96(2497), 428-430 (1942).
    • (1942) Science , vol.96 , Issue.2497 , pp. 428-430
    • Miller, B.F.1    Abrams, R.2    Dorfman, A.3    Klein, M.4
  • 45
    • 0000220470 scopus 로고
    • Bactericidal action of histone
    • Hirsch JG. Bactericidal action of histone. J. Exp. Med. 108(6), 925-944 (1958).
    • (1958) J. Exp. Med , vol.108 , Issue.6 , pp. 925-944
    • Hirsch, J.G.1
  • 46
    • 0036499180 scopus 로고    scopus 로고
    • Endotoxin-neutralizing antimicrobial proteins of the human placenta
    • Kim HS, Cho JH, Park HW, Yoon H, Kim MS, Kim SC. Endotoxin-neutralizing antimicrobial proteins of the human placenta. J. Immunol. 168(5), 2356-2364 (2002).
    • (2002) J. Immunol , vol.168 , Issue.5 , pp. 2356-2364
    • Kim, H.S.1    Cho, J.H.2    Park, H.W.3    Yoon, H.4    Kim, M.S.5    Kim, S.C.6
  • 47
    • 2242429813 scopus 로고    scopus 로고
    • Anti-microbial properties of histone H2A from skin secretions of rainbow trout Oncorhynchus mykiss
    • Fernandes JM, Kemp GD, Molle MG, Smith VJ. Anti-microbial properties of histone H2A from skin secretions of rainbow trout, Oncorhynchus mykiss. Biochem. J. 368(Pt 2), 611-620 (2002).
    • (2002) Biochem. J , vol.368 , pp. 611-620
    • Fernandes, J.M.1    Kemp, G.D.2    Molle, M.G.3    Smith, V.J.4
  • 48
    • 36749079320 scopus 로고    scopus 로고
    • Characterization of a hemolytic protein, identified as histone H4, from the skin of the Japanese tree frog Hyla japonica (Hylidae)
    • Kawasaki H, Iwamuro S, Goto Y, Nielsen PF, Conlon JM. Characterization of a hemolytic protein, identified as histone H4, from the skin of the Japanese tree frog Hyla japonica (Hylidae). Comp. Biochem. Physiol. B Biochem. Mol. Biol. 149(1), 120-125 (2008).
    • (2008) Comp. Biochem. Physiol. B Biochem. Mol. Biol , vol.149 , Issue.1 , pp. 120-125
    • Kawasaki, H.1    Iwamuro, S.2    Goto, Y.3    Nielsen, P.F.4    Conlon, J.M.5
  • 49
    • 0034194257 scopus 로고    scopus 로고
    • Large-scale synthesis and functional elements for the antimicrobial activity of defensins
    • Raj PA, Antonyraj KJ, Karunakaran T. Large-scale synthesis and functional elements for the antimicrobial activity of defensins. Biochem. J. 347 Pt 3, 633-641 (2000).
    • (2000) Biochem. J , vol.347 , pp. 633-641
    • Raj, P.A.1    Antonyraj, K.J.2    Karunakaran, T.3
  • 51
    • 84897397119 scopus 로고    scopus 로고
    • FAF and SufA: Proteins of Finegoldia magna that modulate the antibacterial activity of histones
    • Murphy EC, Mohanty T, Frick IM. FAF and SufA: proteins of Finegoldia magna that modulate the antibacterial activity of histones. J. Innate Immun. 6(3), 394-404 (2014).
    • (2014) J. Innate Immun , vol.6 , Issue.3 , pp. 394-404
    • Murphy, E.C.1    Mohanty, T.2    Frick, I.M.3
  • 52
    • 36949054570 scopus 로고
    • Effect of histones and protamine on the infectivity of Semliki Forest virus and its ribonucleic acid
    • Connolly JH. Effect of histones and protamine on the infectivity of Semliki Forest virus and its ribonucleic acid. Nature 212(5064), 858 (1966).
    • (1966) Nature , vol.212 , Issue.5064 , pp. 858
    • Connolly, J.H.1
  • 53
    • 32944463724 scopus 로고    scopus 로고
    • Neutrophil extracellular traps capture and kill Candida albicans yeast and hyphal forms
    • Urban CF, Reichard U, Brinkmann V, Zychlinsky A. Neutrophil extracellular traps capture and kill Candida albicans yeast and hyphal forms. Cell Microbiol. 8(4), 668-676 (2006).
    • (2006) Cell Microbiol , vol.8 , Issue.4 , pp. 668-676
    • Urban, C.F.1    Reichard, U.2    Brinkmann, V.3    Zychlinsky, A.4
  • 54
    • 0013994322 scopus 로고
    • Natural host resistance to infection with Cryptococcus neoformans. IV. the effect of some cationic proteins on the experimental disease
    • Gadebusch HH, Johnson AG. Natural host resistance to infection with Cryptococcus neoformans. IV. The effect of some cationic proteins on the experimental disease. J. Infect. Dis. 116(5), 551-565 (1966).
    • (1966) J. Infect. Dis , vol.116 , Issue.5 , pp. 551-565
    • Gadebusch, H.H.1    Johnson, A.G.2
  • 55
    • 52449132868 scopus 로고    scopus 로고
    • Potential roles of histones in host defense as antimicrobial agents
    • Kawasaki H, Iwamuro S. Potential roles of histones in host defense as antimicrobial agents. Infect. Disord. Drug Targets 8(3), 195-205 (2008).
    • (2008) Infect. Disord. Drug Targets , vol.8 , Issue.3 , pp. 195-205
    • Kawasaki, H.1    Iwamuro, S.2
  • 56
    • 0032489294 scopus 로고    scopus 로고
    • Mechanism of action of the antimicrobial peptide buforin II: Buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions
    • Park CB, Kim HS, Kim SC. Mechanism of action of the antimicrobial peptide buforin II: buforin II kills microorganisms by penetrating the cell membrane and inhibiting cellular functions. Biochem. Biophys. Res. Commun. 244(1), 253-257 (1998).
    • (1998) Biochem. Biophys. Res. Commun , vol.244 , Issue.1 , pp. 253-257
    • Park, C.B.1    Kim, H.S.2    Kim, S.C.3
  • 57
    • 43549102840 scopus 로고    scopus 로고
    • Investigating the nucleic acid interactions and antimicrobial mechanism of buforin II
    • Uyterhoeven ET, Butler CH, Ko D, Elmore DE. Investigating the nucleic acid interactions and antimicrobial mechanism of buforin II. FEBS Lett. 582(12), 1715-1718 (2008).
    • (2008) FEBS Lett , vol.582 , Issue.12 , pp. 1715-1718
    • Uyterhoeven, E.T.1    Butler, C.H.2    Ko, D.3    Elmore, D.E.4
  • 58
    • 44649183244 scopus 로고    scopus 로고
    • Structure- activity relations of parasin I, a histone H2A-derived antimicrobial peptide
    • Koo YS, Kim JM, Park IY et al. Structure- activity relations of parasin I, a histone H2A-derived antimicrobial peptide. Peptides 29(7), 1102-1108 (2008).
    • (2008) Peptides , vol.29 , Issue.7 , pp. 1102-1108
    • Koo, Y.S.1    Kim, J.M.2    Park, I.Y.3
  • 59
    • 84903692790 scopus 로고    scopus 로고
    • Modular analysis of hipposin, a histone-derived antimicrobial peptide consisting of membrane translocating and membrane permeabilizing fragments
    • Bustillo ME, Fischer AL, Labouyer MA, Klaips JA, Webb AC, Elmore DE. Modular analysis of hipposin, a histone-derived antimicrobial peptide consisting of membrane translocating and membrane permeabilizing fragments. Biochim. Biophys. Acta 1838(9), 2228-2233 (2014).
    • (2014) Biochim. Biophys. Acta , vol.1838 , Issue.9 , pp. 2228-2233
    • Bustillo, M.E.1    Fischer, A.L.2    Labouyer, M.A.3    Klaips, J.A.4    Webb, A.C.5    Elmore, D.E.6
  • 60
    • 17644377258 scopus 로고    scopus 로고
    • How neutrophils kill microbes
    • Segal AW. How neutrophils kill microbes. Annu. Rev. Immunol. 23, 197-223 (2005).
    • (2005) Annu. Rev. Immunol , vol.23 , pp. 197-223
    • Segal, A.W.1
  • 61
    • 84874223141 scopus 로고    scopus 로고
    • NET balancing: A problem in inflammatory lung diseases
    • Cheng OZ, Palaniyar N. NET balancing: a problem in inflammatory lung diseases. Front. Immunol. 4, 1 (2013).
    • (2013) Front. Immunol , vol.4 , Issue.1
    • Cheng, O.Z.1    Palaniyar, N.2
  • 62
    • 73649099522 scopus 로고    scopus 로고
    • Neutrophil extracellular traps contain calprotectin, a cytosolic protein complex involved in host defense against Candida albicans
    • Urban CF, Ermert D, Schmid M et al. Neutrophil extracellular traps contain calprotectin, a cytosolic protein complex involved in host defense against Candida albicans. PLoS Pathog. 5(10), e1000639 (2009).
    • (2009) PLoS Pathog , vol.5 , Issue.10
    • Urban, C.F.1    Ermert, D.2    Schmid, M.3
  • 63
    • 78049496216 scopus 로고    scopus 로고
    • Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps
    • Papayannopoulos V, Metzler KD, Hakkim A, Zychlinsky A. Neutrophil elastase and myeloperoxidase regulate the formation of neutrophil extracellular traps. J. Cell. Biol. 191(3), 677-691 (2010).
    • (2010) J. Cell. Biol , vol.191 , Issue.3 , pp. 677-691
    • Papayannopoulos, V.1    Metzler, K.D.2    Hakkim, A.3    Zychlinsky, A.4
  • 64
    • 84903719906 scopus 로고    scopus 로고
    • Deimination of linker histones links neutrophil extracellular trap release with autoantibodies in systemic autoimmunity
    • Dwivedi N, Neeli I, Schall N et al. Deimination of linker histones links neutrophil extracellular trap release with autoantibodies in systemic autoimmunity. FASEB J. 28(7), 2840-2851 (2014).
    • (2014) FASEB J , vol.28 , Issue.7 , pp. 2840-2851
    • Dwivedi, N.1    Neeli, I.2    Schall, N.3
  • 65
    • 84923838311 scopus 로고    scopus 로고
    • DNA is an antimicrobial component of neutrophil extracellular traps
    • Halverson TW, Wilton M, Poon KK, Petri B, Lewenza S. DNA is an antimicrobial component of neutrophil extracellular traps. PLoS Pathog. 11(1), e1004593 (2015).
    • (2015) PLoS Pathog , vol.11 , Issue.1
    • Halverson, T.W.1    Wilton, M.2    Poon, K.K.3    Petri, B.4    Lewenza, S.5
  • 66
    • 84925506325 scopus 로고    scopus 로고
    • Inhibition of PAD4 activity is sufficient to disrupt mouse and human NET formation
    • Lewis HD, Liddle J, Coote JE et al. Inhibition of PAD4 activity is sufficient to disrupt mouse and human NET formation. Nat. Chem. Biol. 11(3), 189-191 (2015).
    • (2015) Nat. Chem. Biol , vol.11 , Issue.3 , pp. 189-191
    • Lewis, H.D.1    Liddle, J.2    Coote, J.E.3
  • 67
    • 77956245423 scopus 로고    scopus 로고
    • PAD4 is essential for antibacterial innate immunity mediated by neutrophil extracellular traps
    • Li P, Li M, Lindberg MR, Kennett MJ, Xiong N, Wang Y. PAD4 is essential for antibacterial innate immunity mediated by neutrophil extracellular traps. J. Exp. Med. 207(9), 1853-1862 (2010).
    • (2010) J. Exp. Med , vol.207 , Issue.9 , pp. 1853-1862
    • Li, P.1    Li, M.2    Lindberg, M.R.3    Kennett, M.J.4    Xiong, N.5    Wang, Y.6
  • 68
    • 84925357077 scopus 로고    scopus 로고
    • PAD4-deficiency does not affect bacteremia in polymicrobial sepsis and ameliorates endotoxemic shock
    • Martinod K, Fuchs TA, Zitomersky NL et al. PAD4-deficiency does not affect bacteremia in polymicrobial sepsis and ameliorates endotoxemic shock. Blood 125(12), 1948-1956 (2015).
    • (2015) Blood , vol.125 , Issue.12 , pp. 1948-1956
    • Martinod, K.1    Fuchs, T.A.2    Zitomersky, N.L.3
  • 69
    • 84907494625 scopus 로고    scopus 로고
    • Proteases, neutrophils, and periodontitis: The NET effect
    • Nauseef WM. Proteases, neutrophils, and periodontitis: the NET effect. J. Clin. Invest. 124(10), 4237-4239 (2014).
    • (2014) J. Clin. Invest , vol.124 , Issue.10 , pp. 4237-4239
    • Nauseef, W.M.1
  • 70
    • 84907486038 scopus 로고    scopus 로고
    • Papillon-Lefevre syndrome patient reveals species-dependent requirements for neutrophil defenses
    • Sorensen OE, Clemmensen SN, Dahl SL et al. Papillon-Lefevre syndrome patient reveals species-dependent requirements for neutrophil defenses. J. Clin. Invest. 124(10), 4539-4548 (2014).
    • (2014) J. Clin. Invest , vol.124 , Issue.10 , pp. 4539-4548
    • Sorensen, O.E.1    Clemmensen, S.N.2    Dahl, S.L.3
  • 71
    • 78650636987 scopus 로고    scopus 로고
    • A novel mechanism of rapid nuclear neutrophil extracellular trap formation in response to Staphylococcus aureus
    • Pilsczek FH, Salina D, Poon KK et al. A novel mechanism of rapid nuclear neutrophil extracellular trap formation in response to Staphylococcus aureus. J. Immunol. 185(12), 7413-7425 (2010).
    • (2010) J. Immunol , vol.185 , Issue.12 , pp. 7413-7425
    • Pilsczek, F.H.1    Salina, D.2    Poon, K.K.3
  • 72
    • 84891505072 scopus 로고    scopus 로고
    • NETosis: How vital is it?
    • Yipp BG, Kubes P. NETosis: how vital is it? Blood 122(16), 2784-2794 (2013).
    • (2013) Blood , vol.122 , Issue.16 , pp. 2784-2794
    • Yipp, B.G.1    Kubes, P.2
  • 73
    • 84868632379 scopus 로고    scopus 로고
    • Infectioninduced NETosis is a dynamic process involving neutrophil multitasking in vivo
    • Yipp BG, Petri B, Salina D et al. Infectioninduced NETosis is a dynamic process involving neutrophil multitasking in vivo. Nat. Med. 18(9), 1386-1393 (2012).
    • (2012) Nat. Med , vol.18 , Issue.9 , pp. 1386-1393
    • Yipp, B.G.1    Petri, B.2    Salina, D.3
  • 74
    • 84924059048 scopus 로고    scopus 로고
    • SK3 channel and mitochondrial ROS mediate NADPH oxidase-independent NETosis induced by calcium influx
    • Douda DN, Khan MA, Grasemann H, Palaniyar N. SK3 channel and mitochondrial ROS mediate NADPH oxidase-independent NETosis induced by calcium influx. Proc. Natl Acad. Sci. USA 112(9), 2817-2822 (2015).
    • (2015) Proc. Natl Acad. Sci. USA , vol.112 , Issue.9 , pp. 2817-2822
    • Douda, D.N.1    Khan, M.A.2    Grasemann, H.3    Palaniyar, N.4
  • 75
    • 84868113151 scopus 로고    scopus 로고
    • Cytokines induced neutrophil extracellular traps formation: Implication for the inflammatory disease condition
    • Keshari RS, Jyoti A, Dubey M et al. Cytokines induced neutrophil extracellular traps formation: implication for the inflammatory disease condition. PLoS ONE 7(10), e48111 (2012).
    • (2012) PLoS ONE , vol.7 , Issue.10
    • Keshari, R.S.1    Jyoti, A.2    Dubey, M.3
  • 76
    • 84923838626 scopus 로고    scopus 로고
    • Virus-induced NETs-critical component of host defense or pathogenic mediator?
    • Jenne CN, Kubes P. Virus-induced NETs-critical component of host defense or pathogenic mediator? PLoS Pathog. 11(1), e1004546 (2015).
    • (2015) PLoS Pathog , vol.11 , Issue.1
    • Jenne, C.N.1    Kubes, P.2
  • 78
    • 80052510176 scopus 로고    scopus 로고
    • Excessive neutrophils and neutrophil extracellular traps contribute to acute lung injury of influenza pneumonitis
    • Narasaraju T, Yang E, Samy RP et al. Excessive neutrophils and neutrophil extracellular traps contribute to acute lung injury of influenza pneumonitis. Am. J. Pathol. 179(1), 199-210 (2011).
    • (2011) Am. J. Pathol , vol.179 , Issue.1 , pp. 199-210
    • Narasaraju, T.1    Yang, E.2    Samy, R.P.3
  • 79
    • 79960144716 scopus 로고    scopus 로고
    • PAD4-mediated neutrophil extracellular trap formation is not required for immunity against influenza infection
    • Hemmers S, Teijaro JR, Arandjelovic S, Mowen KA. PAD4-mediated neutrophil extracellular trap formation is not required for immunity against influenza infection. PLoS ONE 6(7), e22043 (2011).
    • (2011) PLoS ONE , vol.6 , Issue.7
    • Hemmers, S.1    Teijaro, J.R.2    Arandjelovic, S.3    Mowen, K.A.4
  • 80
    • 84873918079 scopus 로고    scopus 로고
    • Neutrophils recruited to sites of infection protect from virus challenge by releasing neutrophil extracellular traps
    • Jenne CN, Wong CH, Zemp FJ et al. Neutrophils recruited to sites of infection protect from virus challenge by releasing neutrophil extracellular traps. Cell Host Microbe 13(2), 169-180 (2013).
    • (2013) Cell Host Microbe , vol.13 , Issue.2 , pp. 169-180
    • Jenne, C.N.1    Wong, C.H.2    Zemp, F.J.3
  • 81
    • 84872723949 scopus 로고    scopus 로고
    • Neutrophil extracellular trap-associated protein activation of the NLRP3 inflammasome is enhanced in lupus macrophages
    • Kahlenberg JM, Carmona-Rivera C, Smith CK, Kaplan MJ. Neutrophil extracellular trap-associated protein activation of the NLRP3 inflammasome is enhanced in lupus macrophages. J. Immunol. 190(3), 1217-1226 (2013).
    • (2013) J. Immunol , vol.190 , Issue.3 , pp. 1217-1226
    • Kahlenberg, J.M.1    Carmona-Rivera, C.2    Smith, C.K.3    Kaplan, M.J.4
  • 82
    • 79952468782 scopus 로고    scopus 로고
    • Neutrophils activate plasmacytoid dendritic cells by releasing self-DNA-peptide complexes in systemic lupus erythematosus
    • Lande R, Ganguly D, Facchinetti V et al. Neutrophils activate plasmacytoid dendritic cells by releasing self-DNA-peptide complexes in systemic lupus erythematosus. Sci. Transl Med. 3(73), 73ra19 (2011).
    • (2011) Sci. Transl Med , vol.3 , Issue.73
    • Lande, R.1    Ganguly, D.2    Facchinetti, V.3
  • 83
    • 77953088427 scopus 로고    scopus 로고
    • Impairment of neutrophil extracellular trap degradation is associated with lupus nephritis
    • Hakkim A, Furnrohr BG, Amann K et al. Impairment of neutrophil extracellular trap degradation is associated with lupus nephritis. Proc. Natl Acad. Sci. USA 107(21), 9813-9818 (2010).
    • (2010) Proc. Natl Acad. Sci. USA , vol.107 , Issue.21 , pp. 9813-9818
    • Hakkim, A.1    Furnrohr, B.G.2    Amann, K.3
  • 84
    • 84871978237 scopus 로고    scopus 로고
    • Fighting against the dark side of neutrophil extracellular traps in disease: Manoeuvres for host protection
    • Saffarzadeh M, Preissner KT. Fighting against the dark side of neutrophil extracellular traps in disease: manoeuvres for host protection. Curr. Opin Hematol. 20(1), 3-9 (2013).
    • (2013) Curr. Opin Hematol , vol.20 , Issue.1 , pp. 3-9
    • Saffarzadeh, M.1    Preissner, K.T.2
  • 85
    • 77956426154 scopus 로고    scopus 로고
    • CXCR2 mediates NADPH oxidaseindependent neutrophil extracellular trap formation in cystic fibrosis airway inflammation
    • Marcos V, Zhou Z, Yildirim AO et al. CXCR2 mediates NADPH oxidaseindependent neutrophil extracellular trap formation in cystic fibrosis airway inflammation. Nat. Med. 16(9), 1018-1023 (2010).
    • (2010) Nat. Med , vol.16 , Issue.9 , pp. 1018-1023
    • Marcos, V.1    Zhou, Z.2    Yildirim, A.O.3
  • 86
    • 84930641094 scopus 로고    scopus 로고
    • Neutrophil extracellular trap (NET) formation characterises stable and exacerbated COPD and correlates with airflow limitation
    • Grabcanovic-Musija F, Obermayer A, Stoiber W et al. Neutrophil extracellular trap (NET) formation characterises stable and exacerbated COPD and correlates with airflow limitation. Respir. Res. 16, 59 (2015).
    • (2015) Respir. Res , vol.16 , Issue.59
    • Grabcanovic-Musija, F.1    Obermayer, A.2    Stoiber, W.3
  • 87
    • 84857591047 scopus 로고    scopus 로고
    • Neutrophil extracellular traps directly induce epithelial and endothelial cell death: A predominant role of histones
    • Saffarzadeh M, Juenemann C, Queisser MA et al. Neutrophil extracellular traps directly induce epithelial and endothelial cell death: a predominant role of histones. PLoS ONE 7(2), e32366 (2012).
    • (2012) PLoS ONE , vol.7 , Issue.2
    • Saffarzadeh, M.1    Juenemann, C.2    Queisser, M.A.3
  • 88
    • 84871196677 scopus 로고    scopus 로고
    • Extracellular histone release in response to traumatic injury: Implications for a compensatory role of activated protein C
    • Kutcher ME, Xu J, Vilardi RF, Ho C, Esmon CT, Cohen MJ. Extracellular histone release in response to traumatic injury: implications for a compensatory role of activated protein C. J. Trauma Acute Care Surg. 73(6), 1389-1394 (2012).
    • (2012) J. Trauma Acute Care Surg , vol.73 , Issue.6 , pp. 1389-1394
    • Kutcher, M.E.1    Xu, J.2    Vilardi, R.F.3    Ho, C.4    Esmon, C.T.5    Cohen, M.J.6
  • 89
    • 80052395881 scopus 로고    scopus 로고
    • Extracellular histones increase plasma thrombin generation by impairing thrombomodulin-dependent protein C activation
    • Ammollo CT, Semeraro F, Xu J, Esmon NL, Esmon CT. Extracellular histones increase plasma thrombin generation by impairing thrombomodulin-dependent protein C activation. J. Thromb. Haemost. 9(9), 1795-1803 (2011).
    • (2011) J. Thromb. Haemost , vol.9 , Issue.9 , pp. 1795-1803
    • Ammollo, C.T.1    Semeraro, F.2    Xu, J.3    Esmon, N.L.4    Esmon, C.T.5
  • 90
    • 80051884192 scopus 로고    scopus 로고
    • Extracellular histones promote thrombin generation through platelet-dependent mechanisms: Involvement of platelet TLR2 and TLR4
    • Semeraro F, Ammollo CT, Morrissey JH et al. Extracellular histones promote thrombin generation through platelet-dependent mechanisms: involvement of platelet TLR2 and TLR4. Blood 118(7), 1952-1961 (2011).
    • (2011) Blood , vol.118 , Issue.7 , pp. 1952-1961
    • Semeraro, F.1    Ammollo, C.T.2    Morrissey, J.H.3
  • 91
    • 84882257853 scopus 로고    scopus 로고
    • Blood levels of histone-complexed DNA fragments are associated with coagulopathy, inflammation and endothelial damage early after trauma
    • Johansson PI, Windelov NA, Rasmussen LS, Sorensen AM, Ostrowski SR. Blood levels of histone-complexed DNA fragments are associated with coagulopathy, inflammation and endothelial damage early after trauma. J. Emerg. Trauma Shock 6(3), 171-175 (2013).
    • (2013) J. Emerg. Trauma Shock , vol.6 , Issue.3 , pp. 171-175
    • Johansson, P.I.1    Windelov, N.A.2    Rasmussen, L.S.3    Sorensen, A.M.4    Ostrowski, S.R.5
  • 92
    • 80053354116 scopus 로고    scopus 로고
    • Histones induce rapid and profound thrombocytopenia in mice
    • Fuchs TA, Bhandari AA, Wagner DD. Histones induce rapid and profound thrombocytopenia in mice. Blood 118(13), 3708-3714 (2011).
    • (2011) Blood , vol.118 , Issue.13 , pp. 3708-3714
    • Fuchs, T.A.1    Bhandari, A.A.2    Wagner, D.D.3
  • 93
    • 84883367417 scopus 로고    scopus 로고
    • Histones activate the NLRP3 inflammasome in Kupffer cells during sterile inflammatory liver injury
    • Huang H, Chen HW, Evankovich J et al. Histones activate the NLRP3 inflammasome in Kupffer cells during sterile inflammatory liver injury. J. Immunol. 191(5), 2665-2679 (2013).
    • (2013) J. Immunol , vol.191 , Issue.5 , pp. 2665-2679
    • Huang, H.1    Chen, H.W.2    Evankovich, J.3
  • 94
    • 80051882006 scopus 로고    scopus 로고
    • Extracellular histones are mediators of death through TLR2 and TLR4 in mouse fatal liver injury
    • Xu J, Zhang X, Monestier M, Esmon NL, Esmon CT. Extracellular histones are mediators of death through TLR2 and TLR4 in mouse fatal liver injury. J. Immunol. 187(5), 2626-2631 (2011).
    • (2011) J. Immunol , vol.187 , Issue.5 , pp. 2626-2631
    • Xu, J.1    Zhang, X.2    Monestier, M.3    Esmon, N.L.4    Esmon, C.T.5
  • 95
    • 84883317004 scopus 로고    scopus 로고
    • Human CRP defends against the toxicity of circulating histones
    • Abrams ST, Zhang N, Dart C et al. Human CRP defends against the toxicity of circulating histones. J. Immunol. 191(5), 2495-2502 (2013).
    • (2013) J. Immunol , vol.191 , Issue.5 , pp. 2495-2502
    • Abrams, S.T.1    Zhang, N.2    Dart, C.3
  • 96
    • 84890506255 scopus 로고    scopus 로고
    • Extracellular histones are essential effectors of C5aR- and C5L2-mediated tissue damage and inflammation in acute lung injury
    • Bosmann M, Grailer JJ, Ruemmler R et al. Extracellular histones are essential effectors of C5aR- and C5L2-mediated tissue damage and inflammation in acute lung injury. FASEB J. 27(12), 5010-5021 (2013).
    • (2013) FASEB J , vol.27 , Issue.12 , pp. 5010-5021
    • Bosmann, M.1    Grailer, J.J.2    Ruemmler, R.3
  • 97
    • 84863548610 scopus 로고    scopus 로고
    • Platelets induce neutrophil extracellular traps in transfusion-related acute lung injury
    • Caudrillier A, Kessenbrock K, Gilliss BM et al. Platelets induce neutrophil extracellular traps in transfusion-related acute lung injury. J. Clin. Invest. 122(7), 2661-2671 (2012).
    • (2012) J. Clin. Invest , vol.122 , Issue.7 , pp. 2661-2671
    • Caudrillier, A.1    Kessenbrock, K.2    Gilliss, B.M.3
  • 98
    • 84862532317 scopus 로고    scopus 로고
    • Platelet-neutrophil interactions as a target for prevention and treatment of transfusion-related acute lung injury
    • Caudrillier A, Looney MR. Platelet-neutrophil interactions as a target for prevention and treatment of transfusion-related acute lung injury. Curr. Pharm. Des. 18(22), 3260-3266 (2012).
    • (2012) Curr. Pharm. des , vol.18 , Issue.22 , pp. 3260-3266
    • Caudrillier, A.1    Looney, M.R.2
  • 99
    • 84884752631 scopus 로고    scopus 로고
    • Recombinant thrombomodulin protects mice against histone-induced lethal thromboembolism
    • Nakahara M, Ito T, Kawahara K et al. Recombinant thrombomodulin protects mice against histone-induced lethal thromboembolism. PLoS ONE 8(9), e75961 (2013).
    • (2013) PLoS ONE , vol.8 , Issue.9
    • Nakahara, M.1    Ito, T.2    Kawahara, K.3
  • 100
    • 84878126448 scopus 로고    scopus 로고
    • Neutrophil histone modification by peptidylarginine deiminase 4 is critical for deep vein thrombosis in mice
    • Martinod K, Demers M, Fuchs TA et al. Neutrophil histone modification by peptidylarginine deiminase 4 is critical for deep vein thrombosis in mice. Proc. Natl Acad. Sci. USA 110(21), 8674-8679 (2013).
    • (2013) Proc. Natl Acad. Sci. USA , vol.110 , Issue.21 , pp. 8674-8679
    • Martinod, K.1    Demers, M.2    Fuchs, T.A.3
  • 101
    • 70449107044 scopus 로고    scopus 로고
    • Extracellular histones are major mediators of death in sepsis
    • Xu J, Zhang X, Pelayo R et al. Extracellular histones are major mediators of death in sepsis. Nat. Med. 15(11), 1318-1321 (2009).
    • (2009) Nat. Med , vol.15 , Issue.11 , pp. 1318-1321
    • Xu, J.1    Zhang, X.2    Pelayo, R.3
  • 102
    • 84926615692 scopus 로고    scopus 로고
    • Inter-alpha inhibitor protein and its associated glycosaminoglycans protect against histone-induced injury
    • Chaaban H, Keshari RS, Silasi-Mansat R et al. Inter-alpha inhibitor protein and its associated glycosaminoglycans protect against histone-induced injury. Blood 125(14), 2286-2296 (2015).
    • (2015) Blood , vol.125 , Issue.14 , pp. 2286-2296
    • Chaaban, H.1    Keshari, R.S.2    Silasi-Mansat, R.3
  • 103
    • 84908302078 scopus 로고    scopus 로고
    • LL-37 modulates human phagocyte responses to influenza A virus
    • Tripathi S, White MR, Wang G, Hartshorn K. LL-37 modulates human phagocyte responses to influenza A virus. J. Leukoc. Biol. 96(5), 931-938 (2014).
    • (2014) J. Leukoc. Biol , vol.96 , Issue.5 , pp. 931-938
    • Tripathi, S.1    White, M.R.2    Wang, G.3    Hartshorn, K.4
  • 104
    • 77953301125 scopus 로고    scopus 로고
    • Review: Defensins and cathelicidins in lung immunity
    • Tecle T, Tripathi S, Hartshorn KL. Review: defensins and cathelicidins in lung immunity. Innate Immun. 16(3), 151-159 (2010).
    • (2010) Innate Immun , vol.16 , Issue.3 , pp. 151-159
    • Tecle, T.1    Tripathi, S.2    Hartshorn, K.L.3
  • 106
    • 20544442905 scopus 로고    scopus 로고
    • Alarmins: Chemotactic activators of immune responses
    • Oppenheim JJ, Yang D. Alarmins: chemotactic activators of immune responses. Curr. Opin Immunol. 17(4), 359-365 (2005).
    • (2005) Curr. Opin Immunol , vol.17 , Issue.4 , pp. 359-365
    • Oppenheim, J.J.1    Yang, D.2
  • 107
    • 84914145530 scopus 로고    scopus 로고
    • The amazing innate immune response to influenza A virus infection
    • Tripathi S, White MR, Hartshorn KL. The amazing innate immune response to influenza A virus infection. Innate Immun. 21(1), 73-98 (2015).
    • (2015) Innate Immun , vol.21 , Issue.1 , pp. 73-98
    • Tripathi, S.1    White, M.R.2    Hartshorn, K.L.3
  • 108
    • 67449116312 scopus 로고    scopus 로고
    • Effects of the cathelicidin LL-37 on intestinal epithelial barrier integrity
    • Otte JM, Zdebik AE, Brand S et al. Effects of the cathelicidin LL-37 on intestinal epithelial barrier integrity. Regul. Pept. 156(1-3), 104-117 (2009).
    • (2009) Regul. Pept , vol.156 , Issue.1-3 , pp. 104-117
    • Otte, J.M.1    Zdebik, A.E.2    Brand, S.3
  • 109
    • 37049030173 scopus 로고    scopus 로고
    • In vitro and in vivo wound healing-promoting activities of human cathelicidin LL-37
    • Carretero M, Escamez MJ, Garcia M et al. In vitro and in vivo wound healing-promoting activities of human cathelicidin LL-37. J. Invest. Dermatol. 128(1), 223-236 (2008).
    • (2008) J. Invest. Dermatol , vol.128 , Issue.1 , pp. 223-236
    • Carretero, M.1    Escamez, M.J.2    Garcia, M.3


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