메뉴 건너뛰기




Volumn 8, Issue 11, 2013, Pages

Capture of lipopolysaccharide (endotoxin) by the blood clot: A comparative study

Author keywords

[No Author keywords available]

Indexed keywords

FIBRIN; LIPOPOLYSACCHARIDE; LIPOPROTEIN; THROMBOPLASTIN;

EID: 84894227375     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0080192     Document Type: Article
Times cited : (24)

References (57)
  • 1
    • 77952869965 scopus 로고    scopus 로고
    • Blood clotting in Limulus immunity: Physiological impairment of clot-entrapped bacteria
    • Bosniak PA, Armstrong PB (2004) Blood clotting in Limulus immunity: physiological impairment of clot-entrapped bacteria. BiolBull(Woods Hole) 207: 172.
    • (2004) BiolBull(Woods Hole) , vol.207 , pp. 172
    • Bosniak, P.A.1    Armstrong, P.B.2
  • 2
    • 77955410626 scopus 로고    scopus 로고
    • Reciprocal coupling of coagulation and innate immunity via neutrophil serine proteases
    • Massberg S, Grahl L, von Bruehl ML, Manukyan D, Pfeiler S, et al. (2010) Reciprocal coupling of coagulation and innate immunity via neutrophil serine proteases. NatMed 16: 887-896.
    • (2010) NatMed , vol.16 , pp. 887-896
    • Massberg, S.1    Grahl, L.2    Von Bruehl, M.L.3    Manukyan, D.4    Pfeiler, S.5
  • 3
    • 0027057013 scopus 로고
    • Role of fibrin deposition in the pathogenesis of intraabdominal infection
    • Rotstein OD (1992) Role of fibrin deposition in the pathogenesis of intraabdominal infection. EurJClinMicrobiolInfectDis 11: 1064-1068.
    • (1992) EurJClinMicrobiolInfectDis , vol.11 , pp. 1064-1068
    • Rotstein, O.D.1
  • 4
    • 80052397217 scopus 로고    scopus 로고
    • Coagulation, an ancestral serine protease cascade, exerts a novel function in early immune defense
    • Loof TG, Morgelin M, Johansson L, Oehmcke S, Olin AI, et al. (2011) Coagulation, an ancestral serine protease cascade, exerts a novel function in early immune defense. Blood 118: 2589-2598.
    • (2011) Blood , vol.118 , pp. 2589-2598
    • Loof, T.G.1    Morgelin, M.2    Johansson, L.3    Oehmcke, S.4    Olin, A.I.5
  • 5
    • 0032159526 scopus 로고    scopus 로고
    • Evolution and phylogeny of defense molecules associated with innate immunity in horseshoe crab
    • Iwanaga S, Kawabata S (1998) Evolution and phylogeny of defense molecules associated with innate immunity in horseshoe crab. Front Biosci 3: D973-D984.
    • (1998) Front Biosci , vol.3
    • Iwanaga, S.1    Kawabata, S.2
  • 6
    • 0039483335 scopus 로고    scopus 로고
    • Molecular basis of blood coagulation
    • Hoffman R, Benz EJ, Shattil SJ, Furie B, Cohen HJ, et al., editors. 3rd ed. New York: Churchill Livingstone
    • Furie B, Furie B C (2000) Molecular basis of blood coagulation. In: Hoffman R, Benz EJ, Shattil SJ, Furie B, Cohen HJ, et al., editors. Hematology - Basic Principles and Practice. 3rd ed. New York: Churchill Livingstone. pp. 1783-1804.
    • (2000) Hematology - Basic Principles and Practice , pp. 1783-1804
    • Furie, B.1    Furie, B.C.2
  • 7
    • 0035997382 scopus 로고    scopus 로고
    • Lipopolysaccharide endotoxins
    • DOI 10.1146/annurev.biochem.71.110601.135414
    • Raetz CR, Whitfield C (2002) Lipopolysaccharide endotoxins. AnnuRevBiochem 71: 635-700. (Pubitemid 34800232)
    • (2002) Annual Review of Biochemistry , vol.71 , pp. 635-700
    • Raetz, C.R.H.1    Whitfield, C.2
  • 8
    • 0030854780 scopus 로고    scopus 로고
    • Epidemiology of sepsis syndrome in 8 academic medical centers
    • Academic Medical Center Consortium Sepsis Project Working Group
    • Sands KE, Bates DW, Lanken PN, Graman PS, Hibberd PL, et al. (1997) Epidemiology of sepsis syndrome in 8 academic medical centers. Academic Medical Center Consortium Sepsis Project Working Group. JAMA 278: 234-240.
    • (1997) JAMA , vol.278 , pp. 234-240
    • Sands, K.E.1    Bates, D.W.2    Lanken, P.N.3    Graman, P.S.4    Hibberd, P.L.5
  • 9
    • 0018728995 scopus 로고
    • Ontogeny and phylogeny of response to gram-negative endotoxins among the marine invertebrates
    • Cohen E, Bang FB, Levin J, Marchalonis JJ, Pistole TG, et al., editors. New York, N.Y.: Alan R. Liss
    • Bang FB (1979) Ontogeny and phylogeny of response to gram-negative endotoxins among the marine invertebrates. In: Cohen E, Bang FB, Levin J, Marchalonis JJ, Pistole TG, et al., editors. Biomedical Applications of the Horseshoe Crab (Limulidae). New York, N.Y.: Alan R. Liss. pp. 109-123.
    • (1979) Biomedical Applications of the Horseshoe Crab (Limulidae) , pp. 109-123
    • Bang, F.B.1
  • 10
    • 19044385630 scopus 로고    scopus 로고
    • Detoxifying endotoxin: Time, place and person
    • Munford RS (2005) Detoxifying endotoxin: time, place and person. JEndotoxinRes 11: 69-84.
    • (2005) JEndotoxinRes , vol.11 , pp. 69-84
    • Munford, R.S.1
  • 11
    • 77952533715 scopus 로고    scopus 로고
    • Interactions between lipid A and serum proteins
    • Gutsmann T, Muller M, Schromm AB (2009) Interactions between lipid A and serum proteins. Adv Exp Med Biol 667: 39-51.
    • (2009) Adv Exp Med Biol , vol.667 , pp. 39-51
    • Gutsmann, T.1    Muller, M.2    Schromm, A.B.3
  • 12
    • 27444437755 scopus 로고    scopus 로고
    • Fibrin but not adsorbed fibrinogen supports fibronectin assembly by spread platelets: Effects of the interaction of alphaIIb beta3 with the C terminus of the fibrinogen gamma-chain
    • DOI 10.1074/jbc.M506289200
    • Cho J, Degen JL, Coller BS, Mosher DF (2005) Fibrin but not adsorbed fibrinogen supports fibronectin assembly by spread platelets. Effects of the interaction of alphaIIb beta3 with the C terminus of the fibrinogen gamma-chain. JBiolChem 280: 35490-35498. (Pubitemid 41532739)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.42 , pp. 35490-35498
    • Cho, J.1    Degen, J.L.2    Coller, B.S.3    Mosher, D.F.4
  • 13
    • 0014410251 scopus 로고
    • The reaction of phenylglyoxal with arginine residues in proteins
    • Takahashi K (1968) The reaction of phenylglyoxal with arginine residues in proteins. J Biol Chem 243: 6171-6179.
    • (1968) J Biol Chem , vol.243 , pp. 6171-6179
    • Takahashi, K.1
  • 14
    • 0022387772 scopus 로고
    • Adenosine 5'-phosphosulfate kinase from Penicillium chrysogenum. Determining ligand dissociation constants of binary and ternary complexes from the kinetics of enzyme inactivation
    • Renosto F, Seubert PA, Knudson P, Segel IH (1985) Adenosine 5′-phosphosulfate kinase from Penicillium chrysogenum. Determining ligand dissociation constants of binary and ternary complexes from the kinetics of enzyme inactivation. J Biol Chem 260: 11903-11913. (Pubitemid 16228345)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.22 , pp. 11903-11913
    • Renosto, F.1    Seubert, P.A.2    Knudson, P.3    Segel, I.H.4
  • 15
    • 80055119093 scopus 로고    scopus 로고
    • Blood collection from the American horseshoe crab, Limulus polyphemus
    • Armstrong P, Conrad M (2008) Blood collection from the American horseshoe crab, Limulus polyphemus. JVisExp 20: http://www.jove.com/index/details.stp?ID= 958.
    • (2008) JVisExp , vol.20
    • Armstrong, P.1    Conrad, M.2
  • 16
    • 33845604949 scopus 로고    scopus 로고
    • Histochemical evidence for lipid A (endotoxin) in eukaryote chloroplasts
    • Armstrong MT, Theg SM, Braun N, Wainwright N, Pardy RL, et al. (2006) Histochemical evidence for lipid A (endotoxin) in eukaryote chloroplasts. FASEB J 20: 2145-2146.
    • (2006) FASEB J , vol.20 , pp. 2145-2146
    • Armstrong, M.T.1    Theg, S.M.2    Braun, N.3    Wainwright, N.4    Pardy, R.L.5
  • 17
    • 0036799775 scopus 로고    scopus 로고
    • Real-time in vivo imaging of platelets, tissue factor and fibrin during arterial thrombus formation in the mouse
    • Falati S, Gross P, Merrill-Skoloff G, Furie BC, Furie B (2002) Real-time in vivo imaging of platelets, tissue factor and fibrin during arterial thrombus formation in the mouse. NatMed 8: 1175-1181.
    • (2002) NatMed , vol.8 , pp. 1175-1181
    • Falati, S.1    Gross, P.2    Merrill-Skoloff, G.3    Furie, B.C.4    Furie, B.5
  • 18
    • 34147187419 scopus 로고    scopus 로고
    • Real time in vivo imaging of platelets during thrombus formation
    • Michelson AD, editor. Amsterdam, The Netherlands: Academic Press/Elsevier
    • Dubois C, Atkinson B, Furie BC, Furie B (2006) Real time in vivo imaging of platelets during thrombus formation. In: Michelson AD, editor. Platelets. Amsterdam, The Netherlands: Academic Press/Elsevier. pp. 611-626.
    • (2006) Platelets , pp. 611-626
    • Dubois, C.1    Atkinson, B.2    Furie, B.C.3    Furie, B.4
  • 20
    • 0021794075 scopus 로고
    • Detection of endotoxin in the plasma of patients with gram-negative bacterial sepsis by the Limulus amoebocyte lysate assay
    • Pearson FC, Dubczak J, Weary M, Bruszer G, Donohue G (1985) Detection of endotoxin in the plasma of patients with gram- negative bacterial sepsis by the Limulus amoebocyte lysate assay. JClinMicrobiol 21: 865-868. (Pubitemid 15058928)
    • (1985) Journal of Clinical Microbiology , vol.21 , Issue.6 , pp. 865-868
    • Pearson, F.C.1    Dubczak, J.2    Weary, M.3
  • 21
    • 0021166726 scopus 로고
    • Role of endogenous proteinase inhibitors in the regulation of the blood clotting system of the horseshoe crab, Limulus polyphemus
    • Armstrong PB, Levin J, Quigley JP (1984) Role of endogenous proteinase inhibitors in the regulation of the blood clotting system of the horseshoe crab, Limulus polyphemus. ThrombHaemost 52: 117-120. (Pubitemid 14023992)
    • (1984) Thrombosis and Haemostasis , vol.52 , Issue.2 , pp. 117-120
    • Armstrong, P.B.1    Levin, J.2    Quigley, J.P.3
  • 22
    • 3042853063 scopus 로고    scopus 로고
    • C-reactive protein: A predominant LPS-binding acute phase protein responsive to Pseudomonas infection
    • DOI 10.1179/096805104225004833
    • Ng PM, Jin Z, Tan SS, Ho B, Ding JL (2004) C-reactive protein. A predominant LPS-binding acute phase protein responsive to Pseudomonas infection. JEndotoxin Res 10: 163-174. (Pubitemid 38877736)
    • (2004) Journal of Endotoxin Research , vol.10 , Issue.3 , pp. 163-174
    • Ng, P.M.L.1    Jin, Z.2    Tan, S.S.H.3    Ho, B.4    Ding, J.L.5
  • 23
    • 84951825337 scopus 로고    scopus 로고
    • Role of a2-macroglobulin in the immune response of invertebrates
    • Armstrong PB (2010) Role of a2-macroglobulin in the immune response of invertebrates. InvertSurvival J 7: 165-180.
    • (2010) InvertSurvival J , vol.7 , pp. 165-180
    • Armstrong, P.B.1
  • 24
    • 0018680866 scopus 로고
    • The Limulus test: A status report
    • Levin J (1979) The Limulus test: a status report. ProgClinBiolRes 29: 235-244.
    • (1979) ProgClinBiolRes , vol.29 , pp. 235-244
    • Levin, J.1
  • 26
    • 0023040655 scopus 로고
    • Lipopolysaccharide-sensitive serine-protease zymogen (factor C) found in Limulus hemocytes. Isolation and characterization
    • Nakamura T, Morita T, Iwanaga S (1986) Lipopolysaccharide-sensitive serine-protease zymogen (factor C) found in Limulus hemocytes. Isolation and characterization. EurJBiochem 154: 511-521.
    • (1986) EurJBiochem , vol.154 , pp. 511-521
    • Nakamura, T.1    Morita, T.2    Iwanaga, S.3
  • 27
    • 0020398633 scopus 로고
    • Endotoxin-induced degranulation of the Limulus amebocyte
    • DOI 10.1016/0014-4827(82)90150-1
    • Armstrong PB, Rickles FR (1982) Endotoxin-induced degranulation of the Limulus amebocyte. ExpCell Res 140: 15-24. (Pubitemid 13237741)
    • (1982) Experimental Cell Research , vol.140 , Issue.1 , pp. 15-24
    • Armstrong, P.B.1    Rickles, F.R.2
  • 28
    • 0014799610 scopus 로고
    • Detection of endotoxin in human blood and demonstration of an inhibitor
    • Levin J, Tomasulo PA, Oser RS (1970) Detection of endotoxin in human blood and demonstration of an inhibitor. JLabClinMed 75: 903-911.
    • (1970) JLabClinMed , vol.75 , pp. 903-911
    • Levin, J.1    Tomasulo, P.A.2    Oser, R.S.3
  • 29
    • 17444392120 scopus 로고    scopus 로고
    • Fibrinogen and fibrin
    • Weisel JW (2005) Fibrinogen and fibrin. AdvProtein Chem 70: 247-299.
    • (2005) AdvProtein Chem , vol.70 , pp. 247-299
    • Weisel, J.W.1
  • 30
    • 0642336966 scopus 로고    scopus 로고
    • The decorated clot: Binding of agents of the innate immune system to the fibrils of the limulus blood clot
    • Armstrong PB, Armstrong MT (2003) The decorated clot: Binding of agents of the innate immune system to the fibrils of the limulus blood clot. BiolBull 205: 201-203.
    • (2003) BiolBull , vol.205 , pp. 201-203
    • Armstrong, P.B.1    Armstrong, M.T.2
  • 31
    • 0034660537 scopus 로고    scopus 로고
    • A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins
    • DOI 10.1016/S0969-2126(00)00143-X
    • Ferguson AD, Welte W, Hofmann E, Lindner B, Holst O, et al. (2000) A conserved structural motif for lipopolysaccharide recognition by procaryotic and eucaryotic proteins. Structure 8: 585-592. (Pubitemid 30409311)
    • (2000) Structure , vol.8 , Issue.6 , pp. 585-592
    • Ferguson, A.D.1    Welte, W.2    Hofmann, E.3    Lindner, B.4    Holst, O.5    Coulton, J.W.6    Diederichs, K.7
  • 32
    • 0026677582 scopus 로고
    • Conformation of tachyplesin I from Tachypleus tridentatus when interacting with lipid matrices
    • DOI 10.1021/bi00163a038
    • Park NG, Lee S, Oishi O, Aoyagi H, Iwanaga S, et al. (1992) Conformation of tachyplesin I from Tachypleus tridentatus when interacting with lipid matrices. Biochemistry 31: 12241-12247. (Pubitemid 23011373)
    • (1992) Biochemistry , vol.31 , Issue.48 , pp. 12241-12247
    • Nam, G.P.1    Lee, S.2    Oishi, O.3    Aoyagi, H.4    Iwanaga, S.5    Yamashita, S.6    Ohno, M.7
  • 33
    • 34250788226 scopus 로고    scopus 로고
    • In vivo thrombus formation
    • DOI 10.1111/j.1538-7836.2006.02262.x, State of the Art 2007: XXI Congress of the International Society on Thrombosis and Haemostasis
    • Furie B, Furie BC (2007) In vivo thrombus formation. JThrombHaemost 5 Suppl 1: 12-17. (Pubitemid 46958811)
    • (2007) Journal of Thrombosis and Haemostasis , vol.5 , Issue.SUPPL. 1 , pp. 12-17
    • Furie, B.1    Furie, B.C.2
  • 34
    • 34250736946 scopus 로고    scopus 로고
    • Fibrin and fibrinolysis in infection and host defense
    • DOI 10.1111/j.1538-7836.2007.02519.x, State of the Art 2007: XXI Congress of the International Society on Thrombosis and Haemostasis
    • Degen JL, Bugge TH, Goguen JD (2007) Fibrin and fibrinolysis in infection and host defense. JThrombHaemost 5 Suppl 1: 24-31. (Pubitemid 46958813)
    • (2007) Journal of Thrombosis and Haemostasis , vol.5 , Issue.SUPPL. 1 , pp. 24-31
    • Degen, J.L.1    Bugge, T.H.2    Goguen, J.D.3
  • 35
    • 33646384915 scopus 로고    scopus 로고
    • Proteases and protease inhibitors: A balance of activities in host-pathogen interaction
    • Armstrong PB (2006) Proteases and protease inhibitors: a balance of activities in host-pathogen interaction. Immunobiology 211: 263-281.
    • (2006) Immunobiology , vol.211 , pp. 263-281
    • Armstrong, P.B.1
  • 36
    • 0039015218 scopus 로고
    • The fine structure of the amebocyte in the blood of Limulus polyphemus. II. The amebocyte cytoskeleton: A morphological analysis of native, activated, and endotoxin-stimulated amebocytes
    • Tablin F, Levin J (1988) The fine structure of the amebocyte in the blood of Limulus polyphemus . II. The amebocyte cytoskeleton: a morphological analysis of native, activated, and endotoxin-stimulated amebocytes. BiolBull(Woods Hole) 175: 417-429.
    • (1988) BiolBull(Woods Hole) , vol.175 , pp. 417-429
    • Tablin, F.1    Levin, J.2
  • 37
    • 0041856152 scopus 로고    scopus 로고
    • The conversion of fibrinogen to fibrin at the surface of curliated Escherichia coli bacteria leads to the generation of proinflammatory fibrinopeptides
    • DOI 10.1074/jbc.M302522200
    • Persson K, Russell W, Morgelin M, Herwald H (2003) The conversion of fibrinogen to fibrin at the surface of curliated Escherichia coli bacteria leads to the generation of proinflammatory fibrinopeptides. JBiolChem 278: 31884-31890. (Pubitemid 37048373)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.34 , pp. 31884-31890
    • Persson, K.1    Russell, W.2    Morgelin, M.3    Herwald, H.4
  • 38
    • 0018037049 scopus 로고
    • The effects of bacterial endotoxins on host mediation systems. A review
    • Morrison DC, Ulevitch RJ (1978) The effects of bacterial endotoxins on host mediation systems. A review. Am J Pathol 93: 526-618.
    • (1978) Am J Pathol , vol.93 , pp. 526-618
    • Morrison, D.C.1    Ulevitch, R.J.2
  • 39
    • 0022534483 scopus 로고
    • Effects of fibrinogen derivatives upon the inflammatory response. Studies with human fibrinopeptide B
    • Senior RM, Skogen WF, Griffin GL, Wilner GD (1986) Effects of fibrinogen derivatives upon the inflammatory response. Studies with human fibrinopeptide B. JClinInvest 77: 1014-1019. (Pubitemid 16067979)
    • (1986) Journal of Clinical Investigation , vol.77 , Issue.3 , pp. 1014-1019
    • Senior, R.M.1    Skogen, W.F.2    Griffin, G.L.3    Wilner, G.D.4
  • 40
    • 33751579326 scopus 로고    scopus 로고
    • The contact system - A novel branch of innate immunity generating antibacterial peptides
    • DOI 10.1038/sj.emboj.7601422, PII 7601422
    • Frick IM, Akesson P, Herwald H, Morgelin M, Malmsten M, et al. (2006) The contact system-a novel branch of innate immunity generating antibacterial peptides. EMBO J 25: 5569-5578. (Pubitemid 44847197)
    • (2006) EMBO Journal , vol.25 , Issue.23 , pp. 5569-5578
    • Frick, I.-M.1    Akesson, P.2    Herwald, H.3    Morgelin, M.4    Malmsten, M.5    Nagler, D.K.6    Bjorck, L.7
  • 41
    • 0034703094 scopus 로고    scopus 로고
    • A link between blood coagulation and prophenol oxidase activation in arthropod host defense
    • DOI 10.1074/jbc.M002556200
    • Nagai T, Kawabata S (2000) A link between blood coagulation and prophenol oxidase activation in arthropod host defense. JBiolChem 275: 29264-29267. (Pubitemid 32043795)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.38 , pp. 29264-29267
    • Nagai, T.1    Kawabata, S.-I.2
  • 42
    • 71849099103 scopus 로고    scopus 로고
    • Factor C acts as a lipopolysaccharide-responsive C3 convertase in horseshoe crab complement activation
    • Ariki S, Takahara S, Shibata T, Fukuoka T, Ozaki A, et al. (2008) Factor C acts as a lipopolysaccharide-responsive C3 convertase in horseshoe crab complement activation. JImmunol 181: 7994-8001.
    • (2008) JImmunol , vol.181 , pp. 7994-8001
    • Ariki, S.1    Takahara, S.2    Shibata, T.3    Fukuoka, T.4    Ozaki, A.5
  • 43
    • 0000631035 scopus 로고
    • The role of endotoxin in the extracellular coagulation of Limulus blood
    • Levin J, Bang FB (1964) The role of endotoxin in the extracellular coagulation of Limulus blood. BullJohns Hopkins Hosp 115: 265-274.
    • (1964) BullJohns Hopkins Hosp , vol.115 , pp. 265-274
    • Levin, J.1    Bang, F.B.2
  • 44
    • 0023799779 scopus 로고
    • The horseshoe crab: A model for gram-negative sepsis in marine organisms and humans
    • Levin J (1988) The horseshoe crab: a model for gram-negative sepsis in marine organisms and humans. ProgClinBiolRes 272: 3-15.
    • (1988) ProgClinBiolRes , vol.272 , pp. 3-15
    • Levin, J.1
  • 45
  • 46
    • 27144539508 scopus 로고    scopus 로고
    • Platelets express functional Toll-like receptor-4
    • DOI 10.1182/blood-2005-03-0916
    • Andonegui G, Kerfoot SM, McNagny K, Ebbert KV, Patel KD, et al. (2005) Platelets express functional Toll-like receptor-4. Blood 106: 2417-2423. (Pubitemid 41510815)
    • (2005) Blood , vol.106 , Issue.7 , pp. 2417-2423
    • Andonegui, G.1    Kerfoot, S.M.2    McNagny, K.3    Ebbert, K.V.J.4    Patel, K.D.5    Kubes, P.6
  • 47
    • 33645579382 scopus 로고    scopus 로고
    • Lipopolysaccharide from enterohemorrhagic Escherichia coli binds to platelets through TLR4 and CD62 and is detected on circulating platelets in patients with hemolytic uremic syndrome
    • DOI 10.1182/blood-2005-08-3219
    • Stahl AL, Svensson M, Morgelin M, Svanborg C, Tarr PI, et al. (2006) Lipopolysaccharide from enterohemorrhagic Escherichia coli binds to platelets through TLR4 and CD62 and is detected on circulating platelets in patients with hemolytic uremic syndrome. Blood 108: 167-176. (Pubitemid 43990625)
    • (2006) Blood , vol.108 , Issue.1 , pp. 167-176
    • Stahl, A.-L.1    Svensson, M.2    Morgelin, M.3    Svanborg, C.4    Tarr, P.I.5    Mooney, J.C.6    Watkins, S.L.7    Johnson, R.8    Karpman, D.9
  • 48
    • 33947507505 scopus 로고    scopus 로고
    • A structural perspective on the interaction between lipopolysaccharide and factor C, a receptor involved in recognition of gram-negative bacteria
    • DOI 10.1074/jbc.M609198200
    • Koshiba T, Hashii T, Kawabata S (2007) A structural perspective on the interaction between lipopolysaccharide and factor C, a receptor involved in recognition of Gram-negative bacteria. JBiolChem 282: 3962-3967. (Pubitemid 47084439)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.6 , pp. 3962-3967
    • Koshiba, T.1    Hashii, T.2    Kawabata, S.-I.3
  • 50
    • 0031951337 scopus 로고    scopus 로고
    • Limulus antilipopolysaccharide factor prevents mortality late in the course of endotoxemia
    • Roth RI, Su D, Child AH, Wainwright NR, Levin J (1998) Limulus antilipopolysaccharide factor prevents mortality late in the course of endotoxemia. JInfectDis 177: 388-394. (Pubitemid 28063764)
    • (1998) Journal of Infectious Diseases , vol.177 , Issue.2 , pp. 388-394
    • Roth, R.I.1    Su, D.2    Child, A.H.3    Wainwright, N.R.4    Levin, J.5
  • 51
    • 34547515353 scopus 로고    scopus 로고
    • The host response to endotoxin, antilipopolysaccharide strategies, and the management of severe sepsis
    • Opal SM (2007) The host response to endotoxin, antilipopolysaccharide strategies, and the management of severe sepsis. Int J Med Microbiol 297: 365-377.
    • (2007) Int J Med Microbiol , vol.297 , pp. 365-377
    • Opal, S.M.1
  • 52
    • 84961014004 scopus 로고
    • A bacterial disease of Limulus polyphemus
    • Bang FB (1956) A bacterial disease of Limulus polyphemus. BullJohns Hopkins Hosp 98: 325-351.
    • (1956) BullJohns Hopkins Hosp , vol.98 , pp. 325-351
    • Bang, F.B.1
  • 54
    • 34547510802 scopus 로고    scopus 로고
    • Structural biology of the LPS recognition
    • Jerala R (2007) Structural biology of the LPS recognition. Int J Med Microbiol 297: 353-363.
    • (2007) Int J Med Microbiol , vol.297 , pp. 353-363
    • Jerala, R.1
  • 55
    • 67349182481 scopus 로고    scopus 로고
    • The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex
    • Park BS, Song DH, Kim HM, Choi BS, Lee H, et al. (2009) The structural basis of lipopolysaccharide recognition by the TLR4-MD-2 complex. Nature 458: 1191-1195.
    • (2009) Nature , vol.458 , pp. 1191-1195
    • Park, B.S.1    Song, D.H.2    Kim, H.M.3    Choi, B.S.4    Lee, H.5
  • 56
    • 0002431489 scopus 로고
    • Outer membrane
    • Niedhardt FC, Ingraham JL, Low KB, Magasanik B, Schaechter M, et al., editors. Washington, D.C.: American Society for Microbiology
    • Nikaido H, Vaara M (1987) Outer membrane. In: Niedhardt FC, Ingraham JL, Low KB, Magasanik B, Schaechter M, et al., editors. Escherichia coli and Salmonella typhimurium Cellular and Molecular Biology. Washington, D.C.: American Society for Microbiology. pp. 7-22.
    • (1987) Escherichia Coli and Salmonella Typhimurium Cellular and Molecular Biology , pp. 7-22
    • Nikaido, H.1    Vaara, M.2
  • 57
    • 80053289935 scopus 로고    scopus 로고
    • Morphology, size distribution, and aggregate structure of lipopolysaccharide and lipid A dispersions from enterobacterial origin
    • Richter W, Vogel V, Howe J, Steiniger F, Brauser A, et al. (2011) Morphology, size distribution, and aggregate structure of lipopolysaccharide and lipid A dispersions from enterobacterial origin. InnateImmun 17: 427-438.
    • (2011) InnateImmun , vol.17 , pp. 427-438
    • Richter, W.1    Vogel, V.2    Howe, J.3    Steiniger, F.4    Brauser, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.