메뉴 건너뛰기




Volumn 26, Issue 7, 2002, Pages 790-798

Molecular biology of endotoxin antagonism

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; ENDOTOXIN; LIPOPOLYSACCHARIDE BINDING PROTEIN; PEPTIDE; CARRIER PROTEIN; LIPOPOLYSACCHARIDE;

EID: 0036631561     PISSN: 03642313     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00268-002-4054-4     Document Type: Conference Paper
Times cited : (10)

References (96)
  • 1
    • 0028302526 scopus 로고
    • Gram-negative bacterial sepsis and sepsis syndrome
    • Dunn DL. Gram-negative bacterial sepsis and sepsis syndrome. Surg. Clin. North Am. 1994;74:621-635
    • (1994) Surg. Clin. North Am. , vol.74 , pp. 621-635
    • Dunn, D.L.1
  • 2
    • 0020007321 scopus 로고
    • Bacterial endotoxins: Chemical structure, biological activity and role in septicaemia
    • Rietschel ET, Schade U, Jensen M, et al. Bacterial endotoxins: chemical structure, biological activity and role in septicaemia. Scand. J. Infect. Dis. Suppl. 1982;31:8-21
    • (1982) Scand. J. Infect. Dis. Suppl. , vol.31 , pp. 8-21
    • Rietschel, E.T.1    Schade, U.2    Jensen, M.3
  • 3
    • 0023079312 scopus 로고
    • Endotoxins and disease mechanisms
    • Morrison DC, Ryan JL. Endotoxins and disease mechanisms. Annu. Rev. Med. 1987;38:417-432
    • (1987) Annu. Rev. Med. , vol.38 , pp. 417-432
    • Morrison, D.C.1    Ryan, J.L.2
  • 4
    • 0020574914 scopus 로고
    • Immunobiological activities of synthetic lipid A analogs and related compounds as compared with those of bacterial lipopolysaccharide, re-glycolipid, lipid A, and muramyl dipeptide
    • Kotani S, Takada H, Tsujimoto M, et al. Immunobiological activities of synthetic lipid A analogs and related compounds as compared with those of bacterial lipopolysaccharide, re-glycolipid, lipid A, and muramyl dipeptide. Infect. Immun. 1983;41:758-766
    • (1983) Infect. Immun. , vol.41 , pp. 758-766
    • Kotani, S.1    Takada, H.2    Tsujimoto, M.3
  • 5
    • 0024487086 scopus 로고
    • Structural requirements of lipid A for endotoxicity and other biological activities
    • Takada H, Kotani S. Structural requirements of lipid A for endotoxicity and other biological activities. CRC Crit. Rev. Microbiol. 1989;16:477-487
    • (1989) CRC Crit. Rev. Microbiol. , vol.16 , pp. 477-487
    • Takada, H.1    Kotani, S.2
  • 6
    • 0028941601 scopus 로고
    • Enzymatically deacylated lipopolysaccharide (LPS) can antagonize LPS at multiple sites in the LPS recognition pathway
    • Kitchens RL, Munford RS. Enzymatically deacylated lipopolysaccharide (LPS) can antagonize LPS at multiple sites in the LPS recognition pathway. J. Biol. Chem. 1995;270:9904-9910
    • (1995) J. Biol. Chem. , vol.270 , pp. 9904-9910
    • Kitchens, R.L.1    Munford, R.S.2
  • 7
    • 0030857849 scopus 로고    scopus 로고
    • Diphosphoryl lipid A from Rhodobacter sphaeroides inhibits complexes that form in vitro between lipopolysaccharide (LPS)-binding protein, soluble CD14, and spectrally pure LPS
    • Jarvis BW, Lichenstein H, Qureshi N. Diphosphoryl lipid A from Rhodobacter sphaeroides inhibits complexes that form in vitro between lipopolysaccharide (LPS)-binding protein, soluble CD14, and spectrally pure LPS. Infect. Immun. 1997;65:3011-3016
    • (1997) Infect. Immun. , vol.65 , pp. 3011-3016
    • Jarvis, B.W.1    Lichenstein, H.2    Qureshi, N.3
  • 8
    • 0026088437 scopus 로고
    • Lipid A-like molecules that antagonize the effects of endotoxins on human monocytes
    • Golenbock DT, Hampton RY, Qureshi N, et al. Lipid A-like molecules that antagonize the effects of endotoxins on human monocytes. J. Biol. Chem. 1991;266:19490-19498
    • (1991) J. Biol. Chem. , vol.266 , pp. 19490-19498
    • Golenbock, D.T.1    Hampton, R.Y.2    Qureshi, N.3
  • 9
    • 0022462376 scopus 로고
    • Isolation of a lipopolysacharide-binding acute phase reactant from rabbit serum
    • Tobias P, Soldau K, Ulevitch R. Isolation of a lipopolysacharide-binding acute phase reactant from rabbit serum. J. Exp. Med. 1986;164:777-793
    • (1986) J. Exp. Med. , vol.164 , pp. 777-793
    • Tobias, P.1    Soldau, K.2    Ulevitch, R.3
  • 10
    • 0028144711 scopus 로고
    • Changes in polymorphonuclear leukocyte surface and plasma bactericidal/permeability-increasing protein and plasma lipopolysaccharide binding protein during endotoxemia or sepsis
    • Calvano SE, Thompson WA, Marra MN, et al. Changes in polymorphonuclear leukocyte surface and plasma bactericidal/permeability-increasing protein and plasma lipopolysaccharide binding protein during endotoxemia or sepsis. Arch. Surg. 1994;129:220-226
    • (1994) Arch. Surg. , vol.129 , pp. 220-226
    • Calvano, S.E.1    Thompson, W.A.2    Marra, M.N.3
  • 11
    • 0025107568 scopus 로고
    • Structure and function of lipopolysaccharide binding protein
    • Schumann RR, Leong SR, Flaggs GW, et al. Structure and function of lipopolysaccharide binding protein. Science 1990;249:1429-1433
    • (1990) Science , vol.249 , pp. 1429-1433
    • Schumann, R.R.1    Leong, S.R.2    Flaggs, G.W.3
  • 12
    • 0026757195 scopus 로고
    • Enhancement of murine macrophage binding of and response to bacterial lipopolysaccharide (LPS) by LPS-binding protein
    • Corradin SB, Mauel J, Gallay P, et al. Enhancement of murine macrophage binding of and response to bacterial lipopolysaccharide (LPS) by LPS-binding protein. J. Leukoc. Biol. 1992;52:363-368
    • (1992) J. Leukoc. Biol. , vol.52 , pp. 363-368
    • Corradin, S.B.1    Mauel, J.2    Gallay, P.3
  • 13
    • 0025166114 scopus 로고
    • CD14 serves as the cellular receptor for complexes of lipopolysaccharide with lipopolysaccharide-binding protein
    • Wright SD, Ramos RA, Tobias PS, et al. CD14 serves as the cellular receptor for complexes of lipopolysaccharide with lipopolysaccharide-binding protein. Science 1990;249:1431-1433
    • (1990) Science , vol.249 , pp. 1431-1433
    • Wright, S.D.1    Ramos, R.A.2    Tobias, P.S.3
  • 14
    • 0030685133 scopus 로고    scopus 로고
    • Lipopolysaccharide-binding protein is required to combat a murine gram-negative bacterial infection
    • Jack RS, Fan X, Bernheiden M, et al. Lipopolysaccharide-binding protein is required to combat a murine gram-negative bacterial infection. Nature 1997;389:742-745
    • (1997) Nature , vol.389 , pp. 742-745
    • Jack, R.S.1    Fan, X.2    Bernheiden, M.3
  • 15
    • 0032523815 scopus 로고    scopus 로고
    • LPS-binding protein protects mice from septic shock caused by LPS or gram-negative bacteria
    • Lamping N, Dettmer R, Schroder NW, et al. LPS-binding protein protects mice from septic shock caused by LPS or gram-negative bacteria. J. Clin. Invest. 1998;101:2065-2071
    • (1998) J. Clin. Invest. , vol.101 , pp. 2065-2071
    • Lamping, N.1    Dettmer, R.2    Schroder, N.W.3
  • 16
    • 0023761244 scopus 로고
    • A family of lipopolysaccharide binding proteins involved in responses to gram-negative sepsis
    • Tobias PS, Mathison JC, Ulevitch RJ. A family of lipopolysaccharide binding proteins involved in responses to gram-negative sepsis. J. Biol. Chem. 1988;263:13479-13481
    • (1988) J. Biol. Chem. , vol.263 , pp. 13479-13481
    • Tobias, P.S.1    Mathison, J.C.2    Ulevitch, R.J.3
  • 17
    • 0024327707 scopus 로고
    • Cloning of the cDNA of a human neutrophil bactericidal protein: Structure and functional correlations
    • Gray PW, Flaggs G, Leong SR, et al. Cloning of the cDNA of a human neutrophil bactericidal protein: structure and functional correlations. J. Biol. Chem. 1989;264:9505-9509
    • (1989) J. Biol. Chem. , vol.264 , pp. 9505-9509
    • Gray, P.W.1    Flaggs, G.2    Leong, S.R.3
  • 18
    • 0028305216 scopus 로고
    • Complete cDNA encoding human phospholipid transfer protein from human endothelial cells
    • Day JR, Albers JJ, Lofton-Day CE, et al. Complete cDNA encoding human phospholipid transfer protein from human endothelial cells. J. Biol. Chem. 1994;269:9388-9391
    • (1994) J. Biol. Chem. , vol.269 , pp. 9388-9391
    • Day, J.R.1    Albers, J.J.2    Lofton-Day, C.E.3
  • 19
    • 0017804093 scopus 로고
    • Purification and characterization of a potent bactericidal and membrane active protein from the granules of human polymorphonuclear leukocytes
    • Weiss J, Elsbach P, Olsson I, et al. Purification and characterization of a potent bactericidal and membrane active protein from the granules of human polymorphonuclear leukocytes. J. Biol. Chem. 1978;253:2664-2672
    • (1978) J. Biol. Chem. , vol.253 , pp. 2664-2672
    • Weiss, J.1    Elsbach, P.2    Olsson, I.3
  • 20
    • 0018577634 scopus 로고
    • Separation and purification of a potent bactericidal/permeability-increasing protein and a closely associated phospholipase A2 from rabbit polymorphonuclear leukocytes: Observations on their relationship
    • Elsbach P, Weiss J, Franson RC, et al. Separation and purification of a potent bactericidal/permeability-increasing protein and a closely associated phospholipase A2 from rabbit polymorphonuclear leukocytes: observations on their relationship. J. Biol. Chem. 1979;254:11000-11009
    • (1979) J. Biol. Chem. , vol.254 , pp. 11000-11009
    • Elsbach, P.1    Weiss, J.2    Franson, R.C.3
  • 21
    • 0022655561 scopus 로고
    • Physiological effects of a bactericidal protein from human polymorphonuclear leukocytes on Pseudomonas aeruginosa
    • Hovde CJ, Gray BH. Physiological effects of a bactericidal protein from human polymorphonuclear leukocytes on Pseudomonas aeruginosa. Infect. Immun. 1986;52:90-95
    • (1986) Infect. Immun. , vol.52 , pp. 90-95
    • Hovde, C.J.1    Gray, B.H.2
  • 22
    • 0028167416 scopus 로고
    • Competition between rBPI23, a recombinant fragment of bactericidal/permeability-increasing protein, and lipopolysaccharide (LPS)-binding protein for binding to LPS and gram-negative bacteria
    • Gazzano-Santoro H, Meszaros K, Birr C, et al. Competition between rBPI23, a recombinant fragment of bactericidal/permeability-increasing protein, and lipopolysaccharide (LPS)-binding protein for binding to LPS and gram-negative bacteria. Infect. Immun. 1994;62:1185-1191
    • (1994) Infect. Immun. , vol.62 , pp. 1185-1191
    • Gazzano-Santoro, H.1    Meszaros, K.2    Birr, C.3
  • 23
    • 0028225343 scopus 로고
    • Bactericidal activity of synthetic peptides based on the structure of the 55-kilodalton bactericidal protein from human neutrophils
    • Gray BH, Haseman JR. Bactericidal activity of synthetic peptides based on the structure of the 55-kilodalton bactericidal protein from human neutrophils. Infect. Immun. 1994;62:1732-1739
    • (1994) Infect. Immun. , vol.62 , pp. 1732-1739
    • Gray, B.H.1    Haseman, J.R.2
  • 24
    • 0027171383 scopus 로고
    • Crystal structure of an endotoxin-neutralizing protein from the horseshoe crab, Limulus anti-LPS factor, at 1.5 Å resolution
    • Hoess A, Watson S, Siber GR, et al. Crystal structure of an endotoxin-neutralizing protein from the horseshoe crab, Limulus anti-LPS factor, at 1.5 Å resolution. EMBO J. 1993;12:3351-3356
    • (1993) EMBO J. , vol.12 , pp. 3351-3356
    • Hoess, A.1    Watson, S.2    Siber, G.R.3
  • 25
    • 0030760314 scopus 로고    scopus 로고
    • Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution
    • Beamer LJ, Carroll SF, Eisenberg D. Crystal structure of human BPI and two bound phospholipids at 2.4 angstrom resolution. Science 1997;276:1861-1864
    • (1997) Science , vol.276 , pp. 1861-1864
    • Beamer, L.J.1    Carroll, S.F.2    Eisenberg, D.3
  • 26
    • 0029948769 scopus 로고    scopus 로고
    • Three-dimensional profiles for measuring compatibility of amino acid sequence with three-dimensional structure
    • Bowie JU, Zhang K, Wilmanns M, et al. Three-dimensional profiles for measuring compatibility of amino acid sequence with three-dimensional structure. Methods Enzymol. 1996;266:598-616
    • (1996) Methods Enzymol. , vol.266 , pp. 598-616
    • Bowie, J.U.1    Zhang, K.2    Wilmanns, M.3
  • 27
    • 0018948016 scopus 로고
    • Principles of a quantitative assay for bacterial endotoxins in blood that uses Limulus lysate and a chromogenic substrate
    • Webster CJ. Principles of a quantitative assay for bacterial endotoxins in blood that uses Limulus lysate and a chromogenic substrate. J. Clin. Microbiol. 1980;12:644-650
    • (1980) J. Clin. Microbiol. , vol.12 , pp. 644-650
    • Webster, C.J.1
  • 28
    • 0020416253 scopus 로고
    • Limulus anti-LPS factor: An anticoagulant which inhibits the endotoxin mediated activation of Limulus coagulation system
    • Tanaka S, Nakamura T, Morita T, et al. Limulus anti-LPS factor: an anticoagulant which inhibits the endotoxin mediated activation of Limulus coagulation system. Biochem. Biophys. Res. Commun. 1982;105:717-723
    • (1982) Biochem. Biophys. Res. Commun. , vol.105 , pp. 717-723
    • Tanaka, S.1    Nakamura, T.2    Morita, T.3
  • 29
    • 0021799698 scopus 로고
    • Isolation and biological activities of limulus anticoagulant (anti-LPS factor) which interacts with lipopolysaccharide (LPS)
    • Morita T, Ohtsubo S, Nakamura T, et al. Isolation and biological activities of limulus anticoagulant (anti-LPS factor) which interacts with lipopolysaccharide (LPS). J. Biochem. (Tokyo) 1985;97:1611-1620
    • (1985) J. Biochem. (Tokyo) , vol.97 , pp. 1611-1620
    • Morita, T.1    Ohtsubo, S.2    Nakamura, T.3
  • 30
    • 0022887258 scopus 로고
    • Primary structure of Limulus anticoagulant anti-lipopolysaccharide factor
    • Aketagawa J, Miyata T, Ohtsubo S, et al. Primary structure of Limulus anticoagulant anti-lipopolysaccharide factor. J. Biol. Chem. 1986;261:7357-7365
    • (1986) J. Biol. Chem. , vol.261 , pp. 7357-7365
    • Aketagawa, J.1    Miyata, T.2    Ohtsubo, S.3
  • 31
    • 0026780772 scopus 로고
    • Binding and neutralization of endotoxin by Limulus antilipopolysaccharide factor
    • Warren HS, Glennon ML, Wainwright N, et al. Binding and neutralization of endotoxin by Limulus antilipopolysaccharide factor. Infect. Immun. 1992;60:2506-2513
    • (1992) Infect. Immun. , vol.60 , pp. 2506-2513
    • Warren, H.S.1    Glennon, M.L.2    Wainwright, N.3
  • 32
    • 0027437736 scopus 로고
    • Lipopolysaccharide detoxification by endotoxin neutralizing protein
    • Fletcher MA, McKenna TM, Quance JL, et al. Lipopolysaccharide detoxification by endotoxin neutralizing protein. J. Surg. Res. 1993;55:147-154
    • (1993) J. Surg. Res. , vol.55 , pp. 147-154
    • Fletcher, M.A.1    McKenna, T.M.2    Quance, J.L.3
  • 33
    • 0029087339 scopus 로고
    • Peptide derivatives of three distinct lipopolysaccharide binding proteins inhibit lipopolysaccharide-induced tumor necrosis factor-α secretion in vitro
    • Battafarano RJ, Dahlberg PS, Ratz CA, et al. Peptide derivatives of three distinct lipopolysaccharide binding proteins inhibit lipopolysaccharide-induced tumor necrosis factor-α secretion in vitro. Surgery 1995;118:318-324
    • (1995) Surgery , vol.118 , pp. 318-324
    • Battafarano, R.J.1    Dahlberg, P.S.2    Ratz, C.A.3
  • 34
    • 0029902934 scopus 로고    scopus 로고
    • High affinity endotoxin-binding and neutralizing peptides based on the crystal structure of recombinant Limulus anti-lipopolysaccharide factor
    • Ried C, Wahl C, Miethke T, et al. High affinity endotoxin-binding and neutralizing peptides based on the crystal structure of recombinant Limulus anti-lipopolysaccharide factor. J. Biol. Chem. 1996;271:28120-28127
    • (1996) J. Biol. Chem. , vol.271 , pp. 28120-28127
    • Ried, C.1    Wahl, C.2    Miethke, T.3
  • 35
    • 0026518709 scopus 로고
    • Transfection of CD14 into 70Z/3 cells dramatically enhances the sensitivity to complexes of lipopolysaccharide (LPS) and LPS binding protein
    • Lee J-D Kato, K Tobias, PS, et al. Transfection of CD14 into 70Z/3 cells dramatically enhances the sensitivity to complexes of lipopolysaccharide (LPS) and LPS binding protein. J. Exp. Med. 1992;175:1697-1705
    • (1992) J. Exp. Med. , vol.175 , pp. 1697-1705
    • Lee, J.-D.1    Kato, K.2    Tobias, P.S.3
  • 36
    • 0026463120 scopus 로고
    • Soluble CD14 participates in the response of cells to lipopolysaccharide
    • Frey EA, Miller DS, Jahr TG, et al. Soluble CD14 participates in the response of cells to lipopolysaccharide. J. Exp. Med. 1992;176:1665-1671
    • (1992) J. Exp. Med. , vol.176 , pp. 1665-1671
    • Frey, E.A.1    Miller, D.S.2    Jahr, T.G.3
  • 37
    • 0027446922 scopus 로고
    • Lipopolysaccharide (LPS) activation of human endothelial and epithelial cells is mediated by LPS binding protein and soluble CD14
    • Pugin J, Schurer-Maly CC, Leturcq D, et al: Lipopolysaccharide (LPS) activation of human endothelial and epithelial cells is mediated by LPS binding protein and soluble CD14. Proc. Natl. Acad. Sci. U.S.A. 1993;90:2744-2748
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 2744-2748
    • Pugin, J.1    Schurer-Maly, C.C.2    Leturcq, D.3
  • 38
    • 0029919991 scopus 로고    scopus 로고
    • Resistance to endotoxin shock and reduced dissemination of gram-negative bacteria in CD14-deficient mice
    • Haziot A, Ferrero E, Kontgen F, et al. Resistance to endotoxin shock and reduced dissemination of gram-negative bacteria in CD14-deficient mice. Immunity 1996;4:407-414
    • (1996) Immunity , vol.4 , pp. 407-414
    • Haziot, A.1    Ferrero, E.2    Kontgen, F.3
  • 39
    • 0032521268 scopus 로고    scopus 로고
    • The induction of acute phase proteins by lipopolysaccharide uses a novel pathway that is CD14-independent
    • Haziot A, Lin XY, Zhang F, et al. The induction of acute phase proteins by lipopolysaccharide uses a novel pathway that is CD14-independent. J. Immunol. 1998;160:2570-2572
    • (1998) J. Immunol. , vol.160 , pp. 2570-2572
    • Haziot, A.1    Lin, X.Y.2    Zhang, F.3
  • 40
    • 0028957668 scopus 로고
    • Identification of a lipopolysaccharide binding domain in CD14 between amino acids 57 and 64
    • Juan TS-C, Hailman E, Kelly MJ, et al. Identification of a lipopolysaccharide binding domain in CD14 between amino acids 57 and 64. J. Biol. Chem. 1995;270:5219-5224
    • (1995) J. Biol. Chem. , vol.270 , pp. 5219-5224
    • Juan, T.S.-C.1    Hailman, E.2    Kelly, M.J.3
  • 41
    • 0028962319 scopus 로고
    • CD14: Physical properties and identification of an exposed site that is protected by lipopolysaccharide
    • McGinley MD, Narhi LO, Kelley MJ, et al. CD14: Physical properties and identification of an exposed site that is protected by lipopolysaccharide. J. Biol. Chem. 1995;270:5213-5218
    • (1995) J. Biol. Chem. , vol.270 , pp. 5213-5218
    • McGinley, M.D.1    Narhi, L.O.2    Kelley, M.J.3
  • 42
    • 0031774181 scopus 로고    scopus 로고
    • Human toll-like receptor 2 conveys responsiveness to bacterial lipopolysaccharide
    • Kirschning CJ, Wesche H, Ayres TM, et al. Human toll-like receptor 2 conveys responsiveness to bacterial lipopolysaccharide. J. Exp. Med. 1998;188:2091-2097
    • (1998) J. Exp. Med. , vol.188 , pp. 2091-2097
    • Kirschning, C.J.1    Wesche, H.2    Ayres, T.M.3
  • 43
    • 0032541661 scopus 로고    scopus 로고
    • Toll-like receptor-2 mediates lipopolysaccharide-induced cellular signaling
    • Yang RB, Mark MR, Gray A, et al. Toll-like receptor-2 mediates lipopolysaccharide-induced cellular signaling. Nature 1998;17:284-288
    • (1998) Nature , vol.17 , pp. 284-288
    • Yang, R.B.1    Mark, M.R.2    Gray, A.3
  • 44
    • 0032509295 scopus 로고    scopus 로고
    • Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: Mutations in Tlr4 gene
    • Poltorak A, He X, Smirnova I, et al. Defective LPS signaling in C3H/HeJ and C57BL/10ScCr mice: mutations in Tlr4 gene. Science 1998;282:2085-2088
    • (1998) Science , vol.282 , pp. 2085-2088
    • Poltorak, A.1    He, X.2    Smirnova, I.3
  • 45
    • 0033120081 scopus 로고    scopus 로고
    • Cutting edge: Toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide: Evidence for TLR4 as the Lps gene product
    • Hoshino K, Takeuchi O, Kawai T, et al. Cutting edge: toll-like receptor 4 (TLR4)-deficient mice are hyporesponsive to lipopolysaccharide: evidence for TLR4 as the Lps gene product. J. Immunol. 1999;162:3749-3752
    • (1999) J. Immunol. , vol.162 , pp. 3749-3752
    • Hoshino, K.1    Takeuchi, O.2    Kawai, T.3
  • 46
    • 0032526861 scopus 로고    scopus 로고
    • The human toll signaling pathway: Divergence of nuclear factor kappaB and JNK/SAPK activation upstream of tumor necrosis factor receptor-associated factor 6 (TRAF6)
    • Muzio M, Natoli G, Saccani S, et al. The human toll signaling pathway: divergence of nuclear factor kappaB and JNK/SAPK activation upstream of tumor necrosis factor receptor-associated factor 6 (TRAF6). J. Exp. Med. 1998;187:2097-2101
    • (1998) J. Exp. Med. , vol.187 , pp. 2097-2101
    • Muzio, M.1    Natoli, G.2    Saccani, S.3
  • 47
    • 0033583034 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharide activates nuclear factor-kappaB through interleukin-1 signaling mediators in cultured human dermal endothelial cells and mononuclear phagocytes
    • Zhang FX, Kirschning CJ, Mancinelli R, et al. Bacterial lipopolysaccharide activates nuclear factor-kappaB through interleukin-1 signaling mediators in cultured human dermal endothelial cells and mononuclear phagocytes. J. Biol. Chem. 1999;274:7611-7614
    • (1999) J. Biol. Chem. , vol.274 , pp. 7611-7614
    • Zhang, F.X.1    Kirschning, C.J.2    Mancinelli, R.3
  • 48
    • 0020261616 scopus 로고
    • Immunotherapy of gram-negative bacterial sepsis: Enhanced survival in a guinea pig model by use of rabbit antiserum to Escherichia coli J5
    • Dunn DL, Ferguson RM. Immunotherapy of gram-negative bacterial sepsis: enhanced survival in a guinea pig model by use of rabbit antiserum to Escherichia coli J5. Surgery 1982;92:212-219
    • (1982) Surgery , vol.92 , pp. 212-219
    • Dunn, D.L.1    Ferguson, R.M.2
  • 49
    • 0021877432 scopus 로고
    • Enhanced survival during murine gram-negative bacterial sepsis by use of a murine monoclonal antibody
    • Dunn DL, Bogard WC Jr, Cerra FB. Enhanced survival during murine gram-negative bacterial sepsis by use of a murine monoclonal antibody. Arch. Surg. 1985;120:50-53
    • (1985) Arch. Surg. , vol.120 , pp. 50-53
    • Dunn, D.L.1    Bogard W.C., Jr.2    Cerra, F.B.3
  • 50
    • 0022641923 scopus 로고
    • Immunotherapy of gram-negative bacterial sepsis: A single murine monoclonal antibody provides cross-genera protection
    • Dunn DL, Ewald DC, Chandan N, et al. Immunotherapy of gram-negative bacterial sepsis: a single murine monoclonal antibody provides cross-genera protection. Arch. Surg. 1986;121:58-62
    • (1986) Arch. Surg. , vol.121 , pp. 58-62
    • Dunn, D.L.1    Ewald, D.C.2    Chandan, N.3
  • 51
    • 0024411873 scopus 로고
    • Treatment of toxic shock syndrome with endotoxin-neutralizing antibody
    • Priest BP, Schlievert PM, Dunn DL. Treatment of toxic shock syndrome with endotoxin-neutralizing antibody. J. Surg. Res. 1989;46:527-531
    • (1989) J. Surg. Res. , vol.46 , pp. 527-531
    • Priest, B.P.1    Schlievert, P.M.2    Dunn, D.L.3
  • 52
    • 0025917510 scopus 로고
    • A controlled trial of E5 murine monoclonal IgM antibody to endotoxin in the treatment of gram-negative sepsis
    • Greenman RL, Schein RM, Martin MA, et al. A controlled trial of E5 murine monoclonal IgM antibody to endotoxin in the treatment of gram-negative sepsis. J.A.M.A. 1991;266:1097-1102
    • (1991) J.A.M.A. , vol.266 , pp. 1097-1102
    • Greenman, R.L.1    Schein, R.M.2    Martin, M.A.3
  • 53
    • 0029043636 scopus 로고
    • A second large controlled clinical trial of E5, a monoclonal antibody to endotoxin: Results of a prospective, multicenter, randomized, controlled trial
    • Bone RC, Balk RA, Fein AM, et al. A second large controlled clinical trial of E5, a monoclonal antibody to endotoxin: results of a prospective, multicenter, randomized, controlled trial. Crit. Care Med. 1995;23:994-1006
    • (1995) Crit. Care Med. , vol.23 , pp. 994-1006
    • Bone, R.C.1    Balk, R.A.2    Fein, A.M.3
  • 54
    • 0026293815 scopus 로고
    • Immunotherapy with antibodies to core lipopolysaccharide: A critical appraisal
    • Baumgartner JD. Immunotherapy with antibodies to core lipopolysaccharide: a critical appraisal. Infect. Dis. Clin. North Am. 1991;5:915-927
    • (1991) Infect. Dis. Clin. North Am. , vol.5 , pp. 915-927
    • Baumgartner, J.D.1
  • 55
    • 0027396598 scopus 로고
    • Assessment of ability of murine and human anti-lipid A monoclonal antibodies to bind and neutralize lipopolysaccharide
    • Warren HS, Amato SF, Fitting C, et al. Assessment of ability of murine and human anti-lipid A monoclonal antibodies to bind and neutralize lipopolysaccharide. J. Exp. Med. 1993;177:89-97
    • (1993) J. Exp. Med. , vol.177 , pp. 89-97
    • Warren, H.S.1    Amato, S.F.2    Fitting, C.3
  • 56
    • 0015501530 scopus 로고
    • Type-specific and cross-reactive antibodies in gram-negative bacteremia
    • McCabe W, Kreger B, Johns M. Type-specific and cross-reactive antibodies in gram-negative bacteremia. N. Engl. J. Med. 1972;287:261-267
    • (1972) N. Engl. J. Med. , vol.287 , pp. 261-267
    • McCabe, W.1    Kreger, B.2    Johns, M.3
  • 57
    • 0017233228 scopus 로고
    • Effects of IgM and IgG antibody in patients with bacteremia due to gram-negative bacilli
    • Zinner S, McCabe W. Effects of IgM and IgG antibody in patients with bacteremia due to gram-negative bacilli. J. Infect. Dis. 1976;133:37-45
    • (1976) J. Infect. Dis. , vol.133 , pp. 37-45
    • Zinner, S.1    McCabe, W.2
  • 58
    • 0028997703 scopus 로고
    • Natural cytokine antagonists and endogenous antiendotoxin core antibodies in sepsis syndrome: The Sepsis Intervention Group
    • Goldie AS, Fearon KC, Ross JA, et al. Natural cytokine antagonists and endogenous antiendotoxin core antibodies in sepsis syndrome: the Sepsis Intervention Group. J.A.M.A. 1995;274:172-177
    • (1995) J.A.M.A. , vol.274 , pp. 172-177
    • Goldie, A.S.1    Fearon, K.C.2    Ross, J.A.3
  • 59
    • 0032968238 scopus 로고    scopus 로고
    • Relationship of antibodies to endotoxin core to mortality in medical patients with sepsis syndrome
    • Strutz F, Heller G, Krasemann K, et al. Relationship of antibodies to endotoxin core to mortality in medical patients with sepsis syndrome. Intensive Care Med. 1999;25:435-444
    • (1999) Intensive Care Med. , vol.25 , pp. 435-444
    • Strutz, F.1    Heller, G.2    Krasemann, K.3
  • 60
    • 0027481311 scopus 로고
    • Sequential anti-core glycolipid immunoglobulin antibody activities in patients with and without septic shock and their relation to outcome
    • Nys M, Damas P, Joassin L, et al. Sequential anti-core glycolipid immunoglobulin antibody activities in patients with and without septic shock and their relation to outcome. Ann. Surg. 1993;217:300-306
    • (1993) Ann. Surg. , vol.217 , pp. 300-306
    • Nys, M.1    Damas, P.2    Joassin, L.3
  • 61
    • 0027166126 scopus 로고
    • A broadly cross-protective monoclonal antibody binding to Escherichia coli and Salmonella lipopolysaccharides
    • Di Padova FE, Brade H, Barclay GR, et al. A broadly cross-protective monoclonal antibody binding to Escherichia coli and Salmonella lipopolysaccharides. Infect. Immun. 1993;61:3863-3872
    • (1993) Infect. Immun. , vol.61 , pp. 3863-3872
    • Di Padova, F.E.1    Brade, H.2    Barclay, G.R.3
  • 62
    • 0033004504 scopus 로고    scopus 로고
    • Endotoxin-core antibodies: Time for a reappraisal?
    • Barclay GR. Endotoxin-core antibodies: time for a reappraisal? Intensive Care Med. 1999;25:427-429
    • (1999) Intensive Care Med. , vol.25 , pp. 427-429
    • Barclay, G.R.1
  • 63
    • 0032775709 scopus 로고    scopus 로고
    • Antiendotoxin agents share molecular homology within their lipopolysaccharide binding domains
    • Kellogg TA, Weiss CA III, Johnston JW, et al. Antiendotoxin agents share molecular homology within their lipopolysaccharide binding domains. J. Surg. Res. 1999;85:136-141
    • (1999) J. Surg. Res. , vol.85 , pp. 136-141
    • Kellogg, T.A.1    Weiss C.A. III2    Johnston, J.W.3
  • 64
    • 0027964493 scopus 로고
    • Comparison of a recombinant endotoxin-neutralizing protein with a human monoclonal antibody to endotoxin for the treatment of Escherichia coli sepsis in rats
    • Kuppermann N, Nelson DS, Saladino RA, et al. Comparison of a recombinant endotoxin-neutralizing protein with a human monoclonal antibody to endotoxin for the treatment of Escherichia coli sepsis in rats. J. Infect. Dis. 1994;170:630-635
    • (1994) J. Infect. Dis. , vol.170 , pp. 630-635
    • Kuppermann, N.1    Nelson, D.S.2    Saladino, R.A.3
  • 65
    • 0028110893 scopus 로고
    • Effect of a recombinant endotoxin-neutralizing protein on endotoxin shock in rabbits
    • Garcia C, Saladino R, Thompson C, et al. Effect of a recombinant endotoxin-neutralizing protein on endotoxin shock in rabbits. Crit. Care Med. 1994;22:1211-1218
    • (1994) Crit. Care Med. , vol.22 , pp. 1211-1218
    • Garcia, C.1    Saladino, R.2    Thompson, C.3
  • 66
    • 0031951337 scopus 로고    scopus 로고
    • Limulus antilipopolysaccharide factor prevents mortality late in the course of endotoxemia
    • Roth RI, Su D, Child AH, et al. Limulus antilipopolysaccharide factor prevents mortality late in the course of endotoxemia. J. Infect. Dis. 1998;177:388-394
    • (1998) J. Infect. Dis. , vol.177 , pp. 388-394
    • Roth, R.I.1    Su, D.2    Child, A.H.3
  • 67
    • 0030007745 scopus 로고    scopus 로고
    • High-dose recombinant endotoxin neutralizing protein improves survival in rabbits with Escherichia coli sepsis
    • Saladino RA, Stack AM, Thompson C, et al. High-dose recombinant endotoxin neutralizing protein improves survival in rabbits with Escherichia coli sepsis. Crit. Care Med. 1996;24:1203-1207
    • (1996) Crit. Care Med. , vol.24 , pp. 1203-1207
    • Saladino, R.A.1    Stack, A.M.2    Thompson, C.3
  • 68
    • 0029788248 scopus 로고    scopus 로고
    • Comparison of early and late treatment with a recombinant endotoxin neutralizing protein in a rat model of Escherichia coli sepsis
    • Weiner DL, Kuppermann N, Saladino RA, et al. Comparison of early and late treatment with a recombinant endotoxin neutralizing protein in a rat model of Escherichia coli sepsis. Crit. Care Med. 1996;24:1514-1517
    • (1996) Crit. Care Med. , vol.24 , pp. 1514-1517
    • Weiner, D.L.1    Kuppermann, N.2    Saladino, R.A.3
  • 69
    • 0028297677 scopus 로고
    • An amino-terminal fragment of human lipopolysaccharide-binding protein retains lipid A binding but not CD14-stimulatory activity
    • Theofan G, Horwitz AH, Williams RE, et al. An amino-terminal fragment of human lipopolysaccharide-binding protein retains lipid A binding but not CD14-stimulatory activity. J. Immunol. 1994;152:3623-3629
    • (1994) J. Immunol. , vol.152 , pp. 3623-3629
    • Theofan, G.1    Horwitz, A.H.2    Williams, R.E.3
  • 70
    • 0028286765 scopus 로고
    • Lipopolysaccharide (LPS) binding protein, truncated at Ile-197, binds LPS but does not transfer LPS to CD14
    • Han J, Mathison JC, Ulevitch RJ, et al. Lipopolysaccharide (LPS) binding protein, truncated at Ile-197, binds LPS but does not transfer LPS to CD14. J. Biol. Chem. 1994;269:8172-8175
    • (1994) J. Biol. Chem. , vol.269 , pp. 8172-8175
    • Han, J.1    Mathison, J.C.2    Ulevitch, R.J.3
  • 71
    • 0028825935 scopus 로고
    • Activity of lipopolysaccharide-binding protein-bactericidal/permeability-increasing protein fusion peptide in an experimental model of Pseudomonas sepsis
    • Opal SM, Palardy JE, Jhung JW, et al. Activity of lipopolysaccharide-binding protein-bactericidal/permeability-increasing protein fusion peptide in an experimental model of Pseudomonas sepsis. Antimicrob. Agents Chemother. 1995;39:2813-2815
    • (1995) Antimicrob. Agents Chemother. , vol.39 , pp. 2813-2815
    • Opal, S.M.1    Palardy, J.E.2    Jhung, J.W.3
  • 72
    • 0028924148 scopus 로고
    • Protection against endotoxic shock by bactericidal/permeability-increasing protein in rats
    • Jin H, Yang R, Marsters S, et al. Protection against endotoxic shock by bactericidal/permeability-increasing protein in rats. J. Clin. Invest. 1995;95:1947-1952
    • (1995) J. Clin. Invest. , vol.95 , pp. 1947-1952
    • Jin, H.1    Yang, R.2    Marsters, S.3
  • 73
    • 0028324317 scopus 로고
    • Human neutrophil bactericidal/permeability-increasing protein reduces mortality rate from endotoxin challenge: A placebo-controlled study
    • Fisher CJJ, Marra MN, Palardy JE, et al. Human neutrophil bactericidal/permeability-increasing protein reduces mortality rate from endotoxin challenge: a placebo-controlled study. Crit. Care Med. 1994;22:553-558
    • (1994) Crit. Care Med. , vol.22 , pp. 553-558
    • Fisher, C.J.J.1    Marra, M.N.2    Palardy, J.E.3
  • 74
    • 0028214566 scopus 로고
    • Endotoxin-binding and -neutralizing properties of recombinant bactericidal/permeability-increasing protein and monoclonal antibodies HA-1A and E5
    • Marra MN, Thornton MB, Snable JL, et al. Endotoxin-binding and -neutralizing properties of recombinant bactericidal/permeability-increasing protein and monoclonal antibodies HA-1A and E5. Crit. Care Med. 1994;22:559-565
    • (1994) Crit. Care Med. , vol.22 , pp. 559-565
    • Marra, M.N.1    Thornton, M.B.2    Snable, J.L.3
  • 75
    • 0023525873 scopus 로고
    • A 25-kDa NH2-terminal fragment carries all the antibacterial activities of the human neutrophil 60-kDa bactericidal/permeability-increasing protein
    • Ooi CE, Weiss J, Elsbach P, et al. A 25-kDa NH2-terminal fragment carries all the antibacterial activities of the human neutrophil 60-kDa bactericidal/permeability-increasing protein. J. Biol. Chem. 1987;262:14891-14894
    • (1987) J. Biol. Chem. , vol.262 , pp. 14891-14894
    • Ooi, C.E.1    Weiss, J.2    Elsbach, P.3
  • 76
    • 0026779276 scopus 로고
    • Human bactericidal/permeability-increasing protein and a recombinant NH2-terminal fragment cause killing of serum-resistant gram-negative bacteria in whole blood and inhibit tumor necrosis factor release induced by the bacteria
    • Weiss J, Elsbach P, Shu C, et al. Human bactericidal/permeability-increasing protein and a recombinant NH2-terminal fragment cause killing of serum-resistant gram-negative bacteria in whole blood and inhibit tumor necrosis factor release induced by the bacteria. J. Clin. Invest. 1992;90:1122-1130
    • (1992) J. Clin. Invest. , vol.90 , pp. 1122-1130
    • Weiss, J.1    Elsbach, P.2    Shu, C.3
  • 77
    • 0027368661 scopus 로고
    • Protective effect of a recombinant amino-terminal fragment of bactericidal/permeability-increasing protein in experimental endotoxemia
    • Kohn FR, Ammons WS, Horwitz A, et al. Protective effect of a recombinant amino-terminal fragment of bactericidal/permeability-increasing protein in experimental endotoxemia. J. Infect. Dis. 1993;168:1307-1310
    • (1993) J. Infect. Dis. , vol.168 , pp. 1307-1310
    • Kohn, F.R.1    Ammons, W.S.2    Horwitz, A.3
  • 78
    • 0028542299 scopus 로고
    • Protective effects of a recombinant N-terminal fragment of bactericidal/permeability increasing protein on endotoxic shock in conscious rabbits
    • Lin Y, Ammons WS, Leach WJ, et al. Protective effects of a recombinant N-terminal fragment of bactericidal/permeability increasing protein on endotoxic shock in conscious rabbits. Shock 1994;2:324-331
    • (1994) Shock , vol.2 , pp. 324-331
    • Lin, Y.1    Ammons, W.S.2    Leach, W.J.3
  • 79
    • 0028020765 scopus 로고
    • Protective effects of an N-terminal fragment of bactericidal/permeability-increasing protein in rodent models of gram-negative sepsis: Role of bactericidal properties
    • Ammons WS, Kohn FR, Kung AH. Protective effects of an N-terminal fragment of bactericidal/permeability-increasing protein in rodent models of gram-negative sepsis: role of bactericidal properties. J. Infect. Dis. 1994;170:1473-1482
    • (1994) J. Infect. Dis. , vol.170 , pp. 1473-1482
    • Ammons, W.S.1    Kohn, F.R.2    Kung, A.H.3
  • 80
    • 0030025638 scopus 로고    scopus 로고
    • Synergistic effect of a recombinant N-terminal fragment of bactericidal/permeability-increasing protein and cefamandole in treatment of rabbit gram-negative sepsis
    • Lin Y, Leach WJ, Ammons WS. Synergistic effect of a recombinant N-terminal fragment of bactericidal/permeability-increasing protein and cefamandole in treatment of rabbit gram-negative sepsis. Antimicrob. Agents Chemother. 1996;40:65-69
    • (1996) Antimicrob. Agents Chemother. , vol.40 , pp. 65-69
    • Lin, Y.1    Leach, W.J.2    Ammons, W.S.3
  • 81
    • 0029385205 scopus 로고
    • The recombinant 23-kDa N-terminal fragment of bactericidal/permeability-increasing protein (rBPI23) decreases Escherichia coli-induced mortality and organ injury during immunosuppression-related neutropenia
    • Lechner AJ, Lamprech KE, Johanns CA, et al. The recombinant 23-kDa N-terminal fragment of bactericidal/permeability-increasing protein (rBPI23) decreases Escherichia coli-induced mortality and organ injury during immunosuppression-related neutropenia. Shock 1995;4:298-306
    • (1995) Shock , vol.4 , pp. 298-306
    • Lechner, A.J.1    Lamprech, K.E.2    Johanns, C.A.3
  • 82
    • 0028798378 scopus 로고
    • Protective effects of a recombinant amino-terminal fragment of human bactericidal/permeability-increasing protein in an animal model of gram-negative sepsis
    • Evans TJ, Carpenter A, Moyes D, et al. Protective effects of a recombinant amino-terminal fragment of human bactericidal/permeability-increasing protein in an animal model of gram-negative sepsis. J. Infect. Dis. 1995;171:153-160
    • (1995) J. Infect. Dis. , vol.171 , pp. 153-160
    • Evans, T.J.1    Carpenter, A.2    Moyes, D.3
  • 83
    • 0030077332 scopus 로고    scopus 로고
    • A phase I safety and pharmacokinetic study of a recombinant amino terminal fragment of bactericidal/permeability-increasing protein in healthy male volunteers
    • Bauer RJ, White ML, Wedel N, et al. A phase I safety and pharmacokinetic study of a recombinant amino terminal fragment of bactericidal/permeability-increasing protein in healthy male volunteers. Shock 1996;5:91-96
    • (1996) Shock , vol.5 , pp. 91-96
    • Bauer, R.J.1    White, M.L.2    Wedel, N.3
  • 84
    • 0031583752 scopus 로고    scopus 로고
    • Preliminary evaluation of recombinant amino-terminal fragment of human bactericidal/permeability-increasing protein in children with severe meningococcal sepsis
    • Giroir BP, Quint PA, Barton P, et al. Preliminary evaluation of recombinant amino-terminal fragment of human bactericidal/permeability-increasing protein in children with severe meningococcal sepsis. Lancet 1997;350:1439-1443
    • (1997) Lancet , vol.350 , pp. 1439-1443
    • Giroir, B.P.1    Quint, P.A.2    Barton, P.3
  • 85
    • 0032941856 scopus 로고    scopus 로고
    • Bactericidal/permeability-increasing protein (rBPI21) in patients with hemorrhage due to trauma: Results of a multicenter phase II clinical trial
    • rBPI21 Acute Hemorrhagic Trauma Study Group
    • Demetriades D, Smith JS, Jacobson LE, et al. Bactericidal/permeability-increasing protein (rBPI21) in patients with hemorrhage due to trauma: results of a multicenter phase II clinical trial. rBPI21 Acute Hemorrhagic Trauma Study Group. J. Trauma 1999;46:667-676
    • (1999) J. Trauma , vol.46 , pp. 667-676
    • Demetriades, D.1    Smith, J.S.2    Jacobson, L.E.3
  • 86
    • 0032544997 scopus 로고    scopus 로고
    • Affinities of different proteins and peptides for lipopolysaccharide as determined by biosensor technology
    • De Haas CJ, Haas PJ, van Kessel KP, et al. Affinities of different proteins and peptides for lipopolysaccharide as determined by biosensor technology. Biochem. Biophys. Res. Commun. 1998;252:492-496
    • (1998) Biochem. Biophys. Res. Commun. , vol.252 , pp. 492-496
    • De Haas, C.J.1    Haas, P.J.2    Van Kessel, K.P.3
  • 87
    • 0032538127 scopus 로고    scopus 로고
    • Designed beta-sheet-forming peptide 33mers with potent human bactericidal/permeability increasing protein-like bactericidal and endotoxin neutralizing activities
    • Mayo KH, Haseman J, Ilyina E, et al. Designed beta-sheet-forming peptide 33mers with potent human bactericidal/permeability increasing protein-like bactericidal and endotoxin neutralizing activities. Biochim. Biophys. Acta 1998;1425:81-92
    • (1998) Biochim. Biophys. Acta , vol.1425 , pp. 81-92
    • Mayo, K.H.1    Haseman, J.2    Ilyina, E.3
  • 88
    • 12644278299 scopus 로고    scopus 로고
    • Design of a potent novel endotoxin antagonist
    • Uknis ME, Wasiluk KR, Acton RD, et al. Design of a potent novel endotoxin antagonist. Surgery 1997;122:380-385
    • (1997) Surgery , vol.122 , pp. 380-385
    • Uknis, M.E.1    Wasiluk, K.R.2    Acton, R.D.3
  • 89
    • 0029951814 scopus 로고    scopus 로고
    • A novel endotoxin antagonist attenuates tumor necrosis factor-alpha secretion
    • Dahlberg PS, Acton RD, Battafarano RJ, et al. A novel endotoxin antagonist attenuates tumor necrosis factor-alpha secretion. J. Surg. Res. 1996;63:44-48
    • (1996) J. Surg. Res. , vol.63 , pp. 44-48
    • Dahlberg, P.S.1    Acton, R.D.2    Battafarano, R.J.3
  • 90
    • 0029854969 scopus 로고    scopus 로고
    • Macrophages expressing a fusion protein derived from bactericidal/permeability-increasing protein and IgG are resistant to endotoxin
    • Dahlberg PS, Acton RD, Uknis ME, et al. Macrophages expressing a fusion protein derived from bactericidal/permeability-increasing protein and IgG are resistant to endotoxin. Arch. Surg. 1996;131:1173-1177
    • (1996) Arch. Surg. , vol.131 , pp. 1173-1177
    • Dahlberg, P.S.1    Acton, R.D.2    Uknis, M.E.3
  • 91
    • 0029044454 scopus 로고
    • B/PI-derived synthetic peptides: Synergistic effects in tethered bactericidal and endotoxin neutralizing peptides
    • Gray BH, Haseman JR, Mayo KH. B/PI-derived synthetic peptides: synergistic effects in tethered bactericidal and endotoxin neutralizing peptides. Biochim. Biophys. Acta 1995;1244:185-190
    • (1995) Biochim. Biophys. Acta , vol.1244 , pp. 185-190
    • Gray, B.H.1    Haseman, J.R.2    Mayo, K.H.3
  • 92
    • 0027379689 scopus 로고
    • Lipopolysaccharide-binding protein as a major plasma protein responsible for endotoxemic shock
    • Gallay P, Heumann D, Le Roy D, et al. Lipopolysaccharide-binding protein as a major plasma protein responsible for endotoxemic shock. Proc. Natl. Acad. Sci. U.S.A. 1993;90:9935-9938
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 9935-9938
    • Gallay, P.1    Heumann, D.2    Le Roy, D.3
  • 93
    • 0028108442 scopus 로고
    • Mode of action of antilipopolysaccharide-binding protein antibodies for prevention of endotoxemic shock in mice
    • Gallay P, Heumann D, Le Roy D, et al. Mode of action of antilipopolysaccharide-binding protein antibodies for prevention of endotoxemic shock in mice. Proc. Natl. Acad. Sci. U.S.A. 1994;91:7922-7926
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 7922-7926
    • Gallay, P.1    Heumann, D.2    Le Roy, D.3
  • 94
    • 0032754358 scopus 로고    scopus 로고
    • Relationship between plasma levels of lipopolysaccharide (LPS) and LPS-binding protein in patients with severe sepsis and septic shock
    • Opal SM, Scannon PJ, Vincent JL, et al. Relationship between plasma levels of lipopolysaccharide (LPS) and LPS-binding protein in patients with severe sepsis and septic shock. J. Infect. Dis. 1999;180:1584-1589
    • (1999) J. Infect. Dis. , vol.180 , pp. 1584-1589
    • Opal, S.M.1    Scannon, P.J.2    Vincent, J.L.3
  • 95
    • 0032506137 scopus 로고    scopus 로고
    • Anti-CD14 mAb treatment provides therapeutic benefit after in vivo exposure to endotoxin
    • Schimke J, Mathison J, Morgiewicz J, et al. Anti-CD14 mAb treatment provides therapeutic benefit after in vivo exposure to endotoxin. Proc. Natl. Acad. Sci. U.S.A. 1998;95:13875-13880
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 13875-13880
    • Schimke, J.1    Mathison, J.2    Morgiewicz, J.3
  • 96
    • 0029848826 scopus 로고    scopus 로고
    • Antibodies against CD14 protect primates from endotoxin-induced shock
    • Leturcq DJ, Moriarty AM, Talbott G, et al. Antibodies against CD14 protect primates from endotoxin-induced shock. J. Clin. Invest. 1996;98:1533-1538
    • (1996) J. Clin. Invest. , vol.98 , pp. 1533-1538
    • Leturcq, D.J.1    Moriarty, A.M.2    Talbott, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.