메뉴 건너뛰기




Volumn 13, Issue 11, 2012, Pages 1458-1471

Recent approaches to novel antibacterials designed after LPS structure and biochemistry

Author keywords

Antibacterials; Gram negative bacteria; Kdo; LPS; Septic shock; Toll like receptor 4

Indexed keywords

ANTIINFECTIVE AGENT; AURANOFIN; BACTERIAL ENZYME; BACTERIUM LIPOPOLYSACCHARIDE; CD14 ANTIGEN; DALCETRAPIB; E 5531; ENDOTOXIN; ERITORAN; L 161240; LIPID A; N PYRENEMALEIMIDE; PROTEIN MD 2; RECEPTOR BLOCKING AGENT; TOLL LIKE RECEPTOR 4; TOLL LIKE RECEPTOR 4 ANTAGONIST; TU 517; UNCLASSIFIED DRUG;

EID: 84866916500     PISSN: 13894501     EISSN: 18735592     Source Type: Journal    
DOI: 10.2174/138945012803530242     Document Type: Review
Times cited : (13)

References (153)
  • 1
    • 33845707975 scopus 로고    scopus 로고
    • Antibiotics-an investment worth making?
    • Christoffersen RE. Antibiotics-an investment worth making? Nat Biotechnol 2006; 24: 1512-4.
    • (2006) Nat Biotechnol , vol.24 , pp. 1512-1514
    • Christoffersen, R.E.1
  • 2
    • 58249108035 scopus 로고    scopus 로고
    • Recent advances in the chemistry and biology of naturally occurring antibiotics
    • Nicolaou KC, Chen JS, Edmonds DJ, Entrada AA. Recent advances in the chemistry and biology of naturally occurring antibiotics. Angew Chem Int Ed 2009; 48: 660-719.
    • (2009) Angew Chem Int Ed , vol.48 , pp. 660-719
    • Nicolaou, K.C.1    Chen, J.S.2    Edmonds, D.J.3    Entrada, A.A.4
  • 3
    • 0038587681 scopus 로고    scopus 로고
    • Oxazolidinone structure-activity relationships leading to linezolid
    • Barbachyn MR, Ford CW. Oxazolidinone structure-activity relationships leading to linezolid. Angew Chem Int Ed 2003; 42: 2010-23.
    • (2003) Angew Chem Int Ed , vol.42 , pp. 2010-2023
    • Barbachyn, M.R.1    Ford, C.W.2
  • 4
  • 5
    • 33644544089 scopus 로고    scopus 로고
    • Empirical antibacterial drug discovery-foundation in natural products
    • Singh SB, Barrett JF. Empirical antibacterial drug discovery-foundation in natural products. Biochem Pharmacol 2006; 71: 1006-15.
    • (2006) Biochem Pharmacol , vol.71 , pp. 1006-1015
    • Singh, S.B.1    Barrett, J.F.2
  • 8
    • 16244421046 scopus 로고    scopus 로고
    • Daptomycin: A new drug class for the treatment of Grampositive infections
    • Alder JD. Daptomycin: a new drug class for the treatment of Grampositive infections. Drugs Today 2005; 41: 81-90.
    • (2005) Drugs Today , vol.41 , pp. 81-90
    • Alder, J.D.1
  • 10
    • 14844366787 scopus 로고    scopus 로고
    • For a thematic issue on antibiotic resistance
    • see:Walsh CT, Wright G, editors
    • For a thematic issue on antibiotic resistance, see:Walsh CT, Wright G, editors. Chem. Rev 2005; 105: 391-774
    • (2005) Chem. Rev , vol.105 , pp. 391-774
  • 11
    • 0141785586 scopus 로고    scopus 로고
    • Antimicrobial resistance among gram-positive organisms in the intensive care unit
    • Clark NM, Hershberger E, Zervosc MJ, Lynch JP 3rd. Antimicrobial resistance among gram-positive organisms in the intensive care unit. Curr Opin Crit Care 2003; 9: 403-12.
    • (2003) Curr Opin Crit Care , vol.9 , pp. 403-412
    • Clark, N.M.1    Hershberger, E.2    Zervosc, M.J.3    Lynch III, J.P.4
  • 12
    • 47749093130 scopus 로고    scopus 로고
    • The Bacteria Fight Back
    • Taubes G. The Bacteria Fight Back. Science 2008; 321: 356-61.
    • (2008) Science , vol.321 , pp. 356-361
    • Taubes, G.1
  • 14
    • 76549128410 scopus 로고    scopus 로고
    • Lipopolysaccharide: Biosynthetic pathway and structure modification
    • Wang X, Quinn PJ. Lipopolysaccharide: Biosynthetic pathway and structure modification. Progress Lipid Res 2010; 49: 97-107.
    • (2010) Progress Lipid Res , vol.49 , pp. 97-107
    • Wang, X.1    Quinn, P.J.2
  • 15
    • 66349133664 scopus 로고    scopus 로고
    • Discovery of new biosynthetic pathways: The lipid A story
    • Raetz CRH, Guan Z, Ingram BO, et al. Discovery of new biosynthetic pathways: the lipid A story. J Lipid Res 2009; 50: S103-S108.
    • (2009) J Lipid Res , vol.50
    • Raetz, C.R.H.1    Guan, Z.2    Ingram, B.O.3
  • 16
    • 3142763231 scopus 로고    scopus 로고
    • Endotoxins: Relationships between structure, function, and activity
    • Brandenburg K, Wiese A. Endotoxins: relationships between structure, function, and activity. Curr Top Med Chem 2004; 4: 1127-46.
    • (2004) Curr Top Med Chem , vol.4 , pp. 1127-1146
    • Brandenburg, K.1    Wiese, A.2
  • 17
    • 33646804835 scopus 로고    scopus 로고
    • Kdo2-Lipid A of Escherichia coli, a defined endotoxin that activates macrophages via TLR-4
    • Raetz CRH, Garrett TA, Reynolds CM, et al. Kdo2-Lipid A of Escherichia coli, a defined endotoxin that activates macrophages via TLR-4. J Lipid Res 2006; 47: 1097-111.
    • (2006) J Lipid Res , vol.47 , pp. 1097-1111
    • Raetz, C.R.H.1    Garrett, T.A.2    Reynolds, C.M.3
  • 20
    • 34547842292 scopus 로고    scopus 로고
    • Human MD-2 discrimination of meningococcal lipid A structures and activation of TLR4
    • Zimmer SM, Zughaier SM, Tzeng Y-L, Stephens DS. Human MD-2 discrimination of meningococcal lipid A structures and activation of TLR4. Glycobiology 2007; 17: 847-56.
    • (2007) Glycobiology , vol.17 , pp. 847-856
    • Zimmer, S.M.1    Zughaier, S.M.2    Tzeng, Y-L.3    Stephens, D.S.4
  • 21
    • 0036015492 scopus 로고    scopus 로고
    • Chemical structure of the core region of lipopolysaccharidesan update
    • Holst O. Chemical structure of the core region of lipopolysaccharidesan update. Trends Glycosci Glycotech 2002; 14: 87-103.
    • (2002) Trends Glycosci Glycotech , vol.14 , pp. 87-103
    • Holst, O.1
  • 22
    • 34247894051 scopus 로고    scopus 로고
    • The structures of core regions from enterobacterial lipopolysaccharides-an update
    • Holst O. The structures of core regions from enterobacterial lipopolysaccharides-an update. FEMS Microbiol Lett 2007; 271: 3-11.
    • (2007) FEMS Microbiol Lett , vol.271 , pp. 3-11
    • Holst, O.1
  • 23
    • 23044448465 scopus 로고    scopus 로고
    • The role of galacturonic acid in outer membrane stability in Klebsiella pneumoniae
    • Frirdich E, Bowman C, Vinogradov E, Whitfield C. The role of galacturonic acid in outer membrane stability in Klebsiella pneumoniae. J Biol Chem 2005; 280: 27604-12.
    • (2005) J Biol Chem , vol.280 , pp. 27604-27612
    • Frirdich, E.1    Bowman, C.2    Vinogradov, E.3    Whitfield, C.4
  • 24
    • 0036462606 scopus 로고    scopus 로고
    • Chemical diversity in the sialic acids and related alfa-keto acids: An evolutionary perspective
    • Angata T, Varki A. Chemical diversity in the sialic acids and related alfa-keto acids: an evolutionary perspective. Chem Rev 2002; 102: 439-69.
    • (2002) Chem Rev , vol.102 , pp. 439-469
    • Angata, T.1    Varki, A.2
  • 25
    • 0347479229 scopus 로고    scopus 로고
    • Molecular basis of bacterial outer membrane permeability revisited
    • Nikaido H. Molecular basis of bacterial outer membrane permeability revisited. Microbiol Mol Biol Rev 2003; 67: 593-656.
    • (2003) Microbiol Mol Biol Rev , vol.67 , pp. 593-656
    • Nikaido, H.1
  • 27
    • 33746356503 scopus 로고    scopus 로고
    • Biosynthesis and assembly of capsular polysaccharides in Escherichia coli
    • Whitfield C. Biosynthesis and assembly of capsular polysaccharides in Escherichia coli. Annu Rev Biochem 2006; 75: 39-68.
    • (2006) Annu Rev Biochem , vol.75 , pp. 39-68
    • Whitfield, C.1
  • 29
    • 0034981082 scopus 로고    scopus 로고
    • Lipopolysaccharide biosynthesis: Which steps do bacteria need to survive?
    • Gronow S, Brade H. Lipopolysaccharide biosynthesis: which steps do bacteria need to survive? J Endotoxin Res 2001; 7: 3-23.
    • (2001) J Endotoxin Res , vol.7 , pp. 3-23
    • Gronow, S.1    Brade, H.2
  • 30
    • 0035428081 scopus 로고    scopus 로고
    • Lipopolysaccharide as a target for the development of novel therapeutics in Gram-negative bacteria
    • Yethon JA, Whitfield C. Lipopolysaccharide as a target for the development of novel therapeutics in Gram-negative bacteria. Curr Drug Targets-Infect Dis 2001; 1: 91-106.
    • (2001) Curr Drug Targets-Infect Dis , vol.1 , pp. 91-106
    • Yethon, J.A.1    Whitfield, C.2
  • 31
    • 13144306075 scopus 로고    scopus 로고
    • Role of Mg2+ and pH in the modification of Salmonella lipid A after endocytosis by macrophage tumour cells
    • Gibbons HS, Kalb SR, Cotter RJ, Raetz CRH. Role of Mg2+ and pH in the modification of Salmonella lipid A after endocytosis by macrophage tumour cells. Mol Microbiol 2005; 55: 425-40.
    • (2005) Mol Microbiol , vol.55 , pp. 425-440
    • Gibbons, H.S.1    Kalb, S.R.2    Cotter, R.J.3    Raetz, C.R.H.4
  • 32
    • 23744504984 scopus 로고    scopus 로고
    • Recognition of antimicrobial peptides by a bacterial sensor kinase
    • Bader MW, Sanowar S, Daley ME, et al. Recognition of antimicrobial peptides by a bacterial sensor kinase. Cell 2005; 122: 461-72.
    • (2005) Cell , vol.122 , pp. 461-472
    • Bader, M.W.1    Sanowar, S.2    Daley, M.E.3
  • 33
    • 77953084208 scopus 로고    scopus 로고
    • Proteins Required for lipopolysaccharide assembly in Escherichia coli form a transenvelope complex
    • And refs cited therein
    • Chng S-S, Gronenberg LS, Kahne D. Proteins Required for lipopolysaccharide assembly in Escherichia coli form a transenvelope complex. Biochemistry 2010; 49: 4565-7 and refs cited therein.
    • (2010) Biochemistry , vol.49 , pp. 4565-4567
    • Chng, S-S.1    Gronenberg, L.S.2    Kahne, D.3
  • 34
    • 70350044410 scopus 로고    scopus 로고
    • Replacement of lipopolysaccharide with free lipid A molecules in Escherichia coli mutants lacking all core sugars
    • Reynolds CM, Raetz CRH. Replacement of lipopolysaccharide with free lipid A molecules in Escherichia coli mutants lacking all core sugars. Biochemistry 2009; 48: 9627-40.
    • (2009) Biochemistry , vol.48 , pp. 9627-9640
    • Reynolds, C.M.1    Raetz, C.R.H.2
  • 35
    • 0029015263 scopus 로고
    • Overproduction and one-step purification of Escherichia coli 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase and oxygen transfer studies during catalysis using isotopic-shifted heteronuclear NMR
    • Dotson GD, Dua RK, Clemens JC, Wooten EW, Woodard RW. Overproduction and one-step purification of Escherichia coli 3-deoxy-D-manno-octulosonic acid 8-phosphate synthase and oxygen transfer studies during catalysis using isotopic-shifted heteronuclear NMR. J Biol Chem 1995; 270: 13698-705.
    • (1995) J Biol Chem , vol.270 , pp. 13698-13705
    • Dotson, G.D.1    Dua, R.K.2    Clemens, J.C.3    Wooten, E.W.4    Woodard, R.W.5
  • 36
    • 0038719689 scopus 로고    scopus 로고
    • Escherichia coli YrbI is 3-deoxy-d-mannooctulosonate 8-phosphate phosphatase
    • Wu J, Woodard RW. Escherichia coli YrbI is 3-deoxy-d-mannooctulosonate 8-phosphate phosphatase. J Biol Chem 2003; 278: 18117-23.
    • (2003) J Biol Chem , vol.278 , pp. 18117-18123
    • Wu, J.1    Woodard, R.W.2
  • 37
    • 0021803094 scopus 로고
    • Molecular cloning of the structural gene coding for CTP:CMP-3-deoxy-manno-octulosonate cytidylyltransferase from Escherichia coli K-12
    • Goldman RC, Kohlbrenner WE. Molecular cloning of the structural gene coding for CTP:CMP-3-deoxy-manno-octulosonate cytidylyltransferase from Escherichia coli K-12. J Bacteriol 1985; 163: 256-61.
    • (1985) J Bacteriol , vol.163 , pp. 256-261
    • Goldman, R.C.1    Kohlbrenner, W.E.2
  • 39
    • 0026705047 scopus 로고
    • A novel 3-deoxy-Dmanno-octulosonic acid transferase from Chlamydia trachomatis required for expression of the genus-specific epitope
    • Belunis CJ, Mdluli KE, Raetz CRH, Nano FE. A novel 3-deoxy-Dmanno-octulosonic acid transferase from Chlamydia trachomatis required for expression of the genus-specific epitope. J Biol Chem 1992; 267: 18702-7.
    • (1992) J Biol Chem , vol.267 , pp. 18702-18707
    • Belunis, C.J.1    Mdluli, K.E.2    Raetz, C.R.H.3    Nano, F.E.4
  • 40
    • 0023018056 scopus 로고
    • Primary structure of CTP:CMP-3-deoxy-D-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase) from Escherichia coli
    • Goldman RC, Bolling TJ, Kohlbrenner WE, Kim Y, Fox JL. Primary structure of CTP:CMP-3-deoxy-D-manno-octulosonate cytidylyltransferase (CMP-KDO synthetase) from Escherichia coli. J Biol Chem 1986; 261: 15831-5.
    • (1986) J Biol Chem , vol.261 , pp. 15831-15835
    • Goldman, R.C.1    Bolling, T.J.2    Kohlbrenner, W.E.3    Kim, Y.4    Fox, J.L.5
  • 41
    • 26444482378 scopus 로고    scopus 로고
    • Identification of GutQ from Escherichia coli as a D-Arabinose 5-Phosphate Isomerase
    • Meredith TC, Woodard RW. Identification of GutQ from Escherichia coli as a D-Arabinose 5-Phosphate Isomerase. J Bacteriol 2005; 187: 6936-42.
    • (2005) J Bacteriol , vol.187 , pp. 6936-6942
    • Meredith, T.C.1    Woodard, R.W.2
  • 42
    • 0042357436 scopus 로고    scopus 로고
    • Escherichia coli YrbH Is a D-Arabinose 5-Phosphate Isomerase
    • Meredith TC, Woodard RW. Escherichia coli YrbH Is a D-Arabinose 5-Phosphate Isomerase. J Biol Chem 2003; 278: 32771-7.
    • (2003) J Biol Chem , vol.278 , pp. 32771-32777
    • Meredith, T.C.1    Woodard, R.W.2
  • 43
    • 33645754945 scopus 로고    scopus 로고
    • Characterization of Escherichia coli D-arabinose 5-phosphate isomerise encoded by kpsF: Implications for group 2 capsule biosynthesis
    • Meredith TC, Woodard RW. Characterization of Escherichia coli D-arabinose 5-phosphate isomerise encoded by kpsF: implications for group 2 capsule biosynthesis. Biochem J 2006; 395: 427-32.
    • (2006) Biochem J , vol.395 , pp. 427-432
    • Meredith, T.C.1    Woodard, R.W.2
  • 44
    • 33745974919 scopus 로고    scopus 로고
    • Non-essential KDO biosynthesis and new essential cell envelope biogenesis genes in the Escherichia coli yrbG-yhbG locus
    • Sperandeo P, Pozzi C, Dehò G, Polissi A. Non-essential KDO biosynthesis and new essential cell envelope biogenesis genes in the Escherichia coli yrbG-yhbG locus. Res Microbiol 2006; 157: 547-58.
    • (2006) Res Microbiol , vol.157 , pp. 547-558
    • Sperandeo, P.1    Pozzi, C.2    Dehò, G.3    Polissi, A.4
  • 45
    • 69249230757 scopus 로고    scopus 로고
    • Structure prediction and functional analysis of KdsD, an enzyme involved in lipopolysaccharide biosynthesis
    • Sommaruga S, De Gioia L, Tortora P, Polissi A. Structure prediction and functional analysis of KdsD, an enzyme involved in lipopolysaccharide biosynthesis. Biochem Biophys Res Commun 2009; 388: 222-7.
    • (2009) Biochem Biophys Res Commun , vol.388 , pp. 222-227
    • Sommaruga, S.1    de Gioia, L.2    Tortora, P.3    Polissi, A.4
  • 46
    • 41449099596 scopus 로고    scopus 로고
    • Structure and function of sedoheptulose-7-phosphate isomerase, a critical enzyme for lipopolysaccharide biosynthesis and a target for antbiotic adjuvants
    • Taylor PL, Blakely KM, de Leon GP, et al. Structure and function of sedoheptulose-7-phosphate isomerase, a critical enzyme for lipopolysaccharide biosynthesis and a target for antbiotic adjuvants. J Biol Chem 2008; 283: 2835-45.
    • (2008) J Biol Chem , vol.283 , pp. 2835-2845
    • Taylor, P.L.1    Blakely, K.M.2    de Leon, G.P.3
  • 47
    • 75749093343 scopus 로고    scopus 로고
    • Targeting bacterial membranes: NMR characterization of substrate recognition and binding requirements of D-arabinose 5P Isomerase, a key enzyme in the biosynthesis of LPS
    • Airoldi C, Sommaruga S, Merlo S, et al. Targeting bacterial membranes: NMR characterization of substrate recognition and binding requirements of D-arabinose 5P Isomerase, a key enzyme in the biosynthesis of LPS. Chem Eur J 2010; 16: 1897-902.
    • (2010) Chem Eur J , vol.16 , pp. 1897-1902
    • Airoldi, C.1    Sommaruga, S.2    Merlo, S.3
  • 48
    • 79952647273 scopus 로고    scopus 로고
    • Targeting bacterial membranes: Identification of Pseudomonas aeruginosa D-arabinose-5P Isomerase and NMR characterisation of its substrate recognition and binding properties
    • Airoldi C, Sommaruga S, Merlo S, et al. Targeting bacterial membranes: identification of Pseudomonas aeruginosa D-arabinose-5P Isomerase and NMR characterisation of its substrate recognition and binding properties ChemBioChem 2011; 12: 719-27.
    • (2011) Chem Bio Chem , vol.12 , pp. 719-727
    • Airoldi, C.1    Sommaruga, S.2    Merlo, S.3
  • 49
    • 0024240284 scopus 로고
    • 3-Deoxy-D-manno-octulosonate-8-phosphate synthase catalyzes the C-O bond cleavage of phosphoenolpyruvate
    • Hedstrom L, Abeles R. 3-Deoxy-D-manno-octulosonate-8-phosphate synthase catalyzes the C-O bond cleavage of phosphoenolpyruvate. Biochem Biophys Res Commun 1988; 157: 816-20.
    • (1988) Biochem Biophys Res Commun , vol.157 , pp. 816-820
    • Hedstrom, L.1    Abeles, R.2
  • 50
    • 0034725580 scopus 로고    scopus 로고
    • A metal bridge between two enzyme families. 3-deoxy-D-manno-octulosonate-8-phosphate synthase from Aquifex aeolicus requires a divalent metal for activity
    • Duewel HS, Woodard RW. A metal bridge between two enzyme families. 3-deoxy-D-manno-octulosonate-8-phosphate synthase from Aquifex aeolicus requires a divalent metal for activity. J Biol Chem 2000; 275: 22824-31.
    • (2000) J Biol Chem , vol.275 , pp. 22824-22831
    • Duewel, H.S.1    Woodard, R.W.2
  • 51
    • 0037060468 scopus 로고    scopus 로고
    • Helicobacter pylori 3-deoxy-Dmanno-octulosonate-8-phosphate (KDO-8-P) synthase is a zincmetalloenzyme
    • Krosky DJ, Alm R, Berg M, et al. Helicobacter pylori 3-deoxy-Dmanno-octulosonate-8-phosphate (KDO-8-P) synthase is a zincmetalloenzyme. Biochim Biophys Acta 2002; 1594: 297-306.
    • (2002) Biochim Biophys Acta , vol.1594 , pp. 297-306
    • Krosky, D.J.1    Alm, R.2    Berg, M.3
  • 52
    • 22544458784 scopus 로고    scopus 로고
    • Crystal structures of Escherichia coli KDO8P Synthase complexes reveal the source of catalytic irreversibility
    • Vainer R, Belakhov V, Rabkin E, Baasov T, Adir N. Crystal structures of Escherichia coli KDO8P Synthase complexes reveal the source of catalytic irreversibility. J Mol Biol 2005; 351: 641-52.
    • (2005) J Mol Biol , vol.351 , pp. 641-652
    • Vainer, R.1    Belakhov, V.2    Rabkin, E.3    Baasov, T.4    Adir, N.5
  • 53
    • 7244231234 scopus 로고    scopus 로고
    • A reciprocal single mutation affects the metal requirement of 3-deoxy-D-manno-2-octulosonate-8-phosphate (KDO8P) synthases from Aquifex pyrophilus and Escherichia coli
    • Shulami S, Furdui C, Adir N, Shoham Y, Anderson KS, Baasov T. A reciprocal single mutation affects the metal requirement of 3-deoxy-D-manno-2-octulosonate-8-phosphate (KDO8P) synthases from Aquifex pyrophilus and Escherichia coli. J Biol Chem 2004; 43: 45110-20.
    • (2004) J Biol Chem , vol.43 , pp. 45110-45120
    • Shulami, S.1    Furdui, C.2    Adir, N.3    Shoham, Y.4    Anderson, K.S.5    Baasov, T.6
  • 54
    • 0030807448 scopus 로고    scopus 로고
    • Catalytic mechanism of KDO8P synthase: Synthesis and evaluation of a putative reaction intermediate
    • Liang P-H, Kohen A, Baasov T, Anderson KS. Catalytic mechanism of KDO8P synthase: synthesis and evaluation of a putative reaction intermediate. Bioorg Med Chem Lett 1997; 7: 2457-62.
    • (1997) Bioorg Med Chem Lett , vol.7 , pp. 2457-2462
    • Liang, P-H.1    Kohen, A.2    Baasov, T.3    Anderson, K.S.4
  • 55
    • 0042021429 scopus 로고    scopus 로고
    • A snapshot of enzyme catalysis using electrospray ionization mass spectrometry
    • Li Z, Sau AK, Shen S, Whitehouse C, Baasov T, Anderson KS. A snapshot of enzyme catalysis using electrospray ionization mass spectrometry. J Am Chem Soc 2003; 125: 9938-9.
    • (2003) J Am Chem Soc , vol.125 , pp. 9938-9939
    • Li, Z.1    Sau, A.K.2    Shen, S.3    Whitehouse, C.4    Baasov, T.5    Anderson, K.S.6
  • 56
    • 0037448881 scopus 로고    scopus 로고
    • Inhibition mode of a bisubstrate inhibitor of KDO8P synthase: A frequency-selective REDOR solid-state and solution NMR characterization
    • Kaustov L, Kababya S, Belakhov V, Baasov T, Shoham Y, Schmidt A. Inhibition mode of a bisubstrate inhibitor of KDO8P synthase: a frequency-selective REDOR solid-state and solution NMR characterization. J Am Chem Soc 2003; 125: 4662-9.
    • (2003) J Am Chem Soc , vol.125 , pp. 4662-4669
    • Kaustov, L.1    Kababya, S.2    Belakhov, V.3    Baasov, T.4    Shoham, Y.5    Schmidt, A.6
  • 57
    • 18644365356 scopus 로고    scopus 로고
    • The Use of (E)-and (Z)-phosphoenol-3-fluoropyruvate as mechanistic probes reveals significant differences between the active sites of KDO8P and DAHP Synthases
    • Furdui CM, Sau AK, Yaniv O, et al. The Use of (E)-and (Z)-phosphoenol-3-fluoropyruvate as mechanistic probes reveals significant differences between the active sites of KDO8P and DAHP Synthases. Biochemistry 2005; 44: 7326-35.
    • (2005) Biochemistry , vol.44 , pp. 7326-7335
    • Furdui, C.M.1    Sau, A.K.2    Yaniv, O.3
  • 58
    • 0014010868 scopus 로고
    • The biosynthesis of cell wall lipopolysaccharide in Escherichia coli. V. Purification and properties of 3-deoxy-D-manno-octulosonate aldolase
    • Ghalambor MA, Heath EC. The biosynthesis of cell wall lipopolysaccharide in Escherichia coli. V. Purification and properties of 3-deoxy-D-manno-octulosonate aldolase. J Biol Chem 1966; 241: 3222-7.
    • (1966) J Biol Chem , vol.241 , pp. 3222-3227
    • Ghalambor, M.A.1    Heath, E.C.2
  • 59
    • 0016677986 scopus 로고
    • Isolation of 3-deoxy-2-octulosonate 8-phosphate phosphatase, a new specific enzyme in the biosynthesis of lipopolysaccharide
    • Berger H, Hammerschmid F. Isolation of 3-deoxy-2-octulosonate 8-phosphate phosphatase, a new specific enzyme in the biosynthesis of lipopolysaccharide. Biochem Soc Trans 1975; 3: 1096-7.
    • (1975) Biochem Soc Trans , vol.3 , pp. 1096-1097
    • Berger, H.1    Hammerschmid, F.2
  • 60
    • 0018944778 scopus 로고
    • Purification and characterization of specific 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase from Escherichia coli B
    • Ray PH, Benedict CD. Purification and characterization of specific 3-deoxy-D-manno-octulosonate 8-phosphate phosphatase from Escherichia coli B. J Bacteriol 1980; 142: 60-8.
    • (1980) J Bacteriol , vol.142 , pp. 60-68
    • Ray, P.H.1    Benedict, C.D.2
  • 61
    • 70549088808 scopus 로고    scopus 로고
    • The tail of KdsC conformational changes control the activity of a haloacid dehalogenase superfamily phosphatise
    • Biswas T, Yi L, Aggarwal P, et al. The tail of KdsC conformational changes control the activity of a haloacid dehalogenase superfamily phosphatise J Biol Chem 2009; 284: 30594-603.
    • (2009) J Biol Chem , vol.284 , pp. 30594-30603
    • Biswas, T.1    Yi, L.2    Aggarwal, P.3
  • 62
    • 0036499628 scopus 로고    scopus 로고
    • From structure to function: YrbI From Haemophilus influenzae (HI1679) is a phosphatase
    • Parsons JF, Lim K, Tempczyk A, et al. From structure to function: YrbI From Haemophilus influenzae (HI1679) is a phosphatase. Proteins 2002; 46: 393-404.
    • (2002) Proteins , vol.46 , pp. 393-404
    • Parsons, J.F.1    Lim, K.2    Tempczyk, A.3
  • 63
    • 33846023053 scopus 로고    scopus 로고
    • Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family
    • Kuznetsova E, Proudfoot M, Gonzalez CF, et al. Genome-wide analysis of substrate specificities of the Escherichia coli haloacid dehalogenase-like phosphatase family. J Biol Chem 2006; 281: 36149-61.
    • (2006) J Biol Chem , vol.281 , pp. 36149-36161
    • Kuznetsova, E.1    Proudfoot, M.2    Gonzalez, C.F.3
  • 64
    • 0035902464 scopus 로고    scopus 로고
    • BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: Structure of a BeF(3)(-) complex with phosphoserine phosphatase
    • Cho H, Wang W, Kim R, et al. BeF(3)(-) acts as a phosphate analog in proteins phosphorylated on aspartate: structure of a BeF(3)(-) complex with phosphoserine phosphatase. Proc Natl Acad Sci USA 2001; 98: 8525-30.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 8525-8530
    • Cho, H.1    Wang, W.2    Kim, R.3
  • 65
    • 4344585269 scopus 로고    scopus 로고
    • Phosphoryl group transfer: Evolution of a catalytic scaffold
    • Allen KN, Dunaway-Mariano D. Phosphoryl group transfer: evolution of a catalytic scaffold. Trends Biochem Sci 2004; 29: 495-503.
    • (2004) Trends Biochem Sci , vol.29 , pp. 495-503
    • Allen, K.N.1    Dunaway-Mariano, D.2
  • 66
    • 70349765004 scopus 로고    scopus 로고
    • A survey of chemical methods for sugar-nucleotide synthesis
    • Wagner GK, Pesnot T, Field RA. A survey of chemical methods for sugar-nucleotide synthesis. Nat Prod Rep 2009; 26: 1172-94.
    • (2009) Nat Prod Rep , vol.26 , pp. 1172-1194
    • Wagner, G.K.1    Pesnot, T.2    Field, R.A.3
  • 67
    • 0026709527 scopus 로고
    • Capsules of Escherichia coli, expression and biological significance
    • Jann K, Jann B. Capsules of Escherichia coli, expression and biological significance. Can J Microbiol 1992; 38: 705-10.
    • (1992) Can J Microbiol , vol.38 , pp. 705-710
    • Jann, K.1    Jann, B.2
  • 68
    • 0037192148 scopus 로고    scopus 로고
    • Catalytic mechanism of CMP:2-keto-3-deoxy-manno-octonic acid synthetase as derived from complexes with reaction educt and product
    • Jelakovic S, Schulz GE. Catalytic mechanism of CMP:2-keto-3-deoxy-manno-octonic acid synthetase as derived from complexes with reaction educt and product Biochemistry 2002; 41: 1174-81.
    • (2002) Biochemistry , vol.41 , pp. 1174-1181
    • Jelakovic, S.1    Schulz, G.E.2
  • 69
    • 0037240249 scopus 로고    scopus 로고
    • Crystallization and preliminary X-ray crystallographic studies of 3-deoxymanno-octulosonate cytidylyltransferase from Haemophilus influenzae
    • Ku MJ, Yoon HJ, Ahn HJ, Kim HW, Baek SH, Suh SW. Crystallization and preliminary X-ray crystallographic studies of 3-deoxymanno-octulosonate cytidylyltransferase from Haemophilus influenzae. Acta Crystallogr D Biol Crystallogr 2003; 59: 180-2.
    • (2003) Acta Crystallogr D Biol Crystallogr , vol.59 , pp. 180-182
    • Ku, M.J.1    Yoon, H.J.2    Ahn, H.J.3    Kim, H.W.4    Baek, S.H.5    Suh, S.W.6
  • 70
    • 56649085224 scopus 로고    scopus 로고
    • Structure of 3-deoxymanno-octulosonate cytidylyltransferase from Haemophilus influenzae complexed with the substrate 3-deoxy-mannooctulosonate in the β-configuration
    • Yoon H-J, Ku M-J, Mikami B, Suh SW. Structure of 3-deoxymanno-octulosonate cytidylyltransferase from Haemophilus influenzae complexed with the substrate 3-deoxy-mannooctulosonate in the β-configuration. Acta Cryst 2008; D64: 1292-4.
    • (2008) Acta Cryst , vol.D64 , pp. 1292-1294
    • Yoon, H-J.1    Ku, M-J.2    Mikami, B.3    Suh, S.W.4
  • 71
    • 24644505760 scopus 로고    scopus 로고
    • Structural analysis of a set of proteins resulting from a bacterial genomics project
    • Badger J, Sauder M, Adams JM, et al. Structural analysis of a set of proteins resulting from a bacterial genomics project. Proteins 2005; 60: 787-96.
    • (2005) Proteins , vol.60 , pp. 787-796
    • Badger, J.1    Sauder, M.2    Adams, J.M.3
  • 72
    • 72149113859 scopus 로고    scopus 로고
    • Structure-based mechanism of CMP-2-keto-3-deoxymanno-octulonic acid synthetase: Convergent evolution of a sugar-activating enzyme with DNA/RNA polymerases
    • Heyes DJ, Levy C, Lafite P, et al. Structure-based mechanism of CMP-2-keto-3-deoxymanno-octulonic acid synthetase: convergent evolution of a sugar-activating enzyme with DNA/RNA polymerases. J Biol Chem 2009; 284: 35514-23.
    • (2009) J Biol Chem , vol.284 , pp. 35514-35523
    • Heyes, D.J.1    Levy, C.2    Lafite, P.3
  • 73
    • 0023149134 scopus 로고
    • A 2-deoxy analogue of KDO as the first inhibitor of the enzyme CMP-KDO synthetase. Biochem
    • Claesson K, Luthman K, Gustafsson K, Bondesson G. A 2-deoxy analogue of KDO as the first inhibitor of the enzyme CMP-KDO synthetase. Biochem. Biophys Res Commun 1987; 143: 1063-8.
    • (1987) Biophys Res Commun , vol.143 , pp. 1063-1068
    • Claesson, K.1    Luthman, K.2    Gustafsson, K.3    Bondesson, G.4
  • 75
    • 37749010573 scopus 로고    scopus 로고
    • Single amino acid substitutions in either YhjD or MsbA confer viability to 3-deoxy-dmanno-oct-2-ulosonic acid-depleted Escherichia coli
    • Mamat U, Meredith TC, Aggarwal P, et al. Single amino acid substitutions in either YhjD or MsbA confer viability to 3-deoxy-dmanno-oct-2-ulosonic acid-depleted Escherichia coli. Mol Microbiol 2008; 67: 633-48.
    • (2008) Mol Microbiol , vol.67 , pp. 633-648
    • Mamat, U.1    Meredith, T.C.2    Aggarwal, P.3
  • 76
    • 0346099266 scopus 로고    scopus 로고
    • Synergistic effect of CMP/KDO synthase inhibitors with antimicrobial agents on inhibition of production and release of vero toxin by enterohaemorrhagic Escherichia coli O157:H7
    • Kondo K-I, Doi H, Adachi H, Nishimura Y. Synergistic effect of CMP/KDO synthase inhibitors with antimicrobial agents on inhibition of production and release of vero toxin by enterohaemorrhagic Escherichia coli O157:H7. Bioorg Med Chem Lett 2004; 14: 467-70.
    • (2004) Bioorg Med Chem Lett , vol.14 , pp. 467-470
    • Kondo, K-I.1    Doi, H.2    Adachi, H.3    Nishimura, Y.4
  • 77
    • 79952809277 scopus 로고    scopus 로고
    • New targets for antibacterial design: Kdo biosynthesis and LPS machinery transport to the cell surface
    • Reviewed in
    • Reviewed in Cipolla L, Polissi A, Airoldi C, Gabrielli L, Merlo S, Nicotra F. New targets for antibacterial design: Kdo biosynthesis and LPS machinery transport to the cell surface. Curr Med Chem 2011; 18: 830-52.
    • (2011) Curr Med Chem , vol.18 , pp. 830-852
    • Cipolla, L.1    Polissi, A.2    Airoldi, C.3    Gabrielli, L.4    Merlo, S.5    Nicotra, F.6
  • 78
    • 79955468269 scopus 로고    scopus 로고
    • Enediol mimics as inhibitors of the D-arabinose 5-phosphate isomerase (KdsD) from Francisella tularensis
    • Yep A, Sorenson RJ, Wilson MR, et al. Enediol mimics as inhibitors of the D-arabinose 5-phosphate isomerase (KdsD) from Francisella tularensis. Bioorg Med Chem Lett 2011; 21: 2679-82.
    • (2011) Bioorg Med Chem Lett , vol.21 , pp. 2679-2682
    • Yep, A.1    Sorenson, R.J.2    Wilson, M.R.3
  • 80
    • 0034721459 scopus 로고    scopus 로고
    • Identification of a slow tightbinding inhibitor of 3-deoxy-d-manno-octulosonic acid 8-phosphate synthase
    • Birck MR, Holler TP, Woodard RV. Identification of a slow tightbinding inhibitor of 3-deoxy-d-manno-octulosonic acid 8-phosphate synthase. J Am Chem Soc 2000; 122: 9334-35.
    • (2000) J Am Chem Soc , vol.122 , pp. 9334-9335
    • Birck, M.R.1    Holler, T.P.2    Woodard, R.V.3
  • 81
    • 33646396234 scopus 로고    scopus 로고
    • Synthesis and inhibitory activity of 8-substituted 2-deoxy-beta-KDO against CMP-KDO synthetase
    • Adachi H, Kondo KI, Kojima F, et al. Synthesis and inhibitory activity of 8-substituted 2-deoxy-beta-KDO against CMP-KDO synthetase. Nat Prod Res Part B: Bioactive Nat Prod 2006; 20: 361-70.
    • (2006) Nat Prod Res Part B: Bioactive Nat Prod , vol.20 , pp. 361-370
    • Adachi, H.1    Kondo, K.I.2    Kojima, F.3
  • 82
    • 0028844306 scopus 로고
    • A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase
    • Raetz CRH, Roderick SL. A left-handed parallel beta helix in the structure of UDP-N-acetylglucosamine acyltransferase. Science 1995; 270: 997-1000
    • (1995) Science , vol.270 , pp. 997-1000
    • Raetz, C.R.H.1    Roderick, S.L.2
  • 83
    • 0033578887 scopus 로고    scopus 로고
    • The active site of Escherichia coli UDPN-acetylglucosamine acyltransferase. Chemical modification and site-directed mutagenesis
    • Wyckoff TJ, Raetz CRH. The active site of Escherichia coli UDPN-acetylglucosamine acyltransferase. Chemical modification and site-directed mutagenesis. J Biol Chem 1999; 274: 27047-27055.
    • (1999) J Biol Chem , vol.274 , pp. 27047-27055
    • Wyckoff, T.J.1    Raetz, C.R.H.2
  • 84
    • 0042123525 scopus 로고    scopus 로고
    • Structure of the LpxC deacetylase with a bound substrate-analog inhibitor
    • Coggins BE, Li X, McClerren AL, et al. Structure of the LpxC deacetylase with a bound substrate-analog inhibitor. Nat Struct Biol 2003; 10: 645-51.
    • (2003) Nat Struct Biol , vol.10 , pp. 645-651
    • Coggins, B.E.1    Li, X.2    McClerren, A.L.3
  • 86
    • 33745602267 scopus 로고    scopus 로고
    • Mechanistic inferences from the binding of ligands to LpxC, a metal-dependent deacetylase
    • Gennadios HA, Whittington DA, Li X, Fierke CA, Christianson DW. Mechanistic inferences from the binding of ligands to LpxC, a metal-dependent deacetylase. Biochemistry 2006; 45: 7940-8.
    • (2006) Biochemistry , vol.45 , pp. 7940-7948
    • Gennadios, H.A.1    Whittington, D.A.2    Li, X.3    Fierke, C.A.4    Christianson, D.W.5
  • 87
    • 34247642136 scopus 로고    scopus 로고
    • Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis
    • Buetow L, Smith TK, Dawson A, Fyffe S, Hunter WN. Structure and reactivity of LpxD, the N-acyltransferase of lipid A biosynthesis. Proc Natl Acad Sci USA 2007; 104: 4321-6.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 4321-4326
    • Buetow, L.1    Smith, T.K.2    Dawson, A.3    Fyffe, S.4    Hunter, W.N.5
  • 88
    • 0035895351 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the bacterial metalloamidase UDP-(3-O-acyl)-N-acetylglucosamine deacetylase (LpxC). Identification of the zinc binding site
    • Jackman JE, Raetz CRH, Fierke CA. Site-directed mutagenesis of the bacterial metalloamidase UDP-(3-O-acyl)-N-acetylglucosamine deacetylase (LpxC). Identification of the zinc binding site. Biochemistry 2001; 40: 514-23.
    • (2001) Biochemistry , vol.40 , pp. 514-523
    • Jackman, J.E.1    Raetz, C.R.H.2    Fierke, C.A.3
  • 89
    • 10544252685 scopus 로고    scopus 로고
    • Antibacterial agents that inhibit Lipid A biosynthesis
    • Onishi HR, Pelak BA, Gerckens LS, et al. Antibacterial agents that inhibit Lipid A biosynthesis. Science 1996; 274: 980-2.
    • (1996) Science , vol.274 , pp. 980-982
    • Onishi, H.R.1    Pelak, B.A.2    Gerckens, L.S.3
  • 90
    • 0034646694 scopus 로고    scopus 로고
    • Antibacterial agents that target lipid a biosynthesis in gram-negative bacteria: Inhibition of diverse UDP-3-O-(R-3-hydroxymyristoyl)-n-acetylglucosamine deacetylases by substrate analogs containing zinc binding motifs
    • Jackman JE, Fierke CA, Tumey LN, et al. Antibacterial agents that target lipid a biosynthesis in gram-negative bacteria: inhibition of diverse UDP-3-O-(R-3-hydroxymyristoyl)-n-acetylglucosamine deacetylases by substrate analogs containing zinc binding motifs. J Biol Chem 2000; 275: 11002-9.
    • (2000) J Biol Chem , vol.275 , pp. 11002-11009
    • Jackman, J.E.1    Fierke, C.A.2    Tumey, L.N.3
  • 91
    • 0026756436 scopus 로고
    • Biosynthesis of endotoxins purification and catalytic propreties of deoxy-D-manno-octolusonic acid transferase from Escherichia Coli
    • Belunis CJ, Raetz CR. Biosynthesis of endotoxins purification and catalytic propreties of deoxy-D-manno-octolusonic acid transferase from Escherichia Coli. J Biol Chem 1992; 267: 9988-97.
    • (1992) J Biol Chem , vol.267 , pp. 9988-9997
    • Belunis, C.J.1    Raetz, C.R.2
  • 92
    • 0032102175 scopus 로고    scopus 로고
    • Cloning and characterization of 3-deoxy-d-manno-oct-2-ulosonic acid (Kdo) transferase genes (kdtA) from Acinetobacter baumannii and Acinetobacter haemolyticus
    • Bode CE, Brabetz W, Brade H. Cloning and characterization of 3-deoxy-d-manno-oct-2-ulosonic acid (Kdo) transferase genes (kdtA) from Acinetobacter baumannii and Acinetobacter haemolyticus. Eur J Biochem 1998; 254: 404-12.
    • (1998) Eur J Biochem , vol.254 , pp. 404-412
    • Bode, C.E.1    Brabetz, W.2    Brade, H.3
  • 93
    • 0029561119 scopus 로고
    • Molecular cloning, sequence analysis, and functional characterization of the lipopolysaccharide biosynthetic gene kdtA encoding 3-deoxy-alpha-D-mannooctulosonic acid transferase of Chlamydia pneumoniae strain TW-183
    • Lobau S, Mamat U, Brabetz W, Brade H. Molecular cloning, sequence analysis, and functional characterization of the lipopolysaccharide biosynthetic gene kdtA encoding 3-deoxy-alpha-D-mannooctulosonic acid transferase of Chlamydia pneumoniae strain TW-183. Mol Microbiol 1995; 18: 391-9.
    • (1995) Mol Microbiol , vol.18 , pp. 391-399
    • Lobau, S.1    Mamat, U.2    Brabetz, W.3    Brade, H.4
  • 94
    • 71849097295 scopus 로고    scopus 로고
    • WO 9825940 A1 19980618 Application: WO 97-US22713 19971210
    • Wong CH, Hayashi T PCT Int. Appl. (1998), WO 9825940 A1 19980618 Application: WO 97-US22713 19971210.
    • (1998) PCT Int. Appl
    • Wong, C.H.1    Hayashi, T.2
  • 95
    • 3242743729 scopus 로고    scopus 로고
    • Sorting of lipoproteins to the outer membrane in E. coli
    • Tokuda H, Matsuyama S. Sorting of lipoproteins to the outer membrane in E. coli. Biochim Biophys Acta 2004; 1693: 5-13.
    • (2004) Biochim Biophys Acta , vol.1693 , pp. 5-13
    • Tokuda, H.1    Matsuyama, S.2
  • 96
    • 0028965644 scopus 로고
    • Receptor-dependent mechanisms of cell stimulation by bacterial endotoxin
    • Ulevitch RJ, Tobias PS. Receptor-dependent mechanisms of cell stimulation by bacterial endotoxin. Annu Rev Immunol 1995; 13: 437-57.
    • (1995) Annu Rev Immunol , vol.13 , pp. 437-457
    • Ulevitch, R.J.1    Tobias, P.S.2
  • 97
    • 34548222514 scopus 로고    scopus 로고
    • Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran
    • Kim HM, Park BS, Kim J-I, et al. Crystal structure of the TLR4-MD-2 complex with bound endotoxin antagonist Eritoran. Cell 2007; 130: 906-17.
    • (2007) Cell , vol.130 , pp. 906-917
    • Kim, H.M.1    Park, B.S.2    Kim, J-I.3
  • 98
    • 34250813748 scopus 로고    scopus 로고
    • Crystal structures of human MD-2 and its complex with antiendotoxic lipid IVa
    • Ohto U, Fukase K, Miyake K, Satow Y. Crystal structures of human MD-2 and its complex with antiendotoxic lipid IVa. Science 2007; 316: 16324.
    • (2007) Science , vol.316 , pp. 16324
    • Ohto, U.1    Fukase, K.2    Miyake, K.3    Satow, Y.4
  • 99
    • 1642384019 scopus 로고    scopus 로고
    • Innate recognition of lipopolysaccharide by Toll-like receptor 4-MD-2
    • Miyake K. Innate recognition of lipopolysaccharide by Toll-like receptor 4-MD-2. Trends Microbiol 2004; 12: 186-92.
    • (2004) Trends Microbiol , vol.12 , pp. 186-192
    • Miyake, K.1
  • 100
    • 33745712575 scopus 로고    scopus 로고
    • Shield as signal: Lipopolysaccharides and the evolution of immunity to gram-negative bacteria
    • Munford RS, Varley AW. Shield as signal: lipopolysaccharides and the evolution of immunity to gram-negative bacteria. PLOS Pathogens 2006; 2: 467-71.
    • (2006) PLOS Pathogens , vol.2 , pp. 467-471
    • Munford, R.S.1    Varley, A.W.2
  • 101
    • 0034958947 scopus 로고    scopus 로고
    • Epidemiology of severe sepsis in the United States: Analysis of incidence, outcome, and associated costs of care
    • Angus DC, Linde-Zwirble WT, Lidicker J, Clermont G, Carcillo J, Pinsky MR. Epidemiology of severe sepsis in the United States: Analysis of incidence, outcome, and associated costs of care. Crit Care Med 2001; 29: 1303-10.
    • (2001) Crit Care Med , vol.29 , pp. 1303-1310
    • Angus, D.C.1    Linde-Zwirble, W.T.2    Lidicker, J.3    Clermont, G.4    Carcillo, J.5    Pinsky, M.R.6
  • 102
    • 67349182481 scopus 로고    scopus 로고
    • The structural basis of lipopolysaccharide recognitionby the TLR4-MD-2 complex
    • Park BS, Song DH, Kim HM, Choi BS, Lee H, Lee JO. The structural basis of lipopolysaccharide recognitionby the TLR4-MD-2 complex. Nature 2009; 458: 1191-5.
    • (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    Lee, J.O.6
  • 103
    • 34548608447 scopus 로고    scopus 로고
    • Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide
    • Jin MS, Kim ES, Heo JY, et al. Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide. Cell 2007; 130: 1071-82.
    • (2007) Cell , vol.130 , pp. 1071-1082
    • Jin, M.S.1    Kim, E.S.2    Heo, J.Y.3
  • 104
    • 42349090335 scopus 로고    scopus 로고
    • Structural basis of toll-like receptor 3 signaling with double-stranded RNA
    • Liu L, Botos I, Wang Y, et al. Structural basis of toll-like receptor 3 signaling with double-stranded RNA. Science 2008; 320: 379-81.
    • (2008) Science , vol.320 , pp. 379-381
    • Liu, L.1    Botos, I.2    Wang, Y.3
  • 106
    • 0037442501 scopus 로고    scopus 로고
    • Blocking of responses to endotoxin by E5564 in healthy volunteers with experimental endotoxemia
    • Lynn M., Rossignol DP, Wheeler JL, et al. Blocking of responses to endotoxin by E5564 in healthy volunteers with experimental endotoxemia. J Infect Dis 2003; 187: 631-9.
    • (2003) J Infect Dis , vol.187 , pp. 631-639
    • Lynn, M.1    Rossignol, D.P.2    Wheeler, J.L.3
  • 107
    • 0036015491 scopus 로고    scopus 로고
    • Chemical structure of lipid A-the primary immunomodulatory center of bacterial lipopolysaccharides
    • Alexander C, Zahringer U. Chemical structure of lipid A-the primary immunomodulatory center of bacterial lipopolysaccharides. Trends Glycosci Glycotechnol 2002; 14: 69-86.
    • (2002) Trends Glycosci Glycotechnol , vol.14 , pp. 69-86
    • Alexander, C.1    Zahringer, U.2
  • 109
    • 0034007076 scopus 로고    scopus 로고
    • Physical contact between lipopolysaccharide and toll-like receptor 4 revealed by genetic complementation
    • Poltorak A, Ricciardi-Castagnoli P, Citterio S, Beutler B. Physical contact between lipopolysaccharide and toll-like receptor 4 revealed by genetic complementation. Proc Natl Acad Sci USA 2000; 97: 2163-67.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 2163-2167
    • Poltorak, A.1    Ricciardi-Castagnoli, P.2    Citterio, S.3    Beutler, B.4
  • 110
    • 0034002247 scopus 로고    scopus 로고
    • Toll-like receptor 4 imparts ligand-specific recognition of bacterial lipopolysaccharide
    • Lien E, Means TK, Heine H, et al. Toll-like receptor 4 imparts ligand-specific recognition of bacterial lipopolysaccharide. J Clin Invest 2000; 105: 497-504.
    • (2000) J Clin Invest , vol.105 , pp. 497-504
    • Lien, E.1    Means, T.K.2    Heine, H.3
  • 111
    • 0036084367 scopus 로고    scopus 로고
    • MD-2, a novel accessory molecule, is involved in species-specific actions of salmonella lipid A
    • Muroi M, Ohnishi T, Tanamoto K. MD-2, a novel accessory molecule, is involved in species-specific actions of salmonella lipid A. Infect Immun 2002; 70: 3546-50.
    • (2002) Infect Immun , vol.70 , pp. 3546-3550
    • Muroi, M.1    Ohnishi, T.2    Tanamoto, K.3
  • 112
    • 33748875900 scopus 로고    scopus 로고
    • Virulence factors of Yersinia pestis are overcome by a strong lipopolysaccharide response
    • Montminy SW, Khan N, McGrath S, et al. Virulence factors of Yersinia pestis are overcome by a strong lipopolysaccharide response. Nat Immunol 2006; 7: 1066-73.
    • (2006) Nat Immunol , vol.7 , pp. 1066-1073
    • Montminy, S.W.1    Khan, N.2    McGrath, S.3
  • 113
    • 0344235273 scopus 로고    scopus 로고
    • Physicochemical properties of bacterial glycopolymers in relation to bioactivity
    • Brandenburg K, Andrä J, Müller M, Koch MH, Garidel P. Physicochemical properties of bacterial glycopolymers in relation to bioactivity. Carbohydr Res 2003; 338: 2477-89.
    • (2003) Carbohydr Res , vol.338 , pp. 2477-2489
    • Brandenburg, K.1    Andrä, J.2    Müller, M.3    Koch, M.H.4    Garidel, P.5
  • 114
    • 0347659154 scopus 로고    scopus 로고
    • Structural basis for endotoxic and antagonistic activities: Investigation with novel synthetic lipid A analogs
    • Kusumoto S, Fukase K, Fukase Y, et al. Structural basis for endotoxic and antagonistic activities: investigation with novel synthetic lipid A analogs Endotoxin Res 2003; 9: 361-66.
    • (2003) Endotoxin Res , vol.9 , pp. 361-366
    • Kusumoto, S.1    Fukase, K.2    Fukase, Y.3
  • 116
    • 84855721698 scopus 로고    scopus 로고
    • Therapeutic targeting of innate immunity with Toll-like receptor 4 (TLR4) antagonists
    • DOI: 10.1016/j.biotechadv.2011.05.014
    • Peri F, Piazza M. Therapeutic targeting of innate immunity with Toll-like receptor 4 (TLR4) antagonists. Biotechnol Adv 2011;DOI: 10.1016/j.biotechadv.2011.05.014.
    • (2011) Biotechnol Adv
    • Peri, F.1    Piazza, M.2
  • 117
    • 0025188131 scopus 로고
    • Cytokine induction by lipopolysaccharide (LPS) corresponds to lethal toxicity and is inhibited by nontoxic Rhodobacter capsulatus LPS
    • Loppnow H, Libby P, Freudenberg M, Krauss JH, Weckesser J, Mayer H. Cytokine induction by lipopolysaccharide (LPS) corresponds to lethal toxicity and is inhibited by nontoxic Rhodobacter capsulatus LPS. Infect Immun 1990; 58: 3743-50.
    • (1990) Infect Immun , vol.58 , pp. 3743-3750
    • Loppnow, H.1    Libby, P.2    Freudenberg, M.3    Krauss, J.H.4    Weckesser, J.5    Mayer, H.6
  • 118
    • 0028941067 scopus 로고
    • E5531, a pure endotoxin antagonist of high potency
    • Christ W, Asano O, Robidoux A, et al. E5531, a pure endotoxin antagonist of high potency. Science 1995; 268: 80-3.
    • (1995) Science , vol.268 , pp. 80-83
    • Christ, W.1    Asano, O.2    Robidoux, A.3
  • 119
    • 0032823099 scopus 로고    scopus 로고
    • Lipoprotein distribution of a novel endotoxin antagonist, E5531, in plasma from human subjects with various lipid levels
    • Wasan K, Strobel F, Parrott S, et al. Lipoprotein distribution of a novel endotoxin antagonist, E5531, in plasma from human subjects with various lipid levels. Antimicrob Agents Chemother 1999; 43: 2562-4.
    • (1999) Antimicrob Agents Chemother , vol.43 , pp. 2562-2564
    • Wasan, K.1    Strobel, F.2    Parrott, S.3
  • 121
    • 74049125175 scopus 로고    scopus 로고
    • Phase 2 trial of eritoran tetrasodium (E5564), a tolllike receptor 4 antagonist, in patients with severe sepsis
    • Tidswell M, Tillis W, Larosa SP, et al. Phase 2 trial of eritoran tetrasodium (E5564), a tolllike receptor 4 antagonist, in patients with severe sepsis. Crit Care Med 2010; 38: 72-83
    • (2010) Crit Care Med , vol.38 , pp. 72-83
    • Tidswell, M.1    Tillis, W.2    Larosa, S.P.3
  • 122
    • 0036954040 scopus 로고    scopus 로고
    • Antagonism of in vivo and ex vivo response to endotoxin by E5564, a synthetic lipid A analogue
    • Rossignol D, Lynn M. Antagonism of in vivo and ex vivo response to endotoxin by E5564, a synthetic lipid A analogue. J Endotoxin Res 2002; 8: 483-8.
    • (2002) J Endotoxin Res , vol.8 , pp. 483-488
    • Rossignol, D.1    Lynn, M.2
  • 123
    • 0037372661 scopus 로고    scopus 로고
    • Inhibition of endotoxin response by E5564, a novel Toll-like receptor 4-directed endotoxin antagonist
    • Mullarkey M, Rose J, Bristol J, et al. Inhibition of endotoxin response by E5564, a novel Toll-like receptor 4-directed endotoxin antagonist. J Pharmacol Exp Ther 2003; 304: 1093-102.
    • (2003) J Pharmacol Exp Ther , vol.304 , pp. 1093-1102
    • Mullarkey, M.1    Rose, J.2    Bristol, J.3
  • 124
    • 64349098670 scopus 로고    scopus 로고
    • Glycolipids and benzylammonium lipids as novel antisepsis agents: Synthesis and biological characterization
    • Piazza M, Rossini C, Della Fiorentina S, et al. Glycolipids and benzylammonium lipids as novel antisepsis agents: synthesis and biological characterization. J Med Chem 2009; 52: 1209-13.
    • (2009) J Med Chem , vol.52 , pp. 1209-1213
    • Piazza, M.1    Rossini, C.2    Della Fiorentina, S.3
  • 125
    • 73149119782 scopus 로고    scopus 로고
    • Evidence of a specific interaction between new synthetic antisepsis agents and CD14
    • Piazza M, Yu L, Teghanemt A, et al. Evidence of a specific interaction between new synthetic antisepsis agents and CD14. Biochemistry 2009; 48: 12337-44.
    • (2009) Biochemistry , vol.48 , pp. 12337-12344
    • Piazza, M.1    Yu, L.2    Teghanemt, A.3
  • 126
    • 39149097579 scopus 로고    scopus 로고
    • Opal SM Host-pathogen interactions in sepsis
    • van der Poll T. Opal SM Host-pathogen interactions in sepsis. Lancet Infect Dis 2008; 8: 32-43.
    • (2008) Lancet Infect Dis , vol.8 , pp. 32-43
    • van der Poll, T.1
  • 127
    • 77954909395 scopus 로고    scopus 로고
    • Role of regulatory T cells in long-term immune dysfunction associated with severe sepsis
    • Nascimento DC, Alves-Filho JC, Sonego F, et al. Role of regulatory T cells in long-term immune dysfunction associated with severe sepsis. Crit Care Med 2010; 38: 1718-25.
    • (2010) Crit Care Med , vol.38 , pp. 1718-1725
    • Nascimento, D.C.1    Alves-Filho, J.C.2    Sonego, F.3
  • 128
    • 78650624395 scopus 로고    scopus 로고
    • Genome-wide transcription profiling of human sepsis: A systematic review
    • Tang BM, Huang SJ, McLean AS. Genome-wide transcription profiling of human sepsis: a systematic review. Crit Care 2010; 14: R237.
    • (2010) Crit Care , vol.14
    • Tang, B.M.1    Huang, S.J.2    McLean, A.S.3
  • 129
    • 79251537742 scopus 로고    scopus 로고
    • Sepsis induces early alterations in innate immunity that impact mortality to secondary infection
    • Delano MJ, Thayer T, Gabrilovich S, et al. Sepsis induces early alterations in innate immunity that impact mortality to secondary infection. J Immunol 2011; 186: 195-202.
    • (2011) J Immunol , vol.186 , pp. 195-202
    • Delano, M.J.1    Thayer, T.2    Gabrilovich, S.3
  • 130
    • 14544299688 scopus 로고    scopus 로고
    • Bernard Therapeutic intervention and targets for sepsis
    • Todd W. Rice and Gordon R. Bernard Therapeutic intervention and targets for sepsis Annu Rev Med 2005; 56: 225-48.
    • (2005) Annu Rev Med , vol.56 , pp. 225-248
    • Rice, T.W.1    Gordon, R.2
  • 131
    • 82355173296 scopus 로고    scopus 로고
    • New concepts in the pathogenesis, diagnosis and treatment of bacteremia and sepsis
    • Huttunen R, Aittoniemi J New concepts in the pathogenesis, diagnosis and treatment of bacteremia and sepsis. J Infect 2011; 63: 407-19.
    • (2011) J Infect , vol.63 , pp. 407-419
    • Huttunen, R.1    Aittoniemi, J.2
  • 132
    • 0037454946 scopus 로고    scopus 로고
    • Inhibition of interleukin 1 receptor/Toll-like receptor signaling through the alternatively spliced, short form of MyD88 is due to its failure to recruit IRAK-4
    • Burns K, Janssens S, Brissoni B, Olivos N, Beyaert R, Tschopp J. Inhibition of interleukin 1 receptor/Toll-like receptor signaling through the alternatively spliced, short form of MyD88 is due to its failure to recruit IRAK-4. J Exp Med 2003; 197: 263-8.
    • (2003) J Exp Med , vol.197 , pp. 263-268
    • Burns, K.1    Janssens, S.2    Brissoni, B.3    Olivos, N.4    Beyaert, R.5    Tschopp, J.6
  • 133
    • 0035336425 scopus 로고    scopus 로고
    • A novel pathway regulating lipopolysaccharide-induced shock by ST2/T1 via inhibition of Tolllike receptor 4 expression
    • Sweet MJ, Leung BP, Kang D, et al. A novel pathway regulating lipopolysaccharide-induced shock by ST2/T1 via inhibition of Tolllike receptor 4 expression. J Immunol 2001; 166: 6633-9.
    • (2001) J Immunol , vol.166 , pp. 6633-6639
    • Sweet, M.J.1    Leung, B.P.2    Kang, D.3
  • 134
    • 0029057595 scopus 로고
    • Recombinant soluble CD14 prevents mortality in mice treated with endotoxin (lipopolysaccharide)
    • Haziot A, Rong GW, Lin XY, Silver J, Goyert SM. Recombinant soluble CD14 prevents mortality in mice treated with endotoxin (lipopolysaccharide). J Immunol 1995; 154: 6529-32.
    • (1995) J Immunol , vol.154 , pp. 6529-6532
    • Haziot, A.1    Rong, G.W.2    Lin, X.Y.3    Silver, J.4    Goyert, S.M.5
  • 135
    • 2442565752 scopus 로고    scopus 로고
    • CD14 receptor occupancy in severe sepsis: Results of a phase I clinical trial with a recombinant chimeric evolving concepts associated with sepsis CD14 monoclonal antibody (IC14)
    • Reinhart K, Gluck T, Ligtenberg J, et al. CD14 receptor occupancy in severe sepsis: results of a phase I clinical trial with a recombinant chimeric evolving concepts associated with sepsis CD14 monoclonal antibody (IC14). Crit Care Med 2004; 32: 1100-8.
    • (2004) Crit Care Med , vol.32 , pp. 1100-1108
    • Reinhart, K.1    Gluck, T.2    Ligtenberg, J.3
  • 136
    • 0037636527 scopus 로고    scopus 로고
    • Preclinical assessment of the efficacy of mycograb, a human recombinant antibody against fungal HSP90
    • Matthews RC, Rigg G, Hodgetts S, et al. Preclinical assessment of the efficacy of mycograb, a human recombinant antibody against fungal HSP90. Antimicrob Agents Chemother 2003; 47: 2208-16.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 2208-2216
    • Matthews, R.C.1    Rigg, G.2    Hodgetts, S.3
  • 137
    • 33646455866 scopus 로고    scopus 로고
    • A randomized, blinded, multicenter trial of lipid-associated amphotericin B alone versus in combination with an antibody-based inhibitor of heat shock protein in patients with invasive candidiasis
    • Pachl J, Svoboda P, Jacobs F, et al. A randomized, blinded, multicenter trial of lipid-associated amphotericin B alone versus in combination with an antibody-based inhibitor of heat shock protein in patients with invasive candidiasis. Clin Infect Dis 2006; 42: 1404-13.
    • (2006) Clin Infect Dis , vol.42 , pp. 1404-1413
    • Pachl, J.1    Svoboda, P.2    Jacobs, F.3
  • 138
    • 77956403940 scopus 로고    scopus 로고
    • Delayed administration of anti-PD-1 antibody reverses immune dysfunction and improves survival during sepsis
    • Brahmamdam P, Inoue S, Unsinger J, Chang KC, McDunn JE, Hotchkiss RS. Delayed administration of anti-PD-1 antibody reverses immune dysfunction and improves survival during sepsis. J Leukoc Biol 2010; 88: 233-40.
    • (2010) J Leukoc Biol , vol.88 , pp. 233-240
    • Brahmamdam, P.1    Inoue, S.2    Unsinger, J.3    Chang, K.C.4    McDunn, J.E.5    Hotchkiss, R.S.6
  • 139
    • 78649460067 scopus 로고    scopus 로고
    • PD-L1 blockade improves survival in experimental sepsis by inhibiting lymphocyte apoptosis and reversing monocyte dysfunction
    • Zhang Y, Zhou Y, Lou J, et al. PD-L1 blockade improves survival in experimental sepsis by inhibiting lymphocyte apoptosis and reversing monocyte dysfunction. Crit Care 2010; 14: R220.
    • (2010) Crit Care , vol.14
    • Zhang, Y.1    Zhou, Y.2    Lou, J.3
  • 141
    • 79953709110 scopus 로고    scopus 로고
    • Regulation of inflammation, autoimmunity, and infection immunity by HVEM-BTLA signaling
    • Shui JW, Steinberg MW, Kronenberg M. Regulation of inflammation, autoimmunity, and infection immunity by HVEM-BTLA signaling. J Leukoc Biol 2011; 89: 517-23.
    • (2011) J Leukoc Biol , vol.89 , pp. 517-523
    • Shui, J.W.1    Steinberg, M.W.2    Kronenberg, M.3
  • 143
    • 78650233801 scopus 로고    scopus 로고
    • Endotoxin removal devices for the treatment of sepsis and septic shock
    • Davies B, Cohen J. Endotoxin removal devices for the treatment of sepsis and septic shock. Lancet Infect Dis 2011; 11: 65-71.
    • (2011) Lancet Infect Dis , vol.11 , pp. 65-71
    • Davies, B.1    Cohen, J.2
  • 144
    • 73949109493 scopus 로고    scopus 로고
    • Nitrite protects against morbidity and mortality associated with TNF-or LPS-induced shock in a soluble guanylate cyclase-dependent manner
    • Cauwels A, Buys ES, Thoonen R, et al. Nitrite protects against morbidity and mortality associated with TNF-or LPS-induced shock in a soluble guanylate cyclase-dependent manner. J Exp Med 2009; 206: 2915-24.
    • (2009) J Exp Med , vol.206 , pp. 2915-2924
    • Cauwels, A.1    Buys, E.S.2    Thoonen, R.3
  • 145
    • 38049110809 scopus 로고    scopus 로고
    • Hydrocortisone therapy for patients with septic shock
    • Sprung CL, Annane D, Keh D, et al. Hydrocortisone therapy for patients with septic shock. N Engl J Med 2008; 358: 111-24.
    • (2008) N Engl J Med , vol.358 , pp. 111-124
    • Sprung, C.L.1    Annane, D.2    Keh, D.3
  • 146
    • 84855986635 scopus 로고    scopus 로고
    • Systemic Steroids in Severe Sepsis and Septic Shock
    • Patel GP, Balk RA. Systemic Steroids in Severe Sepsis and Septic Shock. Am J Respir Crit Care Med 2012; 185: 133-9.
    • (2012) Am J Respir Crit Care Med , vol.185 , pp. 133-139
    • Patel, G.P.1    Balk, R.A.2
  • 147
    • 0035826096 scopus 로고    scopus 로고
    • Efficacy and safety of recombinant human activated protein C for severe sepsis
    • Bernard GR, Vincent JL, Laterre PF, et al. Efficacy and safety of recombinant human activated protein C for severe sepsis. N Engl J Med 2001; 344: 699-709.
    • (2001) N Engl J Med , vol.344 , pp. 699-709
    • Bernard, G.R.1    Vincent, J.L.2    Laterre, P.F.3
  • 148
    • 77957690690 scopus 로고    scopus 로고
    • The effect of statins on mortality from severe infections and sepsis: A systematic review and meta-analysis
    • Janda S, Young A, Fitzgerald JM, Etminan M, Swiston J. The effect of statins on mortality from severe infections and sepsis: a systematic review and meta-analysis. J Crit Care 2010; 25: 656e7-22.
    • (2010) J Crit Care , vol.25
    • Janda, S.1    Young, A.2    Fitzgerald, J.M.3    Etminan, M.4    Swiston, J.5
  • 149
    • 36448938357 scopus 로고    scopus 로고
    • Use of polyclonal immunoglobulins as adjunctive therapy for sepsis or septic shock
    • Kreymann KG, de Heer G, Nierhaus A, Kluge S. Use of polyclonal immunoglobulins as adjunctive therapy for sepsis or septic shock. Crit Care Med 2007; 35: 2677-85
    • (2007) Crit Care Med , vol.35 , pp. 2677-2685
    • Kreymann, K.G.1    de Heer, G.2    Nierhaus, A.3    Kluge, S.4
  • 150
    • 33751079066 scopus 로고    scopus 로고
    • Intravenous polyclonal IgM-enriched immunoglobulin therapy in sepsis: A review of clinical efficacy in relation to microbiological aetiology and severity of sepsis
    • Norrby-Teglund A, Haque KN, Hammarstrom L. Intravenous polyclonal IgM-enriched immunoglobulin therapy in sepsis: a review of clinical efficacy in relation to microbiological aetiology and severity of sepsis. J Intern Med 2006; 260: 509-16.
    • (2006) J Intern Med , vol.260 , pp. 509-516
    • Norrby-Teglund, A.1    Haque, K.N.2    Hammarstrom, L.3
  • 151
    • 78049433417 scopus 로고    scopus 로고
    • Interleukin-7 (IL-7) treatment accelerates neutrophil recruitment through gamma deltaT-cell IL-17 production in a murine model of sepsis
    • Kasten KR, Prakash PS, Unsinger J, et al. Interleukin-7 (IL-7) treatment accelerates neutrophil recruitment through gamma deltaT-cell IL-17 production in a murine model of sepsis. Infect Immun 2010; 78: 4714-22.
    • (2010) Infect Immun , vol.78 , pp. 4714-4722
    • Kasten, K.R.1    Prakash, P.S.2    Unsinger, J.3
  • 152
    • 77949317183 scopus 로고    scopus 로고
    • IL-15 prevents apoptosis, reverses innate and adaptive immune dysfunction, and improves survival in sepsis
    • Inoue S, Unsinger J, Davis CG, et al. IL-15 prevents apoptosis, reverses innate and adaptive immune dysfunction, and improves survival in sepsis. J Immunol 2010; 184: 1401-9.
    • (2010) J Immunol , vol.184 , pp. 1401-1409
    • Inoue, S.1    Unsinger, J.2    Davis, C.G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.