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Part:K1363200

Designed by: CHANGXU WANG   Group: iGEM14_USTC-China   (2014-09-28)
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Anti-LPS factor(LALF) regulated by lacI

Reference

  • Alpert G, Baldwin G, Thompson C, Wainwright N, Novitsky T J, Gillis , Parsonnet J, Fleisher G R, Siber G R. Limulus antilipopolysaccharide factor protects rabbits from meningococcal endotoxin shock. J Infect Dis. 1992;165:494–500. [PubMed]
  • Bannerman D D, Goldblum S E. Endotoxin induces endothelial barrier dysfunction through protein tyrosine phosphorylation. Am J Physiol. 1997;273:L217–L226. [PubMed]
  • Battafaraono R J, Dahlberg P S, Ratz C A, Johnston J W, Gray B H, Haseman J R, Mayo K H, Dunn D L. Peptide derivatives of three distinct lipopolysaccharide binding proteins inhibit lipopolysaccharide-induced tumor necrosis factor-alpha secretion in vitro. Surgery. 1995;118:318–324. [PubMed]
  • Cooperstock M S. Inactivation of endotoxin by polymyxin B. Antimicrob Agents Chemother. 1974;6:422–425. [PMC free article] [PubMed]
  • Evans T J, Carpenter A, Moyes D, Martin R, Cohen J. 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. [PubMed]
  • Fletcher M A, Mckena T M, Quance J L, Wainwright N R, Williams T J. Lipopolysaccharide detoxification by endotoxin neutralizing protein. J Surg Res. 1993;55:147–154. [PubMed]
  • Frey E A, Miller D S, Jahr T G, Sundan A, Bazil V, Espevik T, Finlay B B, Wright S D. Soluble CD14 participates in the response of cells to lipopolysaccharide. J Exp Med. 1992;176:1665–1671. [PMC free article] [PubMed]
  • Goldblum S E, Brann T W, Ding X, Pugin J, Tobias P S. Lipopolysaccharide (LPS)-binding protein and soluble CD14 function as accessory molecules for LPS-induced changes in endothelial barrier function, in vitro. J Clin Invest. 1994;93:692–702. [PMC free article] [PubMed]
  • Goldblum S E, Ding X, Brann T W, Campbell-Washington J. Bacterial lipopolysaccharide induces actin reorganization, intercellular gap formation, and endothelial barrier dysfunction in pulmonary vascular endothelial cells: concurrent F-actin depolymerization and new actin synthesis. J Cell Physiol. 1993;157:13–23. [PubMed]
  • Hirata M, Zhong J, Wright S C, Larrick J W. Structure and functions of endotoxin-binding peptides derived from CAP18. Prog Clin Biol Res. 1995;392:317–326. [PubMed]
  • Hoess A, Watson S, Siber G R, Liddington R. Crystal structure of endotoxin-neutralizing protein from the horseshoe crab, Limulus anti-LPS factor, at 1.5 A resolution. EMBO J. 1993;12:3351–3356. [PMC free article] [PubMed]
  • Levine D M, Parker T S, Donelly T M, Walsh A, Rubin A L. In vivo protection against endotoxin by plasma high density lipoprotein. Proc Natl Acad Sci USA. 1993;90:12040–12044. [PMC free article] [PubMed]
  • Morita T, Ohtsubo S, Nakamura T, Tanaka S, Iwanaga S, Ohashi K, Niwa M. Isolation and biological activities of limulus anticoagulant (anti-LPS factor) which interacts with lipopolysaccharide (LPS) J Biochem (Tokyo) 1985;97:1611–1620. [PubMed]
  • Morrison D C, Jacobs D M. Binding of polymyxin B to the lipid A portion of bacterial lipopolysaccharides. Immunochemistry. 1976;13:813–818. [PubMed]
  • Muta T, Miyata T, Tokunaga F, Nakamura T, Iwanaga S. Primary structure of anti-lipopolysaccharide factor from American horseshoe crab, Limulus polyphemus. J Biochem (Tokyo) 1987;101:1321–1330. [PubMed]
  • Netea M G, Demacker P N M, Kullberg B J, Boerman O C, Verschueren I, Stalenhoef A F H, van der Meer J W M. Low-density lipoprotein receptor-deficient mice are protected against lethal endotoxemia and severe Gram-negative infections. J Clin Invest. 1996;97:1366–1372. [PMC free article] [PubMed]
  • Ulevitch R J, Tobias P S. Recognition of endotoxin by cells leading to transmembrane signaling. Curr Opin Immunol. 1994;6:125–130. [PubMed]
  • Wainwright N R, Miller R J, Paus E, Novitsky T J, Fletcher M A, McKenna T M, Williams T. Endotoxin binding and neutralizing activity by a protein from Limulus polyphemus. In: Levin J, Alving C R, Munford R S, Stutz P L, editors. Cellular and molecular aspects of endotoxin reactions. New York, N.Y: Elsevier Science Publishers; 1990. pp. 315–325.
  • Warren H S, Novitsky T J, Bucklin A, Kania S A, Siber G R. Endotoxin neutralization with rabbit antisera to Escherichi


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


[edit]
Categories
Parameters
None