Registro:

Referencias:

• Amersfoort, E., Van Berkel, T., Kuiper, J., Receptors, mediators, and mechanisms involved in bacterial sepsis and septic shock (2003) Clin. Microbiol. Rev., 16, pp. 379-414
• Chaby, R., Strategies for the control of LPS-mediated pathophysiological disorders (1999) Drug Disc Today, 4, pp. 209-221
• Takahashi, I., Kotani, S., Takada, H., Tsujimoto, M., Ogawa, T., Shiba, T., Kusumoto, S., Tamura, T., Requirement of a properly acylated β(1 → 6)-d-glucosamine disaccharide biphosphate structure for efficient manifestation of full endotoxic and associated bioactivities of lipid A (1987) Infect. Immunol., 65, pp. 57-68
• Rietschel, E.T., Kirikae, T., Schade, U.F., Ulmer, A.J., Holst, O., Brade, H., Schmidt, G., Zahringer, U., The chemical structure of bacterial endotoxin in relation to bioactivity (1993) Immunobiology, 187, pp. 169-190
• Zahringer, U., Lindner, B., Rietschel, E.T., Molecular structure of lipid A, the endotoxic center of bacterial lipopolysaccharides (1994) Adv. Carbohydr. Chem. Biochem., 50, pp. 211-276
• Taylor, A.H., Heavner, G., Nedelman, M., Sherris, D., Brunt, E., Knight, D., Ghrayeb, J., Lipopolysaccharide (LPS) neutralizing peptides reveal a lipid A binding site of LPS binding protein (1995) J. Biol. Chem., 270, pp. 17934-17938
• Hoess, A., Watson, S., Siber, G.R., Liddington, R., Crystal structure of an endotoxin-neutralizing protein from the horseshoe crab, limulus anti-LPS factor, at 1.5 A resolution (1993) EMBO J., 12, pp. 3351-3356
• Weiss, J., Eslbach, P., Olsson, I., Oderberg, H., Purification and characterization of a potent bactericidal and membrane active protein from the granules of human polymorphonuclear leukocytes (1978) J. Biol. Chem., 253, pp. 2664-2672
• Thomas, C.J., Gangadhar, B.P., Surolia, N., Surolia, A., Kinetics and mechanism of the recognition of endotoxin by polymyxin B (1998) J. Am. Chem. Soc., 120, pp. 12428-12434
• Priano, G., Battaglini, F., Use of an antimicrobial protein for endotoxin detection in a competitive electrochemical assay (2005) Anal. Chem., 77, pp. 4976-4984
• Limoges, B., Saveant, J.-M., Yazidi, D., Quantitative analysis of catalysis and inhibition at horseradish peroxidase monolayers immobilized on an electrode surface (2003) J. Am. Chem. Soc., 125, pp. 9192-9203
• Santos, N., Silva, A., Castanho, M., Martins-Silva, J., Saldanha, C., Evaluation of lipopolysaccharide aggregation by light scattering spectroscopy (2003) Chem. Bio. Chem., 4, pp. 96-100
• Petsch, D., Anspach, F.J., Endotoxin removal from protein solutions (2000) J. Biotechnol., 76, pp. 97-119
• Shands, J., Chun, P., The dispersion of gram-negative lipopolysaccharide by deoxycholate: Subunit molecular weight (1980) J. Biol. Chem., 255, pp. 1221-1226
• Snyder, S., Kim, D., McIntosh, T., Lipopolysaccharide bilayer structure: effect of chemotype, core mutations, divalent cations, and temperature (1999) Biochemistry, 38, pp. 10758-10767
• Luk, J.M., Kumar, A., Tsang, R., Staunton, D., Biotinylated lipopolysaccharide binds to endotoxin receptor in endothelial and monocytic cells (1995) Anal. Biochem., 232, pp. 217-224
• Visintin, A., Latz, E., Monks, B.G., Espevik, T., Golenbock, D.T., Lysines 128 and 132 enable lipopolysaccharide binding to MD-2, leading to Toll-like receptor-4 aggregation and signal transduction (2003) J. Biol. Chem., 278, pp. 48313-48320
• Hermanson, G., (1996) Bioconjugate Techniques, , Academic Press, San Diego, CA
• Green, N.M., Avidin: I. The use of [14C]biotin for kinetic studies and for assay (1963) Biochem. J., 89, pp. 585-591
• Wilchek, M., Bayer, E.A., Foreword and introduction to the book (strept)avidin-biotin system (1999) Biomol. Eng., 16, pp. 1-4
• Rosano, C., Arioso, P., Bolognesi, M., The X-ray three-dimensional structure of avidin (1999) Biomol. Eng., 16, pp. 5-12
• Cortón, E., Danilowicz, C., Battaglini, F., Osmium complexes bearing functional groups: Building blocks for integrated chemical systems (1998) J. Electroanal. Chem., 445, pp. 89-94
• Triantafilou, K., Triantafilou, M., Fernandez, N., Lipopolysaccharide (LPS) labeled with Alexa 488 hydrazide as a novel probe for LPS binding studies (2000) Cytometry, 41, pp. 316-320
• Warren, H.S., Glennon, M.L., Wainwright, N., Amato, S.F., Black, K.M., Kirsch, S.J., Riveau, G.R., Novitsky, T.J., Binding and neutralization of endotoxin by limulus antilipopolysaccharide factor (1992) Infect. Immunol., 60, pp. 2506-2513
• Ried, C., Wahl, C., Miethke, T., Wellnhofer, G., Landgraf, C., Schneider-Mergener, J., Hoess, A., High affinity endotoxin-binding and neutralizing peptides based on the crystal structure of recombinant limulus anti-lipopolysaccharide factor (1996) J. Biol. Chem., 271, pp. 28120-28127
• Bannerman, D., Fitzpatrick, M., Anderson, D., Bhattarcharjee, A., Novitsky, T., Hasday, J., Cross, A., Goldblum, S., Endotoxin-neutralizing protein protects against endotoxin-induced endothelial barrier dysfunction (1998) Infect. Immunol, 66, pp. 1400-1407
• Brandenburg, K., Andrä, J., Müller, M., Koch, M.H.J., Garidel, P., Physicochemical properties of bacterial glycopolymers in relation to bioactivity (2003) Carbohydr. Res., 338, pp. 2477-2489
• Whittaker, M.M., Ballou, D.P., Whittaker, J.W., Kinetic isotope effects as probes of the mechanism of galactose oxidase (1998) Biochemistry, 37, pp. 8426-8436
• Aurell, C.A., Wiström, A., Critical aggregation concentrations of gram-negative bacterial lipopolysaccharides (LPS) (1998) Biochem. Biophys. Res. Commun., 253, pp. 119-123
• Wetter, L.R., Deutsch, H.F., Immunological studies on egg white proteins: IV. Immunochemical and physical studies of lysozyme (1951) J. Biol. Chem., 192, pp. 237-242
• Canfield, R.E., The amino acid sequence of egg white lysozyme (1963) J. Biol. Chem., 238, pp. 2698-2707
• Sophianopoulos, A.J., Rhodes, C.K., Holcomb, D.N., Van Holde, K.E., Physical studies of lysozyme: I. Characterization (1962) J. Biol. Chem., 237, pp. 1107-1112
• Jonson, U., Malmqvist, M., Real time biospecific interaction analysis (1992) Adv. Biosens., 2, pp. 291-336
• Polzius, R., Schneider, T., Bier, F., Bilitewski, U., Koschinski, W., Optimization of biosensing using grating couplers: Immobilization on tantalum oxide waveguides (1996) Biosens. Bioelectron., 11, pp. 503-514
• Österberg, E., Bergström, K., Holmberg, K., Schuman, T.P., Riggs, J.A., Burns, N.L., Van Alstine, J.M., Harris, J.M., Protein-rejecting ability of surface-bound dextran in end-on and side-on configurations: comparison to PEG (1995) J. Biomed. Mater. Res., 29, pp. 741-747
• Davies, C., (2001) The Immunoassay Handbook. 2nd ed., , Wild D. (Ed), Nature Publishing Group, New York chap. 1

Citas:

---------- APA ----------

---------- CHICAGO ----------

---------- MLA ----------

---------- VANCOUVER ----------