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© 1992 Nature Publishing Group
© 1992 Nature Publishing Group
© 1992 Nature Publishing Group
© 1992 Nature Publishing Group
© 1992 Nature Publishing Group
© 1992 Nature Publishing Group
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Mutations defining functional regions of the superantigen staphylococcal enterotoxin B.
Structure of the superantigen staphylococcal enterotoxin B in complex with TCR and peptide-MHC demonstrates absence of TCR-peptide contacts.
Assessment of the functional regions of the superantigen staphylococcal enterotoxin B.
Accessory function of human mononuclear phagocytes for lymphocyte responses to the superantigen staphylococcal enterotoxin B.
Memory T cells are anergic to the superantigen staphylococcal enterotoxin B.
Regulation of staphylococcal enterotoxin B.
Bacterial Toxins-Staphylococcal Enterotoxin B.
Inhibition of immunospecific inactivation of staphylococcal enterotoxin B-bacteriophage conjugate by bovine antibodies: a sensitive assay for staphylococcal enterotoxin B.
Binding of flavonoids to staphylococcal enterotoxin B.
Staphylococcal enterotoxin-like X (SElX) is a unique superantigen with functional features of two major families of staphylococcal virulence factors.
Chromosomal locus for staphylococcal enterotoxin B.
T-cell antigen receptor binding sites for the microbial superantigen staphylococcal enterotoxin A.
Superantigen staphylococcal enterotoxin B-induced T-helper cell activation is independent of CD4 molecules and phosphatidylinositol hydrolysis.
T cell-mediated lethal shock triggered in mice by the superantigen staphylococcal enterotoxin B: critical role of tumor necrosis factor.
Protein A insensitive ELISA detection of staphylococcal enterotoxin B.
Localisation of the mitogenic epitope of staphylococcal enterotoxin B.
Identification of functionally active fragments of staphylococcal enterotoxin B.
Iodination of staphylococcal enterotoxin B by use of chloramine-T.
Neutralization of staphylococcal enterotoxin B by an aptamer antagonist.
Effects of staphylococcal enterotoxin B on rodent mast cells.
Mitogenicity of formalinized toxoids of staphylococcal enterotoxin B.
Effect of minerals on staphylococcal enterotoxin B production.
Sulfasalazine attenuates staphylococcal enterotoxin B-induced immune responses.
Evidence for the alpha-helicity of class II MHC molecular binding sites for the superantigen, staphylococcal enterotoxin A.
Crystal structure of staphylococcal enterotoxin B, a superantigen.
The three-dimensional structure of staphylococcal enterotoxin B, which is both a toxin and a super-antigen, has been determined to a resolution of 2.5...
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Mutations defining functional regions of the superantigen staphylococcal enterotoxin B.
Structure of the superantigen staphylococcal enterotoxin B in complex with TCR and peptide-MHC demonstrates absence of TCR-peptide contacts.
Assessment of the functional regions of the superantigen staphylococcal enterotoxin B.
Accessory function of human mononuclear phagocytes for lymphocyte responses to the superantigen staphylococcal enterotoxin B.
Memory T cells are anergic to the superantigen staphylococcal enterotoxin B.
Regulation of staphylococcal enterotoxin B.
Bacterial Toxins-Staphylococcal Enterotoxin B.
Inhibition of immunospecific inactivation of staphylococcal enterotoxin B-bacteriophage conjugate by bovine antibodies: a sensitive assay for staphylococcal enterotoxin B.
Binding of flavonoids to staphylococcal enterotoxin B.
Staphylococcal enterotoxin-like X (SElX) is a unique superantigen with functional features of two major families of staphylococcal virulence factors.
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