Identification of the staphylococcal enterotoxin A superantigen binding site in the beta 1 domain of the human histocompatibility antigen HLA-DR.
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Sequences in both class II major histocompatibility complex alpha and beta chains contribute to the binding of the superantigen toxic shock syndrome toxin 1Cross-linking of major histocompatibility complex class II molecules by staphylococcal enterotoxin A superantigen is a requirement for inflammatory cytokine gene expressionStaphylococcal enterotoxin A induces small clusters of HLA-DR1 on B cellsCrystal structure of the superantigen staphylococcal enterotoxin type AThe Co-crystal structure of staphylococcal enterotoxin type A with Zn2+ at 2.7 A resolution. Implications for major histocompatibility complex class II bindingStaphylococcus-mediated T-cell activation and spontaneous natural killer cell activity in the absence of major histocompatibility complex class II molecules.Stimulation with specific antigen can block superantigen-mediated deletion of T cells in vivo.Molecular characterization of Mls-1.Biological activities of staphylococcal enterotoxin type A mutants with N-terminal substitutionsBiochemical and mutational analysis of the histidine residues of staphylococcal enterotoxin A.A mutation of F47 to A in staphylococcus enterotoxin A activates the T-cell receptor Vbeta repertoire in vivoEvidence that the murine AIDS defective virus does not encode a superantigen.Identification of HLA-DR1 beta chain residues critical for binding staphylococcal enterotoxins A and E.Identification of HLA-DR alpha chain residues critical for binding of the toxic shock syndrome toxin superantigen.Selective binding of bacterial toxins to major histocompatibility complex class II-expressing cells is controlled by invariant chain and HLA-DM.T cell receptor interaction with peptide/major histocompatibility complex (MHC) and superantigen/MHC ligands is dominated by antigen.T cell receptor-major histocompatibility complex class II interaction is required for the T cell response to bacterial superantigens.Evidence for a functional interaction between the beta chain of major histocompatibility complex class II and the T cell receptor alpha chain during recognition of a bacterial superantigenCharacterization and biological properties of a new staphylococcal exotoxinAn insulin peptide that binds an alternative site in class II major histocompatibility complex.Different superantigens interact with distinct sites in the Vbeta domain of a single T cell receptor.Zinc regulates the function of two superantigens.Superantigen staphylococcal enterotoxin B-induced T-helper cell activation is independent of CD4 molecules and phosphatidylinositol hydrolysis.Distinct binding sites on HLA-DR for invariant chain and staphylococcal enterotoxins.Expression of bacterial superantigen genes in mice induces localized mononuclear cell inflammatory responses.Major histocompatibility complex class I molecule serves as a ligand for presentation of the superantigen staphylococcal enterotoxin B to T cells.The Forgotten: Identification and Functional Characterization of MHC Class II Molecules H2-Eb2 and RT1-Db2.Staphylococcal enterotoxin A has two cooperative binding sites on major histocompatibility complex class II.A natural mutation of the amino acid residue at position 60 destroys staphylococcal enterotoxin A murine T-cell mitogenicity.Bacterial pyrogenic exotoxins as superantigens.Functional analysis of Mycoplasma arthritidis-derived mitogen interactions with class II molecules.Relative abilities of distinct isotypes of human major histocompatibility complex class II molecules to bind streptococcal pyrogenic exotoxin types A and B.Predictions of T-cell receptor- and major histocompatibility complex-binding sites on staphylococcal enterotoxin C1.Bacterial superantigens--mechanism of T cell activation by the superantigens and their role in the pathogenesis of infectious diseases.Characterization of two distinct MHC class II binding sites in the superantigen staphylococcal enterotoxin A.Cellular distribution of a mixed MHC class II heterodimer between DRalpha and a chimeric DObeta chain.The crystal structure of staphylococcal enterotoxin type D reveals Zn2+-mediated homodimerization.Binding sites for bacterial and endogenous retroviral superantigens can be dissociated on major histocompatibility complex class II molecules.Staphylococcal enterotoxins A, D, and E. Structure and function, including mechanism of T-cell superantigenicity.Targeted superantigens for immunotherapy of haematopoietic tumours.
P2860
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P2860
Identification of the staphylococcal enterotoxin A superantigen binding site in the beta 1 domain of the human histocompatibility antigen HLA-DR.
description
1991 nî lūn-bûn
@nan
1991年の論文
@ja
1991年学术文章
@wuu
1991年学术文章
@zh-cn
1991年学术文章
@zh-hans
1991年学术文章
@zh-my
1991年学术文章
@zh-sg
1991年學術文章
@yue
1991年學術文章
@zh
1991年學術文章
@zh-hant
name
Identification of the staphylo ...... ocompatibility antigen HLA-DR.
@en
Identification of the staphylo ...... ocompatibility antigen HLA-DR.
@nl
type
label
Identification of the staphylo ...... ocompatibility antigen HLA-DR.
@en
Identification of the staphylo ...... ocompatibility antigen HLA-DR.
@nl
prefLabel
Identification of the staphylo ...... ocompatibility antigen HLA-DR.
@en
Identification of the staphylo ...... ocompatibility antigen HLA-DR.
@nl
P2093
P2860
P356
P1476
Identification of the staphylo ...... ocompatibility antigen HLA-DR.
@en
P2093
J Thibodeau
J W Kappler
N Labrecque
R P Sekaly
P2860
P304
P356
10.1073/PNAS.88.22.9954
P407
P577
1991-11-01T00:00:00Z