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Refined structures of three crystal forms of toxic shock syndrome toxin-1 and of a tetramutant with reduced activityCross-linking of major histocompatibility complex class II molecules by staphylococcal enterotoxin A superantigen is a requirement for inflammatory cytokine gene expressionStructure of streptococcal pyrogenic exotoxin A reveals a novel metal clusterCrystal structure of a superantigen bound to MHC class II displays zinc and peptide dependenceZinc-mediated dimerization and its effect on activity and conformation of staphylococcal enterotoxin type CCrystal 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 bindingSmall but versatile: the extraordinary functional and structural diversity of the beta-grasp foldIdentification and characterization of staphylococcal enterotoxin types G and I from Staphylococcus aureusMapping of staphylococcal enterotoxin A functional binding sites and presentation by monoclonal antibodies and fusion proteinsBiological 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 vivoStructure of Staphylococcal Enterotoxin E in Complex with TCR Defines the Role of TCR Loop Positioning in Superantigen Recognition.Superantigen binding to a T cell receptor beta chain of known three-dimensional structure.Sensitive, Rapid, Quantitative and in Vitro Method for the Detection of Biologically Active Staphylococcal Enterotoxin Type E.The natural history of ubiquitin and ubiquitin-related domains.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.Involvement of zinc in the binding of Mycoplasma arthritidis-derived mitogen to the proximity of the HLA-DR binding groove regardless of histidine 81 of the beta chain.Characterization of two distinct MHC class II binding sites in the superantigen staphylococcal enterotoxin A.The crystal structure of staphylococcal enterotoxin type D reveals Zn2+-mediated homodimerization.Analysis of functional regions of YPM, a superantigen derived from gram-negative bacteria.Two adjacent residues in staphylococcal enterotoxins A and E determine T cell receptor V beta specificity.Staphylococcal enterotoxins B and C. Structural requirements for superantigenic and entertoxigenic activities.Staphylococcal enterotoxins A, D, and E. Structure and function, including mechanism of T-cell superantigenicity.Zinc in pharmacological doses suppresses allogeneic reaction without affecting the antigenic response.Zinc and the immune systemThe Spectral and Thermodynamic Properties of Staphylococcal Enterotoxin A, E, and Variants Suggest That Structural Modifications Are Important to Control Their Function
P2860
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P2860
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on June 1992
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Zinc regulates the function of two superantigens.
@en
Zinc regulates the function of two superantigens.
@nl
type
label
Zinc regulates the function of two superantigens.
@en
Zinc regulates the function of two superantigens.
@nl
prefLabel
Zinc regulates the function of two superantigens.
@en
Zinc regulates the function of two superantigens.
@nl
P2093
P2860
P356
P1476
Zinc regulates the function of two superantigens.
@en
P2093
P2860
P304
P356
10.1073/PNAS.89.12.5507
P407
P577
1992-06-01T00:00:00Z