Structural basis of superantigen action inferred from crystal structure of toxic-shock syndrome toxin-1. (Q34335699)

1 August 2017

title

Structural basis of superantigen action inferred from crystal structure of toxic-shock syndrome toxin-1. (English)

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1 August 2017

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Acharya KR

1

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Passalacqua EF

2

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Harlos K

4

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Stuart DI

5

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Brehm RD

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Tranter HS

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language of work or name

English

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publication date

1 January 1994

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volume

367

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issue

6458

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1 August 2017

page(s)

94-97

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The Vβ-specific superantigen staphylococcal enterotoxin B: Stimulation of mature T cells and clonal deletion in neonatal mice

1 August 2017

cites work

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7 January 2021

T-cell responses to Mls and to bacterial proteins that mimic its behavior

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7 January 2021

T cell stimulation by staphylococcal enterotoxins. Clonally variable response and requirement for major histocompatibility complex class II molecules on accessory or target cells

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7 January 2021

Crystal structure of staphylococcal enterotoxin B, a superantigen

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7 January 2021

The staphylococcal enterotoxins and their relatives.

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7 January 2021

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7 January 2021

Activation of in vitro proliferation of human T cells by a synthetic peptide of toxic shock syndrome toxin 1

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7 January 2021

Identification of binding domains on the superantigen, toxic shock syndrome-1, for class II MHC molecules

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7 January 2021

Neutralization of toxic shock syndrome toxin-1 by monoclonal antibodies in vitro and in vivo.

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7 January 2021

Mutants of staphylococcal toxic shock syndrome toxin 1: mitogenicity and recognition by a neutralizing monoclonal antibody

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7 January 2021

Structural basis for differential binding of staphylococcal enterotoxin A and toxic shock syndrome toxin 1 to class II major histocompatibility molecules

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7 January 2021

Mutations defining functional regions of the superantigen staphylococcal enterotoxin B.

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7 January 2021

Enterotoxin residues determining T-cell receptor V beta binding specificity

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7 January 2021

Sequences in both class II major histocompatibility complex alpha and beta chains contribute to the binding of the superantigen toxic shock syndrome toxin 1

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7 January 2021

Identification of HLA-DR alpha chain residues critical for binding of the toxic shock syndrome toxin superantigen

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7 January 2021

Identification of the region of T cell receptor β chain that interacts with the self-superantigen MIs-1a

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7 January 2021

Analysis of the interaction site for the self superantigen Mls-1a on T cell receptor V beta

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7 January 2021

How do T-cell receptors, MHC molecules and superantigens get together?

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7 January 2021

Purification, crystallization and preliminary X-ray analysis of toxic shock syndrome toxin-1 from Staphylococcus aureus

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7 January 2021

Methodology employed for the structure determination of tumour necrosis factor, a case of high non-crystallographic symmetry

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7 January 2021

Diffraction methods for biological macromolecules. Interactive computer graphics: FRODO

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7 January 2021

Crystallographic R factor refinement by molecular dynamics

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7 January 2021

Model for the interaction of T-cell receptors with peptide/MHC complexes

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7 January 2021

Residues of the variable region of the T-cell-receptor β-chain that interact with S. aureus toxin superantigens

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7 January 2021

Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1.

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7 January 2021

Identifiers

DOI

10.1038/367094A0

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Dimensions Publication ID

1 August 2017

1046052726

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