Biological analysis of the deletion mutants of Staphylococcal enterotoxin C2 (original) (raw)

Enhancement of superantigen activity and antitumor response of staphylococcal enterotoxin C2 by site-directed mutagenesis

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Cancer Immunology Immunotherapy, 2009

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Functional analysis of the disulphide loop mutant of staphylococcal enterotoxin C2

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Applied Microbiology and Biotechnology, 2009

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Superantigen Vaccines: A Comparative Study of Genetically Attenuated Receptor-Binding Mutants of Staphylococcal Enterotoxin A

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Journal of Infectious Diseases, 1996

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A structural and functional comparison of staphylococcal enterotoxins A and C2 reveals remarkable similarity and dissimilarity1

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Journal of molecular …, 1997

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The Spectral and Thermodynamic Properties of Staphylococcal Enterotoxin A, E, and Variants Suggest That Structural Modifications Are Important to Control Their Function

Daniel Otzen

Journal of Biological Chemistry, 2000

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T-cell antigen receptor binding sites for the microbial superantigen staphylococcal enterotoxin A

Nicholas Gascoigne

Proceedings of the National Academy of Sciences, 1992

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Mutational analysis and molecular modeling of the binding of Staphylococcus aureus enterotoxin C2 to a murine T cell receptor Vβ10 chain

Vincent Mutel

European Journal of Immunology, 2002

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Crystal Structure of Staphylococcal Enterotoxin I (SEI) in Complex with a Human Major Histocompatibility Complex Class II Molecule

Marisa Fernandez

Journal of Biological Chemistry, 2006

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Staphylococcal enterotoxin-like X (SElX) is a unique superantigen with functional features of two major families of staphylococcal virulence factors

Fiona Radcliff

PLOS Pathogens

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A Mutational Analysis of the Binding of Staphylococcal Enterotoxins B and C3 to the T Cell Receptor Chain and Major Histocompatibility Complex Class II

Hongmin Li

Journal of Experimental Medicine, 1998

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Molecular characterization of the putative T-cell receptor cavity of the superantigen staphylococcal enterotoxin B

Jerome Gabriel

Immunology, 1998

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Staphylococcal Enterotoxin-Like Toxins U2 and V, Two New Staphylococcal Superantigens Arising from Recombination within the Enterotoxin Gene Cluster

Marie-Lise Gougeon

Infection and Immunity, 2007

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Superantigen natural affinity maturation revealed by the crystal structure of staphylococcal enterotoxin G and its binding to T-cell receptor Vβ8.2

Emilio Malchiodi, Marisa Fernandez

Proteins: Structure, Function, and Bioinformatics, 2007

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Identification of the Antigenic Epitopes in Staphylococcal Enterotoxins A and E and Design of a Superantigen for Human Cancer Therapy

Björn Walse

Journal of Molecular Biology, 2003

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Characterization of a Novel Staphylococcal Enterotoxin-Like Superantigen, a Member of the Group V Subfamily of Pyrogenic Toxins†

Paul Orwin

Biochemistry, 2002

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Structural basis for abrogated binding between staphylococcal enterotoxin A superantigen vaccine and MHC-IIα

Bernhard Rupp

Protein Science, 2009

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Identification of a Transcytosis Epitope on Staphylococcal Enterotoxins

Jeffrey Shupp, Carol Pontzer

Infection and Immunity, 2002

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Structure of staphylococcal enterotoxin C2 at various pH levels

William Furey

Acta Crystallographica Section D Biological Crystallography, 2001

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Rapid clearance of the bacterial superantigen staphylococcal enterotoxin B in vivo

Klaus Heeg

Infection and immunity, 1996

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Cells V{alpha}Specific Expansion of T Staphylococcal Enterotoxin H Induces

Björn Walse

2000

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Conservation and variation in superantigen structure and activity highlighted by the three-dimensional structures of two new superantigens from Streptococcus pyogenes

Vickery Arcus

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Generation, characterization, and epitope mapping of neutralizing and protective monoclonal antibodies against staphylococcal enterotoxin B-induced lethal shock

Avanish Varshney

2011

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Staphylococcal Enterotoxin C—An Update on SEC Variants, Their Structure and Properties, and Their Role in Foodborne Intoxications

Sophia Johler

Toxins

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Construction of a Single-Chain Variable-Fragment Antibody against the Superantigen Staphylococcal Enterotoxin B

Suang Rungpragayphan

2010

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Identification of a Secondary Zinc-binding Site in Staphylococcal Enterotoxin C2: IMPLICATIONS FOR SUPERANTIGEN RECOGNITION

Sayed Goda

Journal of Biological Chemistry, 2003

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A natural mutation of the amino acid residue at position 60 destroys staphylococcal enterotoxin A murine T-cell mitogenicity

Jacques Hebert

Infection and immunity, 1995

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Staphylococcal Enterotoxin D Is a Promiscuous Superantigen Offering Multiple Modes of Interactions With the MHC Class II Receptors

Pierre Étongué Mayer

The Journal of Immunology

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