The structural basis of T cell activation by superantigens.
about
HLA-DR alpha 2 mediates negative signalling via binding to Tirc7 leading to anti-inflammatory and apoptotic effects in lymphocytes in vitro and in vivoGram-positive bacterial superantigen outside-in signaling causes toxic shock syndromeCrystal structure of staphylococcal enterotoxin I (SEI) in complex with a human major histocompatibility complex class II moleculeCrystal structure of a Staphylococcus aureus protein A domain complexed with the Fab fragment of a human IgM antibody: structural basis for recognition of B-cell receptors and superantigen activityStructural basis of metal hypersensitivityStaphylococcus aureus and its food poisoning toxins: characterization and outbreak investigationStaphylococcal superantigens in colonization and diseaseStaphylococcal enterotoxin A induces small clusters of HLA-DR1 on B cellsZinc Induces Dimerization of the Class II Major Histocompatibility Complex Molecule That Leads to Cooperative Binding to a SuperantigenCrystal structure of a complete ternary complex of TCR, superantigen and peptide-MHCCrystal Structure of Mycoplasma arthritidis Mitogen Complexed with HLA-DR1 Reveals a Novel Superantigen Fold and a Dimerized Superantigen-MHC ComplexCrystal Structure of the Mycoplasma arthritidis-Derived Mitogen in Apo Form Reveals a 3D Domain-Swapped DimerCrystal Structure of Staphylococcal Enterotoxin G (SEG) in Complex with a Mouse T-cell Receptor ChainPfit Is a Structurally Novel Crohn's Disease-Associated SuperantigenStructural basis for the neutralization and specificity of Staphylococcal enterotoxin B against its MHC Class II binding siteαβ T cell receptors that do not undergo major histocompatibility complex-specific thymic selection possess antibody-like recognition specificitiesThe postnatal maternal environment affects autoimmune disease susceptibility in A/J mice.Crystallographic and mutational data show that the streptococcal pyrogenic exotoxin J can use a common binding surface for T-cell receptor binding and dimerization.Uptake and intracellular trafficking of superantigens in dendritic cells.A hexamer peptide ligand that binds selectively to staphylococcal enterotoxin B: isolation from a solid phase combinatorial library.Secreted virulence factor comparison between methicillin-resistant and methicillin-sensitive Staphylococcus aureus, and its relevance to atopic dermatitis.The innate immune system is activated by stimulation of vaginal epithelial cells with Staphylococcus aureus and toxic shock syndrome toxin 1.Interferon gamma-dependent intestinal pathology contributes to the lethality in bacterial superantigen-induced toxic shock syndromeExpression of mouse mammary tumor virus superantigen accelerates tumorigenicity of myeloma cells.Potent neutralization of staphylococcal enterotoxin B by synergistic action of chimeric antibodiesHerpes B virus gD interaction with its human receptor--an in silico analysis approach.Glycolipid antigen induces long-term natural killer T cell anergy in mice.Cytomegalovirus-specific responses of CD38⁺ memory T cells are skewed towards IFN-γ and dissociated from CD154 in HIV-1 infectionFunctional characterization of streptococcal pyrogenic exotoxin J, a novel superantigen.Staphylococcal superantigens interact with multiple host receptors to cause serious diseases.Clarifying the mechanism of superantigen toxicitySequence variation and linkage disequilibrium in the human T-cell receptor beta (TCRB) locusChimeric anti-staphylococcal enterotoxin B antibodies and lovastatin act synergistically to provide in vivo protection against lethal doses of SEB.Staphylococcus aureus enterotoxins: a key in airway disease?Pseudomonas fluorescens encodes the Crohn's disease-associated I2 sequence and T-cell superantigenStaphylococcal superantigens cause lethal pulmonary disease in rabbits.Immunological changes in mesothelioma patients and their experimental detection.Staphylococcal and streptococcal superantigen exotoxinsRoles of Toll-like receptor 2 (TLR2) and superantigens on adaptive immune responses during CNS staphylococcal infection.Evaluation of a recombinant double mutant of staphylococcal enterotoxin B (SEB-H32Q/K173E) with enhanced antitumor activity effects and decreased pyrexia.
P2860
Q21562298-06053F0E-2019-4F37-A711-779B19BBF6BDQ24607551-B105C64A-ED03-4112-AB74-27C803D92DDAQ24648495-EB51689C-BE8E-48CD-B27D-186F6C23D6DDQ24656700-22E3382F-C171-407F-9A6C-D1F2453642A2Q26853141-88682052-441A-4C2C-A7C9-239C6CA0D077Q26862019-B47CC5E4-799D-48A8-9977-6891DCF311AFQ26995577-FE8F515D-E644-4BBB-83FA-47910521F100Q27346703-B3C6A2CA-4690-4A29-968A-F7F7AE70DBF0Q27640743-A3EF03BA-0881-4E3C-97AC-E4A12BBEBFB7Q27641131-FE069136-DEEC-4E75-9C8A-83FC91DCC1E1Q27643132-5CD9933D-BE52-4A44-9FFF-79AA5B61119DQ27660820-A43A41B7-BB71-41F6-9D86-5F827817585DQ27665660-2FE16BBF-CCB5-4610-AD5A-0145C2DDCBF1Q27681161-651D7511-2881-429B-99E1-2894CC2BA0E8Q27681324-A021278A-9CD2-474C-8B5F-8AFB25D477BCQ28256382-6DB66ECC-A989-4407-83DE-C9AECD501B89Q30433603-23264BCA-2DE3-4F07-A3C5-5316D868A645Q30942706-D5EA9E09-280B-4EB0-96E3-6088E89D1438Q31120808-67C8AB4F-BAF8-444F-A85B-684DBA08346FQ33204711-06EFC717-F018-487A-B15A-720938846D0AQ33622670-14974242-7806-410F-9351-E5CD9A3B5F14Q33769457-1FD8B7B6-A39E-42AB-8306-64E3D98BDDA0Q33815281-0599AA43-5C86-41DE-822C-9BA97CC79061Q33873627-086C84F5-32FE-4051-8907-EA5D8C9E13DDQ33877190-6AE693A3-FCCE-46E0-9439-86E8CD386D91Q33930801-9081BD0D-E989-4A00-B7DD-41F4D1EB4759Q33930869-AB20E63A-F467-4197-B4A6-56634BE8A9C8Q33943390-A6D162D7-50D7-40C8-9656-DF42FFF0F816Q34006242-BEDC545B-677C-445C-BA50-7B30877375F2Q34016794-0BF5DBF9-0FF0-452A-9A04-A1E42A2DB3BBQ34022965-CADFDEC8-8D64-4942-A389-EBBF68DFE275Q34044334-922C377F-67D8-46C4-925C-8A7926FFA4C6Q34079264-CA94358A-1FD2-4934-A25E-B8769EBDD161Q34129972-2A3DE373-DF40-4C11-A1AE-ADD52D3B6C47Q34259452-AE220823-2152-487E-81AE-9CE0D466D686Q34280083-91FB9DCA-8246-4ACD-9FDD-D722688BB3AAQ34342625-777BA490-4772-416F-BE15-E422BAFE28B2Q34355243-CF7412DE-ED7C-4C15-A6A8-3A1D151935FCQ34507688-9C661FE5-B11C-4A8F-B893-3D2DAC5AFF65Q34584576-931FE341-9DA5-4F4E-9522-8610105AB5A3
P2860
The structural basis of T cell activation by superantigens.
description
1999 nî lūn-bûn
@nan
1999 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
The structural basis of T cell activation by superantigens.
@ast
The structural basis of T cell activation by superantigens.
@en
type
label
The structural basis of T cell activation by superantigens.
@ast
The structural basis of T cell activation by superantigens.
@en
prefLabel
The structural basis of T cell activation by superantigens.
@ast
The structural basis of T cell activation by superantigens.
@en
P1476
The structural basis of T cell activation by superantigens
@en
P2093
P304
P356
10.1146/ANNUREV.IMMUNOL.17.1.435
P577
1999-01-01T00:00:00Z