Staphylococcal protein A consists of five IgG-binding domains.
about
A Staphylococcus aureus small RNA is required for bacterial virulence and regulates the expression of an immune-evasion moleculeDual RNA regulatory control of a Staphylococcus aureus virulence factorStaphylococcal protein A: unfolding pathways, unfolded states, and differences between the B and E domainsThe Staphylococcal Biofilm: Adhesins, Regulation, and Host ResponsePolyclonal and monoclonal IgG binding on protein A resins-Evidence of competitive binding effects.Cysteine-terminated B-domain of Staphylococcus aureus protein A as a scaffold for targeting GABA(A) receptorsAnti-idiotypic protein domains selected from protein A-based affibody libraries.Detection and characterization of individual intermolecular bonds using optical tweezersDistribution of protein A on the surface of Staphylococcus aureusEvolutional selection of a combinatorial phage library displaying randomly-rearranged various single domains of immunoglobulin (Ig)-binding proteins (IBPs) with four kinds of Ig molecules.Production of specific antibodies against protein A fusion proteinsMultiple mechanisms for the activation of human platelet aggregation by Staphylococcus aureus: roles for the clumping factors ClfA and ClfB, the serine-aspartate repeat protein SdrE and protein A.Functions of the Fc receptors for immunoglobulin G.Immunoglobulin purification by affinity chromatography using protein A mimetic ligands prepared by combinatorial chemical synthesis.The statistical conformation of a highly flexible protein: small-angle X-ray scattering of S. aureus protein A.Uniform fluorescent nanobioprobes for pathogen detection.In vitro molecular evolution yields an NEIBM with a potential novel IgG binding property.Quantum dot imaging platform for single-cell molecular profiling.Protein A is released into the Staphylococcus aureus culture supernatant with an unprocessed sorting signalThe Sbi protein is a multifunctional immune evasion factor of Staphylococcus aureusAffinity proteomics to study endogenous protein complexes: pointers, pitfalls, preferences and perspectives.Intramammary Immunization of Pregnant Mice with Staphylococcal Protein A Reduces the Post-Challenge Mammary Gland Bacterial Load but Not Pathology.Multiplexed In-cell Immunoassay for Same-sample Protein Expression Profiling.The WalKR system controls major staphylococcal virulence genes and is involved in triggering the host inflammatory responsePresentation of antigen in immune complexes is boosted by soluble bacterial immunoglobulin binding proteins.Innate Immune Signaling Activated by MDR Bacteria in the AirwayImmunopathogenesis of Staphylococcus aureus pulmonary infection.Aleutian mink disease parvovirus infection of mink macrophages and human macrophage cell line U937: demonstration of antibody-dependent enhancement of infection.A Robust Workflow for Native Mass Spectrometric Analysis of Affinity-Isolated Endogenous Protein Assemblies.Protein A mimetic peptide ligand for affinity purification of antibodies.Improved native isolation of endogenous Protein A-tagged protein complexes.Regioselective covalent immobilization of recombinant antibody-binding proteins A, G, and L for construction of antibody arrays.Denaturant-induced expansion and compaction of a multi-domain protein: IgG.Shedding of tumor necrosis factor receptor 1 induced by protein A decreases tumor necrosis factor alpha availability and inflammation during systemic Staphylococcus aureus infection.Development of an immunoFET biosensor for the detection of biotinylated PCR product.Surface Plasmon Resonance Investigations of Bioselective Element Based on the Recombinant Protein A for Immunoglobulin Detection.Structural and functional role of Staphylococcus aureus surface components recognizing adhesive matrix molecules of the host.Innate immunity in the respiratory epithelium.Coupling of antibodies via protein Z on modified polyoma virus-like particles.Staphylococcus aureus protein A activates TACE through EGFR-dependent signaling.
P2860
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P2860
Staphylococcal protein A consists of five IgG-binding domains.
description
1986 nî lūn-bûn
@nan
1986年の論文
@ja
1986年学术文章
@wuu
1986年学术文章
@zh-cn
1986年学术文章
@zh-hans
1986年学术文章
@zh-my
1986年学术文章
@zh-sg
1986年學術文章
@yue
1986年學術文章
@zh
1986年學術文章
@zh-hant
name
Staphylococcal protein A consists of five IgG-binding domains.
@en
Staphylococcal protein A consists of five IgG-binding domains.
@nl
type
label
Staphylococcal protein A consists of five IgG-binding domains.
@en
Staphylococcal protein A consists of five IgG-binding domains.
@nl
prefLabel
Staphylococcal protein A consists of five IgG-binding domains.
@en
Staphylococcal protein A consists of five IgG-binding domains.
@nl
P2093
P2860
P1433
P1476
Staphylococcal protein A consists of five IgG-binding domains.
@en
P2093
P2860
P304
P356
10.1111/J.1432-1033.1986.TB09625.X
P407
P577
1986-05-01T00:00:00Z