Binding of Efb from Staphylococcus aureus to fibrinogen blocks neutrophil adherence.
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A Structurally Dynamic N-terminal Helix Is a Key Functional Determinant in Staphylococcal Complement Inhibitor (SCIN) ProteinsExtracellular Fibrinogen-binding Protein (Efb) from Staphylococcus aureus Inhibits the Formation of Platelet-Leukocyte ComplexesBorrelia burgdorferi BBK32 Inhibits the Classical Pathway by Blocking Activation of the C1 Complement ComplexA novel Pfs38 protein complex on the surface of Plasmodium falciparum blood-stage merozoitesPhagocytosis escape by a Staphylococcus aureus protein that connects complement and coagulation proteins at the bacterial surfaceProteomics identification of novel fibrinogen-binding proteins of Streptococcus suis contributing to antiphagocytosisAttenuation of Staphylococcus aureus-Induced Bacteremia by Human Mini-Antibodies Targeting the Complement Inhibitory Protein EfbStaphylococcus aureus virulence is enhanced by secreted factors that block innate immune defenses.Nasopharyngeal colonization elicits antibody responses to staphylococcal and pneumococcal proteins that are not associated with a reduced risk of subsequent carriage.Immunization routes in cattle impact the levels and neutralizing capacity of antibodies induced against S. aureus immune evasion proteinsLeptospira Immunoglobulin-Like Protein B (LigB) Binds to Both the C-Terminal 23 Amino Acids of Fibrinogen αC Domain and Factor XIII: Insight into the Mechanism of LigB-Mediated Blockage of Fibrinogen α Chain Cross-Linking.Staphylococcal protein Ecb impairs complement receptor-1 mediated recognition of opsonized bacteria.Coagulase and Efb of Staphylococcus aureus Have a Common Fibrinogen Binding Motif.Binding of Human Fibrinogen to MRP Enhances Streptococcus suis Survival in Host Blood in a αXβ2 Integrin-dependent MannerMolecular characterization of endocarditis-associated Staphylococcus aureusBacteria under stress by complement and coagulation.Fibrinogen Is at the Interface of Host Defense and Pathogen Virulence in Staphylococcus aureus Infection.The Staphylococcus aureus polysaccharide capsule and Efb-dependent fibrinogen shield act in concert to protect against phagocytosis.Staphylococcus aureus Manipulates Innate Immunity through Own and Host-Expressed ProteasesCell Wall-Anchored Surface Proteins of Staphylococcus aureus: Many Proteins, Multiple Functions.Human Immunoglobulin G Cannot Inhibit Fibrinogen Binding by the Genetically Diverse A Domain of Staphylococcus aureus Fibronectin-Binding Protein A.Antibody-Based Agents in the Management of Antibiotic-Resistant Staphylococcus aureus Diseases.A novel peptide can mimic extracellular fibrinogen-binding protein to block the activation of complement system
P2860
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P2860
Binding of Efb from Staphylococcus aureus to fibrinogen blocks neutrophil adherence.
description
2011 nî lūn-bûn
@nan
2011 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2011年の論文
@ja
2011年論文
@yue
2011年論文
@zh-hant
2011年論文
@zh-hk
2011年論文
@zh-mo
2011年論文
@zh-tw
2011年论文
@wuu
name
Binding of Efb from Staphylococcus aureus to fibrinogen blocks neutrophil adherence.
@ast
Binding of Efb from Staphylococcus aureus to fibrinogen blocks neutrophil adherence.
@en
Binding of Efb from Staphylococcus aureus to fibrinogen blocks neutrophil adherence.
@nl
type
label
Binding of Efb from Staphylococcus aureus to fibrinogen blocks neutrophil adherence.
@ast
Binding of Efb from Staphylococcus aureus to fibrinogen blocks neutrophil adherence.
@en
Binding of Efb from Staphylococcus aureus to fibrinogen blocks neutrophil adherence.
@nl
prefLabel
Binding of Efb from Staphylococcus aureus to fibrinogen blocks neutrophil adherence.
@ast
Binding of Efb from Staphylococcus aureus to fibrinogen blocks neutrophil adherence.
@en
Binding of Efb from Staphylococcus aureus to fibrinogen blocks neutrophil adherence.
@nl
P2093
P2860
P356
P1476
Binding of Efb from Staphylococcus aureus to fibrinogen blocks neutrophil adherence
@en
P2093
C Wayne Smith
Jay L Degen
Magnus Höök
Ya-Ping Ko
P2860
P304
P356
10.1074/JBC.M110.199687
P407
P577
2011-01-19T00:00:00Z