A novel fibronectin binding motif in MSCRAMMs targets F3 modules.
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Borrelia burgdorferi Protein BBK32 Binds to Soluble Fibronectin via the N-terminal 70-kDa Region, Causing Fibronectin to Undergo Conformational ExtensionMultifunctional and Redundant Roles of Borrelia burgdorferi Outer Surface Proteins in Tissue Adhesion, Colonization, and Complement EvasionBorrelia burgdorferi BBK32 Inhibits the Classical Pathway by Blocking Activation of the C1 Complement ComplexIdentification of Tp0751 (Pallilysin) as a Treponema pallidum Vascular Adhesin by Heterologous Expression in the Lyme disease Spirochete.The Structure of Treponema pallidum Tp0751 (Pallilysin) Reveals a Non-canonical Lipocalin Fold That Mediates Adhesion to Extracellular Matrix Components and Interactions with Host Cells.Vascular binding of a pathogen under shear force through mechanistically distinct sequential interactions with host macromolecules.Biomechanics of Borrelia burgdorferi Vascular InteractionsPlasma fibronectin stabilizes Borrelia burgdorferi-endothelial interactions under vascular shear stress by a catch-bond mechanismConformational remodeling of the fibronectin matrix selectively regulates VEGF signaling.Invasion of eukaryotic cells by Borrelia burgdorferi requires β(1) integrins and Src kinase activity.Bioluminescent imaging of Borrelia burgdorferi in vivo demonstrates that the fibronectin-binding protein BBK32 is required for optimal infectivityGlycosaminoglycan binding by Borrelia burgdorferi adhesin BBK32 specifically and uniquely promotes joint colonization.Allosteric Regulation of Fibronectin/α5β1 Interaction by Fibronectin-Binding MSCRAMMs.SLLISWD sequence in the 10FNIII domain initiates fibronectin fibrillogenesis.The fibronectin-binding motif within FlpA facilitates Campylobacter jejuni adherence to host cell and activation of host cell signalingStructural and functional role of Staphylococcus aureus surface components recognizing adhesive matrix molecules of the host.Fibronectin: a multidomain host adhesin targeted by bacterial fibronectin-binding proteins.Adhesion mechanisms of Borrelia burgdorferi.Illuminating the roles of the Borrelia burgdorferi adhesinsCryptic activity within the Type III1 domain of fibronectin regulates tissue inflammation and angiogenesis.Borrelia burgdorferi glycosaminoglycan binding protein, Bgp in the B31 strain is not essential for infectivity despite facilitating adherence and tissue colonization.
P2860
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P2860
A novel fibronectin binding motif in MSCRAMMs targets F3 modules.
description
2009 nî lūn-bûn
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name
A novel fibronectin binding motif in MSCRAMMs targets F3 modules.
@en
A novel fibronectin binding motif in MSCRAMMs targets F3 modules.
@nl
type
label
A novel fibronectin binding motif in MSCRAMMs targets F3 modules.
@en
A novel fibronectin binding motif in MSCRAMMs targets F3 modules.
@nl
prefLabel
A novel fibronectin binding motif in MSCRAMMs targets F3 modules.
@en
A novel fibronectin binding motif in MSCRAMMs targets F3 modules.
@nl
P2093
P2860
P1433
P1476
A novel fibronectin binding motif in MSCRAMMs targets F3 modules.
@en
P2093
Jennifer R Potts
Jonathan T Skare
Magnus Höök
Sabitha Prabhakaran
P2860
P356
10.1371/JOURNAL.PONE.0005412
P407
P577
2009-04-30T00:00:00Z