Allosteric Regulation of Fibronectin/α5β1 Interaction by Fibronectin-Binding MSCRAMMs.

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Borrelia burgdorferi Keeps Moving and Carries on: A Review of Borrelial Dissemination and Invasion.Amino acid polymorphisms in the fibronectin-binding repeats of fibronectin-binding protein A affect bond strength and fibronectin conformation.

P2860

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P2860

Allosteric Regulation of Fibronectin/α5β1 Interaction by Fibronectin-Binding MSCRAMMs.

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http://www.wikidata.org/entity/Q36081745

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2016 nî lūn-bûn

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2016年の論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年論文

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2016年论文

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2016年论文

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2016年论文

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name

Allosteric Regulation of Fibronectin/α5β1 Interaction by Fibronectin-Binding MSCRAMMs.

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Allosteric Regulation of Fibronectin/α5β1 Interaction by Fibronectin-Binding MSCRAMMs.

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Allosteric Regulation of Fibronectin/α5β1 Interaction by Fibronectin-Binding MSCRAMMs.

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Allosteric Regulation of Fibronectin/α5β1 Interaction by Fibronectin-Binding MSCRAMMs.

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Allosteric Regulation of Fibronectin/α5β1 Interaction by Fibronectin-Binding MSCRAMMs.

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Allosteric Regulation of Fibronectin/α5β1 Interaction by Fibronectin-Binding MSCRAMMs.

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P1476

Allosteric Regulation of Fibronectin/α5β1 Interaction by Fibronectin-Binding MSCRAMMs.

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P2093

Brandon L Garcia

http://www.w3.org/2001/XMLSchema#string

Jennifer R Potts

http://www.w3.org/2001/XMLSchema#string

Magnus Höök

http://www.w3.org/2001/XMLSchema#string

Nicola A G Meenan

http://www.w3.org/2001/XMLSchema#string

Sabitha Prabhakaran

http://www.w3.org/2001/XMLSchema#string

P2860

Heterologously expressed Staphylococcus aureus fibronectin-binding proteins are sufficient for invasion of host cells

Pathogenic bacteria attach to human fibronectin through a tandem beta-zipper

Structural and Functional Analysis of the Tandem -Zipper Interaction of a Streptococcal Protein with Human Fibronectin

Borrelia burgdorferi Protein BBK32 Binds to Soluble Fibronectin via the N-terminal 70-kDa Region, Causing Fibronectin to Undergo Conformational Extension

Novel antibody-antibiotic conjugate eliminates intracellular S. aureus

Integrins: bidirectional, allosteric signaling machines

Borrelia burgdorferi BBK32 Inhibits the Classical Pathway by Blocking Activation of the C1 Complement Complex

Staphylococcus aureus fibronectin binding protein-A induces motile attachment sites and complex actin remodeling in living endothelial cells.

Characterization of a candidate Borrelia burgdorferi beta3-chain integrin ligand identified using a phage display library.

Evidence of an intracellular reservoir in the nasal mucosa of patients with recurrent Staphylococcus aureus rhinosinusitis.

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e0159118

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scholarly article

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10.1371/JOURNAL.PONE.0159118

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English

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2016-07-19T00:00:00Z

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27434228

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4951027

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Allosteric Regulation of Fibronectin/α5β1 Interaction by Fibronectin-Binding MSCRAMMs.

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P2860

P2860

Allosteric Regulation of Fibronectin/α5β1 Interaction by Fibronectin-Binding MSCRAMMs.

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P1433

P1476

P2093

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