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Structure and reactivity of adsorbed fibronectin films on mica.

Structure and reactivity of adsorbed fibronectin films on mica.

http://www.wikidata.org/entity/Q33300057

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Interactions of the streptococcal C5a peptidase with human fibronectin.Biomedical surface analysis: Evolution and future directions (Review)ToF-SIMS and XPS Characterization of Protein Films Adsorbed onto Bare and Sodium Styrenesulfonate-Grafted Gold Substrates.Atomic force microscopy evidence for conformational changes of fibronectin adsorbed on unmodified and sulfonated polystyrene surfaces.Effect of the Materials Properties of Hydroxyapatite Nanoparticles on Fibronectin Deposition and Conformation.Mechanical matching between a ligand and receptor.

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P2860

Structure and reactivity of adsorbed fibronectin films on mica.

http://www.wikidata.org/entity/Q33300057

description

2007 nî lūn-bûn

@nan

2007 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

Structure and reactivity of adsorbed fibronectin films on mica.

@ast

Structure and reactivity of adsorbed fibronectin films on mica.

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Structure and reactivity of adsorbed fibronectin films on mica.

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type

label

Structure and reactivity of adsorbed fibronectin films on mica.

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Structure and reactivity of adsorbed fibronectin films on mica.

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Structure and reactivity of adsorbed fibronectin films on mica.

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Structure and reactivity of adsorbed fibronectin films on mica.

@ast

Structure and reactivity of adsorbed fibronectin films on mica.

@en

Structure and reactivity of adsorbed fibronectin films on mica.

@nl

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BIOPHYSJ.107.109819

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Biophysical Journal

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Structure and reactivity of adsorbed fibronectin films on mica.

@en

P2093

David G Castner

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Glen S Tamura

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James R Hull

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P2860

The interrelated role of fibronectin and interleukin-1 in biomaterial-modulated macrophage function

Preserving the structure of adsorbed protein films for time-of-flight secondary ion mass spectrometry analysis.

Data analysis of interaction forces measured with the atomic force microscope

Force spectroscopy study of the adhesion of plasma proteins to the surface of a dialysis membrane: role of the nanoscale surface hydrophobicity and topography.

The two polypeptide chains in fibronectin are joined in antiparallel fashion: NMR structural characterization.

Simultaneous height and adhesion imaging of antibody-antigen interactions by atomic force microscopy.

Shapes, domain organizations and flexibility of laminin and fibronectin, two multifunctional proteins of the extracellular matrix.

Time-of-flight secondary ion mass spectrometry: techniques and applications for the characterization of biomaterial surfaces.

The compact conformation of fibronectin is determined by intramolecular ionic interactions.

Limits of detection for time of flight secondary ion mass spectrometry (ToF-SIMS) and X-ray photoelectron spectroscopy (XPS): detection of low amounts of adsorbed protein.

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2852-2860

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