The microenvironment of immobilized Arg-Gly-Asp peptides is an important determinant of cell adhesion (Q42829806)

8 November 2017

The microenvironment of immobilized Arg-Gly-Asp peptides is an important determinant of cell adhesion (English)

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8 November 2017

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B T Houseman

1

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PubMed ID

11311013

8 November 2017

M Mrksich

series ordinal

2

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8 November 2017

1 May 2001

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8 November 2017

13

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inferred from page(s)

published in

Biomaterials

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8 November 2017

22

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8 November 2017

9

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8 November 2017

943-955

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Integrins: versatility, modulation, and signaling in cell adhesion

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An RGD spacing of 440 nm is sufficient for integrin alpha V beta 3-mediated fibroblast spreading and 140 nm for focal contact and stress fiber formation

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Modulation of cell proliferation and differentiation through substrate-dependent changes in fibronectin conformation

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Covalent attachment of an Arg-Gly-Asp sequence peptide to derivatizable polyacrylamide surfaces: support of fibroblast adhesion and long-term growth

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Culture of human vascular endothelial cells on an RGD-containing synthetic peptide attached to a starch-coated polystyrene surface: comparison with fibronectin-coated tissue grade polystyrene

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The fibronectin cell attachment sequence Arg-Gly-Asp-Ser promotes focal contact formation during early fibroblast attachment and spreading

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Fibroblast adhesion to RGDS shows novel features compared with fibronectin

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(Arg-Gly-Asp)n-albumin conjugates as a model substratum for integrin-mediated cell adhesion

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Tailored substrates for studies of attached cell culture

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Adhesion mediated by bonds in series.

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Epidermal growth factor receptor activation of calpain is required for fibroblast motility and occurs via an ERK/MAP kinase signaling pathway

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Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule

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Identifiers

DOI

1 reference

8 November 2017

1 reference

PubMed ID

11311013