The DOI matches its Crossref record; 88 of the 88 references it cites were found in a registry or an index.
The ins and outs of fibronectin matrix assembly
Abstract
Cell phenotype is specified by environmental cues embedded in the architecture and composition of the extracellular matrix (ECM). Much has been learned about matrix organization and assembly through analyses of the ECM protein fibronectin (FN). FN matrix assembly is a cell-mediated process in which soluble dimeric FN is converted into a fibrillar network. Binding of cell surface integrin receptors to FN converts it to an active form, which promotes fibril formation through interactions with other cell-associated FN dimers. As FN fibrils form on the outside of the cell, cytoplasmic domains of integrin receptors organize cytoplasmic proteins into functional complexes inside. Intracellular connections to the actin cytoskeletal network and stimulation of certain key intracellular signaling pathways are essential for FN–integrin interactions and propagation of FN fibril formation. Thus,assembly of native functional ECM depends on exquisite coordination between extracellular events and intracellular pathways.
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The structure and regulation of vinculin
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Integrin-α9 Is Required for Fibronectin Matrix Assembly during Lymphatic Valve Morphogenesis
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Osseointegration – communication of cells
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Metadata
- Authors
- Wierzbicka-Patynowski, I., & Schwarzbauer, J. E.
- Venue
- Journal of Cell Science
- Publisher
- The Company of Biologists
- Published
- 2003-08-15
- Volume
- 116
- Issue
- 16
- Pages
- 3269-3276
- ISSN
- 0021-9533 (ISSN-L)
- 1477-9137
- OpenAlex
- W1967922151
- Cited by
- 473
- References
- 88
- FWCI
- 13.28
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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