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Cited by 445

The DOI matches its Crossref record; 7 of the 7 references it cites were found in a registry or an index.

Fibronectins, Their Fibrillogenesis, and In Vivo Functions

Open access
Schwarzbauer, J. E., DeSimone, D. W.·2011·Cold Spring Harbor Perspectives in Biology

Abstract

Fibronectin (FN) is a multidomain protein with the ability to bind simultaneously to cell surface receptors, collagen, proteoglycans, and other FN molecules. Many of these domains and interactions are also involved in the assembly of FN dimers into a multimeric fibrillar matrix. When, where, and how FN binds to its various partners must be controlled and coordinated during fibrillogenesis. Steps in the process of FN fibrillogenesis including FN self-association, receptor activities, and intracellular pathways have been under intense investigation for years. In this review, the domain organization of FN including the extra domains and variable region that are controlled by alternative splicing are described. We discuss how FN-FN and cell-FN interactions play essential roles in the initiation and progression of matrix assembly using complementary results from cell culture and embryonic model systems that have enhanced our understanding of this process.

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Metadata

Authors
Schwarzbauer, J. E., & DeSimone, D. W.
Venue
Cold Spring Harbor Perspectives in Biology
Published
2011-05-16
Volume
3
Issue
7
Pages
a005041-a005041
ISSN
1943-0264 (ISSN-L)
OpenAlex
W2142761181
Cited by
445
References
7
Type
posted content
Language
en
Open access
green

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CoChat. (2026). Citation check: Fibronectins, Their Fibrillogenesis, and In Vivo Functions. https://app.cochat.ai/papers/10.1101/cshperspect.a005041
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Schwarzbauer, J. E., & DeSimone, D. W. (2011). Fibronectins, Their Fibrillogenesis, and In Vivo Functions. Cold Spring Harbor Perspectives in Biology. https://doi.org/10.1101/cshperspect.a005041

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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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