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Cited by 278

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Biochemical and Structural Properties of the Integrin-Associated Cytoskeletal Protein Talin

Critchley, David R.·2009·Annual Review of Biophysics

Abstract

Interaction of cells with the extracellular matrix is fundamental to a wide variety of biological processes, such as cell proliferation, cell migration, embryogenesis, and organization of cells into tissues, and defects in cell-matrix interactions are an important element in many diseases. Cell-matrix interactions are frequently mediated by the integrin family of cell adhesion molecules, transmembrane alphabeta-heterodimers that are typically linked to the actin cytoskeleton by one of a number of adaptor proteins including talin, alpha-actinin, filamin, tensin, integrin-linked kinase, melusin, and skelemin. The focus of this review is talin, which appears unique among these proteins in that it also induces a conformational change in integrins that is propagated across the membrane, and increases the affinity of the extracellular domain for ligand. Particular emphasis is given to recent progress on the structure of talin, its interaction with binding partners, and its mode of regulation.

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Crossref · 10.1146/annurev.biophys.050708.133744

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Metadata

Authors
Critchley, D. R.
Venue
Annual Review of Biophysics
Published
2009-06
Volume
38
Issue
1
Pages
235-254
ISSN
  • 1936-122X (ISSN-L)
  • 1936-1238
OpenAlex
W2124903948
Cited by
278
References
4
FWCI
1.83
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Biochemical and Structural Properties of the Integrin-Associated Cytoskeletal Protein Talin. https://app.cochat.ai/papers/10.1146/annurev.biophys.050708.133744
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Critchley, D. R. (2009). Biochemical and Structural Properties of the Integrin-Associated Cytoskeletal Protein Talin. Annual Review of Biophysics. https://doi.org/10.1146/annurev.biophys.050708.133744

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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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