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The DOI matches its Crossref record; 84 of the 84 references it cites were found in a registry or an index.

Integrin cytoplasmic domain-binding proteins

Open access
Liu, Shouchun, Calderwood, David A., Ginsberg, Mark H.·2000·Journal of Cell Science

Abstract

Integrins are a large family of cell surface receptors that mediate cell adhesion and influence migration, signal transduction, and gene expression. The cytoplasmic domains of integrins play a pivotal role in these integrin-mediated cellular functions. Through interaction with the cytoskeleton, signaling molecules, and other cellular proteins, integrin cytoplasmic domains transduce signals from both the outside and inside of the cell and regulate integrin-mediated biological functions. Identification and functional analyses of integrin cytoplasmic domain-binding proteins have been pursued intensively. In recent years, more cellular proteins have been reported to directly interact with integrin cytoplasmic domains and some of these interactions may play important roles in integrin-mediated biological responses. Integrin β chains, for example, interact with actin-binding proteins (e.g. talin and filamin), which form mechanical links to the cytoskeleton. These and other proteins (e.g. FAK, ILK and novel proteins such as TAP20) might also link integrins to signaling mechanisms and, in some cases (e.g. JAB1) mediate integrin-dependent gene regulation.

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Metadata

Authors
Liu, S., Calderwood, D. A., & Ginsberg, M. H.
Venue
Journal of Cell Science
Published
2000-10-15
Volume
113
Issue
20
Pages
3563-3571
ISSN
  • 0021-9533 (ISSN-L)
  • 1477-9137
OpenAlex
W2164330595
Cited by
572
References
84
FWCI
15.60
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Integrin cytoplasmic domain-binding proteins. https://app.cochat.ai/papers/10.1242/jcs.113.20.3563
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Liu, S., Calderwood, D. A., & Ginsberg, M. H. (2000). Integrin cytoplasmic domain-binding proteins. Journal of Cell Science. https://doi.org/10.1242/jcs.113.20.3563

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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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