The DOI matches its Crossref record.
Focal contacts: Transmembrane links between the extracellular matrix and the cytoskeleton
Abstract
The sites of tightest adhesion that form between cells and substrate surfaces in tissue culture are termed focal contacts. The external faces of focal contacts include specific receptors, belonging to the integrin family of proteins, for fibronectin and vitronectin, two common components of extracellular matrices. On the internal (cytoplasmic) side of focal contacts, several proteins, including talin and vinculin, mediate interactions with the actin filament bundles of the cytoskeleton. The changes that occur in focal contacts as a result of viral transformation are discussed.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cited by
Mediation of biomaterial-cell interactions by adsorbed proteins: a review
Wilson, C. J., Clegg, R. E., Leavesley, D. I., & Pearcy, M. J. (2005) · Tissue Engineering · doi:10.1089/ten.2005.11.1 · Cited by 1,696
Cancer-associated fibroblasts promote directional cancer cell migration by aligning fibronectin
Erdogan, B., Ao, M., White, L. M., Means, A. L., Brewer, B. M., Yang, L., Washington, M. K., Shi, C., Franco, O. E., Weaver, A. M., et al. (2017) · Journal of Cell Biology · doi:10.1083/jcb.201704053 · Cited by 552
Cheng, C. Y., & Mruk, D. D. (2002) · Physiological Reviews · doi:10.1152/physrev.00009.2002 · Cited by 567
Verrier, S., Blaker, J. J., Maquet, V., Hench, L. L., & Boccaccini, A. R. (2004) · Biomaterials · doi:10.1016/j.biomaterials.2003.09.081 · Cited by 304
Regulation of focal adhesion dynamics and disassembly by phosphorylation of FAK at tyrosine 397
Hamadi, A., Bouali, M., Dontenwill, M., Stoeckel, H., Takeda, K., & Rondé, P. (2005) · Journal of Cell Science · doi:10.1242/jcs.02565 · Cited by 257
Metadata
- Authors
- Burridge, K., & Fath, K.
- Venue
- BioEssays
- Publisher
- Wiley
- Published
- 1989-04
- Volume
- 10
- Issue
- 4
- Pages
- 104-108
- ISSN
- 0265-9247 (ISSN-L)
- 1521-1878
- OpenAlex
- W1992138200
- Cited by
- 189
- References
- 0
- FWCI
- 0.98
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Focal contacts: Transmembrane links between the extracellular matrix and the cytoskeleton. https://app.cochat.ai/papers/10.1002/bies.950100403
- The paper
- Burridge, K., & Fath, K. (1989). Focal contacts: Transmembrane links between the extracellular matrix and the cytoskeleton. BioEssays. https://doi.org/10.1002/bies.950100403
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
