The DOI matches its Crossref record; 52 of the 52 references it cites were found in a registry or an index.
Physiology of Fibronectin
Abstract
Fibronectin is a major protein of blood and tissues. It has been intensively studied because of its many interactions with cells and other macromolecules. Fibronectin is a principal component of the extracellular matrix, and its most important function seems to be in tissue remodelling during embryogenesis and wound healing. It may influence a number of other physiological processes, including phagocytosis. The concentration of plasma fibronectin and the distribution of tissue fibronectin are altered in disease states, although diseases specifically caused by quantitative or qualitative abnormalities of fibronectin have not been identified.
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
Cites
Binding of soluble form of fibroblast surface protein, fibronectin, to collagen
Engvall, E., & Ruoslahti, E. (1977) · International Journal of Cancer · doi:10.1002/ijc.2910200102 · Cited by 1,947
Fibronectins: multifunctional modular glycoproteins.
Hynes, R. O., & Yamada, K. M. (1982) · The Journal of cell biology · doi:10.1083/jcb.95.2.369 · Cited by 1,326
Clark, R. A. F., Lanigan, J. M., DellaPelle, P., Manseau, E., Dvorak, H. F., & Colvin, R. B. (1982) · Journal of Investigative Dermatology · doi:10.1111/1523-1747.ep12500075 · Cited by 695
Alteration of Cell-Surface Proteins by Viral Transformation and by Proteolysis
Hynes, R. O. (1973) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.70.11.3170 · Cited by 659
Cross-linking of cold-insoluble globulin by fibrin-stabilizing factor
Mosher, D. (1975) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)41110-1 · Cited by 566
Self-citationSinger, I. I. (1979) · Cell · doi:10.1016/0092-8674(79)90040-0 · Cited by 527
Vaheri, A., & Mosher, D. F. (1978) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/0304-419x(78)90002-1 · Cited by 508
Self-citationSerum spreading factor (vitronectin) is present at the cell surface and in tissues.
Hayman, E. G., Pierschbacher, M. D., Ohgren, Y., & Ruoslahti, E. (1983) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.80.13.4003 · Cited by 450
Pierschbacher, M. D., Hayman, E. G., & Ruoslahti, E. (1981) · Cell · doi:10.1016/0092-8674(81)90308-1 · Cited by 439
Relationships between fibronectin (LETS protein) and actin
Hynes, R. O., & Destree, A. T. (1978) · Cell · doi:10.1016/0092-8674(78)90272-6 · Cited by 427
Cited by
Humphries, M. J., Akiyama, S. K., Komoriya, A., Olden, K., & Yamada, K. M. (1986) · The Journal of cell biology · doi:10.1083/jcb.103.6.2637 · Cited by 438
Humphries, M. J., Komoriya, A., Akiyama, S. K., Olden, K., & Yamada, K. M. (1987) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)48327-5 · Cited by 347
Saliva-Bacterium Interactions in Oral Microbial Ecology
Scannapieco, F. A. (1994) · Critical Reviews in Oral Biology & Medicine · doi:10.1177/10454411940050030201 · Cited by 328
Proteomics characterisation of the L929 cell supernatant and its role in BMDM differentiation
Heap, R. E., Marín-Rubio, J. L., Peltier, J., Heunis, T., Dannoura, A., Moore, A., & Trost, M. (2021) · Life Science Alliance · doi:10.26508/lsa.202000957 · Cited by 80
Mcdonald, J. A. (1988) · The Molecular and Cellular Biology of Wound Repair · doi:10.1007/978-1-4615-1795-5_18 · Cited by 15
Metadata
- Authors
- Mosher, D. F.
- Venue
- Annual Review of Medicine
- Publisher
- Annual Reviews
- Published
- 1984-02
- Volume
- 35
- Issue
- 1
- Pages
- 561-575
- ISSN
- 0066-4219 (ISSN-L)
- 1545-326X
- OpenAlex
- W2170282446
- Cited by
- 316
- References
- 52
- FWCI
- 12.91
- 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: Physiology of Fibronectin. https://app.cochat.ai/papers/10.1146/annurev.me.35.020184.003021
- The paper
- Mosher, D. F. (1984). Physiology of Fibronectin. Annual Review of Medicine. https://doi.org/10.1146/annurev.me.35.020184.003021
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.