The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
The ADAMs family of metalloproteases: multidomain proteins with multiple functions
Open accessAbstract
The ADAMs family of transmembrane proteins belongs to the zinc protease superfamily. Members of the family have a modular design, characterized by the presence of metalloprotease and integrin receptor-binding activities, and a cytoplasmic domain that in many family members specifies binding sites for various signal transducing proteins. The ADAMs family has been implicated in the control of membrane fusion, cytokine and growth factor shedding, and cell migration, as well as processes such as muscle development, fertilization, and cell fate determination. Pathologies such as inflammation and cancer also involve ADAMs family members. Excellent reviews covering various facets of the ADAMs literature-base have been published over the years and we recommend their examination (Black and White 1998; Schlondorff and Blobel 1999; Primakoff and Myles 2000; Evans 2001; Kheradmand and Werb 2002). In this review, we will first discuss the properties of each of the domains of the ADAMs. We will then go on to describe the involvement of ADAMs in selected biological processes. Then, we will highlight recent interesting findings suggesting roles for ADAMs in human disease. Finally, we look to the future and discuss some of the open issues in ADAMs function and regulation.
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
A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cells
Black, R. A., Rauch, C. T., Kozlosky, C. J., Peschon, J. J., Slack, J. L., Wolfson, M. F., Castner, B. J., Stocking, K. L., Reddy, P., Srinivasan, S., et al. (1997) · Nature · doi:10.1038/385729a0 · Cited by 3,149
The Biology of Chemokines and their Receptors
Rossi, D., & Zlotnik, A. (2000) · Annual Review of Immunology · doi:10.1146/annurev.immunol.18.1.217 · Cited by 2,410
Van Wart, H. E., & Birkedal-Hansen, H. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.14.5578 · Cited by 1,475
Strain-Dependent Epithelial Defects in Mice Lacking the EGF Receptor
Sibilia, M., & Wagner, E. F. (1995) · Science · doi:10.1126/science.7618085 · Cited by 1,002
The Metalloprotease Disintegrin ADAM8
Schlomann, U., Wildeboer, D., Webster, A., Antropova, O., Zeuschner, D., Knight, C. G., Docherty, A. J. P., Lambert, M., Skelton, L., Jockusch, H., et al. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203355200 · Cited by 171
Cited by
EDWARDS, D., HANDSLEY, M., & PENNINGTON, C. (2008) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.08.001 · Cited by 1,161
PORTER, S., CLARK, I. M., KEVORKIAN, L., & EDWARDS, D. R. (2005) · Biochemical Journal · doi:10.1042/bj20040424 · Cited by 779
Metalloproteinases and their inhibitors: Regulators of wound healing
Gill, S. E., & Parks, W. C. (2008) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2007.10.024 · Cited by 742
Scofield, M. D., Heinsbroek, J. A., Gipson, C. D., Kupchik, Y. M., Spencer, S., Smith, A. C. W., Roberts-Wolfe, D., & Kalivas, P. W. (2016) · Pharmacological Reviews · doi:10.1124/pr.116.012484 · Cited by 598
Fox, J. W., & Serrano, S. M. T. (2005) · Toxicon · doi:10.1016/j.toxicon.2005.02.012 · Cited by 587
Metadata
- Authors
- Seals, D. F., & Courtneidge, S. A.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2003-01-01
- Volume
- 17
- Issue
- 1
- Pages
- 7-30
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2145837099
- Cited by
- 1,059
- References
- 5
- Type
- posted content
- Language
- en
- Open access
- diamond
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: The ADAMs family of metalloproteases: multidomain proteins with multiple functions. https://app.cochat.ai/papers/10.1101/gad.1039703
- The paper
- Seals, D. F., & Courtneidge, S. A. (2003). The ADAMs family of metalloproteases: multidomain proteins with multiple functions. Genes & Development. https://doi.org/10.1101/gad.1039703
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.
