The DOI matches its Crossref record; 1 of the 1 references it cites were found in a registry or an index.
The Gene Structure of Tissue Inhibitor of Metalloproteinases (TIMP)-3 and Its Inhibitory Activities Define the Distinct TIMP Gene Family
Open accessAbstract
Matrix metalloproteinases (MMPs) and tissue inhibitors of metalloproteinases (TIMPs) play a critical role in extracellular matrix homeostasis. We have previously cloned human and mouse TIMP-3 cDNAs and mapped their chromosomal loci (Apte, S. S., Mattei, M-G., and Olsen, B. R. (1994) Genomics 19, 86-90; Apte, S. S., Hayashi, K., Seldin, M. F., Mattei, M-G., Hayashi, M., and Olsen, B. R. (1994) Dev. Dynam. 200, 177-197); the identification of TIMP3 mutations in Sorsby's fundus dystrophy has underscored the functional importance of TIMP-3. We now report that TIMP-3 is encoded by five exons spanning over 30 kilobase pairs of mouse genomic DNA. In the attribution of protein domains to specific exons, as well as exon structures, the Timp-3 and Timp-1 genes are similar, confirming the common evolutionary origin of the TIMPs and defining a distinct gene family. We have expressed human and mouse TIMP-3 in mouse NSO myeloma cells. In each case, an N-glycosylated 27-kDa protein was generated, that, like TIMP-1 and TIMP-2, inhibited collagenase-1, stromelysin-1, and gelatinases A and B. TIMP-3 and TIMP-1 inhibition were quantitatively similar, implying that all TIMPs are equally efficient in MMP inhibition. Instead, differential regulation of the TIMP genes or divergent C-terminal protein sequences may underlie distinct biological functions for each TIMP.
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
Weber, B. H. F., Vogt, G., Pruett, R. C., Stöhr, H., & Felbor, U. (1994) · Nature Genetics · doi:10.1038/ng1294-352 · Cited by 656
Cited by
Fitzgerald, M. L., Wang, Z., Park, P. W., Murphy, G., & Bernfield, M. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.148.4.811 · Cited by 367
Self-citationTIMP-3 Binds to Sulfated Glycosaminoglycans of the Extracellular Matrix
Yu, W.-H., Yu, S.-S. C., Meng, Q., Brew, K., & Woessner, J. F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m000907200 · Cited by 328
Fernandez‐Catalan, C., Bode, W., Huber, R., Turk, D., Calvete, J. J., Lichte, A., Tschesche, H., & Maskos, K. (1998) · The EMBO Journal · doi:10.1093/emboj/17.17.5238 · Cited by 321
Advances in animal cell recombinant protein production: GS-NS0 expression system
Barnes, L. M., Bentley, C. M., & Dickson, A. J. (2000) · Cytotechnology · doi:10.1023/a:1008170710003 · Cited by 129
Drusen in patient-derived hiPSC-RPE models of macular dystrophies
Galloway, C. A., Dalvi, S., Hung, S. S. C., MacDonald, L. A., Latchney, L. R., Wong, R. C. B., Guymer, R. H., Mackey, D. A., Williams, D. S., Chung, M. M., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1710430114 · Cited by 123
Nandadasa, S., Kraft, C. M., Wang, L. W., O’Donnell, A., Patel, R., Gee, H. Y., Grobe, K., Cox, T. C., Hildebrandt, F., & Apte, S. S. (2019) · Nature Communications · doi:10.1038/s41467-019-08520-7 · Cited by 76
Self-citationSorsby fundus dystrophy—A review of pathology and disease mechanisms
Christensen, D. R. G., Brown, F. E., Cree, A. J., Ratnayaka, J. A., & Lotery, A. J. (2017) · Experimental Eye Research · doi:10.1016/j.exer.2017.08.014 · Cited by 60
Sorsby fundus dystrophy:Insights from the past and looking to the future
Anand‐Apte, B., Chao, J. R., Singh, R., & Stöhr, H. (2019) · Journal of Neuroscience Research · doi:10.1002/jnr.24317 · Cited by 45
The isolated N-terminal domains of TIMP-1 and TIMP-3 are insufficient for ADAM10 inhibition.
Rapti, M., Atkinson, S. J., Lee, M.-H., Trim, A., Moss, M., & Murphy, G. (2008) · Biochemical Journal · doi:10.1042/bj20071430 · Cited by 43
Self-citation
Metadata
- Authors
- Apte, S. S., Olsen, B. R., & Murphy, G.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1995-06
- Volume
- 270
- Issue
- 24
- Pages
- 14313-14318
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2071583399
- Cited by
- 295
- References
- 1
- FWCI
- 11.13
- Type
- journal article
- Language
- en
- Open access
- hybrid
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
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.
