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Matrix metalloproteinase inhibitors as therapy for inflammatory and vascular diseases
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Citations
Cites
Coussens, L. M., & Werb, Z. (2002) · Nature · doi:10.1038/nature01322 · Cited by 15,111
New functions for the matrix metalloproteinases in cancer progression
Egeblad, M., & Werb, Z. (2002) · Nature Reviews Cancer · doi:10.1038/nrc745 · Cited by 6,108
The immunopathogenesis of sepsis
Cohen, J. (2002) · Nature · doi:10.1038/nature01326 · Cited by 2,742
Matrix metalloproteinases as modulators of inflammation and innate immunity
Parks, W. C., Wilson, C. L., & López-Boado, Y. S. (2004) · Nature Reviews Immunology · doi:10.1038/nri1418 · Cited by 1,929
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
Strategies for MMP inhibition in cancer: innovations for the post-trial era
Overall, C. M., & López-Otín, C. (2002) · Nature Reviews Cancer · doi:10.1038/nrc884 · Cited by 1,349
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Self-citationNovel functions of TIMPs in cell signaling
Chirco, R., Liu, X.-W., Jung, K.-K., & Kim, H.-R. C. (2006) · Cancer and Metastasis Reviews · doi:10.1007/s10555-006-7893-x · Cited by 401
Inhibition of autoimmune encephalomyelitis by a tetracycline
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Microglia emerge from erythromyeloid precursors via Pu.1- and Irf8-dependent pathways
Kierdorf, K., Erny, D., Goldmann, T., Sander, V., Schulz, C., Perdiguero, E. G., Wieghofer, P., Heinrich, A., Riemke, P., Hölscher, C., et al. (2013) · Nature Neuroscience · doi:10.1038/nn.3318 · Cited by 1,457
Self-citationBiochemical and Biological Attributes of Matrix Metalloproteinases
Cui, N., Hu, M., & Khalil, R. A. (2017) · Progress in Molecular Biology and Translational Science · doi:10.1016/bs.pmbts.2017.02.005 · Cited by 1,359
Matrix metalloproteinases and their multiple roles in neurodegenerative diseases
Rosenberg, G. A. (2009) · The Lancet Neurology · doi:10.1016/s1474-4422(09)70016-x · Cited by 594
Brkic, M., Balusu, S., Libert, C., & Vandenbroucke, R. E. (2015) · Mediators of Inflammation · doi:10.1155/2015/620581 · Cited by 205
Matrix metalloproteinase collagenolysis in health and disease
Amar, S., Smith, L., & Fields, G. B. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.04.015 · Cited by 194
Robert, S., Gicquel, T., Victoni, T., Valença, S., Barreto, E., Bailly-Maître, B., Boichot, E., & Lagente, V. (2016) · Bioscience Reports · doi:10.1042/bsr20160107 · Cited by 190
Luo, T., Nocon, A., Fry, J., Sherban, A., Rui, X., Jiang, B., Xu, X. J., Han, J., Yan, Y., Yang, Q., et al. (2016) · Diabetes · doi:10.2337/db15-1122 · Cited by 172
Verma, S., Kumar, M., Gurjav, U., Lum, S., & Nerurkar, V. R. (2010) · Virology · doi:10.1016/j.virol.2009.10.036 · Cited by 151
Popov, Y., Sverdlov, D. Y., Bhaskar, K. R., Sharma, A. K., Millonig, G., Patsenker, E., Krahenbuhl, S., Krahenbuhl, L., & Schuppan, D. (2010) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00394.2009 · Cited by 136
Gerwien, H., Hermann, S., Zhang, X., Korpos, E., Song, J., Kopka, K., Faust, A., Wenning, C., Gross, C. C., Honold, L., et al. (2016) · Science Translational Medicine · doi:10.1126/scitranslmed.aaf8020 · Cited by 113
Self-citationNew strategies for targeting matrix metalloproteinases.
Fields, G. B. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.01.002 · Cited by 98
Extracellular proteolysis in macrophage migration: Losing grip for a breakthrough
Vérollet, C., Charrière, G. M., Labrousse, A., Cougoule, C., Le Cabec, V., & Maridonneau‐Parini, I. (2011) · European Journal of Immunology · doi:10.1002/eji.201141538 · Cited by 91
Folgueras, A. R., Valdés-Sánchez, T., Llano, E., Menéndez, L., Baamonde, A., Denlinger, B. L., Belmonte, C., Juárez, L., Lastra, A., García-Suárez, O., et al. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0908507106 · Cited by 80
Py, N. A., Bonnet, A. E., Bernard, A., Marchalant, Y., Charrat, E., Checler, F., Khrestchatisky, M., Baranger, K., & Rivera, S. (2014) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2014.00247 · Cited by 76
Endogenous and synthetic MMP inhibitors in CNS physiopathology.
Baranger, K., Rivera, S., Liechti, F. D., Grandgirard, D., Bigas, J., Seco, J., Tarrago, T., Leib, S. L., & Khrestchatisky, M. (2014) · Progress in Brain Research · doi:10.1016/b978-0-444-63486-3.00014-1 · Cited by 52
Matrix metalloproteinase 9 opposes diet-induced muscle insulin resistance in mice
Kang, L., Mayes, W. H., James, F. D., Bracy, D. P., & Wasserman, D. H. (2014) · Diabetologia · doi:10.1007/s00125-013-3128-1 · Cited by 48
Metadata
- Authors
- Hu, J., Van den Steen, P. E., Sang, Q.-X. A., & Opdenakker, G.
- Venue
- Nature Reviews Drug Discovery
- Published
- 2007-06
- Volume
- 6
- Issue
- 6
- Pages
- 480-498
- ISSN
- 1474-1776 (ISSN-L)
- 1474-1784
- OpenAlex
- W2053043355
- Cited by
- 795
- References
- 11
- FWCI
- 2.56
- Type
- journal article
- Language
- en
- Open access
- closed
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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.