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Tissue inhibitors of metalloproteinases: evolution, structure and function
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Cites
Mechanism of inhibition of the human matrix metalloproteinase stromelysin-1 by TIMP-1.
Gomis-R¨th, F.-X., Maskos, K., Betz, M., Bergner, A., Huber, R., Suzuki, K., Yoshida, N., Nagase, H., Brew, K., Bourenkov, G. P., et al. (1997) · Nature · doi:10.1038/37995 · Cited by 619
Self-citationBaker, A. H., George, S. J., Zaltsman, A. B., Murphy, G., & Newby, A. C. (1999) · British Journal of Cancer · doi:10.1038/sj.bjc.6690217 · Cited by 286
Cited by
Visse, R., & Nagase, H. (2003) · Circulation Research · doi:10.1161/01.res.0000070112.80711.3d · Cited by 4,575
Self-citationStrategies 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
Molecular mechanisms of blood vessel growth
Conway, E. (2001) · Cardiovascular Research · doi:10.1016/s0008-6363(00)00281-9 · Cited by 1,030
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
The integrin αvβ8 mediates epithelial homeostasis through MT1-MMP–dependent activation of TGF-β1
Mu, D., Cambier, S., Fjellbirkeland, L., Baron, J. L., Munger, J. S., Kawakatsu, H., Sheppard, D., Broaddus, V. C., & Nishimura, S. L. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200109100 · Cited by 729
Oh, J., Takahashi, R., Kondo, S., Mizoguchi, A., Adachi, E., Sasahara, R. M., Nishimura, S., Imamura, Y., Kitayama, H., Alexander, D. B., et al. (2001) · Cell · doi:10.1016/s0092-8674(01)00597-9 · Cited by 728
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
Fisher, G. J., Quan, T., Purohit, T., Shao, Y., Cho, M. K., He, T., Varani, J., Kang, S., & Voorhees, J. J. (2009) · The American Journal of Pathology · doi:10.2353/ajpath.2009.080599 · Cited by 487
Novel 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
Matrix metalloproteinases in brain development and remodeling: Synaptic functions and targets
Ethell, I. M., & Ethell, D. W. (2007) · Journal of Neuroscience Research · doi:10.1002/jnr.21273 · Cited by 378
Increased plasma levels of matrix metalloproteinase-9 in patients with Alzheimer’s disease.
Lorenzl, S. (2003) · Neurochemistry International · doi:10.1016/s0197-0186(03)00004-4 · Cited by 243
The ECM path of senescence in aging: components and modifiers
Levi, N., Papismadov, N., Solomonov, I., Sagi, I., & Krizhanovsky, V. (2020) · The FEBS Journal · doi:10.1111/febs.15282 · Cited by 219
Muir, E. M., Adcock, K. H., Morgenstern, D. A., Clayton, R., von Stillfried, N., Rhodes, K., Ellis, C., Fawcett, J. W., & Rogers, J. H. (2002) · Molecular Brain Research · doi:10.1016/s0169-328x(02)00132-8 · Cited by 206
Gardner, J., & Ghorpade, A. (2003) · Journal of Neuroscience Research · doi:10.1002/jnr.10835 · Cited by 199
Extracellular matrix alterations in hypertensive vascular remodeling
Lemarié, C. A., Tharaux, P.-L., & Lehoux, S. (2010) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2009.09.018 · Cited by 192
Endogenous inhibitors of angiogenesis
Ribatti, D. (2009) · Leukemia Research · doi:10.1016/j.leukres.2008.11.019 · Cited by 191
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
Palosaari, H., Pennington, C. J., Larmas, M., Edwards, D. R., Tjäderhane, L., & Salo, T. (2003) · European Journal Of Oral Sciences · doi:10.1034/j.1600-0722.2003.00026.x · Cited by 188
Mannello, F., & Gazzanelli, G. (2001) · Apoptosis · doi:10.1023/a:1012493808790 · Cited by 185
Mesenchymal stem cells inhibit both endogenous and exogenous MMPs via secreted TIMPs
Lozito, T. P., & Tuan, R. S. (2011) · Journal of Cellular Physiology · doi:10.1002/jcp.22344 · Cited by 171
“Social Life” of Senescent Cells: What Is SASP and Why Study It?
Borodkina, A. V., Deryabin, P. I., Giukova, А. А., & Nikolsky, N. N. (2018) · Acta Naturae · doi:10.32607/20758251-2018-10-1-4-14 · Cited by 170
Molecular and cellular basis of rheumatoid joint destruction
Karouzakis, E., Neidhart, M., Gay, R. E., & Gay, S. (2006) · Immunology Letters · doi:10.1016/j.imlet.2006.04.011 · Cited by 167
Bär, C., de Jesus, B. B., Serrano, R., Tejera, A., Ayuso, E., Jimenez, V., Formentini, I., Bobadilla, M., Mizrahi, J., de Martino, A., et al. (2014) · Nature Communications · doi:10.1038/ncomms6863 · Cited by 162
Matrix metalloproteinases and cellular fibrinolytic activity
Lijnen, H. R. (2002) · Biochemistry (Moscow) · doi:10.1023/a:1013908332232 · Cited by 167
Cardiac remodeling and failure
Fedak, P. W. M., Verma, S., Weisel, R. D., & Li, R.-K. (2005) · Cardiovascular Pathology · doi:10.1016/j.carpath.2005.01.005 · Cited by 120
Byun, H.-O., Lee, Y.-K., Kim, J.-M., & Yoon, G. (2015) · BMB Reports · doi:10.5483/bmbrep.2015.48.10.122 · Cited by 115
Llano, E., Pendás, A. M., Aza-Blanc, P., Kornberg, T. B., & López-Otı́n, C. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m006045200 · Cited by 104
RetractedLlano, E., Adam, G., Pendás, A. M., Quesada, V., Sánchez, L. M., Santamarı́a, I., Noselli, S., & López-Otı́n, C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m200121200 · Cited by 100
Matrix Metalloproteinases as New Targets in Alzheimer’s Disease: Opportunities and Challenges
Zipfel, P., Rochais, C., Baranger, K., Rivera, S., & Dallemagne, P. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00352 · Cited by 94
Lindbohm, J. V., Mars, N., Walker, K. A., Singh‐Manoux, A., Livingston, G., Brunner, E. J., Sipilä, P. N., Saksela, K., Ferrie, J. E., Lovering, R. C., et al. (2022) · Alzheimer's & Dementia · doi:10.1002/alz.12419 · Cited by 70
Kato, T., Okahashi, N., Kawai, S., Kato, T., Inaba, H., Morisaki, I., & Amano, A. (2005) · Journal of Periodontology · doi:10.1902/jop.2005.76.6.941 · Cited by 65
Selvais, C., Gaide Chevronnay, H. P., Lemoine, P., Dedieu, S., Henriet, P., Courtoy, P. J., Marbaix, E., & Emonard, H. (2009) · Endocrinology · doi:10.1210/en.2009-0015 · Cited by 54
Eifan, A. O., Orban, N. T., Jacobson, M. R., & Durham, S. R. (2015) · American Journal of Respiratory and Critical Care Medicine · doi:10.1164/rccm.201502-0339oc · Cited by 49
Ehnert, S., Aspera-Werz, R. H., Ihle, C., Trost, M., Zirn, B., Flesch, I., Schröter, S., Relja, B., & Nussler, A. K. (2019) · Journal of Clinical Medicine · doi:10.3390/jcm8030406 · Cited by 45
“Furthermore, we found a smoking-dependent imbalance in TIMP-1 and TIMP-2 serum levels, which may affect matrix resorption via matrix metalloproteinases (MMPs) [49].”
BackgroundPatruno, A., Pesce, M., Marrone, A., Speranza, L., Grilli, A., De Lutiis, M. A., Felaco, M., & Reale, M. (2012) · Journal of Cellular Physiology · doi:10.1002/jcp.23024 · Cited by 42
Hernández‐Guillamon, M., Delgado, P., Ortega, L., Pares, M., Rosell, A., García‐Bonilla, L., Fernández‐Cadenas, I., Borrell‐Pagès, M., Boada, M., & Montaner, J. (2009) · Journal of Neuroscience Research · doi:10.1002/jnr.22034 · Cited by 39
Could statins constitute a novel treatment for endometriosis? Systematic review of the literature
Gibran, L., Maranhão, R. C., Abrão, M. S., Baracat, E. C., & Podgaec, S. (2014) · European Journal of Obstetrics & Gynecology and Reproductive Biology · doi:10.1016/j.ejogrb.2014.05.028 · Cited by 29
A microarray study to characterize the molecular mechanism of TIMP-3-mediated tumor rejection
Lam, P., Sian Lim, K., Mei Wang, S., & Hui, K. M. (2005) · Molecular Therapy · doi:10.1016/j.ymthe.2005.02.028 · Cited by 22
Preventing obesity, insulin resistance and type 2 diabetes by targeting MT1-MMP
Asthana, P., & Wong, H. L. X. (2024) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2024.167081 · Cited by 13
Metadata
- Authors
- Brew, K., Dinakarpandian, D., & Nagase, H.
- Venue
- Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Publisher
- Elsevier BV
- Published
- 2000-03
- Volume
- 1477
- Issue
- 1-2
- Pages
- 267-283
- ISSN
- 0167-4838 (ISSN-L)
- OpenAlex
- W1491678226
- Cited by
- 1,908
- References
- 2
- FWCI
- 39.48
- Type
- journal article
- Language
- en
- Open access
- closed
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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.