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The cysteine switch: a principle of regulation of metalloproteinase activity with potential applicability to the entire matrix metalloproteinase gene family.
Open accessAbstract
The general applicability of the "cysteine-switch" activation mechanism to the members of the matrix metalloproteinase (MMP) gene family is examined here. All currently known members of the MMP gene family share the characteristic that they are synthesized in a latent, inactive, form. Recent evidence suggests that this latency in human fibroblast collagenase (HFC) is the result of formation of an intramolecular complex between the single cysteine residue in its propeptide domain and the essential zinc atom in the catalytic domain, a complex that blocks the active site. Latent HFC can be activated by multiple means, all of which effect the dissociation of the cysteine residue from the complex. This is referred to as the "cysteine-switch" mechanism of activation. The propeptide domain that contains the critical cysteine residue and the catalytic domain that contains the zinc-binding site are the only two domains common to all of the MMPs. The amino acid sequences surrounding both the critical cysteine residue and a region of the protein chains containing two of the putative histidine zinc-binding ligands are highly conserved in all of the MMPs. A survey of the literature shows that many of the individual MMPs can be activated by the multiple means observed for latent HFC. These observations support the view that the cysteine-switch mechanism is applicable to all members of this gene family. This mechanism is unprecedented in enzymology as far as we know and offers the opportunity for multiple modes of physiological activation of these important enzymes. Since conditions in different cells and tissues may match those necessary to effect one of these activation modes for a given MMP, this may offer metabolic flexibility in the control of MMP activation.
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“The ADAM (A Disintegrin And Metalloprotease) and ADAMTS families of metalloproteases are encoded by over 40 human genes, mediate cell-cell and cell-matrix interactions (20, 21) and are involved in a range of human diseases, including cancer metastasis, inflammatory disorders, neurological diseases and asthma (21, 22).”
From Accurate prediction of protein structures and interactions using a 3-track network (2021) · cites this paper as [21]
Citations
Cites
Electrochemical Photolysis of Water at a Semiconductor Electrode
FUJISHIMA, A., & HONDA, K. (1972) · Nature · doi:10.1038/238037a0 · Cited by 34,169
Wilhelm, S. M., Collier, I. E., Marmer, B. L., Eisen, A. Z., Grant, G. A., & Goldberg, G. I. (1989) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)71480-4 · Cited by 1,109
Collier, I. E., Wilhelm, S. M., Eisen, A. Z., Marmer, B. L., Grant, G. A., Seltzer, J. L., Kronberger, A., He, C. S., Bauer, E. A., & Goldberg, G. I. (1988) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)68680-6 · Cited by 1,044
Springman, E. B., Angleton, E. L., Birkedal‐Hansen, H., & Wart, H. E. V. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.1.364 · Cited by 713
Self-citationEndogenous Activation of Latent Collagenase by Rheumatoid Synovial Cells
Werb, Z., Mainardi, C. L., Vater, C. A., & Harris, E. D. (1977) · New England Journal of Medicine · doi:10.1056/nejm197705052961801 · Cited by 685
Goldberg, G. I., Wilhelm, S. M., Kronberger, A., Bauer, E. A., Grant, G. A., & Eisen, A. Z. (1986) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)84605-7 · Cited by 632
Oxidative Autoactivation of Latent Collagenase by Human Neutrophils
Weiss, S. J., Peppin, G. J., Ortiz, X., Ragsdale, C. G., & Test, S. T. (1985) · Science · doi:10.1126/science.2982211 · Cited by 472
A unique signature identifies a family of zinc‐dependent metallopeptidases
Jongeneel, C. V., Bouvier, J., & Bairoch, A. (1989) · FEBS Letters · doi:10.1016/0014-5793(89)80471-5 · Cited by 462
Comparison of human stromelysin and collagenase by cloning and sequence analysis
Whitham, S. E., Murphy, G., Angel, P. E., Rahmsdorf, H. J., Smith, B. J., Lyons, A., Harris, T. J. R., Reynolds, J. J., Herrlich, P. A., & Docherty, A. (1986) · Biochemical Journal · doi:10.1042/bj2400913 · Cited by 436
Active-site zinc ligands and activated H2O of zinc enzymes.
Vallée, B. L., & Auld, D. S. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.1.220 · Cited by 434
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Items 601–700 of 1,001
Winberg, J., Berg, E., Kolset, S. O., & Uhlin‐Hansen, L. (2003) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2003.03788.x · Cited by 51
Raulo, S. M., Sorsa, T. A., Tervahartiala, T. I., Latvanen, T., Pirilä, E., Hirvonen, J., & Maisi, P. (2002) · Veterinary Immunology and Immunopathology · doi:10.1016/s0165-2427(01)00423-8 · Cited by 51
Angiogenesis in Multiple Myeloma
Vacca, A., Ria, R., Reale, A., & Ribatti, D. (2013) · Chemical immunology/Fortschritte der Allergielehre/Progress in allergy/Chemical immunology and allergy · doi:10.1159/000353312 · Cited by 50
Gargiulo, S., Sottero, B., Gamba, P., Chiarpotto, E., Poli, G., & Leonarduzzi, G. (2011) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2011.05.030 · Cited by 50
Cummings, I., George, S. J., Kelm, J., Schmidt, D., Emmert, M. Y., Weber, B., Zünd, G., & Hoerstrup, S. P. (2011) · European Journal of Cardio-Thoracic Surgery · doi:10.1016/j.ejcts.2011.02.077 · Cited by 50
Inhibitory Antibodies Designed for Matrix Metalloproteinase Modulation
Fischer, T., & Riedl, R. (2019) · Molecules · doi:10.3390/molecules24122265 · Cited by 50
Bahia, M. S., & Silakari, O. (2010) · Chemical Biology & Drug Design · doi:10.1111/j.1747-0285.2010.00950.x · Cited by 50
Matrix Metalloproteinase-1 Produced by Human CXCL12-Stimulated Natural Killer Cells
Goda, S., Inoue, H., Umehara, H., Miyaji, M., Nagano, Y., Harakawa, N., Imai, H., Lee, P., MaCarthy, J. B., Ikeo, T., et al. (2006) · American Journal Of Pathology · doi:10.2353/ajpath.2006.050676 · Cited by 50
Kołaczkowska, E., Arnold, B., & Opdenakker, G. (2007) · Immunobiology · doi:10.1016/j.imbio.2007.07.005 · Cited by 50
Ullah, R., & Lee, E. J. (2023) · Experimental Neurobiology · doi:10.5607/en23014 · Cited by 51
Activity-controlled proteolytic cleavage at the synapse
Sonderegger, P., & Matsumoto, K. (2014) · Trends in Neurosciences · doi:10.1016/j.tins.2014.05.007 · Cited by 50
Electrophilic Fatty Acids Regulate Matrix Metalloproteinase Activity and Expression
Bonacci, G., Schopfer, F. J., Batthyány, C., Rudolph, T. K., Rudolph, V., Khoo, N. K. H., Kelley, E. E., & Freeman, B. Α. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.225029 · Cited by 51
Shirian, J., Arkadash, V., Cohen, I., Sapir, T., Radisky, E. S., Papo, N., & Shifman, J. M. (2018) · FEBS Letters · doi:10.1002/1873-3468.13016 · Cited by 49
Freise, C., Erben, U., Muche, M., Farndale, R. W., Zeitz, M., Somasundaram, R., & Ruehl, M. (2009) · Matrix Biology · doi:10.1016/j.matbio.2009.08.001 · Cited by 51
O’Farrell, T. J., & Pourmotabbed, T. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m003936200 · Cited by 49
Magnoni, S., Baker, A. H., George, S. J., Duncan, W. C., Kerr, L. E., McCulloch, J., & Horsburgh, K. J. (2004) · Neurobiology of Disease · doi:10.1016/j.nbd.2004.07.020 · Cited by 49
Sang, Q. A., Bodden, M., & Windsor, L. J. (1996) · Journal of Protein Chemistry · doi:10.1007/bf01887112 · Cited by 49
Cellular Biology of Cartilage Degradation
Poole, A. R., Alini, M., & Hollander, A. P. (1995) · Elsevier eBooks · doi:10.1016/b978-012340440-4/50041-6 · Cited by 49
Matrix Metalloproteases Role in Bowel Inflammation and Inflammatory Bowel Disease
O’Shea, N. R., & Smith, A. M. (2014) · Inflammatory Bowel Diseases · doi:10.1097/mib.0000000000000163 · Cited by 48
Isolation and cloning of a metalloproteinase from king cobra snake venom
Guo, X.-X., Zeng, L., Lee, W.-H., Zhang, Y., & Jin, Y. (2007) · Toxicon · doi:10.1016/j.toxicon.2007.01.003 · Cited by 48
Identification of Pro-MMP-7 as a Serum Marker for Renal Cell Carcinoma by Use of Proteomic Analysis
Sarkissian, G., Fergelot, P., Lamy, P., Patard, J., Culine, S., Jouin, P., Rioux-Leclercq, N. C., & Darbouret, B. (2008) · Clinical Chemistry · doi:10.1373/clinchem.2007.090837 · Cited by 48
O’Farrell, T. J., & Pourmotabbed, T. (1998) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.1998.0662 · Cited by 48
Saarinen, J., Welgus, H. G., Flizar, C. A., Kalkkinen, N., & Helin, J. (1999) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.1999.00105.x · Cited by 48
Farkas, E., Katz, Y., Bhusare, S. R., Reich, R., Röschenthaler, G., Königsmann, M., & Breuer, E. (2004) · JBIC Journal of Biological Inorganic Chemistry · doi:10.1007/s00775-004-0524-5 · Cited by 48
Suzuki, H., Akakura, K., Komiya, A., Aida, S., Akimoto, S., & Shimazaki, J. (1996) · The Prostate · doi:10.1002/1097-0045(199609)29:3 · Cited by 209
A Cysteine Protease from Maize Isolated in a Complex with Cystatin
Yamada, T., Ohta, H., Shinohara, A., Iwamatsu, A., Shimada, H., Tsuchiya, T., Masuda, T., & Takamiya, K. (2000) · Plant and Cell Physiology · doi:10.1093/pcp/41.2.185 · Cited by 47
The Metalloprotease ofListeria monocytogenesIs Activated by Intramolecular Autocatalysis
Bitar, A. P., Cao, M., & Marquis, H. (2007) · Journal of Bacteriology · doi:10.1128/jb.00852-07 · Cited by 47
Chen, E. I., Li, W., Godzik, A., Howard, E. W., & Smith, J. W. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210324200 · Cited by 47
Matrix Metalloproteinase 2: Involvement in Keratoconus
Smith, V. A., & Easty, D. L. (2000) · European Journal of Ophthalmology · doi:10.1177/112067210001000305 · Cited by 47
Cell-specific Alterations in Expression of Hyperoxia-induced mRNAs of Lung
Veness‐Meehan, K. A., Cheng, E. R. Y., Mercier, C. E., Blixt, S. L., Johnston, C. J., Watkins, R. H., & Horowitz, S. (1991) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/ajrcmb/5.6.516 · Cited by 47
Marchenko, N. D., Marchenko, G. N., & Strongin, A. Y. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m201197200 · Cited by 47
Fik, C. P., Konieczny, S., Pashley, D. H., Waschinski, C. J., Ladisch, R., Salz, U., Bock, T., & Tiller, J. C. (2014) · Macromolecular Bioscience · doi:10.1002/mabi.201400220 · Cited by 46
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Tonti, G. A., Mannello, F., Cacci, E., & Biagioni, S. (2009) · The International Journal of Developmental Biology · doi:10.1387/ijdb.082573gt · Cited by 47
ADAM Proteins- Therapeutic Potential in Cancer
Lu, X., Lu, D., Scully, M. F., & Kakkar, V. V. (2008) · Current Cancer Drug Targets · doi:10.2174/156800908786733478 · Cited by 46
Li, Y., Deng, Y., Zhou, X., & Hu, J. (2017) · Talanta · doi:10.1016/j.talanta.2017.11.057 · Cited by 46
Procyanidins attenuate neuropathic pain by suppressing matrix metalloproteinase-9/2
Pan, C., Wang, C., Zhang, L., Song, L., Chen, Y., Liu, B., Liu, W., Hu, L., & Pan, Y. (2018) · Journal of Neuroinflammation · doi:10.1186/s12974-018-1182-9 · Cited by 46
Antioxidant effect of doxycycline decreases MMP activity and blood pressure in SHR
Antonio, R. C., Ceron, C. S., Rizzi, É., Coelho, E. B., Tanus-Santos, J. E., & Gerlach, R. F. (2013) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-013-1848-7 · Cited by 46
Notni, J., Görls, H., & Anders, E. (2006) · European Journal of Inorganic Chemistry · doi:10.1002/ejic.200500947 · Cited by 46
Lun, H. M., Mak, C. H., & Ko, R. C. (2003) · Parasitology Research · doi:10.1007/s00436-002-0815-0 · Cited by 46
Batra, J., Soares, A. S., Mehner, C., & Radisky, E. S. (2013) · PLoS ONE · doi:10.1371/journal.pone.0075836 · Cited by 45
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Hypoxia-induced increase of endostatin in murine aorta and lung
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Ratnikov, B. I., Deryugina, E. I., & Strongin, A. Y. (2002) · Laboratory Investigation · doi:10.1097/01.lab.0000038555.67772.db · Cited by 45
Travaglino, E., Benatti, C., Malcovati, L., Porta, M. G. D., Gallì, A., Bonetti, E., Rosti, V., Cazzola, M., & Invernizzi, R. (2007) · European Journal Of Haematology · doi:10.1111/j.1600-0609.2007.01012.x · Cited by 45
Reconstructed 19 kDa Catalytic Domain of Gelatinase A Is an Active Proteinase
Ye, Q.-Z., Johnson, L. L., Yu, A. E., & HUPE, D. J. (1995) · Biochemistry · doi:10.1021/bi00014a026 · Cited by 45
Matrix metalloprotease 1a deficiency suppresses tumor growth and angiogenesis
Foley, C., Fanjul‐Fernández, M., Bohm, A., Nguyen, N. T. B., Agarwal, A., Austin, K., Κούκος, Γ., Covic, L., López-Otı́n, C., & Kuliopulos, A. (2013) · Oncogene · doi:10.1038/onc.2013.157 · Cited by 44
Hugenberg, V., Breyholz, H., Riemann, B., Hermann, S., Schober, O., Schäfers, M. A., Gangadharmath, U. B., Mocharla, V. P., Kolb, H. C., Walsh, J. C., et al. (2012) · Journal of Medicinal Chemistry · doi:10.1021/jm300199g · Cited by 44
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von Hoven, G., Rivas, A. J., Neukirch, C., Klein, S., Hamm, C., Qin, Q., Meyenburg, M., Füser, S., Säftig, P., Hellmann, N., et al. (2016) · Biochemical Journal · doi:10.1042/bcj20160062 · Cited by 44
Molecular mechanisms of fission in echinoderms: Transcriptome analysis
Dolmatov, I. Y., Afanasyev, S., & Boyko, A. V. (2018) · PLoS ONE · doi:10.1371/journal.pone.0195836 · Cited by 45
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Arolas, J. L., Goulas, T., Cuppari, A., & Gomis‐Rüth, F. X. (2018) · Chemical Reviews · doi:10.1021/acs.chemrev.8b00030 · Cited by 44
Hasebe, T., Hartman, R., Matsuda, H., & Shi, Y. (2006) · Cell and Tissue Research · doi:10.1007/s00441-005-0099-7 · Cited by 44
Housley, T. J., Baumann, A. P., Braun, I. D., Davis, G. E., Seperack, P. K., & Wilhelm, S. M. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)53634-6 · Cited by 44
Pustovrh, M. C., Jawerbaum, A., Sinner, D. I., Pesaresi, M., Baier, M., Micone, P., Gimeno, M. A. F., & Gonzalez, E. T. (2001) · Reproduction Fertility and Development · doi:10.1071/rd00078 · Cited by 44
McKie, N., Edwards, T., Dallas, D. J., Houghton, A., Stringer, B., Graham, R., Russell, R. G. G., & Croucher, P. I. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1996.5957 · Cited by 44
Unlocking the Potential of Collagenases: Structures, Functions, and Emerging Therapeutic Horizons
Wang, Z., Wang, K., Xu, L.-F., Su, C., Gong, J., Shi, J., Ma, X., Xie, N., & Qian, J.-Y. (2024) · BioDesign Research · doi:10.34133/bdr.0050 · Cited by 45
Sakamoto, K., Kim, M. J., Rhoades, E. R., Allavena, R., Ehrt, S., Wainwright, H., Russell, D. G., & Rohde, K. H. (2012) · Infection and Immunity · doi:10.1128/iai.00906-12 · Cited by 43
Matrix metalloproteinases: key regulators in the pathogenesis of chemotherapy-induced mucositis?
Al‐Dasooqi, N., Gibson, R. J., Bowen, J. M., & Keefe, D. M. K. (2009) · Cancer Chemotherapy and Pharmacology · doi:10.1007/s00280-009-0984-y · Cited by 43
Singh, M., & Tyagi, S. C. (2017) · International Journal of Ophthalmology · doi:10.18240/ijo.2017.08.20 · Cited by 43
Damjanovski, S., Puzianowska‐Kuźnicka, M., Ishizuya‐Oka, A., & Shi, Y. (2000) · The FASEB Journal · doi:10.1096/fasebj.14.3.503 · Cited by 43
Function of the stromal processing peptidase in the chloroplast import pathway
Richter, S., Zhong, R., & Lamppa, G. K. (2005) · Physiologia Plantarum · doi:10.1111/j.1399-3054.2005.00476.x · Cited by 43
Podbilewicz, B. (1996) · Molecular Biology of the Cell · doi:10.1091/mbc.7.12.1877 · Cited by 43
Patruno, 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
Collagenases and their inhibitors: a review
Wu, S., Zhou, X.-W., Jin, Z., & Cheng, H. (2023) · Collagen and Leather · doi:10.1186/s42825-023-00126-6 · Cited by 44
Remnant epitopes, autoimmunity and glycosylation
Opdenakker, G., Dillen, C., Fiten, P., Martens, E., Aelst, I. V., den Steen, P. E. V., Nelissen, I., Starckx, S., Descamps, F. J., Hu, J., et al. (2006) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2005.12.014 · Cited by 42
Membrane-type matrix metalloproteinases: key mediators of leukocyte function
Marco, M., Fortin, C. F., & Fülöp, T. (2013) · Journal of Leukocyte Biology · doi:10.1189/jlb.0612267 · Cited by 42
He, L., Russell, S. J., Wood, D. J., & Tronci, G. (2018) · Journal of Materials Chemistry B · doi:10.1039/c7tb03035e · Cited by 42
ADAMTS13: origins, applications, and prospects
Plautz, W. E., Raval, J. S., Dyer, M., Rollins‐Raval, M. A., Zuckerbraun, B. S., & Neal, M. D. (2018) · Transfusion · doi:10.1111/trf.14804 · Cited by 42
Plant extracellular matrix metalloproteinases
Flinn, B. S. (2008) · Functional Plant Biology · doi:10.1071/fp08182 · Cited by 42
Structural Basis for Potent Slow Binding Inhibition of Human Matrix Metalloproteinase-2 (MMP-2)
Rosenblum, G., Meroueh, S. O., Kleifeld, O., Brown, S., Singson, S. P., Fridman, R. A., Mobashery, S., & Sagi, I. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301139200 · Cited by 42
CHARACTERIZATION OF A NOVEL METALLOPROTEINASE IN DUVERNOY'S GLAND OF RHABDOPHIS TIGRINUS TIGRINUS
KOMORI, K., Konishi, M., MARUTA, Y., Toriba, M., Sakai, A., Matsuda, A., Hori, T., NAKATANI, M., Minamino, N., & Akizawa, T. (2006) · The Journal of Toxicological Sciences · doi:10.2131/jts.31.157 · Cited by 42
Identification of Prodomain Determinants Involved in ADAMTS-1 Biosynthesis
Longpré, J., & Leduc, R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313151200 · Cited by 42
Substrate Specificity and Activation Mechanisms of Collagenase from Human Rheumatoid Synovium
Konttinen, Y. T., Lindy, O., Suomalainen, K., Ritchlin, C. T., Saari, H. T., Vauhkonen, M., Lauhio, A., Santavirta, S. S., & Sorsa, T. A. (1991) · Matrix · doi:10.1016/s0934-8832(11)80194-0 · Cited by 42
Therapeutic potential of ADAM10 modulation in Alzheimer’s disease: a review of the current evidence
Khezri, M. R., Mohebalizadeh, M., & Ghasemnejad‐Berenji, M. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01072-w · Cited by 42
Ishimwe, E., Hodgson, J. J., Clem, R. J., & Passarelli, A. L. (2015) · Virology · doi:10.1016/j.virol.2015.01.027 · Cited by 41
Shetty, V., Spellman, D. S., & Neubert, T. A. (2007) · Journal of the American Society for Mass Spectrometry · doi:10.1016/j.jasms.2007.05.013 · Cited by 43
Modulation of Redox Balance Leaves Murine Diabetogenic TH1 T Cells “LAG-3-ing” Behind
Delmastro-Greenwood, M. M., Styche, A. J., Trucco, M., Workman, C. J., Vignali, D. A. A., & Piganelli, J. D. (2012) · Diabetes · doi:10.2337/db11-1591 · Cited by 41
Matrix metalloproteinases outside vertebrates
Marino‐Puertas, L., Goulas, T., & Gomis‐Rüth, F. X. (2017) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2017.04.003 · Cited by 41
Sphingolipids and Redox Signaling in Renal Regulation and Chronic Kidney Diseases
Bhat, O. M., Yuan, X., Li, G., Lee, R., & Li, P. (2017) · Antioxidants and Redox Signaling · doi:10.1089/ars.2017.7129 · Cited by 41
Birkedal‐Hansen, H., Yamada, S. S., Windsor, L. J., Pollard, A. H., Lyons, J. G., Stetler‐Stevenson, W. G., & BIRKEDAL‐HANSEN, B. (2008) · Current Protocols in Cell Biology · doi:10.1002/0471143030.cb1008s40 · Cited by 41
Self-citationWatanabe, Wang, Hirose, Kivilioto, Osada, Miwa, Oide, Kitamura, Yoneta, Seto, et al. (1998) · Alimentary Pharmacology & Therapeutics · doi:10.1046/j.1365-2036.1998.00408.x · Cited by 41
Matrix Metalloproteinases in the Progression of Heart Failure
Li, Y. Y., & Feldman, A. M. (2001) · Drugs · doi:10.2165/00003495-200161090-00002 · Cited by 41
The role of ADAM33 in the pathogenesis of asthma
Cakebread, J. A., Haitchi, H. M., Holloway, J. W., Powell, R. M., Keith, T. P., Davies, D. E., & Holgate, S. T. (2004) · Springer Seminars in Immunopathology · doi:10.1007/s00281-003-0153-z · Cited by 41
Ranst, M. A. V., Norga, K., Masure, S., Proost, P., Vandekerckhove, F., Auwerx, J. H., Damme, J. V., & Opdenakker, G. (1991) · Cytokine · doi:10.1016/1043-4666(91)90021-5 · Cited by 41
Aimes, R. T., French, D. L., & Quigley, J. P. (1994) · Biochemical Journal · doi:10.1042/bj3000729 · Cited by 41
Overview of MMP Biology and Gene Associations in Human Diseases
Djurić, T., & Živković, M. (2017) · InTech eBooks · doi:10.5772/intechopen.70265 · Cited by 40
Li, C., Zeng, X., Yu, H., Gu, Y., & Zhang, W. (2018) · World Journal of Surgical Oncology · doi:10.1186/s12957-018-1519-y · Cited by 40
Fu, R., Klinngam, W., Heur, M., Edman, M. C., & Hamm‐Alvarez, S. F. (2019) · Eye & Contact Lens Science & Clinical Practice · doi:10.1097/icl.0000000000000641 · Cited by 41
The Versatile Role of Matrix Metalloproteinase for the Diverse Results of Fibrosis Treatment
Chuang, H.-M., Chen, Y.-S., & Harn, H. (2019) · Molecules · doi:10.3390/molecules24224188 · Cited by 41
Fu, L., Tomita, A., Wang, H., Buchholz, D. R., & Shi, Y. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m603041200 · Cited by 40
Wang, Y., Shen, Y., Li, K., Zhang, P., Wang, G., Gao, L., & Bai, C. (2009) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2009.04.006 · Cited by 40
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Metadata
- Authors
- Van Wart, H. E., & Birkedal-Hansen, H.
- Affiliations
- Department of Chemistry, Florida State University, Tallahassee 32306-3015.
- Venue
- Proceedings of the National Academy of Sciences
- Publisher
- National Academy of Sciences
- Published
- 1990-07
- Volume
- 87
- Issue
- 14
- Pages
- 5578-5582
- ISSN
- 0027-8424 (ISSN-L)
- 1091-6490
- PMC
- PMC54368
- OpenAlex
- W2167709602
- Cited by
- 1,475
- References
- 51
- Citations by year
- 2026: 23 · 2025: 28 · 2024: 38 · 2023: 28 · 2022: 34 · 2021: 31 · 2020: 30 · 2019: 28 · 2018: 40 · 2017: 48 · 2016: 33 · 2015: 47 · 2014: 60 · 2013: 45 · 2012: 61
- FWCI
- 14.57
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Proceedings of the National Academy of Sciences (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health (5r01de006028-07, 5r01de009122-05, 5r01gm027939-15)
- National Institute of General Medical Sciences (GM-27939)
- National Institute of Dental and Craniofacial Research (DE06028, DE09122)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Peptidase Inhibition and Analysis
- Keywords
- matrix metalloproteinases, enzyme activation, latent collagenase, zinc binding site, conserved amino acid sequence
- MeSH terms
- Amino Acid Sequence, Animals, Microbial Collagenase, Cysteine, Multigene Family, Humans, Metalloendopeptidases, Molecular Sequence Data, Protein Binding, Rabbits, Sequence Homology, Nucleic Acid, Species Specificity, Zinc, Rats
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