A Disintegrin and Metalloproteinase (ADAM) and ADAM with thrombospondin motifs (ADAMTS) family in vascular biology and disease
Open accessAbstract
A Disintegrin and Metalloproteinase (ADAM) is a family of proteolytic enzymes that possess sheddase function and regulate shedding of membrane-bound proteins, growth factors, cytokines, ligands and receptors. Typically, ADAMs have a pro-domain, and a metalloproteinase, disintegrin, cysteine-rich and a characteristic transmembrane domain. Most ADAMs are activated by proprotein convertases, but can also be regulated by G-protein coupled receptor agonists, Ca 2+ ionophores and protein kinase C activators. A Disintegrin and Metalloproteinase with Thrombospondin Motifs (ADAMTS) is a family of secreted enzymes closely related to ADAMs. Like ADAMs, ADAMTS members have a pro-domain, and a metalloproteinase, disintegrin, and cysteine-rich domain, but they lack a transmembrane domain and instead have characteristic thrombospondin motifs. Activated ADAMs perform several functions and participate in multiple cardiovascular processes including vascular smooth muscle cell proliferation and migration, angiogenesis, vascular cell apoptosis, cell survival, tissue repair, and wound healing. ADAMs may also be involved in pathological conditions and cardiovascular diseases such as atherosclerosis, hypertension, aneurysm, coronary artery disease, myocardial infarction and heart failure. Like ADAMs, ADAMTS have a wide-spectrum role in vascular biology and cardiovascular pathophysiology. ADAMs and ADAMTS activity is naturally controlled by endogenous inhibitors such as tissue inhibitors of metalloproteinases (TIMPs), and their activity can also be suppressed by synthetic small molecule inhibitors. ADAMs and ADAMTS can serve as important diagnostic biomarkers and potential therapeutic targets for cardiovascular disorders. Natural and synthetic inhibitors of ADAMs and ADAMTS could be potential therapeutic tools for the management of cardiovascular diseases.
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
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.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Deficiencies in TANGO2 lead to metabolic disorders, and the protein plays an unknown role in Golgi membrane redistribution into the ER.
“Deficiencies in TANGO2 (transport and Golgi organization protein 2) lead to metabolic disorders, and the protein plays an unknown role in Golgi membrane redistribution into the ER (16, 17).”
From Accurate prediction of protein structures and interactions using a 3-track network (2021) · cites this paper as [17]
The ADAMTS Functions section discusses deficiencies and disorders involving ADAMTS proteins, not TANGO2. Searches for TANGO2 and for Golgi membrane redistribution into the ER found no passage in our copy addressing either part of the claim. (LLM, conf=0.77)
Experimental — accuracy not yet measured
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
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 · see citing works
Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-α
Moss, M. L., Jin, S.-L. C., Milla, M. E., Burkhart, W., Carter, H. L., Chen, W., Clay, W. C., Didsbury, J. R., Hassler, D. F., Hoffman, C. R., et al. (1997) · Nature · doi:10.1038/385733a0 · Cited by 1,611 · see citing works
An Essential Role for Ectodomain Shedding in Mammalian Development
Peschon, J. J., Slack, J. L., Reddy, P., Stocking, K. L., Sunnarborg, S. W., Lee, D. C., Russell, W. E., Castner, B. J., Johnson, R. S., Fitzner, J. N., et al. (1998) · Science · doi:10.1126/science.282.5392.1281 · Cited by 1,606 · see citing works
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 · see citing works
Biochemical 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 · cited 1× · see citing works
“Matrix metalloproteinases (MMPs) are major regulators of ECM protein degradation and tissue remodeling [3, 4].”
BackgroundSelf-citationEdwards, D. R., Handsley, M. M., & Pennington, C. (2008) · Molecular Aspects of Medicine · doi:10.1016/j.mam.2008.08.001 · Cited by 1,165 · see citing works
ADAMs: key components in EGFR signalling and development
Blobel, C. (2005) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1548 · Cited by 1,091 · see citing works
The ADAMs family of metalloproteases: multidomain proteins with multiple functionsPreprint
Seals, D. F., & Courtneidge, S. A. (2003) · Genes & Development · doi:10.1101/gad.1039703 · Cited by 1,058 · see citing works
Distinct roles for ADAM10 and ADAM17 in ectodomain shedding of six EGFR ligands
Şahin, U., Weskamp, G., Kelly, K., Zhou, H., Higashiyama, S., Peschon, J. J., Hartmann, D., Säftig, P., & Blobel, C. (2004) · The Journal of Cell Biology · doi:10.1083/jcb.200307137 · Cited by 979 · see citing works
Zheng, X. L., Chung, D. W., Τakayama, T. K., Majerus, E. M., Sadler, J. E., & Fujikawa, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c100515200 · Cited by 839 · see citing works
PORTER, S., CLARK, I. M., KEVORKIAN, L., & EDWARDS, D. R. (2005) · Biochemical Journal · doi:10.1042/bj20040424 · Cited by 779 · see citing works
Bode, W., Gomis‐Rüth, F. X., & Stöckler, W. (1993) · FEBS Letters · doi:10.1016/0014-5793(93)80312-i · Cited by 762 · see citing works
Matrix Metalloproteinases, Vascular Remodeling, and Vascular Disease
Wang, X. L., & Khalil, R. A. (2017) · Advances in pharmacology · doi:10.1016/bs.apha.2017.08.002 · Cited by 758 · see citing works
Self-citationMatrix metalloproteinases and their inhibitors in vascular remodeling and vascular disease
Raffetto, J. D., & Khalil, R. A. (2007) · Biochemical Pharmacology · doi:10.1016/j.bcp.2007.07.004 · Cited by 755 · see citing works
Self-citationAsakura, M., Kitakaze, M., Takashima, S., Liao, Y., Ishikura, F., Yoshinaka, T., Ohmoto, H., Node, K., Yoshino, K., Ishiguro, H., et al. (2002) · Nature Medicine · doi:10.1038/nm0102-35 · Cited by 724 · see citing works
Hartmann, D. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.21.2615 · Cited by 680 · see citing works
The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) family
Kelwick, R. J. R., Desanlis, I., Wheeler, G. N., & Edwards, D. R. (2015) · Genome biology · doi:10.1186/s13059-015-0676-3 · Cited by 654 · see citing works
Reilly, M. P., Li, M., He, J., Ferguson, J. F., Stylianou, I. M., Mehta, N. N., Burnett, M. S., Devaney, J. M., Knouff, C. W., Thompson, J. R., et al. (2011) · The Lancet · doi:10.1016/s0140-6736(10)61996-4 · Cited by 539 · see citing works
TIMP-3 Is a Potent Inhibitor of Aggrecanase 1 (ADAM-TS4) and Aggrecanase 2 (ADAM-TS5)
Kashiwagi, M., Tortorella, M. D., Nagase, H., & Brew, K. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.c000848200 · Cited by 509 · see citing works
Kuno, K., Kanada, N., Nakashima, E., Fujiki, F., Ichimura, F., & Matsushima, K. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.1.556 · Cited by 505 · see citing works
Functional Analysis of the Domain Structure of Tumor Necrosis Factor-α Converting Enzyme
Reddy, P., Slack, J. L., Davis, R., Cerretti, D. P., Kozlosky, C. J., Blanton, R. A., Shows, D. M., Peschon, J. J., & Black, R. A. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.19.14608 · Cited by 501 · see citing works
Disintegrins: A Family of Integrin Inhibitory Proteins from Viper Venoms
Gould, R. J., Polokoff, M. A., Friedman, P. A., Huang, T., Holt, J., Cook, J. J., & Niewiarowski, S. (1990) · Experimental Biology and Medicine · doi:10.3181/00379727-195-43129b · Cited by 492 · see citing works
Cloning and Characterization of ADAMTS11 , an Aggrecanase from the ADAMTS Family
Abbaszade, I. G., Liu, R., Yang, F., Rosenfeld, S. A., Ross, O. H., Link, J. R., Ellis, D. M., Tortorella, M. D., Pratta, M. A., Hollis, J. M., et al. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.33.23443 · Cited by 490 · see citing works
A metalloprotease-disintegrin participating in myoblast fusion
Yagami-Hiromasa, T., Sato, T., Kurisaki, T., Kamijo, K., Nabeshima, Y.-I., & Fujisawa‐Sehara, A. (1995) · Nature · doi:10.1038/377652a0 · Cited by 480 · see citing works
Tissue inhibitors of metalloproteinases
Murphy, G. (2011) · Genome biology · doi:10.1186/gb-2011-12-11-233 · Cited by 472 · see citing works
The ThrombospondinsPreprint
Adams, J. C., & Lawler, J. (2011) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a009712 · Cited by 468 · see citing works
Vázquez, F., Hastings, G. A., Ortega, M.-A., Lane, T. F., Oikemus, S., Lombardo, M., & Iruela‐Arispe, M. L. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.33.23349 · Cited by 426 · see citing works
Defective valvulogenesis in HB‐EGF and TACE‐null mice is associated with aberrant BMP signaling
Jackson, L. F., Qiu, T. H., Sunnarborg, S. W., Chang, A., Zhang, C., Patterson, C., & Lee, D. C. (2003) · The EMBO Journal · doi:10.1093/emboj/cdg264 · Cited by 417 · see citing works
Sun, M., Chen, M., Dawood, F., Zurawska, U., Li, J. Y., Parker, T., Kassiri, Z., Kirshenbaum, L. A., Arnold, M., Khokha, R., et al. (2007) · Circulation · doi:10.1161/circulationaha.106.643585 · Cited by 383 · see citing works
Anker, S. D., & Coats, A. J. S. (2002) · International Journal of Cardiology · doi:10.1016/s0167-5273(02)00470-9 · Cited by 367 · see citing works
The Disintegrin/Metalloproteinase ADAM10 Is Essential for the Establishment of the Brain Cortex
Jorissen, E., Prox, J., Bernreuther, C., Weber, S., Schwanbeck, R., Serneels, L., Snellinx, A., Craessaerts, K., Thathiah, A., Tesseur, I., et al. (2010) · The Journal of Neuroscience · doi:10.1523/jneurosci.5221-09.2010 · Cited by 363 · see citing works
Metalloprotease-Disintegrins: Links to Cell Adhesion and Cleavage of TNFα and Notch
Blobel, C. (1997) · Cell · doi:10.1016/s0092-8674(00)80519-x · Cited by 356 · see citing works
Ludwig, A., Hundhausen, C., Lambert, M. H., BROADWAY, N. M., Andrews, R. K., Bickett, D. M., Leesnitzer, M. A., & Becherer, J. D. (2005) · Combinatorial Chemistry & High Throughput Screening · doi:10.2174/1386207053258488 · Cited by 356 · see citing works
Lemjabbar, H., & Basbaum, C. B. (2002) · Nature Medicine · doi:10.1038/nm0102-41 · Cited by 355 · see citing works
ADAMs as mediators of EGF receptor transactivation by G protein-coupled receptors
Ohtsu, H., Dempsey, P. J., & Eguchi, S. (2006) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00620.2005 · Cited by 340 · see citing works
Somerville, R. P. T., Longpré, J., Jungers, K. A., Engle, J. M., Ross, M., Evanko, S. P., Wight, T. N., Leduc, R., & Apte, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211009200 · Cited by 324 · see citing works
Schulz, B., Pruessmeyer, J., Maretzky, T., Ludwig, A., Blobel, C., Säftig, P., & Reiß, K. (2008) · Circulation Research · doi:10.1161/circresaha.107.169805 · Cited by 301 · see citing works
ADAMTS proteins in human disorders
Mead, T. J., & Apte, S. (2018) · Matrix Biology · doi:10.1016/j.matbio.2018.06.002 · Cited by 281 · see citing works
Cal, S., Obaya, Á. J., Prada, M. L., Garabaya, C., Quesada, V., & López-Otı́n, C. (2002) · Gene · doi:10.1016/s0378-1119(01)00861-7 · Cited by 273 · see citing works
ADAMTS13 and von Willebrand Factor in Thrombotic Thrombocytopenic Purpura
Zheng, X. L. (2015) · Annual Review of Medicine · doi:10.1146/annurev-med-061813-013241 · Cited by 267 · see citing works
Iba, K., Albrechtsen, R., Gilpin, B., Fröhlich, C., Loechel, F., Żółkiewska, A., Ishiguro, K., Kojima, T., Liu, W., Langford, J. K., et al. (2000) · The Journal of Cell Biology · doi:10.1083/jcb.149.5.1143 · Cited by 247 · see citing works
Jeltsch, M., Jha, S. K., Tvorogov, D., Anisimov, A., Leppänen, V., Holopainen, T., Kivelä, R., Ortega, S., Kärpänen, T., & Alitalo, K. K. (2014) · Circulation · doi:10.1161/circulationaha.113.002779 · Cited by 243 · see citing works
Regulation of the α‐secretase ADAM10 by its prodomain and proprotein convertases
Anders, A., Gilbert, S., Garten, W., Postina, R., & Fahrenholz, F. (2001) · The FASEB Journal · doi:10.1096/fj.01-0007fje · Cited by 241 · see citing works
Soond, S. M., Everson, B., Riches, D. W. H., & Murphy, G. (2005) · Journal of Cell Science · doi:10.1242/jcs.02357 · Cited by 235 · see citing works
Rodrı́guez-Manzaneque, J. C., Westling, J., Thai, S. N.-M., Luque, A., Knäuper, V., Murphy, G., Sandy, J. D., & Iruela‐Arispe, M. L. (2002) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)00254-1 · Cited by 234 · see citing works
Procollagen II Amino Propeptide Processing by ADAMTS-3
Fernandes, R. J., Hirohata, S., Engle, J. M., Colige, A., Cohn, D. H., Eyre, D. R., & Apte, S. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m103466200 · Cited by 230 · see citing works
English, W., Puente, X. S., Freije, J. M. P., Knäuper, V., Amour, A., Merryweather, A., López-Otı́n, C., & Murphy, G. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.19.14046 · Cited by 229 · see citing works
Wang, L., Zheng, J., Bai, X., Liu, B., Liu, C.-J., Xu, Q., Zhu, Y., Wang, N., Kong, W., & Wang, X. (2009) · Circulation Research · doi:10.1161/circresaha.108.188425 · Cited by 220 · see citing works
Crystal structures of VAP1 reveal ADAMs' MDC domain architecture and its unique C‐shaped scaffold
Takeda, S., Igarashi, T., Mori, H., & Araki, S. (2006) · The EMBO Journal · doi:10.1038/sj.emboj.7601131 · Cited by 202 · cited 4× · see citing works
“The discovery of the C-shape scaffold, was a landmark study in deciphering the crystal structure of ADAMs and how they function [9].”
BackgroundInfluentialADAM-TS5, ADAM-TS6, and ADAM-TS7, Novel Members of a New Family of Zinc Metalloproteases
Hurskainen, T. L., Hirohata, S., Seldin, M. F., & Apte, S. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.36.25555 · Cited by 200 · see citing works
Rosendahl, M. S., Ko, S. C., Long, D. L., Brewer, M. T., Rosenzweig, B., Hedl, E., Anderson, L. J., Pyle, S. M., Moreland, J., Meyers, M. A., et al. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.39.24588 · Cited by 197 · see citing works
The Ectodomain Shedding of E-cadherin by ADAM15 Supports ErbB Receptor Activation
Najy, A. J., Day, K. C., & Day, M. L. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801329200 · Cited by 195 · see citing works
Potential Role for ADAM15 in Pathological Neovascularization in Mice
Horiuchi, K., Weskamp, G., Lum, L., Hammes, H., Cai, H., Brodie, T. A., Ludwig, T. E., Chiusaroli, R., Baron, R., Preissner, K. T., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.16.5614-5624.2003 · Cited by 189 · see citing works
Hashimoto, G., Aoki, T., Nakamura, H., Tanzawa, K., & Okada, Y. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02323-7 · Cited by 184 · see citing works
TACE/ADAM17 Processing of EGFR Ligands Indicates a Role as a Physiological Convertase
Lee, D. C., Sunnarborg, S. W., Hinkle, C. L., MYERS, T. J., STEVENSON, M., Russell, W. E., Castner, B. J., GERHART, M. J., Paxton, R. J., Black, R. A., et al. (2003) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2003.tb03207.x · Cited by 184 · see citing works
A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions
Giebeler, N., & Zigrino, P. (2016) · Toxins · doi:10.3390/toxins8040122 · Cited by 184 · see citing works
Klein, T., & Bischoff, R. (2011) · Journal of Proteome Research · doi:10.1021/pr100556z · Cited by 179 · cited 1× · see citing works
“There are 22 ADAMs in human [62], 14 of these ADAMs including ADAM-1, 2, 3, 6, 7, 18, 20, 21, 22, 28, 29, 30, 32 and 33 are restricted to embryo development, and are mainly expressed and conduct their function in the reproductive system such as testis, epididymis and uterus.”
BackgroundADAMTS proteins as modulators of microfibril formation and function
Hubmacher, D., & Apte, S. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.05.004 · Cited by 173 · see citing works
Colige, A., Li, S., Sieroń, A. L., Nusgens, B., Prockop, D. J., & Lapiere, C. M. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.6.2374 · Cited by 171 · see citing works
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 · see citing works
Qian, L.-W., Mizumoto, K., Urashima, T., Nagai, E., Maehara, N., Sato, N., Nakajima, M., & Tanaka, M. (2002) · PubMed · Cited by 166 · see citing works
ADAM and ADAMTS Family Proteins and Snake Venom Metalloproteinases: A Structural Overview
Takeda, S. (2016) · Toxins · doi:10.3390/toxins8050155 · Cited by 164 · see citing works
Horiuchi, K., Zhou, H., Kelly, K., Manova, K., & Blobel, C. (2005) · Developmental Biology · doi:10.1016/j.ydbio.2005.05.004 · Cited by 163 · see citing works
The procollagen N-proteinases ADAMTS2, 3 and 14 in pathophysiology
Bekhouche, M., & Colige, A. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.04.001 · Cited by 163 · see citing works
ADAM-mediated ectodomain shedding of HB-EGF in receptor cross-talk
Higashiyama, S., & Nanba, D. (2005) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2004.11.009 · Cited by 162 · see citing works
Papilin in development; a pericellular protein with a homology to the ADAMTS metalloproteinases
Kramerova, I. A., Kawaguchi, N., Fessler, L. I., Nelson, R. E., Chen, Y., Kramerov, A. A., Kusche‐Gullberg, M., Kramer, J. M., Ackley, B. D., Sieroń, A. L., et al. (2000) · Development · doi:10.1242/dev.127.24.5475 · Cited by 160 · see citing works
Weskamp, G., Schlöndorff, J. S., Lum, L., Becherer, J. D., Kim, T., Säftig, P., Hartmann, D., Murphy, G., & Blobel, C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307974200 · Cited by 157 · see citing works
Wang, R., Li, Y., Tsung, A., Huang, H., Du, Q., Yang, M., Deng, M., Xiong, S., Wang, X., Zhang, L., et al. (2018) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1722100115 · Cited by 156 · see citing works
Stone, A. L., Kröger, M., & Sang, Q. A. (1999) · Journal of Protein Chemistry · doi:10.1023/a:1020692710029 · Cited by 153 · see citing works
Insights on ADAMTS proteases and ADAMTS-like proteins from mammalian genetics
Dubail, J., & Apte, S. (2015) · Matrix Biology · doi:10.1016/j.matbio.2015.03.001 · Cited by 153 · see citing works
Kessler, T., Zhang, L., Liu, Z., Yin, X., Huang, Y., Wang, Y., Fu, Y., Mayr, M., Ge, Q., Xu, Q., et al. (2015) · Circulation · doi:10.1161/circulationaha.114.014072 · Cited by 153 · see citing works
The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs
Amour, A., Knight, C. G., English, W., Webster, A., Slocombe, P. M., Knäuper, V., Docherty, A., Becherer, J. D., Blobel, C., & Murphy, G. (2002) · FEBS Letters · doi:10.1016/s0014-5793(02)03047-8 · Cited by 150 · see citing works
Kutz, W. E., Wang, L. W., Bader, H. L., Majors, A. K., Iwata, K., Traboulsi, E. I., Sakai, L. Y., Keene, D. R., & Apte, S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.231571 · Cited by 149 · see citing works
Kurisaki, T., Masuda, A., Sudo, K., Sakagami, J., Higashiyama, S., Matsuda, Y., Nagabukuro, A., Tsuji, A. B., Nabeshima, Y.-I., Asano, M., et al. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.23.1.55-61.2003 · Cited by 147 · see citing works
Fridman, J. S., Caulder, E., Hansbury, M., Liu, X., Yang, G., Wang, Q., Lo, Y. Y. C., Zhou, B. S., Pan, M., Thomas, S. M., et al. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-2116 · Cited by 145 · see citing works
Tortorella, M. D., Arner, E. C., Hills, R. L., Easton, A. M., Korte-Sarfaty, J., Fok, K. F., Wittwer, A. J., Liu, R., & Malfait, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m313041200 · Cited by 143 · see citing works
Shi-Wu, L. I., ARITA, M., Fertala, A., Bao, Y., Kopen, G. C., Långsjö, T. K., Hyttinen, M. M., Helminen, H. J., & Prockop, D. J. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3550271 · Cited by 143 · see citing works
Zhang, Q. H., Thomas, S. M., Lui, V. W. Y., Xi, S., Siegfried, J. M., Fan, H., Smithgall, T. E., Mills, G. B., & Grandis, J. R. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0509719103 · Cited by 141 · see citing works
Essential Role for ADAM19 in Cardiovascular Morphogenesis
Zhou, H., Weskamp, G., Chesneau, V., Şahin, U., Vortkamp, A., Horiuchi, K., Chiusaroli, R., Hahn, R. T., Wilkes, D. C., Fisher, P. E., et al. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.24.1.96-104.2004 · Cited by 139 · see citing works
Clinical Trials Update: RENEWAL (RENAISSANCE and RECOVER) and ATTACH
Coletta, A. P., Clark, A. L., Banarjee, P., & Cleland, J. G. F. (2002) · European Journal of Heart Failure · doi:10.1016/s1388-9842(02)00121-6 · Cited by 138 · see citing works
Structure, function and evolutionary relationship of proteins containing a disintegrin domain
Blodel, C. P., & White, J. M. (1992) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(92)90098-w · Cited by 136 · see citing works
Metalloprotease-Disintegrin (ADAM) Genes Are Widely and Differentially Expressed in the Adult CNS
Kärkkäinen, I., Rybnikova, E. A., Pelto‐Huikko, M., & Huovila, A. J. (2000) · Molecular and Cellular Neuroscience · doi:10.1006/mcne.2000.0848 · Cited by 132 · see citing works
Evidence for a relationship between Ehlers–Danlos type VII C in humans and bovine dermatosparaxis
Nusgens, B., Verellen-Dumoulin, C., Hermanns‐Lê, T., Paepe, A. D., Nuytinck, L., Pierard, G., & Lapière, C. M. (1992) · Nature Genetics · doi:10.1038/ng0692-214 · Cited by 132 · see citing works
Von Willebrand factor, ADAMTS-13, and thrombotic thrombocytopenic purpura
Moake, J. L. (2004) · Seminars in Hematology · doi:10.1053/j.seminhematol.2003.10.003 · Cited by 131 · see citing works
Purification of ADAM 10 from bovine spleen as a TNFα convertase
Lunn, C. A., Fan, X., Dalie, B. L., Miller, K., Zavodny, P. J., Narula, S. K., & Lundell, D. J. (1997) · FEBS Letters · doi:10.1016/s0014-5793(96)01410-x · Cited by 130 · see citing works
Bauer, R. C., Tohyama, J., Cui, J. G., Cheng, L., Yang, J., Zhang, X., Ou, K., Paschos, G. K., Zheng, X. L., Parmacek, M. S., et al. (2015) · Circulation · doi:10.1161/circulationaha.114.012669 · Cited by 130 · see citing works
Cleavage of the ADAMTS13 Propeptide Is Not Required for Protease Activity
Majerus, E. M., Zheng, X. L., Tuley, E. A., & Sadler, J. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m309872200 · Cited by 129 · see citing works
Proteolytic Processing of Delta-like 1 by ADAM Proteases
Dyczynska, E., Sun, D., Yi, H., Sehara‐Fujisawa, A., Blobel, C., & Żółkiewska, A. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605451200 · Cited by 129 · see citing works
Catalytic Properties of ADAM19
Chesneau, V., Becherer, J. D., Zheng, Y., Erdjument‐Bromage, H., Tempst, P., & Blobel, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302781200 · Cited by 129 · see citing works
Loss of ADAMTS3 activity causes Hennekam lymphangiectasia–lymphedema syndrome 3
Brouillard, P., Dupont, L., Helaers, R., Coulie, R., Tiller, G. E., Peeden, J., Colige, A., & Vikkula, M. (2017) · Human Molecular Genetics · doi:10.1093/hmg/ddx297 · Cited by 127 · see citing works
Colige, A., Ruggiero, F., Vandenberghe, I. H. M., Dubail, J., Kesteloot, F., BEEUMEN, J. V., Beschin, A., Brys, L., Lapiere, C. M., & Nusgens, B. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506458200 · Cited by 125 · see citing works
Moss, M. L., & Rasmussen, F. (2007) · Analytical Biochemistry · doi:10.1016/j.ab.2007.04.043 · Cited by 124 · see citing works
Metalloprotease‐disintegrin ADAM8: Expression analysis and targeted deletion in mice
Kelly, K., Hutchinson, G., Nebenius‐Oosthuizen, D., Smith, A. J. H., Bartsch, J. W., Horiuchi, K., Rittger, A., Manova, K., Docherty, A. J. P., & Blobel, C. (2004) · Developmental Dynamics · doi:10.1002/dvdy.20221 · Cited by 120 · see citing works
Catalytic Activity of Human ADAM33
Zou, J., Zhu, F., Liu, J., Wang, W., Zhang, R., Garlisi, C. G., Liu, Y., Wang, S., Shah, H., Wan, Y., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309696200 · Cited by 118 · see citing works
The cysteine-rich domain regulates ADAM protease function in vivo
Smith, K., Gaultier, A., Cousin, H., Alfandari, D., White, J. M., & DeSimone, D. W. (2002) · The Journal of Cell Biology · doi:10.1083/jcb.200206023 · Cited by 115 · see citing works
Higher sensitivity of Adamts12-deficient mice to tumor growth and angiogenesis
Hour, M. E., Moncada-Pazos, Á., Blacher, S., Masset, A., Cal, S., Berndt, S., Detilleux, J., Host, L., Obaya, Á. J., Maillard, C., et al. (2010) · Oncogene · doi:10.1038/onc.2010.49 · Cited by 115 · see citing works
TACE is required for fetal murine cardiac development and modeling
Shi, W., Chen, H., Sun, J., Buckley, S., Zhao, J., Anderson, K. D., Williams, R. G., & Warburton, D. (2003) · Developmental Biology · doi:10.1016/s0012-1606(03)00315-4 · Cited by 115 · see citing works
Extracellular Matrix Communication and Turnover in Cardiac Physiology and Pathology
Takawale, A. R., Sakamuri, S. S. V. P., & Kassiri, Z. (2015) · Comprehensive physiology · doi:10.1002/cphy.c140045 · Cited by 114 · see citing works
Pu, X., Xiao, Q., Kiechl, S. J., Chan, K., Ng, F. L., Gor, S., Poston, R. N., Fang, C., Patel, A. S., Senver, E. C., et al. (2013) · The American Journal of Human Genetics · doi:10.1016/j.ajhg.2013.01.012 · Cited by 111 · see citing works
Somerville, R. P. T., Longpré, J., Apel, E. D., Lewis, R. M., Wang, L. W., Sanes, J. R., Leduc, R., & Apte, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m402380200 · Cited by 108 · see citing works
Fedak, P. W. M., Moravec, C. S., McCarthy, P. M., Altamentova, S. M., Wong, A. P., Škrtić, M., Verma, S., Weisel, R. D., & Li, R. (2006) · Circulation · doi:10.1161/circulationaha.105.571414 · Cited by 108 · see citing works
Wolf, Z. T., Brand, H., Shaffer, J. R., Leslie, E. J., Arzi, B., Willet, C. E., Cox, T. C., McHenry, T. G., Narayan, N., Feingold, E., et al. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005059 · Cited by 107 · see citing works
Spatially- and temporally-restricted expression of meltrin α (ADAM12) and β (ADAM19) in mouse embryo
Kurisaki, T., Masuda, A., Osumi, N., Nabeshima, Y.-I., & Fujisawa‐Sehara, A. (1998) · Mechanisms of Development · doi:10.1016/s0925-4773(98)00043-4 · Cited by 105 · see citing works
Koo, B.-H., Coe, D. M., Dixon, L. J., Somerville, R. P. T., Nelson, C. M., Wang, L. W., Young, M. E., Lindner, D. J., & Apte, S. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.090655 · Cited by 105 · see citing works
TIMP-3 inhibits the procollagen N-proteinase ADAMTS-2
Wang, W.-M., Ge, G., Lim, N. H., Nagase, H., & Greenspan, D. S. (2006) · Biochemical Journal · doi:10.1042/bj20060630 · Cited by 104 · see citing works
Essential roles of Meltrin β (ADAM19) in heart development
Kurohara, K., Komatsu, K., Kurisaki, T., Masuda, A., Irie, N., Asano, M., Sudo, K., Nabeshima, Y.-I., Iwakura, Y., & Sehara‐Fujisawa, A. (2003) · Developmental Biology · doi:10.1016/j.ydbio.2003.10.021 · Cited by 103 · see citing works
ADAMTS3 activity is mandatory for embryonic lymphangiogenesis and regulates placental angiogenesis
Janssen, L., Dupont, L., Bekhouche, M., Noël, A., Leduc, C., Voz, M. L., Peers, B., Cataldo, D. D., Apte, S., Dubail, J., et al. (2015) · Angiogenesis · doi:10.1007/s10456-015-9488-z · Cited by 102 · see citing works
Mishra, P. K., Tyagi, N., Sen, U., Givvimani, S., & Tyagi, S. C. (2009) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00682.2009 · Cited by 102 · see citing works
Testicular and epididymal ADAMs: expression and function during fertilization
Cho, C. (2012) · Nature Reviews Urology · doi:10.1038/nrurol.2012.167 · Cited by 101 · see citing works
Sahul, Z. H., Mukherjee, R. D., Song, J., McAteer, J. P., Stroud, R. E., Dione, D. P., Staib, L. H., Papademetris, X., Dobrucki, L. W., Duncan, J. S., et al. (2011) · Circulation Cardiovascular Imaging · doi:10.1161/circimaging.110.961854 · Cited by 101 · see citing works
Altered Expression of ADAMs ( A D isintegrin A nd M etalloproteinase) in Fibrillating Human Atria
Arndt, M., Lendeckel, U., Röcken, C., Nepple, K., Wolke, C., Spiess, A., Huth, C., Ansorge, S., Klein, H., & Goette, A. (2002) · Circulation · doi:10.1161/hc0602.103639 · Cited by 98 · see citing works
Protective Actions of H 2 S in Acute Myocardial Infarction and Heart Failure
Donnarumma, E., Trivedi, R. K., & Lefer, D. J. (2017) · Comprehensive physiology · doi:10.1002/cphy.c160023 · Cited by 96 · see citing works
Prada, M. L., Cal, S., Quesada, V., & López-Otı́n, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m211900200 · Cited by 93 · see citing works
Shi-Wu, L. I., ARITA, M., Fertala, A., et al. (2001) · Biochemical Journal · doi:10.1042/bj3550271 · Cited by 92 · see citing works
ADAM15 regulates endothelial permeability and neutrophil migration via Src/ERK1/2 signalling
Sun, C., Wu, M. H., Guo, M., Day, M. L., Lee, E., & Yuan, S. Y. (2010) · Cardiovascular Research · doi:10.1093/cvr/cvq060 · Cited by 91 · see citing works
Colige, A., Beschin, A., Samyn, B., Goebels, Y., BEEUMEN, J. V., Nusgens, B., & Lapiere, C. M. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.28.16724 · Cited by 90 · see citing works
Zheng, X. L., Majerus, E. M., & Sadler, J. E. (2002) · Current Opinion in Hematology · doi:10.1097/00062752-200209000-00001 · Cited by 89 · see citing works
Jha, S. K., Rauniyar, K., Kärpänen, T., Leppänen, V., Brouillard, P., Vikkula, M., Alitalo, K. K., & Jeltsch, M. (2017) · Scientific Reports · doi:10.1038/s41598-017-04982-1 · Cited by 88 · see citing works
Matrix as an Interstitial Transport System
Dong, F., Creemers, E. E., & Kassiri, Z. (2014) · Circulation Research · doi:10.1161/circresaha.114.302335 · Cited by 86 · see citing works
Somerville, R. P. T., Jungers, K. A., & Apte, S. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409036200 · Cited by 81 · see citing works
Dubail, J., Kesteloot, F., Deroanne, C., Motté, P., Lambert, V., Rakic, J., Lapière, C., Nusgens, B., & Colige, A. (2010) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-010-0431-6 · Cited by 80 · see citing works
Critical Role of ADAMTS-4 in the Development of Sporadic Aortic Aneurysm and Dissection in Mice
Ren, P., Hughes, M. S., Krishnamoorthy, S., Zou, S., Zhang, L., Wu, D., Zhang, C., Curci, J. A., Coselli, J. S., Milewicz, D. M., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-12248-z · Cited by 80 · see citing works
Troeberg, L., Lazenbatt, C., Anower-E-Khuda, M. F., Freeman, C. G., Federov, O., Habuchi, H., Habuchi, O., Kimata, K., & Nagase, H. (2014) · Chemistry & Biology · doi:10.1016/j.chembiol.2014.07.014 · Cited by 79 · see citing works
Secreted Metalloproteinase ADAMTS-3 Inactivates Reelin
Ogino, H., Hisanaga, A., Kohno, T., Kondo, Y., Okumura, K., Kamei, T., Sato, T., Asahara, H., Tsuiji, H., Fukata, M., et al. (2017) · Journal of Neuroscience · doi:10.1523/jneurosci.3632-16.2017 · Cited by 74 · see citing works
Arning, A., Hiersche, M., Witten, A., Kurlemann, G., Kurnik, K., Manner, D., Stoll, M., & Nowak‐Göttl, U. (2012) · Blood · doi:10.1182/blood-2012-07-442038 · Cited by 72 · see citing works
Regulation of ADAM12 Cell-surface Expression by Protein Kinase C ϵ
Sundberg, C., Thodeti, C. K., Kveiborg, M., Larsson, C., Parker, P. J., Albrechtsen, R., & Wewer, U. M. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m403753200 · Cited by 70 · see citing works
ADAM‐15: a metalloprotease that mediates inflammation
Charrier‐Hisamuddin, L., LABOISSE, C. L., & Merlin, D. (2007) · The FASEB Journal · doi:10.1096/fj.07-8876rev · Cited by 70 · see citing works
The C-terminal domains of ADAMTS-4 and ADAMTS-5 promote association with N-TIMP-3
Troeberg, L., Fushimi, K., Scilabra, S. D., Nakamura, H., Dive, V., Thøgersen, I. B., Enghild, J. J., & Nagase, H. (2009) · Matrix Biology · doi:10.1016/j.matbio.2009.07.005 · Cited by 70 · see citing works
Intracellular Processing of Metalloprotease Disintegrin ADAM12
Cao, Y., Kang, Q., Zhao, Z., & Żółkiewska, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110814200 · Cited by 68 · see citing works
Association of a nsSNP in ADAMTS14 to some osteoarthritis phenotypes
Rodriguez‐Lopez, J. A., Pombo‐Suárez, M., Loughlin, J. A., Tsezou, A., Blanco, F. J., Meulenbelt, I., Slagboom, P. E., Valdes, A. M., Spector, T. D., Gómez-Reino, J. J., et al. (2008) · Osteoarthritis and Cartilage · doi:10.1016/j.joca.2008.07.012 · Cited by 68 · see citing works
Li, C., Frebelius, S., Swedenborg, J., Wågsäter, D., Williams, K. J., Eriksson, P. O., Folkesson, M., Roy, J., & Liu, M. (2015) · Thrombosis and Haemostasis · doi:10.1160/th14-10-0899 · Cited by 67 · see citing works
Regulation of ADAMTS9 Secretion and Enzymatic Activity by Its Propeptide
Koo, B.-H., Longpré, J., Somerville, R. P. T., Alexander, J. P., Leduc, R., & Apte, S. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m610161200 · Cited by 67 · see citing works
Adam10 is essential for early embryonic cardiovascular development
Zhang, C., Tian, L., Chi, C., Wu, X., Yang, X. Y., Han, M., Xu, T., Zhuang, Y., & Deng, K. (2010) · Developmental Dynamics · doi:10.1002/dvdy.22391 · Cited by 67 · see citing works
Hydrogen sulfide and cardioprotection — Mechanistic insights and clinical translatability
Salloum, F. N. (2015) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2015.04.004 · Cited by 65 · see citing works
Tortorella, M. D., Tomasselli, A. G., Mathis, K. J., Schnute, M. E., Woodard, S. S., Munie, G. E., Williams, J. M., Caspers, N. L., Wittwer, A. J., Malfait, A., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.029116 · Cited by 64 · see citing works
ADAMs family and relatives in cardiovascular physiology and pathology
Zhang, P., Shen, M., Fernández-Patrón, C., & Kassiri, Z. (2015) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2015.10.031 · Cited by 63 · see citing works
Cleavage of von Willebrand factor by ADAMTS-13 on endothelial cells
López, J. A., & Dong, J.-F. (2004) · Seminars in Hematology · doi:10.1053/j.seminhematol.2003.10.004 · Cited by 62 · see citing works
Increased ADAMTS1 mediates SPARC-dependent collagen deposition in the aging myocardium
Toba, H., Brás, L. E. D. C., Baicu, C. F., Zile, M. R., Lindsey, M. L., & Bradshaw, A. D. (2016) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00040.2016 · Cited by 61 · see citing works
Minond, D., Čudić, M., Bionda, N., Giulianotti, M. A., Maida, L. E., Houghten, R. A., & Fields, G. B. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.389114 · Cited by 59 · see citing works
Jin, Y., Liu, Y., Lin, Q., Li, J., Druso, J. E., Antonyak, M. A., Meininger, C. J., Zhang, S. L., Dostal, D. E., Guan, J., et al. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.00650-13 · Cited by 59 · see citing works
Dancevic, C. M., Fraser, F. W., Smith, A. D., Stupka, N., Ward, A. C., & McCulloch, D. R. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.418624 · Cited by 57 · see citing works
ADAM10 and ADAM17 have opposite roles during sprouting angiogenesis
Caolo, V., Swennen, G., Chalaris, A., Wagenaar, A., Verbruggen, S. E. L., Rose‐John, S., Molin, D. G. M., Vooijs, M., & Post, M. J. (2014) · Angiogenesis · doi:10.1007/s10456-014-9443-4 · Cited by 57 · see citing works
Sun, C., Wu, M. H., Lee, E. S., & Yuan, S. Y. (2012) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.112.252205 · Cited by 53 · see citing works
van der Vorst, E. P. C., Keijbeck, A. A., de Winther, M. P. J., & Donners, M. M. P. C. (2012) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2012.04.023 · Cited by 52 · see citing works
Kelwick, R. J. R., Wagstaff, L., Decock, J. V., Roghi, C. H., Cooley, L. S., Robinson, S. D., Arnold, H., Gavrilović, J., Jaworski, D. M., Yamamoto, K., et al. (2014) · International Journal of Cancer · doi:10.1002/ijc.29129 · Cited by 52 · see citing works
Kawai, T., Takayanagi, T., Forrester, S. J., Preston, K. J., Obama, T., Tsuji, T., Kobayashi, T., Boyer, M. J., Cooper, H. A., Kwok, H. F., et al. (2017) · Hypertension · doi:10.1161/hypertensionaha.117.09822 · Cited by 52 · see citing works
Deficits in spatial learning and motor coordination in ADAM11-deficient mice
Takahashi, E., Sagane, K., Oki, T., Yamazaki, K., Nagasu, T., & Kuromitsu, J. (2006) · BMC Neuroscience · doi:10.1186/1471-2202-7-19 · Cited by 50 · see citing works
Dong, F., Takawale, A. R., Shen, M., Wang, W., Wang, X., Basu, R., Oudit, G. Y., & Kassiri, Z. (2015) · Circulation Heart Failure · doi:10.1161/circheartfailure.114.002029 · Cited by 49 · see citing works
Wang, X., Chen, W., Zhang, J., Khan, A. Q., Li, L., Huang, F., Qiu, Z., Wang, L., & Chen, X. (2017) · Hypertension · doi:10.1161/hypertensionaha.116.08581 · Cited by 48 · see citing works
The isolated N-terminal domains of TIMP-1 and TIMP-3 are insufficient for ADAM10 inhibition
Rapti, M., Atkinson, S. J., Lee, M., Trim, A., Moss, M. L., & Murphy, G. (2008) · Biochemical Journal · doi:10.1042/bj20071430 · Cited by 47 · see citing works
Rau, C. D., Romay, M. C., Tuteryan, M., Wang, J., Santolini, M., Ren, S. V., Karma, A., Weiss, J. N., Wang, Y., & Lusis, A. J. (2016) · Cell Systems · doi:10.1016/j.cels.2016.10.016 · Cited by 47 · see citing works
McRobb, L. S., McKay, M. J., Gamble, J. R., Grace, M., Moutrie, V., Santos, E. D., Lee, V. S., Zhao, Z., Molloy, M. P., & Stoodley, M. A. (2017) · Aging · doi:10.18632/aging.101225 · Cited by 47 · see citing works
Cell-surface Processing of the Metalloprotease Pro-ADAMTS9 Is Influenced by the Chaperone GRP94/gp96
Koo, B.-H., & Apte, S. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.039677 · Cited by 46 · see citing works
Positive Selection at Reproductive ADAM Genes with Potential Intercellular Binding Activity
Glassey, B., & Civetta, A. (2004) · Molecular Biology and Evolution · doi:10.1093/molbev/msh080 · Cited by 46 · see citing works
Howard, L., & Glynn, P. (1995) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(95)48025-0 · Cited by 44 · see citing works
Li, M., Liu, Q., Lei, J., Wang, X., Chen, X., & Ding, Y. (2017) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2017.09.031 · Cited by 44 · see citing works
Cong, L., & Jia, J. (2009) · Neurobiology of Aging · doi:10.1016/j.neurobiolaging.2009.01.001 · Cited by 43 · see citing works
Wong, G. E., Zhu, X., Prater, C. E., Oh, E., & Evans, J. P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m101637200 · Cited by 42 · see citing works
Genetic and molecular aspects of acromelic dysplasia.
Goff, C. L., & Cormier‐Daire, V. (2009) · PubMed · Cited by 41 · see citing works
Bai, X., Wang, D., Luan, Y., Yu, X. P., & Liu, C.-J. (2008) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-008-8633-x · Cited by 40 · see citing works
Kveiborg, M., Jacobsen, J., Lee, M., Nagase, H., Wewer, U. M., & Murphy, G. (2010) · Biochemical Journal · doi:10.1042/bj20100649 · Cited by 40 · see citing works
Shen, M., Morton, J. S., Davidge, S. T., & Kassiri, Z. (2016) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2016.12.001 · Cited by 38 · see citing works
Rizza, S., Copetti, M., Cardellini, M., Menghini, R., Pecchioli, C., Luzi, A., Cola, G. D., Porzio, O., Ippoliti, A., Romeo, F., et al. (2015) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2015.01.029 · Cited by 36 · see citing works
ADAMTS14 gene polymorphism associated with knee osteoarthritis in Thai women
Poonpet, T., Honsawek, S., Tammachote, N., Kanitnate, S., & Tammachote, R. (2013) · Genetics and Molecular Research · doi:10.4238/2013.november.7.5 · Cited by 36 · see citing works
Xie, B., Shen, J., Dong, A., Swaim, M., Hackett, S. F., Wyder, L., Worpenberg, S., Barbieri, S., & Campochiaro, P. A. (2008) · The FASEB Journal · doi:10.1096/fj.07-099283 · Cited by 33 · see citing works
Kim, S.-H., Pei, Q.-M., Jiang, P. X., Yang, M., Qian, X., & Liu, J. (2017) · Respiratory Research · doi:10.1186/s12931-016-0490-9 · Cited by 33 · see citing works
Characterization of ADAMTS14, a novel member of the ADAMTS metalloproteinase family
Bolz, H. J., Ramı́rez, A., von Brederlow, B., & Kubisch, C. (2001) · Biochimica et Biophysica Acta (BBA) - Gene Structure and Expression · doi:10.1016/s0167-4781(01)00329-3 · Cited by 32 · see citing works
Canault, M., Certel, K., Schatzberg, D., Wagner, D. D., & Hynes, R. O. (2010) · PLoS ONE · doi:10.1371/journal.pone.0013433 · Cited by 31 · see citing works
Biochemistry and Physiological Functions of ADAMTS7 Metalloprotease
Hanby, H. A. (2013) · Advances in Biochemistry · doi:10.11648/j.ab.20130103.11 · Cited by 31 · see citing works
Lee, C. W., Hwang, I., Park, C.-S., Lee, H., Park, D., Kang, S.-J., Lee, S., Kim, Y., Park, S., & Park, S. (2011) · Journal of Thrombosis and Thrombolysis · doi:10.1007/s11239-011-0673-7 · Cited by 30 · see citing works
Genetic association between polymorphisms in the BTG1 gene and multiple sclerosis
Camiña-Tato, M., Morcillo-Suárez, C., Navarro, A., Fernández, M., Horga, A., Montalbán, X., & Comabella, M. (2009) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2009.05.010 · Cited by 30 · see citing works
Gao, Y., Wu, W., Yu, C., Zhong, F., Li, G., Kong, W., & Zheng, J. (2015) · Science China Life Sciences · doi:10.1007/s11427-015-4959-4 · Cited by 29 · see citing works
Zhu, R., Cheng, M., Lu, T., Yang, N., Ye, S., Pan, Y.-H., Hong, T., Dang, S., & Zhang, W. K. (2017) · American Journal Of Pathology · doi:10.1016/j.ajpath.2017.10.020 · Cited by 29 · see citing works
Takizawa, M., Yatabe, T., Okada, A., Chijiiwa, M., Mochizuki, S., Ghosh, P. B., & Okada, Y. (2008) · FEBS Letters · doi:10.1016/j.febslet.2008.07.036 · Cited by 28 · see citing works
ADAMTS genes and the risk of cerebral aneurysm
Arning, A., Jeibmann, A., Köhnemann, S., Brokinkel, B., Ewelt, C., Berger, K., Wellmann, J., Nowak‐Göttl, U., Stummer, W., Stoll, M., et al. (2016) · Journal of neurosurgery · doi:10.3171/2015.7.jns154 · Cited by 28 · see citing works
Chen, J., Yu, Z. H., Chang, X., Zhang, S., & Dai, D. (2012) · Digestive Diseases and Sciences · doi:10.1007/s10620-012-2379-x · Cited by 27 · see citing works
Boerboom, D., Lafond, J., Zheng, X., Lapointe, É., Mittaz, L., Boyer, A., Pritchard, M. A., DeMayo, F. J., Mort, J. S., Drolet, R., et al. (2011) · Developmental Dynamics · doi:10.1002/dvdy.22662 · Cited by 27 · see citing works
The role of ADAMTS13 in acute myocardial infarction: cause or consequence?
Eerenberg, E. S., Teunissen, P. F. A., van den Born, B. H., Meijers, J. C. M., Hollander, M. R., Jansen, M. F., Tijssen, R., Beliën, J. A. M., van de Ven, P. M., Aly, M. F. A., et al. (2016) · Cardiovascular Research · doi:10.1093/cvr/cvw097 · Cited by 26 · see citing works
Gunes, M., Akpınar, B., Cömertoğlu, İ., Akyol, S., Demirçelik, B., Gurel, O. M., Aynekin, B., Erdemli, H. K., Ateş, M., Eryonucu, B., et al. (2016) · Clinical Laboratory · doi:10.7754/clin.lab.2015.150730 · Cited by 25 · see citing works
Wu, W., Zhou, Y., Li, Y., Li, J., Ke, Y.-N., Wang, Y., & Zheng, J. (2015) · European journal of medical research · doi:10.1186/s40001-015-0118-4 · Cited by 24 · see citing works
Genetic association between polymorphisms in the ADAMTS14 gene and multiple sclerosis
Goertsches, R. H., Comabella, M., Navarro, A., Perkal, H., & Montalbán, X. (2005) · Journal of Neuroimmunology · doi:10.1016/j.jneuroim.2005.04.005 · Cited by 24 · see citing works
Qu, Y., & Zhang, N. (2018) · Experimental and Therapeutic Medicine · doi:10.3892/etm.2018.6720 · Cited by 23 · see citing works
ADAMTS-7 promotes vascular smooth muscle cells proliferation in vitro and in vivo
Zhang, L., Yu, F., Wang, L., Zheng, J., Du, Y., Huang, Y., Liu, B., Wang, X., & Kong, W. (2015) · Science China Life Sciences · doi:10.1007/s11427-015-4843-2 · Cited by 21 · see citing works
Vuohelainen, V., Raitoharju, E., Levula, M., Lehtimäki, T. J., Pelto‐Huikko, M., Honkanen, T., Huovila, A.-P. J., Paavonen, T., Tarkka, M. R., & Mennander, A. (2011) · Scandinavian Journal of Clinical and Laboratory Investigation · doi:10.3109/00365513.2011.591424 · Cited by 19 · see citing works
ADAM and ADAMTS gene expression in native and wound healing human lens epithelial cells.
Hodgkinson, L. M., Wang, L., Duncan, G., Edwards, D. R., & Wormstone, I. M. (2010) · PubMed Central · Cited by 18 · see citing works
Sommer, A., Düppe, M., Baumecker, L., Kordowski, F., Büch, J., Chico, J. F., Fritsch, J. H., Schütze, S., Adam, D., Sperrhacke, M., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.19983 · Cited by 18 · see citing works
ADAMTS4 level in patients with stable coronary artery disease and acute coronary syndromes
Zha, Y., Chen, Y., Xu, F., Li, T. X., Zhao, C., & Cui, L. (2009) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2009.09.012 · Cited by 17 · see citing works
Heijink, I. H., Brandenburg, S. M., Noordhoek, J. A., Slebos, D., Postma, D. S., & van Oosterhout, A. J. M. (2011) · Respiratory Research · doi:10.1186/1465-9921-12-110 · Cited by 17 · see citing works
TNFα Shedding in Mechanically Stressed Cardiomyocytes is Mediated by Src Activation of TACE
Niu, A., Wang, B., & Li, Y. (2014) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25006 · Cited by 16 · see citing works
Recombinant disintegrin domain of ADAM15 inhibits the proliferation and migration of Bel-7402 cells
Hou, Y., Chu, M., Du, F. F., Lei, J. Y., Chen, Y., Zhu, R., Gong, X., Ma, X., & Jin, J. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.05.037 · Cited by 16 · see citing works
McClurg, U. L., Danjo, K., King, H. O., Scott, G. B., Robinson, P. A., & Crabtree, J. E. (2014) · Microbes and Infection · doi:10.1016/j.micinf.2014.11.011 · Cited by 15 · see citing works
Sato, T., Suzuki, H., Shibata, M., Kusuyama, T., Omori, Y., Soda, T., Shoji, M., Iso, Y., Koba, S., Geshi, E., et al. (2006) · Circulation Journal · doi:10.1253/circj.70.1635 · Cited by 15 · see citing works
Expression and cellular localization of metalloproteases ADAMs in high graded carotid artery lesions
Pelisek, J., Pongratz, J., Deutsch, L. S., Reeps, C., Stadlbauer, T. H. W., & Eckstein, H. (2012) · Scandinavian Journal of Clinical and Laboratory Investigation · doi:10.3109/00365513.2012.734394 · Cited by 15 · see citing works
Upregulation of ADAMTS-7 and downregulation of COMP are associated with aortic aneurysm
Qin, W., Cao, Y., Li, L., Chen, W., & Chen, X. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.7293 · Cited by 15 · see citing works
Involvement of the ADAM 12 in Thrombin-Induced Rat's VSMCs Proliferation
Smiljanić, K., Dobutović, B., Obradovic, M. M., Nikolić, D., Marché, P., & Isenović, E. R. (2011) · Current Medicinal Chemistry · doi:10.2174/092986711796504709 · Cited by 14 · see citing works
Zeinieh, M. P., Salehi, A. H., Rajkumar, V. S., & Barker, P. A. (2014) · Journal of Cell Science · doi:10.1242/jcs.152173 · Cited by 14 · see citing works
Chen, L., Yang, L., Zha, Y., & Cui, L. (2011) · Coronary Artery Disease · doi:10.1097/mca.0b013e32834c7565 · Cited by 14 · see citing works
Differentially regulated ADAMTS1, 8, and 18 in gastric adenocarcinoma
Kilic, M. O., Aynekin, B., Kara, A., Icen, D., & Demircan, K. (2017) · Bratislavské lekárske listy/Bratislava medical journal · doi:10.4149/bll_2017_014 · Cited by 13 · see citing works
ADAMTS9, a member of the ADAMTS family, in Xenopus development
Desanlis, I., Felstead, H. L., Edwards, D. R., & Wheeler, G. N. (2018) · Gene Expression Patterns · doi:10.1016/j.gep.2018.06.001 · Cited by 13 · see citing works
Yu, J., Zhou, B., Yu, H., Han, J., Cui, M., Zhang, F., Wang, G., Guo, L., & Gao, W. D. (2016) · Medicine · doi:10.1097/md.0000000000005523 · Cited by 12 · see citing works
Flagged first, then by citations
5 of the 208 references couldn’t be matched to a known paper.
Research works printed but not linked: 1
- [147]Ren P, Hughes M, Krishnamoorthy S, Zou S, Zhang L, Wu D, Critical Role of ADAMTS-4 in the Development of Sporadic Aortic Aneurysm and Dissection in Mice 2017; 7: 12351. PMC5617887 28955046
Cited by
Sorted by citations
Accurate prediction of protein structures and interactions using a 3-track network
Baek, M., DiMaio, F., Anishchenko, I., Dauparas, J., Ovchinnikov, S., Lee, G. R., Wang, J., Cong, Q., Kinch, L. N., Schaeffer, R. D., et al. (2021) · doi:10.1101/2021.06.14.448402 · Cited by 5,542 · see citing works
The Extracellular Matrix in Ischemic and Nonischemic Heart Failure
Frangogiannis, N. G. (2019) · Circulation Research · doi:10.1161/circresaha.119.311148 · Cited by 520 · see citing works
Savin, I. A., Аркадьевна, З. М., & Васильевна, С. А. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232314959 · Cited by 288 · see citing works
Updates in Alzheimer's disease: from basic research to diagnosis and therapies
Liu, E., Zhang, Y., & Wang, J. (2024) · Translational Neurodegeneration · doi:10.1186/s40035-024-00432-x · Cited by 220 · see citing works
Accurate prediction of protein structures and interactions using a three-track neural network
Baek, M., DiMaio, F., Anishchenko, I. V., Dauparas, J., Ovchinnikov, S., Lee, G. R., Wang, J., Cong, Q., Kinch, L. N., Schaeffer, R. D., et al. (2022) · Yearbook of pediatric endocrinology · doi:10.1530/ey.19.15.15 · Cited by 199 · see citing works
Extracellular matrix dynamics in vascular remodeling
Ma, Z., Mao, C., Jia, Y., Fu, Y., & Kong, W. (2020) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00147.2020 · Cited by 129 · see citing works
Matrix Metalloproteinases and Glaucoma Treatment
Weinreb, R. N., Robinson, M. R., Dibas, M. I., & Stamer, W. D. (2020) · Journal of Ocular Pharmacology and Therapeutics · doi:10.1089/jop.2019.0146 · Cited by 117 · see citing works
The Mechanism and Role of ADAMTS Protein Family in Osteoarthritis
Li, T., Peng, J., Li, Q., Shu, Y., Zhu, P., & Hao, L. (2022) · Biomolecules · doi:10.3390/biom12070959 · Cited by 109 · see citing works
Retinopathy of prematurity: A review of pathophysiology and signaling pathways
Fevereiro‐Martins, M., Marques‐Neves, C., Guimarães, H., & Bicho, M. (2022) · Survey of Ophthalmology · doi:10.1016/j.survophthal.2022.11.007 · Cited by 114 · see citing works
Pathogenic mechanisms and the potential of drug therapies for aortic aneurysm
Liu, B., Granville, D. J., Golledge, J., & Kassiri, Z. (2020) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00621.2019 · Cited by 87 · see citing works
MMPs and ADAMs/ADAMTS inhibition therapy of abdominal aortic aneurysm
Li, Y., Wang, W., Li, L., & Khalil, R. A. (2020) · Life Sciences · doi:10.1016/j.lfs.2020.117659 · Cited by 68 · see citing works
Self-citationKim, I.-S., Yang, W., & Kim, C. (2022) · Current Medicinal Chemistry · doi:10.2174/0929867329666220823112731 · Cited by 53 · see citing works
Role of Extracellular Matrix in Gastrointestinal Cancer-Associated Angiogenesis
Andreuzzi, E., Capuano, A., Poletto, E., Pivetta, E., Fejza, A., Favero, A., Doliana, R., Cannizzaro, R., Spessotto, P., & Mongiat, M. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21103686 · Cited by 48 · see citing works
Kaczorowska, A., Miękus, N., Stefanowicz, J., & Adamkiewicz-Drożyńska, E. (2020) · Diagnostics · doi:10.3390/diagnostics10080547 · Cited by 47 · see citing works
Bian, X., Xu, J., Zhao, H., Zheng, Q., Xiao, X., Ma, X., Li, Y., Du, X., & Liu, X. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/1232146 · Cited by 45 · see citing works
Immunomodulatory role of metalloproteinase ADAM17 in tumor development
Wang, K., Xuan, Z., Liu, X., Zheng, M., Yang, C., & Wang, H. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.1059376 · Cited by 44 · see citing works
Platelet Membrane Receptor Proteolysis: Implications for Platelet Function
Wu, J., Heemskerk, J. W. M., & Baaten, C. C. F. M. J. (2021) · Frontiers in Cardiovascular Medicine · doi:10.3389/fcvm.2020.608391 · Cited by 40 · see citing works
Perrelli, A., & Retta, S. F. (2021) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2021.06.021 · Cited by 38 · see citing works
Retinopathy of prematurity: contribution of inflammatory and genetic factors
Fevereiro‐Martins, M., Guimarães, H., Marques‐Neves, C., & Bicho, M. (2022) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-022-04394-4 · Cited by 34 · see citing works
Russell, J. J., Grisanti, L. A., Brown, S. M., Bailey, C. A., Bender, S. B., & Chandrasekar, B. (2021) · Cellular Signalling · doi:10.1016/j.cellsig.2021.109993 · Cited by 29 · see citing works
ADAMTS8 inhibited lung cancer progression through suppressing VEGFA
Zhang, Y., Hu, K., Qu, Z., Xie, Z., & Tian, F. (2022) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2022.01.110 · Cited by 29 · see citing works
Transcriptome for the breast muscle of Jinghai yellow chicken at early growth stages
Wu, P., Zhang, X., Zhang, G., Chen, F., He, M., Zhang, T., Wang, J., Xie, K., & Dai, G. (2020) · PeerJ · doi:10.7717/peerj.8950 · Cited by 28 · see citing works
Peptide-Based Inhibitors of ADAM and ADAMTS Metalloproteinases
Pluda, S., Mazzocato, Y., & Angelini, A. (2021) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.703715 · Cited by 27 · see citing works
ADAM Proteases in Cancer: Biological Roles, Therapeutic Challenges, and Emerging Opportunities
Arora, S., Scott, A. M., & Janes, P. W. (2025) · Cancers · doi:10.3390/cancers17101703 · Cited by 25 · see citing works
The evolution of ADAM gene family in eukaryotes
de Souza, J. S. M., Lisboa, A. B. P., Santos, T. M., de Andrade, M. V. S., Neves, V. B. S., Teles-Souza, J., de Jesus, H. N. R., Bezerra, T. G., Falcão, V. G. O., Oliveira, R. C., et al. (2020) · Genomics · doi:10.1016/j.ygeno.2020.05.010 · Cited by 24 · see citing works
The Pathophysiological Role of Vascular Smooth Muscle Cells in Abdominal Aortic Aneurysm
Shi, D., Zhang, M., Zhang, Y., Shi, Y., Liu, X., Wu, X., & Yang, Z. (2025) · Cells · doi:10.3390/cells14131009 · Cited by 25 · see citing works
Peptides and Peptidomimetics as Inhibitors of Enzymes Involved in Fibrillar Collagen Degradation
Ledwoń, P., Papini, A. M., Rovero, P., & Latajka, R. (2021) · Materials · doi:10.3390/ma14123217 · Cited by 23 · see citing works
Role of ADAM and ADAMTS disintegrin and metalloproteinases in normal pregnancy and preeclampsia
Qu, H., & Khalil, R. A. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115266 · Cited by 24 · see citing works
Self-citationDrees, L., Schneider, S., Riedel, D., Schuh, R., & Behr, M. (2023) · eLife · doi:10.7554/elife.91079 · Cited by 23 · see citing works
Wang, Y., Gao, P., Li, F., & Du, J. (2022) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2022.06.010 · Cited by 22 · see citing works
Butler, A. E., Nandakumar, M., Sathyapalan, T., Brennan, E., & Atkin, S. L. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26010321 · Cited by 21 · see citing works
Vascular Biology of Arterial Aneurysms
Costa, D., Andreucci, M., Ielapi, N., Serraino, G. F., Mastroroberto, P., Bracale, U. M., & Serra, R. (2023) · Annals of Vascular Surgery · doi:10.1016/j.avsg.2023.04.008 · Cited by 19 · see citing works
Łażewski, D., Kucińska, M., Potapskiy, E., Kuźmińska, J., Popenda, Ł., Tężyk, A., Gośliński, T. A., Wierzchowski, M., & Murias, M. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24021467 · Cited by 18 · see citing works
Vascular Pathobiology: Atherosclerosis and Large Vessel Disease
Bonafiglia, Q. A., Bendeck, M. P., & Gotlieb, A. I. (2022) · Elsevier eBooks · doi:10.1016/b978-0-12-822224-9.00006-2 · Cited by 18 · see citing works
Genome-wide association study of early liveweight traits in fat-tailed Akkaraman lambs
Çınar, M. U., Arslan, K., Sohel, M. M. H., Bayram, D., Piel, L. M. W., White, S. N., Daldaban, F., Aksel, E. G., & Akyüz, B. (2023) · PLoS ONE · doi:10.1371/journal.pone.0291805 · Cited by 15 · see citing works
Sharma, D., & Singh, N. K. (2021) · Reviews of physiology, biochemistry and pharmacology · doi:10.1007/112_2021_67 · Cited by 14 · see citing works
Molecular analysis of encapsulated papillary carcinoma of the breast with and without invasion
Schwartz, C. J., Boroujeni, A. M., Khodadadi‐Jamayran, A., Heguy, A., Snuderl, M., Jour, G., Cotzia, P., & Darvishian, F. (2021) · Human Pathology · doi:10.1016/j.humpath.2021.02.005 · Cited by 14 · see citing works
The polymorphisms of extracellular matrix-remodeling genes are associated with pelvic organ prolapse
Li, L., Ma, Y., Yang, H., Sun, Z., Chen, J., & Zhu, L. (2022) · International Urogynecology Journal · doi:10.1007/s00192-021-04917-5 · Cited by 14 · see citing works
Zhu, W., Shi, L., Gong, Y., Zhuo, L., Wang, S., Chen, S., Zhang, B., & Ke, B. (2022) · Thoracic Cancer · doi:10.1111/1759-7714.14354 · Cited by 14 · see citing works
Ye, Z., & Zheng, J. (2021) · Frontiers in Genetics · doi:10.3389/fgene.2021.660989 · Cited by 13 · see citing works
Kilic, T., Okuno, K., Eguchi, S., & Kassiri, Z. (2022) · Hypertension · doi:10.1161/hypertensionaha.122.17963 · Cited by 13 · see citing works
Zhang, L., Zhao, F., Li, C., Li, H., Tang, Q., Chen, Y., Yao, Y., Ding, Z., Xu, Y., Chen, A., et al. (2020) · Placenta · doi:10.1016/j.placenta.2020.02.013 · Cited by 11 · see citing works
Hult, E. M., Gurczynski, S. J., & Moore, B. B. (2021) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00107.2021 · Cited by 10 · see citing works
Advances in targeting the extracellular matrix for glaucoma therapy: current updates
Agarwal, R., & Iezhitsa, I. N. (2023) · Expert Opinion on Therapeutic Targets · doi:10.1080/14728222.2023.2293748 · Cited by 10 · see citing works
Loss of ADAMTS5 promotes vascular calcification via versican/integrin β1/FAK signal
Zhu, Z., Liu, H., Feng, L., Lu, L., Zhu, J., Liang, Q., Lan, Z., Ye, Y., Wang, S., Chen, A., et al. (2025) · Atherosclerosis · doi:10.1016/j.atherosclerosis.2025.119190 · Cited by 10 · see citing works
Qiu, Y., Sha, L., Zhang, X., Li, G., Zhu, W., & Xu, Q. (2022) · Frontiers in Aging Neuroscience · doi:10.3389/fnagi.2022.896522 · Cited by 9 · see citing works
Rhode, H., Lüse, A., Tautkus, B., Nabity, M. B., John-Kroegel, U., Weigel, F., Dost, A., Schitke, J., Metzing, O., Boeckhaus, J., et al. (2023) · Kidney International Reports · doi:10.1016/j.ekir.2023.09.028 · Cited by 9 · see citing works
Xu, S.-Q., Sie, Z.-Y., Hsu, J., & Tan, K. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c01980 · Cited by 9 · see citing works
Oh, S., Lee, S., Jin, H., Choi, S.-H., Cha, C.-K., Lee, J., Kwack, K., Kim, S. G., & Choi, S. (2025) · Scientific Reports · doi:10.1038/s41598-024-84237-y · Cited by 8 · see citing works
Costa, D., Ielapi, N., Minici, R., Bevacqua, E., Ciranni, S., Cristodoro, L., Torcia, G., Taranto, M. D. D., Bracale, U. M., Andreucci, M., et al. (2023) · Journal of Vascular Diseases · doi:10.3390/jvd2030021 · Cited by 8 · see citing works
Wang, W., Zhang, H., Hou, C., Liu, Q., Yang, S.-Y., Zhang, Z., Yang, W., & Yang, X. (2021) · Aging · doi:10.18632/aging.202948 · Cited by 8 · see citing works
Li, S., Tao, W., Huang, Z., Yan, L., Chen, B., Zeng, C., & Chen, F. (2022) · Journal of Inflammation Research · doi:10.2147/jir.s347754 · Cited by 8 · see citing works
Sabaa, A. A., Shen, Q., Lennmyr, E. B., Enblad, A. P., Gammelgård, G., Molin, D. L., Hein, A., Freyhult, E., Kamali‐Moghaddam, M., Höglund, M., et al. (2022) · New Biotechnology · doi:10.1016/j.nbt.2022.06.005 · Cited by 8 · see citing works
Transcriptional regulation of postnatal aortic development
Weiss, D., Yeung, N., Ramachandra, A. B., & Humphrey, J. D. (2024) · Cells and Development · doi:10.1016/j.cdev.2024.203971 · Cited by 7 · see citing works
Protein-Labeling Fluorescent Probe Reveals Ectodomain Shedding of Transmembrane Carbonic Anhydrases
Lin, F.-L., Yen, J.-T., Fang, P.-W., Xu, S.-Q., Lin, J.-C., & Tan, K. (2022) · ACS Chemical Biology · doi:10.1021/acschembio.2c00679 · Cited by 7 · see citing works
Aberrant expression of ADAM9 in ovarian cancer and its clinical significance
Guo, T., Yuan, D., Lin, M., Zhu, D., Xu, N., & Wang, J. (2019) · Journal of Clinical Laboratory Analysis · doi:10.1002/jcla.23136 · Cited by 7 · see citing works
Mariano, A., Russo, R., d’Abusco, A. S., & Superti, F. (2025) · Current Issues in Molecular Biology · doi:10.3390/cimb47090731 · Cited by 6 · see citing works
Exploring the macromolecules for secretory pathway in cancer disease
Selvaraj, C., Panwar, U., Ramalingam, K. R., Vijayakumar, R., & Singh, S. K. (2022) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2022.10.003 · Cited by 6 · see citing works
Protein-Labeling Fluorescent Probe for Folate Receptor α
Fang, P.-W., Lin, Y., Fan, S., Panja, A., Xu, S.-Q., Lee, S., & Tan, K. (2023) · Analytical Chemistry · doi:10.1021/acs.analchem.3c02215 · Cited by 6 · see citing works
miR-520d suppresses rapid pacing-induced apoptosis of atrial myocytes through mediation of ADAM10
Fu, Q., Tang, Y., Peng, J., He, J., Zou, Q., Yan, S., Zheng, Z., & Pan, H. (2021) · Journal of Molecular Histology · doi:10.1007/s10735-020-09938-w · Cited by 6 · see citing works
Li, X., Pan, F., He, B., & Fang, C. (2021) · Open Life Sciences · doi:10.1515/biol-2021-0081 · Cited by 6 · see citing works
The function of metalloproteinases in pathophysiology of inflammatory bowel disease and colon cancer
Manzanares, L. D., Herrnreiter, C. J., Hirst, J., & Sumagin, R. (2025) · Journal of Leukocyte Biology · doi:10.1093/jleuko/qiaf116 · Cited by 5 · see citing works
Nappi, F. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms262210825 · Cited by 4 · see citing works
Function and prognostic value of basement membrane -related genes in lung adenocarcinoma
Zhang, Y., Li, T., Liu, H., & Wang, L. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1185380 · Cited by 4 · see citing works
Gerenčer, M., & McGuffin, L. J. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1177691 · Cited by 4 · see citing works
Večurkovská, I., Stupák, M., Kaťuchová, J., Roškovičová, V., & Mašlanková, J. (2023) · Physiological Research · doi:10.33549/physiolres.935228 · Cited by 4 · see citing works
A failure of forward translation? The case of neuroprotection
Lee, J., Rosand, J. M., & Cruchaga, C. (2021) · Vessel Plus · doi:10.20517/2574-1209.2020.72 · Cited by 4 · see citing works
ADAM10 and ADAM17—Novel Players in Retinoblastoma Carcinogenesis
Meenen, D. V., Doege, A., Alefeld, E., Haase, A., Beier, M., Kiefer, T., Biewald, E. M., Metz, K. A., Dräger, O., Busch, M. A., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232012621 · Cited by 4 · see citing works
Gao, S., Wu, F., Chen, X., Yang, Y., Zhu, Y., Liang, X., Shang, J., Bao, X., Luo, Y., Chen, H., et al. (2021) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2021/1967158 · Cited by 4 · see citing works
Targeting with toxins: an overview of venom peptides in drug delivery
Mazurs, A., Mauriņa, B., Bandere, D., & Logviss, K. (2025) · International Journal of Pharmaceutics · doi:10.1016/j.ijpharm.2025.126193 · Cited by 3 · see citing works
Elevated Expression of ADAM10 Induced by HPV E6 Influences the Prognosis of Cervical Cancer
Guo, X., Dou, Y., Liu, S., Du, Y., Guo, R., Yue, Y., Xu, Y., Liu, X., & Xu, Y. (2023) · Genetic Testing and Molecular Biomarkers · doi:10.1089/gtmb.2022.0170 · Cited by 3 · see citing works
Ji, T., Wang, K., Fan, J., Huang, J., Wang, M.-Q., Dong, X., Shi, Y.-J., Manning, L., Zhang, X., Shao, Z.-Y., et al. (2019) · bioRxiv · doi:10.1101/734830 · Cited by 2 · see citing works
Wang, N., Liu, Y., Sun, K., Chen, B., Sui, Y., Wang, Z., Jiang, X., Li, L., Li, Q., Feng, J., et al. (2025) · American Journal of Physiology-Endocrinology and Metabolism · doi:10.1152/ajpendo.00045.2025 · Cited by 2 · see citing works
Ma, Y., Zhang, J., Gong, J., Yang, W., Huang, J., & Sun, Y. (2025) · Journal of Ethnopharmacology · doi:10.1016/j.jep.2025.120580 · Cited by 2 · see citing works
ADAM and ADAMTS Proteases in Breast Cancer: Molecular Mechanisms and Therapeutic Implications
Badhai, C., Singh, M. R., Dwivedi, S. D., & Singh, D. (2025) · Clinical Breast Cancer · doi:10.1016/j.clbc.2025.12.001 · Cited by 2 · see citing works
Žagar, A. M., Kolobarić, N., Šušnjara, P., Mihaljević, J., Mihaljević, Z., & Drenjancevic, I. (2026) · Life · doi:10.3390/life16040642 · Cited by 2 · see citing works
Liang, C., Howard, H. R., Chen, S., Choi, W., Cao, S., Chien, A., Zou, K., Kassiou, M., Delerue, F., Jung, H. S., et al. (2026) · Advanced Healthcare Materials · doi:10.1002/adhm.202504842 · Cited by 2 · see citing works
Expression of ADAMTS13 in human endometrium and its potential role in recurrent pregnancy loss
Feng, Y., Li, X., Chen, X., Zhao, M., Wang, Q., Bai, J., Mao, M., & Guo, R. (2021) · Archives of Medical Science · doi:10.5114/aoms/133138 · Cited by 2 · see citing works
Dysregulation of metalloproteinases in spinal ligament degeneration
Wang, C., Wei, Z., Yu, T., & Zhang, L. (2023) · Connective Tissue Research · doi:10.1080/03008207.2022.2160327 · Cited by 2 · see citing works
Prospective of Pancreatic Cancer Diagnosis Using Cardiac Sensing
Singh, M., Anvekar, P., Baraskar, B., Pallipamu, N., Gadam, S., Cherukuri, A. S. S., Damani, D. N., Kulkarni, K., & Arunachalam, S. P. (2023) · Journal of Imaging · doi:10.3390/jimaging9080149 · Cited by 3 · see citing works
Adam19 Deficiency Impacts Pulmonary Function: Human GWAS Follow-up in a Mouse Knockout Model
Li, H., House, J. S., Nichols, C. E., Gruzdev, A., Ward, J. M., Li, J., Wyss, A. B., Haque, E., Edin, M. L., Elmore, S. A., et al. (2024) · Lung · doi:10.1007/s00408-024-00738-7 · Cited by 2 · see citing works
Rami, A., Damizadeh, B., Behdani, M., & Kazemi‐Lomedasht, F. (2024) · Protein and Peptide Letters · doi:10.2174/0109298665321842240819073453 · Cited by 2 · see citing works
Kim, H.-D., Choi, H., Park, J.-Y., & Kim, C. (2025) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2025.110436 · Cited by 2 · see citing works
Atmospheric pressure plasma treatment increases the antioxidant capacity of the serum in vitro
Guo, Y., Zhang, X., Xing, Y., Liu, Y., Liu, Y., Jia, L., Xu, L., He, G., Ouyang, J., & Yan, X. (2025) · Scientific Reports · doi:10.1038/s41598-025-03914-8 · Cited by 2 · see citing works
Macaulay, A. D., Ortman, C. S., Moore, K. R. J., & Baltz, J. M. (2022) · Biology of Reproduction · doi:10.1093/biolre/ioac185 · Cited by 2 · see citing works
An overview of the role of MMP-8 and ADAM-33 in bronchial asthma
Celik, K., Tacheva, T., Dimov, D., & Vlaykova, T. I. (2024) · Biotechnology & Biotechnological Equipment · doi:10.1080/13102818.2024.2373855 · Cited by 1 · see citing works
Naidoo, P., & Naicker, T. (2025) · International Journal of Molecular Sciences · doi:10.3390/ijms26094103 · Cited by 1 · see citing works
Anis, H. M., Rakha, N. M., Kassem, D., & Kamal, A. M. (2025) · BMC Cancer · doi:10.1186/s12885-025-14292-9 · Cited by 1 · see citing works
Gorgojo-Galindo, Ó., Álvarez-Bardón, M., García-Concejo, A., López-Herrero, R., Heredia‐Rodríguez, M., Tamayo, E., & Gonzalo‐Benito, H. (2025) · Inflammation Research · doi:10.1007/s00011-025-02056-x · Cited by 1 · see citing works
Mechnine, A., Saih, A., Wakrim, L., & Aarab, A. (2025) · JMIR Bioinformatics and Biotechnology · doi:10.2196/72133 · Cited by 1 · see citing works
Wu, X., Tsuchiya, I., Aung, K. Z., Qiao, Q., Fardo, D. W., Nelson, P. T., Abner, E. L., James, B. D., Norris, C. M., & Katsumata, Y. (2025) · Journal of Alzheimer s Disease · doi:10.1177/13872877251385220 · Cited by 1 · see citing works
Zhang, X., Li, X., Cheng, Y., Wei, L., Liu, F., Li, L., Zhang, W., & Yan, X. (2025) · Food Science & Nutrition · doi:10.1002/fsn3.71223 · Cited by 1 · see citing works
Xu, Y., Xiong, J., Wu, Y., Wu, X., Shi, H. Y., & Xu, S. (2025) · Molecular Neurobiology · doi:10.1007/s12035-025-04977-4 · Cited by 1 · see citing works
Drees, L., Schuh, R., & Behr, M. (2022) · SSRN Electronic Journal · doi:10.2139/ssrn.4178533 · Cited by 1 · see citing works
Extracellular matrix microenvironment and vascular homeostasis
Gao, Y., Zheng, J., & Kong, W. (2022) · Scientia Sinica Vitae · doi:10.1360/ssv-2021-0263
Alper, M., Aydemir, A. T., & KOCKAR, F. T. (2022) · Süleyman Demirel Üniversitesi Sağlık Bilimleri Dergisi · doi:10.22312/sdusbed.1053455
Zarkesh, M., Arab, N., Heydarzadeh, S., Nozhat, Z., Abooshahab, R., Jahromi, M. S., Fanaei, S. A., & Hedayati, M. (2022) · Research Square · doi:10.21203/rs.3.rs-2028260/v1
Extracellular Matrix Remodeling Enzymes as Targets for Natural Antiangiogenic Compounds
Carrillo, P., García‐Caballero, M., Bernal, M., Manrique-Poyato, M. I., Martı́nez-Poveda, B., Quesada, A. R., & Medina, M. Á. (2022) · Biology of extracellular matrix · doi:10.1007/978-3-031-19616-4_6
Yuan, K., Qi, P., Hao, X., Hao, Q., & Zhao, P. (2023) · Journal of Biomaterials and Tissue Engineering · doi:10.1166/jbt.2023.3244
Farahbakhsh, N., Hooshanginezhad, Z., Saleh, S., Alaei, F., Azizi, F., & Shojaie, M. (2023) · PubMed Central · doi:10.48305/arya.2023.41105.2846
- Authors
- Zhong, S., & Khalil, R. A.
- Affiliations
- Brigham and Women's Hospital (US)
- Corresponding author
- Khalil, Raouf A.
- Venue
- Biochemical Pharmacology
- Publisher
- Elsevier BV
- Published
- 2019-06
- Volume
- 164
- Pages
- 188-204
- ISSN
- 0006-2952 (ISSN-L)
- PMC
- PMC6580420
- OpenAlex
- W2923430092
- Cited by
- 119
- References
- 208
- Citations by year
- 2026: 9 · 2025: 26 · 2024: 7 · 2023: 19 · 2022: 27 · 2021: 17 · 2020: 10 · 2019: 4
- FWCI
- 1.39
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Biochemical Pharmacology (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Heart, Lung, and Blood Institute (HL-65998, HL-111775)
- Jilin University
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
- Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
- Health Sciences › Medicine › Cardiology and Cardiovascular Medicine › Renin-Angiotensin System Studies
- Keywords
- Adam, ADAMTS, proteolytic enzymes, protein shedding, vascular biology, cardiovascular disease, atherosclerosis, hypertension, aneurysm, coronary artery disease, myocardial infarction, heart failure, vascular smooth muscle cell proliferation, angiogenesis, tissue inhibitors of metalloproteinases, small molecule inhibitors, biomarkers, therapeutic target
- MeSH terms
- Animals, Endothelium, Vascular, Humans, Vascular Diseases, Disintegrins, Thrombospondins, Amino Acid Motifs, ADAM Proteins, Matrix Metalloproteinase Inhibitors
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
