The ADAMTS metalloproteinases.
By S. Porter, I. Clark, L. Kevorkian, D. Edwards. 2005
807 citations recorded by the source corpus.
Subfields: Cancer Research, Hematology, Immunology and Allergy
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Citations in the corpus
- A Disintegrin and Metalloproteinase (ADAM) and ADAM with Thrombospondin Motifs (ADAMTS) Family in Vascular Biology and Disease (2019, background): “A similar autocatalytic activation process has been reported for ADAMTS-1, 4, 8, 9 and 12 [42], suggesting that this autocatalytic activation and regulation could be a common feature of most ADAMTS proteases [41].”
- Systems Genetics Approach Identifies Gene Pathways and Adamts2 as Drivers of Isoproterenol-Induced Cardiac Hypertrophy and Cardiomyopathy in Mice (2016, neutral): “*p % 0.05; **p % 0.01; ***p % 0.001. severe skin fragility and joint laxity (hyperextensibility) (Porter et al., 2005).”
- CCBE1 Enhances Lymphangiogenesis via A Disintegrin and Metalloprotease With Thrombospondin Motifs-3–Mediated Vascular Endothelial Growth Factor-C Activation (2014, background): “Apart from ADAMTS3, 2 other proteases, ADAMTS2 and ADAMTS14, belong to the procollagenase subfamily of ADAMTS proteases.(24) Interestingly, the ADAMTS1 gene deletion in mice results in deficient ovarian lymphangiogenesis.”
- ADAM and ADAMTS gene expression in native and wound healing human lens epithelial cells (2010, background): “Several ADAM/ ADAMTS enzymes have roles in cell differentiation and cell guidance mechanisms during development [2,3].”
- Association between plasma ADAMTS-7 levels and ventricular remodeling in patients with acute myocardial infarction (2015, neutral): “However, the relevance of the ADAMTS family to cardiovascular disease remains largely unknown [10].”
- The ADAM metalloproteinases (2008, background): “The disintegrin domain is followed in the ADAMs by the cysteine-rich domain, which is also seen in the SVMPs and ADAMTSs, though in the latter the first of a series of C-terminal thrombospondin-like repeats is interposed (Porter et al., 2005).”
- The procollagen N-proteinases ADAMTS2, 3 and 14 in pathophysiology. (2015, methodology): “A similar activation process was also reported for ADAMTS1, 4, 8, 9 and 12 [20], suggesting that this step of regulation could be a common feature of the ADAMTS proteases.”
- Matrix metalloproteinases (MMPs) in health and disease: an overview. (2006, background): “Although MMP-3 (stromelysin-1) is capable of degrading cartilage proteoglycans, ADAMTS-4 and -5 appear to be the main mediators of aggrecan degradation in RA and OA (38, 39).”
- What is Intervertebral Disc Degeneration, and What Causes It? (2006, background): “Disc cells synthesize their matrix and break down existing matrix by producing and activating degradative enzymes, including matrix metalloproteinases (MMPs) and a disintegrin and metalloproteinase (ADAMS).[14-20] Molecular markers of matrix turnover are naturally most plentiful during growth but us”
- Emerging roles of proteases in tumour suppression (2007, background): “ADAMTSs These are members of a family that includes 19 human enzymes, which show some structural relationships with other metallo-proteinases such as MMPs and ADAMs (disintegrin and metalloproteinase domain proteases”
- The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) family (2015, background): “Once again, versican heterozygosity exacerbated the phenotype seen with mice deficient in ADAMTS20 Table 1 ADAMTS genes: their chromosomal positions, major tissue expression locations, expression-inducing factors bstrates, and associations with pathologies Gene Location Expression Factors inducing o”
- Knockout of Adamts7, A Novel CAD Locus in Humans, Reduces Atherosclerosis in Mice (2015, neutral): “specificity.(8,9) Previous research on ADAMTS7 has centered”
- Matrix metalloproteinases: role in arthritis. (2006, background): “Their enzymatic activities are varied and include cleaving collagen propeptides, inhibiting angiogenesis, and degrading cartilage proteoglycans (33).”
- Calcium pentosan polysulfate directly inhibits enzymatic activity of ADAMTS4 (aggrecanase‐1) in osteoarthritic chondrocytes (2008, background): “8, 9 and 15 are known to exhibit the signature aggrecanase activity (cleavage at the Glu(392)–Ala(393) bond) [1,2].”