ADAMTS1 cleaves aggrecan at multiple sites and is differentially inhibited by metalloproteinase inhibitors.
By J. C. Rodríguez-Manzaneque, Jennifer Westling, S. Thai, A. Luque, V. Knäuper, Gillian Murphy, J. Sandy, M. Luisa Iruela-Arispe. 2002
239 citations recorded by the source corpus.
Subfields: Cell Biology, Cellular and Molecular Neuroscience, Oncology
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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): “The function of ADAMTS-1 can be suppressed by TIMP-2 and 3, but is not affected by TIMP-1 and 4 [57].”
- The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) family (2015, background): “The aggrecanase activity of ADAMTS1 is inhibited by both TIMP-2 and −3, but not by TIMP-1 and −4 [36].”
- Biosynthesis and Expression of a Disintegrin-like and Metalloproteinase Domain with Thrombospondin-1 Repeats-15 (2013, background): “The ADAMTS15 zymogen is processed extracellularly, similar to ADAMTS5 and ADAMTS9 (5, 6), and in contrast to ADAMTS1 and ADAMTS4, which are both activated intracellularly (8, 10, 34).”
- Matrix Metalloproteinases, Vascular Remodeling, and Vascular Disease. (2018, background): “…metalloproteinase inhibition profile including ADAM-10, ADAM-12, and ADAM-17 as well as a disintegrin and metalloproteinase with thrombospondin motif ADAMTS-1, ADAMTS-2, ADAMTS-4 and ADAMTS-5 (Amour et al., 2000; Kashiwagi et al., 2001; Rodriguez-Manzaneque et al., 2002; Jacobsen et al., 2008).”