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A Disintegrin-like and Metalloprotease (Reprolysin-type) with Thrombospondin Type 1 Motif (ADAMTS) Superfamily: Functions and Mechanisms
Open accessAbstract
Together with seven ADAMTS-like proteins, the 19 mammalian ADAMTS proteases constitute a superfamily. ADAMTS proteases are secreted zinc metalloproteases whose hallmark is an ancillary domain containing one or more thrombospondin type 1 repeats. ADAMTS-like proteins resemble ADAMTS ancillary domains and lack proteolytic activity. Vertebrate expansion of the superfamily reflects emergence of new substrates, duplication of proteolytic activities in new contexts, and cooperative functions of the duplicated genes. ADAMTS proteases are involved in maturation of procollagen and von Willebrand factor, as well as in extracellular matrix proteolysis relating to morphogenesis, angiogenesis, ovulation, cancer, and arthritis. New insights into ADAMTS mechanisms indicate significant regulatory roles for ADAMTS ancillary domains, propeptide processing, and glycosylation. ADAMTS-like proteins appear to have regulatory roles in the extracellular matrix.
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Colige, A., Sieron, A. L., Li, S.-W., Schwarze, U., Petty, E., Wertelecki, W., Wilcox, W., Krakow, D., Cohn, D. H., Reardon, W., et al. (1999) · The American Journal of Human Genetics · doi:10.1086/302504 · Cited by 370
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Metadata
- Authors
- Apte, S. S.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2009-11
- Volume
- 284
- Issue
- 46
- Pages
- 31493-31497
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W1974537190
- Cited by
- 506
- References
- 1
- FWCI
- 10.10
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: A Disintegrin-like and Metalloprotease (Reprolysin-type) with Thrombospondin Type 1 Motif (ADAMTS) Superfamily: Functions and Mechanisms. https://app.cochat.ai/papers/10.1074/jbc.r109.052340
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- Apte, S. S. (2009). A Disintegrin-like and Metalloprotease (Reprolysin-type) with Thrombospondin Type 1 Motif (ADAMTS) Superfamily: Functions and Mechanisms. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.r109.052340
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