The thrombospondins.
By J. Adams, J. Lawler. 2011
575 citations recorded by the source corpus.
Subfields: Cellular and Molecular Neuroscience, Molecular Biology, Plant Science
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In Molecular Biology
- D. Edwards
- Alexandra Naba
- R. Hynes
- Peter Friedl
- M. Humphries
- Stephanie Alexander
- Jonathan C. Kagan
- R. Medzhitov
Citations in the corpus
- The Pathogenesis of Cardiac Fibrosis (2013, unknown): “TSP1, a potent angiostatic mediator with an essential role in TGF-β activation [144], is upregulated in the infarcted and pressure-overloaded myocardium [141, 145], and is localized in areas with abundant myofibroblasts.”
- Extracellular matrix structure. (2016, background): “Although matricellular proteins are structurally variable, they contain common ECM structural motifs and they exert similar functions [221-225].”
- The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) family (2015, background): “The ancillary domain in all ADAMTS enzymes contains an approximately 50-aminoacid thrombospondin-like repeat (TSR) that is similar to the type I repeats of thrombospondins 1 and 2 [28], followed by a cysteine-rich region of slightly more than 100 amino acid residues (in all except ADAMTS12) that con”
- Overview of the matrisome--an inventory of extracellular matrix constituents and functions. (2012, background): “Similar evolution by duplication and diversification from a primordial gene shared by all bilateria is seen in the case of thrombospondins (see Adams and Lawler 2011), although in this case the diversification has involved more extensive evolution of the domain architecture than is the case for the…”