ADAMTS9 is a cell-autonomously acting, anti-angiogenic metalloprotease expressed by microvascular endothelial cells.

By B. Koo, D. Coe, Laura J. Dixon, R. Somerville, Courtney M. Nelson, Lauren W. Wang, M. Young, D. Lindner, S. Apte. 2010

107 citations recorded by the source corpus.

Subfields: Hematology, Immunology, Molecular Biology

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Hematology

1. Hideaki Nagase
2. D. Edwards
3. Gillian Murphy

In Immunology

1. S. Apte
2. T. Mead

In Molecular Biology

1. Hideaki Nagase
2. S. Apte
3. D. Edwards

Citations in the corpus

• ADAMTS proteins in human disorders (2018, background): “Because efficient ADAMTS9 secretion depends on the activity of one of its modifying enzymes B3GLCT (also known as B3GALTL) [42], it is intriguing that B3GLCT and ADAMTS9 are strongly expressed in the eye [42] and vascular endothelial cells [40] and each is associated with agerelated macular degenera”
• Metalloproteinase‐dependent and ‐independent processes contribute to inhibition of breast cancer cell migration, angiogenesis and liver metastasis by a disintegrin and metalloproteinase with thrombospondin motifs‐15 (2015, background): “Metalloproteinase-dependent antiangiogenic activity is displayed by ADAMTS-9, but the mechanism is as yet unknown as thrombospondin cleavage has been ruled out.(14) The identities of the cryptic angio-inhibitory substrates of ADAMTS-9 and -15 will be important to elucidate.”
• The ADAMTS (A Disintegrin and Metalloproteinase with Thrombospondin motifs) family (2015, background): “Metalloproteinase-dependent anti-angiogenic activity is displayed by ADAMTS9, but the mechanism is as yet unknown as thrombospondin cleavage has been ruled out [119].”