Structure–Function Analysis of the ADAM Family of Disintegrin-Like and Metalloproteinase-Containing Proteins (Review)
By A. Stone, Michael R. Kroeger, Q. Sang. 1999
How researchers see this paper
The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.
- A. Zolkiewska
- B. Hayward
- R. Albrechtsen
- U. Wewer
- S. P. Manning
- D. Torrey
- J. Simon
- Joyce McKenny
Citations in the corpus
- The Cysteine-Rich Domain of Human Adam 12 Supports Cell Adhesion through Syndecans and Triggers Signaling Events That Lead to β1 Integrin–Dependent Cell Spreading (2000, background): “The Journal of Cell Biology, Volume 149, 2000 1144 stitute a recently discovered family of cell adhesion receptors (Wolfsberg and White, 1996; Blobel, 1997; Black and White, 1998; Schlöndorff and Blobel, 1999; Stone et al., 1999; Primakoff and Myles, 2000).”
- A Disintegrin and Metalloprotease (ADAM): Historical Overview of Their Functions (2016, background): “In addition, the tails of some ADAMs have intrinsic signaling activity and regulate proteolysis [5].”
- Association of the ADAM33 gene with asthma and bronchial hyperresponsiveness (2002, background): “The ADAM gene family is a subgroup of the zinc-dependent metalloproteinase superfamil”