The ADAM gene family: surface proteins with adhesion and protease activity.

By P. Primakoff, D. Myles. Trends in Genetics, 2000

602 citations recorded by the source corpus.

Subfields: Immunology and Allergy, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/4112de06636bd229fa0ae88aaa1763af71b04bab

How researchers see this paper

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

In Immunology and Allergy

1. C. Blobel
2. Zena Werb
3. R. Fässler
4. D. Falls

In Molecular Biology

1. D. Edwards
2. C. Blobel
3. M. Handsley
4. C. Pennington
5. R. Baron
6. D. Warburton
7. D. Sheppard
8. S. Buckley

Citations in the corpus

• Metalloprotease‐disintegrin ADAM8: Expression analysis and targeted deletion in mice (2005, background): “…processes, including sperm–egg interactions, neurogenesis, neovascularization, and heart development (Black and White, 1998; Schlöndorff and Blobel, 1999; Primakoff and Myles, 2000; Horiuchi et al., 2003; Jackson et al., 2003; Seals and Courtneidge, 2003; Kurohara et al., 2004; Zhou et al., 2004).”
• Potential Role for ADAM15 in Pathological Neovascularization in Mice (2003, background): “The relevant protein domains are the metalloprotease domain, which is catalytically active in ADAM15 (44); the disintegrin domain and cysteinerich region, which may mediate cell-cell or cell matrix interaction; and the cytoplasmic domain, which may have a role in signaling or intracellular transport”
• Neuregulins: functions, forms, and signaling strategies. (2003, background): “[107] P.”
• Positive selection at reproductive ADAM genes with potential intercellular binding activity. (2004, background): “Members of the ADAM family may also function as proteases based on whether a metalloprotease domain is present and active in the protein (Primakoff and Myles 2000).”
• Phenotypic Analysis of Meltrin α (ADAM12)-Deficient Mice: Involvement of Meltrin α in Adipogenesis and Myogenesis (2003, background): “ADAMs are thought to be involved in various biological functions, including fertilization, myogenesis, neurogenesis, and the development of various epithelial tissues (3, 30, 35).”
• How matrix metalloproteinases regulate cell behavior. (2001, background): “The ADAMs are transmembrane cell surface proteins that have a disintegrin and metalloproteinase domain (Primakoff & Myles 2000).”
• 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): “stitute a recently discovered family of cell adhesion receptors (Wolfsberg and White, 1996; Blobel, 1997; Black and White, 1998; Schlondorff and Blobel, 1999; Stone et al., 1999; Primakoff and Myles, 2000 ).”
• The ADAM metalloproteinases (2008, background): “The first mammalian ADAMs identified were the two subunits of the heterodimeric sperm protein fertilin, ADAM1 (fertilin-a) and ADAM2 (fertilin-b; Blobel et al., 1992) , whose functions have been studied extensively in rodents (Primakoff and Myles, 2000; Primakoff and Myles, 2002) .”