Biochemical properties and functions of membrane-anchored metalloprotease-disintegrin proteins (ADAMs)
- 1 January 2003
- book chapter
- Published by Elsevier
- Vol. 54, 101-123
- https://doi.org/10.1016/s0070-2153(03)54006-6
Abstract
No abstract availableKeywords
This publication has 114 references indexed in Scilit:
- Structure−Activity Relationship of Hydroxamate-Based Inhibitors on the Secretases that Cleave the Amyloid Precursor Protein, Angiotensin Converting Enzyme, CD23, and Pro-Tumor Necrosis Factor-αBiochemistry, 2002
- The Lymphocyte Metalloprotease MDC-L (ADAM 28) Is a Ligand for the Integrin α4β1Journal of Biological Chemistry, 2002
- Metalloprotease-disintegrin ADAM 12 interacts with α-actinin-1Biochemical Journal, 2001
- Expression and Enzymatic Activity of Human Disintegrin and Metalloproteinase ADAM19/Meltrin BetaBiochemical and Biophysical Research Communications, 2001
- ADAM 12-S Cleaves IGFBP-3 and IGFBP-5 and Is Inhibited by TIMP-3Biochemical and Biophysical Research Communications, 2000
- Cloning and characterization of ADAM28: evidence for autocatalytic pro-domain removal and for cell surface localization of mature ADAM28Biochemical Journal, 2000
- Evidence for an interaction of the metalloprotease‒disintegrin tumour necrosis factor α convertase (TACE) with mitotic arrest deficient 2 (MAD2), and of the metalloprotease‒disintegrin MDC9 with a novel MAD2-related protein, MAD2βBiochemical Journal, 1999
- An Essential Role for Ectodomain Shedding in Mammalian DevelopmentScience, 1998
- KB-R7785, a novel matrix metalloproteinase inhibitor, exerts its antidiabetic effect by inhibiting tumor necrosis factor-α productionLife Sciences, 1997
- Metalloproteinase super–families and drug designNature Structural & Molecular Biology, 1994