ADAM, a novel family of membrane proteins containing A Disintegrin And Metalloprotease domain: multipotential functions in cell-cell and cell-matrix interactions.
Open Access
- 15 October 1995
- journal article
- review article
- Published by Rockefeller University Press in The Journal of cell biology
- Vol. 131 (2) , 275-278
- https://doi.org/10.1083/jcb.131.2.275
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- Mouse egg integrin α6β1functions as a sperm receptorCell, 1995
- An old enzyme with a new function: purification and characterization of a distinct matrix-degrading metalloproteinase in rat kidney cortex and its identification as meprin.The Journal of cell biology, 1994
- A 28-kDa Protein with Disintegrin-like Structure (Jararhagin-C) Purified from Bothrops jararaca Venom Inhibits Collagen- and ADP-Induced Platelet AggregationBiochemical and Biophysical Research Communications, 1994
- Membrane Interaction and Conformational Properties of the Putative Fusion Peptide of PH-30, a Protein Active in Sperm-Egg FusionBiochemistry, 1994
- Comparison of Disintegrins with Limited Variation in the RGD Loop in Their Binding to Purified Integrins αIIbβ3, αVβ3 and α5β1 and in Cell Adhesion InhibitionCell Adhesion and Communication, 1994
- Membrane FusionScience, 1992
- A potential fusion peptide and an integrin ligand domain in a protein active in sperm–egg fusionNature, 1992
- Contact and adhesive specificities in the associations, migrations, and targeting of cells and axonsCell, 1992
- Proteolytic processing of a protein involved in sperm-egg fusion correlates with acquisition of fertilization competence.The Journal of cell biology, 1990
- Molecular cloning of cDNA encoding MS2 antigen, a novel cell surface antigen strongly expressed in murine monocytic lineageInternational Immunology, 1990