ADAMs: focus on the protease domain
- 1 October 1998
- journal article
- review article
- Published by Elsevier BV in Current Opinion in Cell Biology
- Vol. 10 (5), 654-659
- https://doi.org/10.1016/s0955-0674(98)80042-2
Abstract
No abstract availableKeywords
This publication has 37 references indexed in Scilit:
- The Metallo-Disintegrin ADAM10 (MADM) from Bovine Kidney Has Type IV Collagenase Activityin VitroBiochemical and Biophysical Research Communications, 1998
- Specific Interaction of the Recombinant Disintegrin-like Domain of MDC-15 (Metargidin, ADAM-15) with Integrin αvβ3Journal of Biological Chemistry, 1998
- Cloning and Initial Characterization of Mouse Meltrin β and Analysis of the Expression of Four MetalloproteaseDisintegrins in Bone CellsPublished by Elsevier BV ,1998
- Cloning of a disintegrin metalloproteinase that processes precursor tumour-necrosis factor-αNature, 1997
- A metalloproteinase disintegrin that releases tumour-necrosis factor-α from cellsNature, 1997
- Purification of ADAM 10 from bovine spleen as a TNFα convertaseFEBS Letters, 1997
- Proteolytic Release of Membrane-Bound Angiotensin-Converting Enzyme: Role of the Juxtamembrane Stalk SequenceBiochemistry, 1996
- A metalloprotease-disintegrin participating in myoblast fusionNature, 1995
- The metzincins — Topological and sequential relations between the astacins, adamalysins, serralysins, and matrixins (collagenases) define a super family of zinc‐peptidasesProtein Science, 1995
- A nonsecretable cell surface mutant of tumor necrosis factor (TNF) kills by cell-to-cell contactCell, 1990