Enzyme theory holds water
Open Access
- 11 October 2006
- journal article
- editorial
- Published by Springer Nature in Nature
- Vol. 444 (7116) , 153-155
- https://doi.org/10.1038/nature05305
Abstract
No abstract availableKeywords
This publication has 11 references indexed in Scilit:
- Crystal structure of a rhomboid family intramembrane proteaseNature, 2006
- Three-dimensional structure of the γ-secretase complexBiochemical and Biophysical Research Communications, 2006
- Electron microscopic structure of purified, active γ-secretase reveals an aqueous intramembrane chamber and two poresProceedings of the National Academy of Sciences, 2006
- Reconstitution of intramembrane proteolysis in vitro reveals that pure rhomboid is sufficient for catalysis and specificityProceedings of the National Academy of Sciences, 2005
- Mechanism of intramembrane proteolysis investigated with purified rhomboid proteasesThe EMBO Journal, 2004
- Proteolysis as a Regulatory MechanismAnnual Review of Genetics, 2004
- Intramembrane Proteolysis: Theme and VariationsScience, 2004
- Proteolysis within the membrane: rhomboids revealedNature Reviews Molecular Cell Biology, 2004
- The rhomboids: a nearly ubiquitous family of intramembrane serine proteases that probably evolved by multiple ancient horizontal gene transfersGenome Biology, 2003
- Drosophila Rhomboid-1 Defines a Family of Putative Intramembrane Serine ProteasesCell, 2001