More of the catalytic triad
- 1 February 1990
- journal article
- Published by Springer Nature in Nature
- Vol. 343 (6260) , 694-695
- https://doi.org/10.1038/343694a0
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
- Structure of human pancreatic lipaseNature, 1990
- A serine protease triad forms the catalytic centre of a triacylglycerol lipaseNature, 1990
- Organization of the human lipoprotein lipase gene and evolution of the lipase gene family.Proceedings of the National Academy of Sciences, 1989
- How do serine proteases really work?Biochemistry, 1989
- The Catalytic Role of the Active Site Aspartic Acid in Serine ProteasesScience, 1987
- Structure and Possible Catalytic Residues of Taka-Amylase AThe Journal of Biochemistry, 1984
- Direct determination of the protonation states of aspartic acid-102 and histidine-57 in the tetrahedral intermediate of the serine proteases: neutron structure of trypsinBiochemistry, 1981
- Crystallographic refinement and atomic models of the intact immunoglobulin molecule Kol and its antigen-binding fragment at 3.0 Å and 1.9 Å resolutionJournal of Molecular Biology, 1980
- Role of a Buried Acid Group in the Mechanism of Action of ChymotrypsinNature, 1969
- Structure of Subtilisin BPN′ at 2.5 Å ResolutionNature, 1969