Extended Substrate Recognition in Caspase-3 Revealed by High Resolution X-ray Structure Analysis
- 23 June 2006
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 359 (5) , 1378-1388
- https://doi.org/10.1016/j.jmb.2006.04.051
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- Ionic interactions near the loop L4 are important for maintaining the active-site environment and the dimer stability of (pro)caspase 3Biochemical Journal, 2004
- Molecular mechanisms of caspase regulation during apoptosisNature Reviews Molecular Cell Biology, 2004
- Irreversible Inhibitors of Serine, Cysteine, and Threonine ProteasesChemical Reviews, 2002
- Structural Basis for the Inhibition of Caspase-3 by XIAPCell, 2001
- The three-dimensional structure of caspase-8: an initiator enzyme in apoptosisStructure, 1999
- Mammalian Caspases: Structure, Activation, Substrates, and Functions During ApoptosisAnnual Review of Biochemistry, 1999
- Purification and catalytic properties of human caspase family membersCell Death & Differentiation, 1999
- PROCHECK: a program to check the stereochemical quality of protein structuresJournal of Applied Crystallography, 1993
- Improved methods for building protein models in electron density maps and the location of errors in these modelsActa Crystallographica Section A Foundations of Crystallography, 1991
- The basic difference in catalyses by serine and cysteine proteinases resides in charge stabilization in the transition stateJournal of Theoretical Biology, 1986