A theoretical approach towards the identification of cleavage-determining amino acid motifs of the 20s proteasome
- 5 March 1999
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 286 (4) , 1251-1265
- https://doi.org/10.1006/jmbi.1998.2530
Abstract
No abstract availableKeywords
This publication has 28 references indexed in Scilit:
- On the size of the active site in proteases. I. PapainPublished by Elsevier ,2005
- Structure of 20S proteasome from yeast at 2.4Å resolutionNature, 1997
- A Single Residue Exchange Within a Viral CTL Epitope Alters Proteasome-Mediated Degradation Resulting in Lack of Antigen PresentationImmunity, 1996
- Incorporation of major histocompatibility complex – encoded subunits LMP2 and LMP7 changes the quality of the 20S proteasome polypeptide processing products independent of interferon‐γEuropean Journal of Immunology, 1995
- Contribution of proteasome-mediated proteolysis to the hierarchy of epitopes presented by major histocompatibility complex class I moleculesImmunity, 1995
- Existence of a molecular ruler in proteasomes suggested by analysis of degradation productsFEBS Letters, 1994
- PRE3, highly homologous to the human major histocompatibility complex‐linked LMP2 (RING12) gene, codes for a yeast proteasome subunit necessary for the peptidylglutamyl‐peptide hydrolyzing activityFEBS Letters, 1994
- Use of serine‐protease inhibitors as probes for the different proteolytic activities of the rat liver multicatalytic proteinase complexEuropean Journal of Biochemistry, 1992
- Pituitary multicatalytic proteinase complex. Specificity of components and aspects of proteolytic activityBiochemistry, 1989
- The apolar surface area of amino acids and its empirical correlation with hydrophobic free energyJournal of Theoretical Biology, 1984