Purification and characterization of a protein inhibitor of the 20S proteasome (macropain)
- 12 March 1992
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1119 (3) , 303-311
- https://doi.org/10.1016/0167-4838(92)90218-3
Abstract
No abstract availableKeywords
This publication has 20 references indexed in Scilit:
- The primary structures of four subunits of the human, high-molecular-weight proteinase, macropain (proteasome), are distinct but homologousBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1991
- Cloning and sequencing of the gene encoding the large (α‐) subunit of the proteasome from Thermoplasma acidophilumFEBS Letters, 1991
- The multicatalytic proteinase complex, a major extralysosomal proteolytic systemBiochemistry, 1990
- Molecular cloning of cDNAs for two subunits of rat multicatalytic proteinaseEuropean Journal of Biochemistry, 1990
- cDNA cloning and sequencing of component C8 of proteasomes from rat hepatoma cellsBiochemical and Biophysical Research Communications, 1990
- cDNA cloning and sequencing of component C5 of proteasomes from rat hepatoma cellsFEBS Letters, 1990
- Relationships among the subunits of the high molecular weight proteinase, macropain (proteasome)Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1990
- The Drosophila PROS-28.1 gene is a member of the proteasome gene familyGene, 1990
- Pituitary multicatalytic proteinase complex. Specificity of components and aspects of proteolytic activityBiochemistry, 1989
- The multicatalytic proteinase of mammalian cellsArchives of Biochemistry and Biophysics, 1989