Post-translational processing of a major histocompatibility complex-encoded proteasome subunit, LMP-2
- 30 September 1993
- journal article
- Published by Elsevier BV in Molecular Immunology
- Vol. 30 (13), 1177-1183
- https://doi.org/10.1016/0161-5890(93)90136-y
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Proteasome subunits encoded in the MHC are not generally required for the processing of peptides bound by MHC class I moleculesNature, 1992
- Ham-2 corrects the class I antigen-processing defect in RMA-S cellsNature, 1992
- Homology of proteasome subunits to a major histocompatibility complex-linked LMP geneNature, 1991
- Structural and serological similarity of MHC-linked LMP and proteasome (multicatalytic proteinase) complexesNature, 1991
- Restored expression of major histocompatibility class I molecules by gene transfer of a putative peptide transporterNature, 1991
- Degradation of oxidized insulin B chain by the multiproteinase complex macropain (proteasome)Biochemistry, 1991
- N‐Terminal sequence similarities between components of the multicatalytic proteinase complexFEBS 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 LMP antigens: A stable MHC-controlled multisubunit protein complexHuman Immunology, 1986
- H–2-linked low-molecular weight polypeptide antigens assemble into an unusual macromolecular complexNature, 1984