Deletion of immunoproteasome subunits imprints on the transcriptome and has a broad impact on peptides presented by major histocompatibility complex I molecules.
de Verteuil, Danielle; Muratore-Schroeder, Tara L; Granados, Diana P; Fortier, Marie-Hélène; Hardy, Marie-Pierre; Bramoullé, Alexandre; Caron, Etienne; Vincent, Krystel; Mader, Sylvie; Lemieux, Sébastien; Thibault, Pierre; Perreault, Claude.
Mol Cell Proteomics
; 9(9): 2034-47, 2010 Sep.
Artigo em Inglês | MEDLINE | ID: mdl-20484733
Global proteome analysis identifies active immunoproteasome subunits in human platelets.
The adaptable major histocompatibility complex (MHC) fold: structure and function of nonclassical and MHC class I-like molecules.
Definition of Proteasomal Peptide Splicing Rules for High-Efficiency Spliced Peptide Presentation by MHC Class I Molecules.
T cell antigen receptor recognition of antigen-presenting molecules.
PA28 and the proteasome immunosubunits play a central and independent role in the production of MHC class I-binding peptides in vivo.
Emerging role of immunoproteasomes in pathophysiology.
Comparative genomic analysis of the major histocompatibility complex class I region in the teleost genus Oryzias.
Why the structure but not the activity of the immunoproteasome subunit low molecular mass polypeptide 2 rescues antigen presentation.
CD8(+) T cells of Listeria monocytogenes-infected mice recognize both linear and spliced proteasome products.
Peptide Splicing in the Proteasome Creates a Novel Type of Antigen with an Isopeptide Linkage.