Joy M. Polefrone

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Deregulation of signaling pathways is a hallmark of malignant transformation. Signaling-associated phosphoproteins can be degraded to generate cancer-specific phosphopeptides that are presented by major histocompatibility complex (MHC) class I and II molecules and recognized by T cells; however, the contribution of these phosphoprotein-specific T cells to(More)
Alterations in phosphorylation of cellular proteins are a hallmark of malignant transformation. Degradation of these phosphoproteins could generate cancer-specific class I MHC-associated phosphopeptides recognizable by CD8+ T lymphocytes. In a comparative analysis of phosphopeptides presented on the surface of melanoma, ovarian carcinoma, and B(More)
phosphorylation sites in PIX and PAK1 Mark W. Mayhew1, Erin D. Jeffery2, Nicholas E. Sherman3, Kristina Nelson3, Joy M. Polefrone2, Stephen J. Pratt1, Jeffrey Shabanowitz2, J. Thomas Parsons4, Jay W. Fox2, Donald F. Hunt2,5 and Alan F. Horwitz1,* Departments of 1Cell Biology, 2Chemistry, 3W. M. Keck Biomedical Mass Spectrometry Laboratory, 4Microbiology,(More)
Although multiple components of the class I MHC processing pathway have been elucidated, the participation of nonproteasomal cytosolic enzymes has been largely unexplored. In this study, we provide evidence for multiple cytosolic mechanisms in the generation of an HLA-A*0201-associated epitope from tyrosinase. This epitope is presented in two isoforms(More)
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