phosphoramidon and epoxomicin

phosphoramidon has been researched along with epoxomicin* in 1 studies

Other Studies

1 other study(ies) available for phosphoramidon and epoxomicin

Article	Year
Production of an antigenic peptide by insulin-degrading enzyme. Nature immunology, 2010, Volume: 11, Issue:5 Most antigenic peptides presented by major histocompatibility complex (MHC) class I molecules are produced by the proteasome. Here we show that a proteasome-independent peptide derived from the human tumor protein MAGE-A3 is produced directly by insulin-degrading enzyme (IDE), a cytosolic metallopeptidase. Cytotoxic T lymphocyte recognition of tumor cells was reduced after metallopeptidase inhibition or IDE silencing. Separate inhibition of the metallopeptidase and the proteasome impaired degradation of MAGE-A3 proteins, and simultaneous inhibition of both further stabilized MAGE-A3 proteins. These results suggest that MAGE-A3 proteins are degraded along two parallel pathways that involve either the proteasome or IDE and produce different sets of antigenic peptides presented by MHC class I molecules. Topics: Antibodies, Blocking; Antigen Presentation; Antigens, Neoplasm; Cell Fractionation; Cell Line, Tumor; Chromatography, High Pressure Liquid; Clone Cells; Cytosol; Glycopeptides; HLA-A1 Antigen; Humans; Insulysin; Interferon-gamma; Mass Spectrometry; Metalloendopeptidases; Neoplasm Proteins; Oligopeptides; Peptide Fragments; Phenanthrolines; Proteasome Inhibitors; RNA, Small Interfering; T-Lymphocytes, Cytotoxic	2010

Article

Year

Production of an antigenic peptide by insulin-degrading enzyme.

Nature immunology, 2010, Volume: 11, Issue:5

Most antigenic peptides presented by major histocompatibility complex (MHC) class I molecules are produced by the proteasome. Here we show that a proteasome-independent peptide derived from the human tumor protein MAGE-A3 is produced directly by insulin-degrading enzyme (IDE), a cytosolic metallopeptidase. Cytotoxic T lymphocyte recognition of tumor cells was reduced after metallopeptidase inhibition or IDE silencing. Separate inhibition of the metallopeptidase and the proteasome impaired degradation of MAGE-A3 proteins, and simultaneous inhibition of both further stabilized MAGE-A3 proteins. These results suggest that MAGE-A3 proteins are degraded along two parallel pathways that involve either the proteasome or IDE and produce different sets of antigenic peptides presented by MHC class I molecules.

Topics: Antibodies, Blocking; Antigen Presentation; Antigens, Neoplasm; Cell Fractionation; Cell Line, Tumor; Chromatography, High Pressure Liquid; Clone Cells; Cytosol; Glycopeptides; HLA-A1 Antigen; Humans; Insulysin; Interferon-gamma; Mass Spectrometry; Metalloendopeptidases; Neoplasm Proteins; Oligopeptides; Peptide Fragments; Phenanthrolines; Proteasome Inhibitors; RNA, Small Interfering; T-Lymphocytes, Cytotoxic

2010