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  • Mice, Transgenic  (2)
  • Proteasome Endopeptidase Complex  (2)
  • 1
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    American Association for the Advancement of Science (AAAS)
    Publikationsdatum: 2003-09-06
    Beschreibung: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yewdell, Jonathan W -- New York, N.Y. -- Science. 2003 Sep 5;301(5638):1334-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, Bethesda, MD 20892-0440, USA. jyewdell@nih.gov〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12958347" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Animals ; Antigen Presentation ; CD8-Positive T-Lymphocytes/immunology ; Codon ; Cysteine Endopeptidases/metabolism ; Epstein-Barr Virus Nuclear Antigens/chemistry/*genetics/*immunology/metabolism ; Herpesvirus 4, Human/physiology ; Histocompatibility Antigens Class I/*immunology ; Humans ; Mice ; Mice, Transgenic ; Multienzyme Complexes/metabolism ; Peptides/genetics/*immunology/*metabolism ; Proteasome Endopeptidase Complex ; *Protein Biosynthesis ; Reading Frames ; Ribosomes/metabolism ; Self Tolerance ; Virus Latency
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
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  • 2
    Publikationsdatum: 2004-05-29
    Beschreibung: "Cross-priming" describes the activation of naive CD8+ T cells by professional antigen-presenting cells that have acquired viral or tumor antigens from "donor" cells. Antigen transfer is believed to be mediated by donor cell-derived molecular chaperones bearing short peptide ligands generated by proteasome degradation of protein antigens. We show here that cross-priming is based on the transfer of proteasome substrates rather than peptides. These findings are potentially important for the rational design of vaccines that elicit CD8+ T cell responses.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Norbury, Christopher C -- Basta, Sameh -- Donohue, Keri B -- Tscharke, David C -- Princiotta, Michael F -- Berglund, Peter -- Gibbs, James -- Bennink, Jack R -- Yewdell, Jonathan W -- AI-056094-01/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2004 May 28;304(5675):1318-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda MD, 20892-0440, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/15166379" target="_blank"〉PubMed〈/a〉
    Schlagwort(e): Acetylcysteine/*analogs & derivatives/pharmacology ; Animals ; *Antigen Presentation ; Antigens/*immunology/metabolism ; Antigens, Viral/immunology/metabolism ; CD8-Positive T-Lymphocytes/*immunology ; Cell Line ; *Cross-Priming ; Cysteine Endopeptidases/*metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; Endoplasmic Reticulum/metabolism ; Humans ; Immunization ; Influenza A virus/immunology ; Lymphocyte Activation ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Molecular Chaperones/metabolism ; Multienzyme Complexes/*metabolism ; Ovalbumin/immunology/metabolism ; Peptide Fragments/immunology ; Proteasome Endopeptidase Complex ; Recombinant Fusion Proteins/immunology/metabolism ; Vaccines/immunology ; Vaccinia virus/genetics/physiology
    Print ISSN: 0036-8075
    Digitale ISSN: 1095-9203
    Thema: Biologie , Chemie und Pharmazie , Informatik , Medizin , Allgemeine Naturwissenschaft , Physik
    Standort Signatur Erwartet Verfügbarkeit
    BibTip Andere fanden auch interessant ...
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