Publikation: Immunoproteasome-Specific Inhibitors and Their Application
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2012
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DOHMEN, R. Jürgen, ed., Martin SCHEFFNER, ed.. Ubiquitin Family Modifiers and the Proteasome. Totowa, NJ: Humana Press, 2012, pp. 391-401. Methods in Molecular Biology. 832. ISBN 978-1-61779-473-5. Available under: doi: 10.1007/978-1-61779-474-2_27
Zusammenfassung
Immunoproteasomes (IPs) containing the interferon-inducible subunits beta1i (LMP2), beta2i (MECL-1), and beta5i (LMP7) alter proteasomal cleavage preference, optimise the generation of peptide ligands of MHC class I molecules, alter cytokine profile, influence T-helper cell differentiation, and play a role in T-cell survival. Small molecule inhibitors are useful tools for probing the role of the immunoproteasome in immune functions. Here, we describe different methods to characterise immunoproteasome-selective inhibitors. Thereby, we provide the methodology to analyse the specificity and cell permeability of immunoproteasome inhibitors, as well as to functionally investigate immunoproteasome inhibitors in antigen presentation.
Zusammenfassung in einer weiteren Sprache
Fachgebiet (DDC)
570 Biowissenschaften, Biologie
Schlagwörter
Proteasome, Immunoproteasome, Inhibitor, Proteasome purification, Activity assay, Permeability, lacZ assay, T-cell hybridomas, Fluorogenic peptides
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BASLER, Michael, Marcus GRÖTTRUP, 2012. Immunoproteasome-Specific Inhibitors and Their Application. In: DOHMEN, R. Jürgen, ed., Martin SCHEFFNER, ed.. Ubiquitin Family Modifiers and the Proteasome. Totowa, NJ: Humana Press, 2012, pp. 391-401. Methods in Molecular Biology. 832. ISBN 978-1-61779-473-5. Available under: doi: 10.1007/978-1-61779-474-2_27BibTex
@incollection{Basler2012Immun-22002,
year={2012},
doi={10.1007/978-1-61779-474-2_27},
title={Immunoproteasome-Specific Inhibitors and Their Application},
number={832},
isbn={978-1-61779-473-5},
publisher={Humana Press},
address={Totowa, NJ},
series={Methods in Molecular Biology},
booktitle={Ubiquitin Family Modifiers and the Proteasome},
pages={391--401},
editor={Dohmen, R. Jürgen and Scheffner, Martin},
author={Basler, Michael and Gröttrup, Marcus}
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<dcterms:abstract xml:lang="eng">Immunoproteasomes (IPs) containing the interferon-inducible subunits beta1i (LMP2), beta2i (MECL-1), and beta5i (LMP7) alter proteasomal cleavage preference, optimise the generation of peptide ligands of MHC class I molecules, alter cytokine profile, influence T-helper cell differentiation, and play a role in T-cell survival. Small molecule inhibitors are useful tools for probing the role of the immunoproteasome in immune functions. Here, we describe different methods to characterise immunoproteasome-selective inhibitors. Thereby, we provide the methodology to analyse the specificity and cell permeability of immunoproteasome inhibitors, as well as to functionally investigate immunoproteasome inhibitors in antigen presentation.</dcterms:abstract>
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