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  Proteolytic dynamics of human 20S thymoproteasome.

Kuckelkorn, U., Stübler, S., Textoris-Taube, K., Killian, C., Niewienda, A., Henklein, P., et al. (2019). Proteolytic dynamics of human 20S thymoproteasome. Journal of Biological Chemistry, 294, 7740-7754. doi:10.1074/jbc.RA118.007347.

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Item Permalink: http://hdl.handle.net/21.11116/0000-0003-46A6-3 Version Permalink: http://hdl.handle.net/21.11116/0000-0003-9637-6
Genre: Journal Article

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 Creators:
Kuckelkorn, U., Author
Stübler, S., Author
Textoris-Taube, K., Author
Killian, C., Author
Niewienda, A., Author
Henklein, P., Author
Janek, K., Author
Stumpf, M. P., Author
Mishto, M., Author
Liepe, J.1, Author              
Affiliations:
1Research Group of Quantitative and System Biology, MPI for Biophysical Chemistry, Max Planck Society, ou_2466694              

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Free keywords: antigen processing; bioinformatics; computational biology; proteasome; protein degradation; thymoproteasome; thymus
 Abstract: An efficient immunosurveillance of CD8+ T cells in the periphery depends on positive/negative selection of thymocytes and thus on the dynamics of antigen degradation and epitope production by thymoproteasome and immunoproteasome in the thymus. Although studies in mouse systems have shown how thymoproteasome activity differs from that of immunoproteasome and strongly impacts on the T cell repertoire, the proteolytic dynamics and the regulation of human thymoproteasome are unknown. By combining biochemical and computational modeling approaches, we show here that human 20S thymoproteasome and immunoproteasome differ not only in the proteolytic activity of the catalytic sites but also in the peptide transport. These differences impinge upon the quantity of peptide products rather than where the substrates are cleaved. The comparison of the two human 20S proteasome isoforms depicts different processing of antigens that are associated to tumors and autoimmune diseases.

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Language(s): eng - English
 Dates: 2019-03-262019-05-10
 Publication Status: Published in print
 Pages: -
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 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1074/jbc.RA118.007347
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Title: Journal of Biological Chemistry
Source Genre: Journal
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Pages: - Volume / Issue: 294 Sequence Number: - Start / End Page: 7740 - 7754 Identifier: -