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Cited by 371

The DOI matches its Crossref record; 32 of the 32 references it cites were found in a registry or an index.

Discrete Cleavage Motifs of Constitutive and Immunoproteasomes Revealed by Quantitative Analysis of Cleavage Products

Open access
Toes, R.E.M., Nussbaum, A.K., Degermann, S., Schirle, M., Emmerich, N.P.N., Kraft, M., Laplace, C., Zwinderman, A., Dick, T.P., Müller, J., Schönfisch, B., Schmid, C., Fehling, H.-J., Stevanovic, S., Rammensee, H.G., Schild, H.·2001·The Journal of Experimental Medicine
DOI 10.1084/jem.194.1.1
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Abstract

Proteasomes are the main proteases responsible for cytosolic protein degradation and the production of major histocompatibility complex class I ligands. Incorporation of the interferon γ–inducible subunits low molecular weight protein (LMP)-2, LMP-7, and multicatalytic endopeptidase complex–like (MECL)-1 leads to the formation of immunoproteasomes which have been associated with more efficient class I antigen processing. Although differences in cleavage specificities of constitutive and immunoproteasomes have been observed frequently, cleavage motifs have not been described previously. We now report that cells expressing immunoproteasomes display a different peptide repertoire changing the overall cytotoxic T cell–specificity as indicated by the observation that LMP-7−/− mice react against cells of LMP-7 wild-type mice. Moreover, using the 436 amino acid protein enolase-1 as an unmodified model substrate in combination with a quantitative approach, we analyzed a large collection of peptides generated by either set of proteasomes. Inspection of the amino acids flanking proteasomal cleavage sites allowed the description of two different cleavage motifs. These motifs finally explain recent findings describing differential processing of epitopes by constitutive and immunoproteasomes and are important to the understanding of peripheral T cell tolerization/activation as well as for effective vaccine development.

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Metadata

Authors
Toes, R. E. M., Nussbaum, A. K., Degermann, S., Schirle, M., Emmerich, N. P. N., Kraft, M., Laplace, C., Zwinderman, A., Dick, T. P., Müller, J., Schönfisch, B., Schmid, C., Fehling, H.-J., Stevanovic, S., Rammensee, H. G., & Schild, H.
Venue
The Journal of Experimental Medicine
Publisher
Rockefeller University Press
Published
2001-06-25
Volume
194
Issue
1
Pages
1-12
ISSN
  • 0022-1007 (ISSN-L)
  • 1540-9538
DOI
10.1084/jem.194.1.1
OpenAlex
W2107198699
Cited by
371
References
32
FWCI
8.90
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Discrete Cleavage Motifs of Constitutive and Immunoproteasomes Revealed by Quantitative Analysis of Cleavage Products. https://app.cochat.ai/papers/10.1084/jem.194.1.1
The paper
Toes, R. E. M., Nussbaum, A. K., Degermann, S., Schirle, M., Emmerich, N. P. N., Kraft, M., Laplace, C., Zwinderman, A., Dick, T. P., Müller, J., Schönfisch, B., Schmid, C., Fehling, H.-J., Stevanovic, S., Rammensee, H. G., & Schild, H. (2001). Discrete Cleavage Motifs of Constitutive and Immunoproteasomes Revealed by Quantitative Analysis of Cleavage Products. The Journal of Experimental Medicine. https://doi.org/10.1084/jem.194.1.1

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.