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Cited by 270Ubiquitin and proteasome pathwaysProtease and Inhibitor MechanismsAutophagy in Disease and Therapy

The DOI matches its Crossref record; 29 of the 29 references it cites were found in a registry or an index.

A proteolytic system that compensates for loss of proteasome function

Overview

Integrity signals

Registry

Crossref · 10.1038/33443

Cites

29 of 29 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

We couldn’t retrieve this paper’s full text, so its claims and self-check weren’t run. The registry and citation checks still apply.

Citations

Cites

Show all 29 references

Cited by

See all 270

Metadata

Authors
Glas, R., Bogyo, M., McMaster, J. S., Gaczynska, M., & Ploegh, H. L.
Affiliations
  • Massachusetts Institute of Technology (US)
  • Harvard University (US)
  • University of Utah (US)
Corresponding author
Ploegh, Hidde L.
Venue
Nature
Published
1998-04
Volume
392
Issue
6676
Pages
618-622
ISSN
  • 0028-0836 (ISSN-L)
  • 1476-4687
OpenAlex
W119139793
Cited by
270
References
29
Citations by year
2026: 1 · 2025: 3 · 2024: 2 · 2023: 4 · 2022: 2 · 2021: 3 · 2019: 3 · 2018: 1 · 2017: 1 · 2016: 5 · 2015: 2 · 2014: 4 · 2013: 8 · 2012: 6
FWCI
7.56
Type
journal article
Language
en
Open access
closed
Licence
www.springer.com/tdm (tdm)
Locations
  • Nature (publishedVersion)
  • PubMed (publishedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
Funders
Swedish Foundation for International Cooperation in Research and Higher Education
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Autophagy in Disease and Therapy
Keywords
proteasome, proteasome inhibitors, inhibitor resistance, protein degradation, protein quality control, cell growth, transcription factor activation, cell cycle regulation, MHC class I peptide presentation
MeSH terms
Adaptation, Physiological, Animals, Cysteine Endopeptidases, Hydrolysis, Multienzyme Complexes, Endopeptidases, Sulfones, Thermoplasma, Tumor Cells, Cultured, Ubiquitins, Histocompatibility Antigens Class I, Cysteine Proteinase Inhibitors, Proteasome Endopeptidase Complex, Mice

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Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

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How to cite

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This page
CoChat. (2026). Citation check: A proteolytic system that compensates for loss of proteasome function. https://app.cochat.ai/papers/10.1038/33443
The paper
Glas, R., Bogyo, M., McMaster, J. S., Gaczynska, M., & Ploegh, H. L. (1998). A proteolytic system that compensates for loss of proteasome function. Nature. https://doi.org/10.1038/33443

Data sources

Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

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.