The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Aggresomes, inclusion bodies and protein aggregation
Open accessAbstract
Intracellular and extracellular accumulation of aggregated protein are linked to many diseases, including ageing-related neurodegeneration and systemic amyloidosis. Cells avoid accumulating potentially toxic aggregates by mechanisms including the suppression of aggregate formation by molecular chaperones and the degradation of misfolded proteins by proteasomes. Once formed, aggregates tend to be refractory to proteolysis and to accumulate in inclusion bodies. This accumulation has been assumed to be a diffusion-limited process, but recent studies suggest that, in animal cells, aggregated proteins are specifically delivered to inclusion bodies by dynein-dependent retrograde transport on microtubules. This microtubule-dependent inclusion body is called an aggresome.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Aggresomes: A Cellular Response to Misfolded Proteins
Johnston, J. A., Ward, C. L., & Kopito, R. R. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.7.1883 · Cited by 2,148
Self-citationRecognition of the polyubiquitin proteolytic signal
Thrower, J. S. (2000) · The EMBO Journal · doi:10.1093/emboj/19.1.94 · Cited by 1,716
The 26S Proteasome: A Molecular Machine Designed for Controlled Proteolysis
Voges, D., Zwickl, P., & Baumeister, W. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.1015 · Cited by 1,608
Rapid degradation of a large fraction of newly synthesized proteins by proteasomes
Schubert, U., Antón, L. C., Gibbs, J., Norbury, C. C., Yewdell, J. W., & Bennink, J. R. (2000) · Nature · doi:10.1038/35008096 · Cited by 1,536
Degradation of CFTR by the ubiquitin-proteasome pathway
Ward, C. L., Omura, S., & Kopito, R. R. (1995) · Cell · doi:10.1016/0092-8674(95)90240-6 · Cited by 1,304
Self-citationSetting the Standards: Quality Control in the Secretory Pathway
Ellgaard, L., Molinari, M., & Helenius, A. (1999) · Science · doi:10.1126/science.286.5446.1882 · Cited by 1,192
Protein aggregation: folding aggregates, inclusion bodies and amyloid
Fink, A. L. (1998) · Folding and Design · doi:10.1016/s1359-0278(98)00002-9 · Cited by 1,157
Posttranslational Quality Control: Folding, Refolding, and Degrading Proteins
Wickner, S., Maurizi, M. R., & Gottesman, S. (1999) · Science · doi:10.1126/science.286.5446.1888 · Cited by 1,071
Quality control in the secretory pathway
Hammond, C., & Helenius, A. (1995) · Current Opinion in Cell Biology · doi:10.1016/0955-0674(95)80009-3 · Cited by 673
Johnston, J. A., Dalton, M. J., Gurney, M. E., & Kopito, R. R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.220417997 · Cited by 607
Self-citation
Research works printed but not linked: 1
- Laszlo, 1991, The latent membrane protein-1 in Epstein–Barr-virus-transformed lymphoblastoid cells is found with ubiquitin–protein conjugates and heat-shock protein 70 in lysosomes oriented around the microtubule organizing centre, J. Pathol., 164, 203, 10.1002/path.1711640305 · doi:10.1002/path.1711640305
Cited by
Dauer, W., & Przedborski, S. (2003) · Neuron · doi:10.1016/s0896-6273(03)00568-3 · Cited by 5,469
Pankiv, S., Clausen, T. H., Lamark, T., Brech, A., Bruun, J.-A., Outzen, H., Øvervatn, A., Bjørkøy, G., & Johansen, T. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702824200 · Cited by 4,578
Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice
Hara, T., Nakamura, K., Matsui, M., Yamamoto, A., Nakahara, Y., Suzuki-Migishima, R., Yokoyama, M., Mishima, K., Saito, I., Okano, H., et al. (2006) · Nature · doi:10.1038/nature04724 · Cited by 3,882
Protein aggregation and neurodegenerative disease
Ross, C. A., & Poirier, M. A. (2004) · Nature Medicine · doi:10.1038/nm1066 · Cited by 3,454
Molecular chaperones in protein folding and proteostasis
Hartl, F. U., Bracher, A., & Hayer-Hartl, M. (2011) · Nature · doi:10.1038/nature10317 · Cited by 3,381
Metadata
- Authors
- Kopito, R. R.
- Venue
- Trends in Cell Biology
- Publisher
- Elsevier BV
- Published
- 2000-12
- Volume
- 10
- Issue
- 12
- Pages
- 524-530
- ISSN
- 0962-8924 (ISSN-L)
- OpenAlex
- W1988146888
- Cited by
- 1,921
- References
- 48
- FWCI
- 3.11
- Type
- journal article
- Language
- en
- Open access
- hybrid
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- creativecommons.org/licenses/by-nc-nd/4.0/ (vor, 363 d)
About these checks
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.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: Aggresomes, inclusion bodies and protein aggregation. https://app.cochat.ai/papers/10.1016/s0962-8924(00)01852-3
- The paper
- Kopito, R. R. (2000). Aggresomes, inclusion bodies and protein aggregation. Trends in Cell Biology. https://doi.org/10.1016/s0962-8924(00)01852-3
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.
