The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition
Open accessAbstract
Proteins of the small ubiquitin-related modifier (SUMO) family are conjugated to proteins to regulate such cellular processes as nuclear transport, transcription, chromosome segregation and DNA repair. Recently, numerous insights into regulatory mechanisms of the SUMO modification pathway have emerged. Although SUMO-conjugating enzymes can discriminate between SUMO targets, many substrates possess characteristics that facilitate their modification. Other post-translational modifications also regulate SUMO conjugation, suggesting that SUMO signalling is integrated with other signal transduction pathways. A better understanding of SUMO regulatory mechanisms will lead to improved approaches for analysing the function of SUMO and substrate conjugation in distinct cellular pathways.
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
RING Domain E3 Ubiquitin Ligases
Deshaies, R. J., & Joazeiro, C. A. P. (2009) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.78.101807.093809 · Cited by 2,679
PCNA, the Maestro of the Replication Fork
Moldovan, G.-L., Pfander, B., & Jentsch, S. (2007) · Cell · doi:10.1016/j.cell.2007.05.003 · Cited by 1,796
Ginkgolic Acid Inhibits Protein SUMOylation by Blocking Formation of the E1-SUMO Intermediate
Fukuda, I., Ito, A., Hirai, G., Nishimura, S., Kawasaki, H., Saitoh, H., Kimura, K.-I., Sodeoka, M., & Yoshida, M. (2009) · Chemistry & Biology · doi:10.1016/j.chembiol.2009.01.009 · Cited by 355
Carbia-Nagashima, A., Gerez, J., Perez-Castro, C., Paez-Pereda, M., Silberstein, S., Stalla, G. K., Holsboer, F., & Arzt, E. (2007) · Cell · doi:10.1016/j.cell.2007.07.044 · Cited by 318
Regulation of MEF2 by Histone Deacetylase 4- and SIRT1 Deacetylase-Mediated Lysine Modifications
Zhao, X., Sternsdorf, T., Bolger, T. A., Evans, R. M., & Yao, T.-P. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.19.8456-8464.2005 · Cited by 264
Gupta, P., Ho, P.-C., Huq, M. M., Ha, S. G., Park, S. W., Khan, A. A., Tsai, N.-P., & Wei, L.-N. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0710561105 · Cited by 74
Cited by
Ultra‐high sensitivity mass spectrometry quantifies single‐cell proteome changes upon perturbation
Brunner, A., Thielert, M., Vasilopoulou, C., Ammar, C., Coscia, F., Mund, A., Hoerning, O. B., Bache, N., Apalategui, A., Lubeck, M., et al. (2022) · Molecular Systems Biology · doi:10.15252/msb.202110798 · Cited by 544
Ticket to a bubble ride: Cargo sorting into exosomes and extracellular vesicles
Anand, S., Samuel, M., Kumar, S., & Mathivanan, S. (2019) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2019.02.005 · Cited by 284
A Discovery Resource of Rare Copy Number Variations in Individuals with Autism Spectrum Disorder
Prasad, A., Merico, D., Thiruvahindrapuram, B., Wei, J., Lionel, A. C., Sato, D., Rickaby, J., Lu, C., Szatmari, P., Roberts, W., et al. (2012) · G3 Genes|Genomes|Genetics · doi:10.1534/g3.112.004689 · Cited by 206
Drisaldi, B., Colnaghi, L., Fioriti, L., Rao, N., Myers, C., Snyder, A. M., Metzger, D. J., Tarasoff, J., Konstantinov, E., Fraser, P. E., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.04.061 · Cited by 120
Capturing a substrate in an activated RING E3/E2–SUMO complex
Streich Jr, F. C., & Lima, C. D. (2016) · Nature · doi:10.1038/nature19071 · Cited by 108
Self-citation
Metadata
- Authors
- Gareau, J. R., & Lima, C. D.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2010-11-23
- Volume
- 11
- Issue
- 12
- Pages
- 861-871
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W2043927273
- Cited by
- 1,105
- References
- 6
- FWCI
- 3.88
- Type
- journal article
- Language
- en
- Open access
- green
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: The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. https://app.cochat.ai/papers/10.1038/nrm3011
- The paper
- Gareau, J. R., & Lima, C. D. (2010). The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition. Nature Reviews Molecular Cell Biology. https://doi.org/10.1038/nrm3011
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.
