The DOI matches its Crossref record; 6 of the 6 references it cites were found in a registry or an index.
SUMO and ubiquitin in the nucleus: different functions, similar mechanisms?
Open accessAbstract
The small ubiquitin-related modifier SUMO posttranslationally modifies many proteins with roles in diverse processes including regulation of transcription, chromatin structure, and DNA repair. Similar to nonproteolytic roles of ubiquitin, SUMO modification regulates protein localization and activity. Some proteins can be modified by SUMO and ubiquitin, but with distinct functional consequences. It is possible that the effects of ubiquitination and SUMOylation are both largely due to binding of proteins bearing specific interaction domains. Both modifications are reversible, and in some cases dynamic cycles of modification may be required for activity. Studies of SUMO and ubiquitin in the nucleus are yielding new insights into regulation of gene expression, genome maintenance, and signal transduction.
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
Interaction of the Fanconi Anemia Proteins and BRCA1 in a Common Pathway
Garcia-Higuera, I., Taniguchi, T., Ganesan, S., Meyn, M. S., Timmers, C., Hejna, J., Grompe, M., & D'Andrea, A. D. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00173-3 · Cited by 1,198
Specific Inhibition of Stat3 Signal Transduction by PIAS3
Chung, C. D., Liao, J., Liu, B., Rao, X., Jay, P., Berta, P., & Shuai, K. (1997) · Science · doi:10.1126/science.278.5344.1803 · Cited by 980
Henry, K. W., Wyce, A., Lo, W.-S., Duggan, L. J., Emre, N. C. T., Kao, C.-F., Pillus, L., Shilatifard, A., Osley, M. A., & Berger, S. L. (2003) · Genes & Development · doi:10.1101/gad.1144003 · Cited by 714
Dynamic Interplay of the SUMO and ERK Pathways in Regulating Elk-1 Transcriptional Activity
Yang, S.-H., Jaffray, E., Hay, R. T., & Sharrocks, A. D. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00265-x · Cited by 253
SUMO-1 modification of histone deacetylase 1 (HDAC1) modulates its biological activities
David, G., Neptune, M. A., & DePinho, R. A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203690200 · Cited by 236 · cited 2×
“SUMO modification of HDAC-1, for example, appears to stimulate deacetylase activity and transcriptional repression by this enzyme (Table 1; David et al. 2002; Cheng et al. 2004).”
BackgroundPotentiation of glucocorticoid receptor transcriptional activity by sumoylation
Le Drean, Y., Mincheneau, N., Le Goff, P., & Michel, D. (2002) · Endocrinology · doi:10.1210/en.2002-220135 · Cited by 159 · cited 2×
“Strikingly, mutation of the SUMO acceptor site in GR or overexpression of SUMO-1 has been shown to increase activity from some GR target promoters but not others (Le Drean et al. 2002; Tian et al. 2002; Holmstrom et al. 2003).”
Background
Cited by
Epigenetic regulation in psychiatric disorders
Tsankova, N., Renthal, W., Kumar, A., & Nestler, E. J. (2007) · Nature reviews. Neuroscience · doi:10.1038/nrn2132 · Cited by 1,400
Feige, J. N., Gelman, L., Michalik, L., Desvergne, B., & Wahli, W. (2006) · Progress in Lipid Research · doi:10.1016/j.plipres.2005.12.002 · Cited by 786
SUMO-Specific Protease 1 Is Essential for Stabilization of HIF1α during Hypoxia
Cheng, J., Kang, X., Zhang, S., & Yeh, E. T. H. (2007) · Cell · doi:10.1016/j.cell.2007.08.045 · Cited by 624
Crosstalk between SUMO and Ubiquitin on PCNA Is Mediated by Recruitment of the Helicase Srs2p
Papouli, E., Chen, S., Davies, A. A., Huttner, D., Krejci, L., Sung, P., & Ulrich, H. D. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.06.001 · Cited by 522
Histone Crosstalk between H2B Monoubiquitination and H3 Methylation Mediated by COMPASS
Lee, J.-S., Shukla, A., Schneider, J., Swanson, S. K., Washburn, M. P., Florens, L., Bhaumik, S. R., & Shilatifard, A. (2007) · Cell · doi:10.1016/j.cell.2007.09.046 · Cited by 438
Metadata
- Authors
- Gill, G.
- Venue
- Genes & Development
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2004-09-01
- Volume
- 18
- Issue
- 17
- Pages
- 2046-2059
- ISSN
- 0890-9369 (ISSN-L)
- 1549-5477
- OpenAlex
- W2051166632
- Cited by
- 756
- References
- 6
- Type
- posted content
- Language
- en
- Open access
- diamond
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: SUMO and ubiquitin in the nucleus: different functions, similar mechanisms? https://app.cochat.ai/papers/10.1101/gad.1214604
- The paper
- Gill, G. (2004). SUMO and ubiquitin in the nucleus: different functions, similar mechanisms? Genes & Development. https://doi.org/10.1101/gad.1214604
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.