The DOI matches its Crossref record; 214 of the 214 references it cites were found in a registry or an index.
SUMO: From Bench to Bedside
Open accessAbstract
Sentrin/small ubiquitin-like modifier (SUMO) is protein modification pathway that regulates multiple biological processes, including cell division, DNA replication/repair, signal transduction, and cellular metabolism. In this review, we will focus on recent advances in the mechanisms of disease pathogenesis, such as cancer, diabetes, seizure, and heart failure, which have been linked to the SUMO pathway. SUMO is conjugated to lysine residues in target proteins through an isopeptide linkage catalyzed by SUMO-specific activating (E1), conjugating (E2), and ligating (E3) enzymes. In steady state, the quantity of SUMO-modified substrates is usually a small fraction of unmodified substrates due to the deconjugation activity of the family Sentrin/SUMO-specific proteases (SENPs). In contrast to the complexity of the ubiquitination/deubiquitination machinery, the biochemistry of SUMOylation and de-SUMOylation is relatively modest. Specificity of the SUMO pathway is achieved through redox regulation, acetylation, phosphorylation, or other posttranslational protein modification of the SUMOylation and de-SUMOylation enzymes. There are three major SUMOs. SUMO-1 usually modifies a substrate as a monomer; however, SUMO-2/3 can form poly-SUMO chains. The monomeric SUMO-1 or poly-SUMO chains can interact with other proteins through SUMO-interactive motif (SIM). Thus SUMO modification provides a platform to enhance protein-protein interaction. The consequence of SUMOylation includes changes in cellular localization, protein activity, or protein stability. Furthermore, SUMO may join force with ubiquitin to degrade proteins through SUMO-targeted ubiquitin ligases (STUbL). After 20 yr of research, SUMO has been shown to play critical roles in most, if not all, biological pathways. Thus the SUMO enzymes could be targets for drug development to treat human diseases.
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
HIFα Targeted for VHL-Mediated Destruction by Proline Hydroxylation: Implications for O 2 Sensing
Ivan, M., Kondo, K., Yang, H., Kim, W., Valiando, J., Ohh, M., Salic, A., Asara, J. M., Lane, W. S., & Kaelin Jr., W. G. (2001) · Science · doi:10.1126/science.1059817 · Cited by 4,735
AMPK: a nutrient and energy sensor that maintains energy homeostasis
Hardie, D. G., Ross, F. A., & Hawley, S. A. (2012) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3311 · Cited by 4,602
The Ubiquitin-Proteasome Proteolytic Pathway: Destruction for the Sake of Construction
Glickman, M. H., & Ciechanover, A. (2002) · Physiological Reviews · doi:10.1152/physrev.00027.2001 · Cited by 4,237
DNA Replication in Eukaryotic Cells
Bell, S. P., & Dutta, A. (2002) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.71.110601.135425 · Cited by 2,060
Pathophysiology and treatment of type 2 diabetes: perspectives on the past, present, and future
Kahn, S. E., Cooper, M. E., & Del Prato, S. (2014) · The Lancet · doi:10.1016/s0140-6736(13)62154-6 · Cited by 1,743
Shen, Z.-X., Chen, G.-Q., Ni, J.-H., Li, X.-S., Xiong, S.-M., Qiu, Q.-Y., Zhu, J., Tang, W., Sun, G.-L., Yang, K.-Q., et al. (1997) · Blood · doi:10.1182/blood.v89.9.3354 · Cited by 1,428
Mahajan, R., Delphin, C., Guan, T., Gerace, L., & Melchior, F. (1997) · Cell · doi:10.1016/s0092-8674(00)81862-0 · Cited by 1,256
A SUMOylation-dependent pathway mediates transrepression of inflammatory response genes by PPAR-γ
Pascual, G., Fong, A. L., Ogawa, S., Gamliel, A., Li, A. C., Perissi, V., Rose, D. W., Willson, T. M., Rosenfeld, M. G., & Glass, C. K. (2005) · Nature · doi:10.1038/nature03988 · Cited by 1,254
A novel potassium channel gene, KCNQ2, is mutated in an inherited epilepsy of newborns
Singh, N. A., Charlier, C., Stauffer, D., DuPont, B. R., Leach, R. J., Melis, R., Ronen, G. M., Bjerre, I., Quattlebaum, T., Murphy, J. V., et al. (1998) · Nature Genetics · doi:10.1038/ng0198-25 · Cited by 1,199
Matunis, M. J., Coutavas, E., & Blobel, G. (1996) · The Journal of cell biology · doi:10.1083/jcb.135.6.1457 · Cited by 1,197
Cited by
Zhong, Q., Xiao, X., Qiu, Y., Xu, Z., Chen, C., Chong, B., Zhao, X., Hai, S., Li, S., An, Z., et al. (2023) · MedComm · doi:10.1002/mco2.261 · Cited by 442
The Role of Sumoylation in the Response to Hypoxia: An Overview
Filippopoulou, C., Simos, G., & Chachami, G. (2020) · Cells · doi:10.3390/cells9112359 · Cited by 56
The function of SUMOylation and its crucial roles in the development of neurological diseases
Chen, X., Zhang, Y., Wang, Q., Qin, Y., Yang, X., Xing, Z., Shen, Y., Wu, H., & Qi, Y. (2021) · The FASEB Journal · doi:10.1096/fj.202002702r · Cited by 39
Acuña, M. L., García-Morin, A., Orozco-Sepúlveda, R., Ontiveros, C., Flores, A., Diaz, A. V., Gutiérrez-Zubiate, I., Patil, A. R., Alvarado, L. A., Roy, S., et al. (2023) · Scientific Reports · doi:10.1038/s41598-023-29357-7 · Cited by 19
Improved Peptide Search for Identification of SUMO and Sequence-Based Modifiers, in MaxSBM
Lennartsson, C., Kyriakidou, P., Nielsen, M. L., Olsen, J. V., Cox, J., & Hendriks, I. A. (2026) · Molecular & Cellular Proteomics · doi:10.1016/j.mcpro.2026.101589
Metadata
- Authors
- Chang, H.-M., & Yeh, E. T. H.
- Venue
- Physiological Reviews
- Publisher
- American Physiological Society
- Published
- 2020-10-01
- Volume
- 100
- Issue
- 4
- Pages
- 1599-1619
- ISSN
- 0031-9333 (ISSN-L)
- 1522-1210
- OpenAlex
- W3043639762
- Cited by
- 355
- References
- 214
- FWCI
- 2.94
- 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: SUMO: From Bench to Bedside. https://app.cochat.ai/papers/10.1152/physrev.00025.2019
- The paper
- Chang, H.-M., & Yeh, E. T. H. (2020). SUMO: From Bench to Bedside. Physiological Reviews. https://doi.org/10.1152/physrev.00025.2019
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.
