The DOI matches its Crossref record; 107 of the 107 references it cites were found in a registry or an index.
Function and regulation of SUMO proteases
Open accessAbstract
Covalent attachment of small ubiquitin-like modifier (SUMO) to proteins is highly dynamic, and both SUMO–protein conjugation and cleavage can be regulated. Protein desumoylation is carried out by SUMO proteases, which control cellular mechanisms ranging from transcription and cell division to ribosome biogenesis. Recent advances include the discovery of two novel classes of SUMO proteases, insights regarding SUMO protease specificity, and revelations of previously unappreciated SUMO protease functions in several key cellular pathways. These developments, together with new connections between SUMO proteases and the recently discovered SUMO-targeted ubiquitin ligases (STUbLs), make this an exciting period to study these enzymes.
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Cites
Breaking the chains: structure and function of the deubiquitinases
Komander, D., Clague, M. J., & Urbé, S. (2009) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2731 · Cited by 1,969
The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition
Gareau, J. R., & Lima, C. D. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3011 · Cited by 1,105
Grisendi, S., Mecucci, C., Falini, B., & Pandolfi, P. P. (2006) · Nature Reviews Cancer · doi:10.1038/nrc1885 · Cited by 850
Control of spontaneous and damage-induced mutagenesis by SUMO and ubiquitin conjugation
Stelter, P., & Ulrich, H. D. (2003) · Nature · doi:10.1038/nature01965 · Cited by 847
Origin and function of ubiquitin-like proteins
Hochstrasser, M. (2009) · Nature · doi:10.1038/nature07958 · Cited by 783
Self-citationA new protease required for cell-cycle progression in yeast
Li, S.-J., & Hochstrasser, M. (1999) · Nature · doi:10.1038/18457 · Cited by 737
Self-citationMossessova, E., & Lima, C. D. (2000) · Molecular Cell · doi:10.1016/s1097-2765(00)80326-3 · Cited by 704
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
Specification of SUMO1- and SUMO2-interacting Motifs
Hecker, C.-M., Rabiller, M., Haglund, K., Bayer, P., & Dikic, I. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m512757200 · Cited by 587
Modification in reverse: the SUMO proteases
Mukhopadhyay, D., & Dasso, M. (2007) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.05.002 · Cited by 575
Cited by
A comprehensive compilation of SUMO proteomics
Hendriks, I. A., & Vertegaal, A. C. O. (2016) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm.2016.81 · Cited by 514
SUMO and the robustness of cancer
Seeler, J.-S., & Dejean, A. (2017) · Nature Reviews Cancer · doi:10.1038/nrc.2016.143 · Cited by 429
Alquezar, C., Arya, S., & Kao, A. W. (2021) · Frontiers in Neurology · doi:10.3389/fneur.2020.595532 · Cited by 367
Chang, H.-M., & Yeh, E. T. H. (2020) · Physiological Reviews · doi:10.1152/physrev.00025.2019 · Cited by 355
The post-translational modification, SUMOylation, and cancer (Review)
Han, Z.-J., Feng, Y.-H., Gu, B.-H., Li, Y.-M., & Chen, H. (2018) · International Journal of Oncology · doi:10.3892/ijo.2018.4280 · Cited by 334
Metadata
- Authors
- Hickey, C. M., Wilson, N. R., & Hochstrasser, M.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2012-11-23
- Volume
- 13
- Issue
- 12
- Pages
- 755-766
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W1993287528
- Cited by
- 638
- References
- 107
- FWCI
- 2.33
- Type
- journal article
- Language
- en
- Open access
- green
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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.
