The DOI matches its Crossref record; 48 of the 48 references it cites were found in a registry or an index.
Modification with SUMO: A role in transcriptional regulation
Open accessAbstract
Small ubiquitin‐related modifier (SUMO) is a protein moiety that is ligated to lysine residues in a variety of target proteins. The addition of SUMO can modulate the ability of proteins to interact with their partners, alter their patterns of subcellular localization and control their stability. It is clear that SUMO influences many different biological processes, but recent data suggest that it is particularly important in the regulation of transcription. Indeed, several transcription factors, such as Sp3, c‐Jun, c‐Myb and various nuclear receptors, have recently been shown to be subject to sumoylation and, although this modification can have a positive influence, a growing body of evidence highlights its role in the negative regulation of transcription. This review summarizes recent experiments focusing on sumoylation and transcriptional repression.
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Cites
RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
Hoege, C., Pfander, B., Moldovan, G.-L., Pyrowolakis, G., & Jentsch, S. (2002) · Nature · doi:10.1038/nature00991 · Cited by 2,198
Themes and variations on ubiquitylation
Weissman, A. M. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056563 · Cited by 1,482
SUMO-1 Modification of IκBα Inhibits NF-κB Activation
Desterro, J. M. P., Rodriguez, M. S., & Hay, R. T. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80133-1 · Cited by 1,038
Functional Heterogeneity of Small Ubiquitin-related Protein Modifiers SUMO-1 versus SUMO-2/3
Saitoh, H., & Hinchey, J. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.9.6252 · Cited by 895
Polymeric Chains of SUMO-2 and SUMO-3 Are Conjugated to Protein Substrates by SAE1/SAE2 and Ubc9
Tatham, M. H., Jaffray, E., Vaughan, O. A., Desterro, J. M. P., Botting, C. H., Naismith, J. H., & Hay, R. T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m104214200 · Cited by 821
The Nucleoporin RanBP2 Has SUMO1 E3 Ligase Activity
Pichler, A., Gast, A., Seeler, J. S., Dejean, A., & Melchior, F. (2002) · Cell · doi:10.1016/s0092-8674(01)00633-x · Cited by 816
Melchior, F. (2000) · Annual Review of Cell and Developmental Biology · doi:10.1146/annurev.cellbio.16.1.591 · Cited by 774
Sumo, ubiquitin's mysterious cousin
Müller, S., Hoege, C., Pyrowolakis, G., & Jentsch, S. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056591 · Cited by 764
An E3-like Factor that Promotes SUMO Conjugation to the Yeast Septins
Johnson, E. S., & Gupta, A. A. (2001) · Cell · doi:10.1016/s0092-8674(01)00491-3 · Cited by 641
Sachdev, S., Bruhn, L., Sieber, H., Pichler, A., Melchior, F., & Grosschedl, R. (2001) · Genes & Development · doi:10.1101/gad.944801 · Cited by 547
Cited by
MYB transcription factors in Arabidopsis
Dubos, C., Stracke, R., Grotewold, E., Weisshaar, B., Martin, C., & Lepiniec, L. (2010) · Trends in Plant Science · doi:10.1016/j.tplants.2010.06.005 · Cited by 4,865
The Ubiquitin Proteasome System in Neurodegenerative Diseases
Ciechanover, A., & Brundin, P. (2003) · Neuron · doi:10.1016/s0896-6273(03)00606-8 · Cited by 982
Melanocytes and the Microphthalmia Transcription Factor Network
Steingrímsson, E., Copeland, N. G., & Jenkins, N. A. (2004) · Annual Review of Genetics · doi:10.1146/annurev.genet.38.072902.092717 · Cited by 771
SUMO and ubiquitin in the nucleus: different functions, similar mechanisms?
Gill, G. (2004) · Genes & Development · doi:10.1101/gad.1214604 · Cited by 756
Mechanisms, regulation and consequences of protein SUMOylation
Wilkinson, K. A., & Henley, J. M. (2010) · Biochemical Journal · doi:10.1042/bj20100158 · Cited by 686
Metadata
- Authors
- Verger, A., Perdomo, J., & Crossley, M.
- Venue
- EMBO reports
- Published
- 2003-02
- Volume
- 4
- Issue
- 2
- Pages
- 137-142
- ISSN
- 1469-221X (ISSN-L)
- 1469-3178
- OpenAlex
- W1744223828
- Cited by
- 440
- References
- 48
- FWCI
- 14.80
- 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).
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