Protein modification by SUMO.

By Erica S. Johnson. Annual Review of Biochemistry, 2004

1,761 citations recorded by the source corpus.

Subfields: Molecular Biology, Oncology, Parasitology

View Paper: https://www.semanticscholar.org/paper/ff0a5f61fa522eced1c95d464d38305634ae1e37

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In Molecular Biology

1. J. Massagué
2. J. Seoane
3. R. J. Lefkowitz
4. D. Wotton
5. Sudha K. Shenoy
6. M. Hochstrasser
7. P. Hasegawa
8. T. Hunter

In Oncology

1. J. Seoane
2. J. Massagué
3. D. Wotton
4. R. J. Lefkowitz
5. T. Hunter
6. M. Hochstrasser
7. Sudha K. Shenoy
8. C. Lima

In Parasitology

1. M. Hochstrasser
2. Sudha K. Shenoy
3. C. Lima
4. C. Sherr
5. Jaclyn R. Gareau
6. R. J. Lefkowitz

Citations in the corpus

• β-arrestin-mediated receptor trafficking and signal transduction (2011, background): “In addition to ubiquitination, β-arrestin2 is SUMOylated (SUMO: small ubiquitin like modifier, that is covalently attached to lysines just as in ubiquitination[51]).”
• Smad transcription factors. (2005, background): “One of the outcomes of sumoylation is the modulation of protein targeting within the cell (Johnson 2004).”
• Conserved function of RNF4 family proteins in eukaryotes: targeting a ubiquitin ligase to SUMOylated proteins (2007, background): “SUMOylated proteins are found either in the nucleus or at the nuclear periphery, implying an important role for SUMOylation in biological processes in the nucleus (Johnson, 2004).”
• SIZ1-Mediated Sumoylation of ICE1 Controls CBF3/DREB1A Expression and Freezing Tolerance in Arabidopsis[W][OA] (2007, background): “Likewise, sumoylation of transcription factors represses activity through processes that involve transcriptional coregulatory complexes (Johnson, 2004; Gill, 2005; Hay, 2005).”
• The multifunctional nucleolus (2007, background): “, is a dynamic and reversible process, and several SUMO-specific proteases that remove SUMO chains from protein substrates have been describe”
• Modification of proteins by ubiquitin and ubiquitin-like proteins. (2006, background): “For example, in vertebrate cells, SUMO localizes to the nucleus and concentrates at nuclear pore complexes and in PML bodies (Johnson 2004).”
• Abiotic stress response in plants : when post-transcriptional and post-translational regulations control transcription (2008, background): “In addition, ubiquitination and sumoylation often have antagonistic effects by acting on the same amino acid residues [120].”
• Divorcing ARF and p53: an unsettled case (2006, methodology): “The addition of the small ubiquitin-like modifier, SUMO, to lysyl e-amino groups in target proteins occurs through a three-enzyme cascade (an E1 activating enzyme, an E2 conjugating enzyme and an E3 ligase) analogous to that which is used for ubiquitylatio”
• The SUMO pathway: emerging mechanisms that shape specificity, conjugation and recognition (2010, background): “jpg"/> Post-translational modification of proteins by members of the small ubiquitin -related modifier (SUMO) protein family regulates diverse cellular processes, including transcription, replication, chromosome segregation and DNA repai”