SUMO: a history of modification.

By Ronald T. Hay. Molecules and Cells, 2005

1,774 citations recorded by the source corpus.

Subfields: Immunology, Molecular Biology, Parasitology

View Paper: https://www.semanticscholar.org/paper/ca638e5d51cb7e607c4562a781e37490bb9684e1

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Immunology

1. Graciana Diez-Roux
2. Christopher K. Glass
3. C. Théry
4. G. Meroni
5. P. Calder
6. I. Tabas

In Molecular Biology

1. Christopher K. Glass
2. Toby J. Gibson
3. Francesca Diella
4. Edit I. Buzás
5. Raymond Schiffelers
6. Imre Mäger
7. Michael G. Rosenfeld
8. P. Hasegawa

In Parasitology

1. Graciana Diez-Roux
2. G. Meroni

Citations in the corpus

• Abiotic stress response in plants : when post-transcriptional and post-translational regulations control transcription (2008, background): “Sumoylation is a post-translational modification of protein substrates based on the covalent conjugation of the SUMO (Small Ubiquitin-like MOdifier) peptide [101].”
• Parallel SUMOylation-dependent pathways mediate gene- and signal-specific transrepression by LXRs and PPARgamma. (2007, background): “Because the conjugated forms of SUMO2 and SUMO3 form a distinct subfamily and are only 50% identical in sequence to SUMO1 (Hay, 2005), we propose that LXRs and PPARg are functionally differentiated based on their differential SUMOylation and represent distinct, parallel transrepression pathways that”
• Small but versatile: the extraordinary functional and structural diversity of the β-grasp fold (2007, background): “SUMO/SMT3) [14,15] 3) conjugation to both a protein target (Apg5p) and the amino group of the lipid phosphatidylethanolamine (Agp8p/Aut7p) in regulation of the distinctly eukaryotic process of autophagy.”
• A Nurr1/CoREST transrepression pathway attenuates neurotoxic inflammation in activated microglia and astrocytes (2009, neutral): “As shown in Figure 3C, knockdown of Ubc9, an essential E2 enzyme for SUMOylation (Hay, 2005), reversed Nurr1-mediated repression of iNOS, suggesting that SUMOylation is required.”
• SIZ1-Mediated Sumoylation of ICE1 Controls CBF3/DREB1A Expression and Freezing Tolerance in Arabidopsis[W][OA] (2007, background): “SUMO and ubiquitin can interact competitively or cooperatively on the same substrate to regulate protein function and biological processes (Hay, 2005; Ulrich, 2005).”
• Obstacles and opportunities in the functional analysis of extracellular vesicle RNA – an ISEV position paper (2017, background): “mono-attachment does not target proteins for degradation, but instead regulates stability and subcellular localisation.[147,148] Interestingly, constitutive activation of”
• Understanding eukaryotic linear motifs and their role in cell signaling and regulation. (2008, background): “RanGAP1 is preferentially modified with SUMO-1 (84), the topoisomerase II with SUMO-2 and -3 (85).”
• TRIM/RBCC, a novel class of ‘single protein RING finger’ E3 ubiquitin ligases (2005, background): “SUMO conjugation is known to target protein transport, to regulate the activity of transcription factors and to inhibit proteasome-mediated protein degradation.((51)) Many NB components, including PML itself, are SUMO conjugated.”