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SUMO proteins, such as SUMO3, and ubiquitin (see MIM 191339) posttranslationally modify numerous cellular proteins and affect their metabolism and function. Zusätzlich bieten wir Ihnen SUMO3 Antikörper (89) und SUMO3 Kits (1) und viele weitere Produktgruppen zu diesem Protein an.
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Increased protein level of HSP27 (zeige HSPB1 Proteine) through SUMO2 (zeige SUMO2 Proteine)/3-mediated SUMOylation plays crucial roles in the progression of primary hepatocellular carcinoma.
Increased post-translational modification of proteins by SUMO-2 (zeige SUMO2 Proteine)/3 is a cytoprotective response against cell stress induced by ischaemia and reperfusion.
Data suggest that PIASy (zeige PIAS4 Proteine) exhibits a SIM (zeige SIM2 Proteine) (SUMO-interacting motif) in addition to the SIM (zeige SIM2 Proteine) identified in homologous proteins in other species; both SIMs are located near C terminus of PIASy (zeige PIAS4 Proteine), and both are required for full ligase activity of PIASy (zeige PIAS4 Proteine); hydrophobic core residues of the new SIM (zeige SIM2 Proteine) are essential in binding to SUMO-3. (PIASy (zeige PIAS4 Proteine) = protein inhibitors of activated STAT (zeige STAT1 Proteine) y; SUMO-3 = small ubiquitin-like modifier 3)
The adenovirus E4-ORF3 protein functions as a SUMO E3 ligase for TIF-1gamma sumoylation and poly-SUMO chain elongation.
FOXP2 (zeige FOXP2 Proteine) can be modified with all three human SUMO proteins and that PIAS1 (zeige PIAS1 Proteine) promotes this process.
Small ubiquitin-related modifier 2 (zeige SUMO2 Proteine)/3 interacts with p65 (zeige GORASP1 Proteine) and stabilizes it in the cytoplasm in HBV-associated hepatocellular carcinoma.
Data indicate that small ubiquitin-like modifiers SUMO1 (zeige SUMO1 Proteine), SUMO2 (zeige SUMO2 Proteine), or SUMO3 were found in nuclear speckles.
Adenovirus E4-ORF3 targets PIAS3 (zeige PIAS3 Proteine) and together with E1B (zeige BCKDHB Proteine)-55K remodels SUMO2/SUMO3 Interactions in the nucleus and at virus genome replication domains.
DBC1 modification by Small Ubiquitin-like Modifier 2 (zeige SUMO2 Proteine)/3 is crucial for p53 (zeige TP53 Proteine) transactivation under genotoxic stress.
Expression of SUMO1 (zeige SUMO1 Proteine)/2/3 is dramatically enhanced by interferons through an miRNA-based mechanism involving the Lin28 (zeige LIN28A Proteine)/let-7.
integrity is required for PLK1 localization with SUMO-1 (zeige SUMO1 Proteine) but not with SUMO-2 (zeige SUMO2 Proteine)/3. Inhibition of SUMOylation disrupts proper meiotic bipolar spindle organization and spindle-kinetochore attachment.
a regulatory role of ZNF451-1 in fine-tuning physiological PML (zeige PML Proteine) levels
Results indicate that a functional SUMO1 (zeige SUMO1 Proteine)-3 expression is essential for emotionality and cognition
Expression levels and not functional differences between SUMO2 (zeige SUMO2 Proteine) and SUMO3 are critical for normal embryogenesis.
The purpose of this study was to perform a comprehensive analysis of the SUMO3-modified proteome regulated by brain ischemia using a novel SUMO transgenic mouse.
Stress-induced phosphorylation of Thr486 in c-Myb (zeige MYB Proteine) by p38 (zeige CRK Proteine) mitogen-activated protein kinases attenuates conjugation of SUMO-2 (zeige SUMO2 Proteine)/3.
post-ischemic activation of SUMO2 (zeige SUMO2 Proteine)/3 conjugation may define the fate of neurons exposed to a transient interruption of blood supply
These results suggest that increased Sumo3 in the hippocampus may be correlated with spatial learning ability in old C57BL/6 mice
When alterations in SUMO substrate conjugation occur, global and posttranslational modifications by ubiquitin may play an important role in the mechanisms underlying this Alzheimer disease model.
activation of SUMO2 (zeige SUMO2 Proteine)/3 conjugation is an endogenous neuroprotective stress response.
cyclin E (zeige CCNE1 Proteine) is dynamically and highly conjugated to SUMO2 (zeige SUMO2 Proteine)/3 on chromatin, independently of Cdk2 (zeige CDK2 Proteine) activity and origin activation.
SUM3 promotes plant defense downstream of salicylic acid, while SUM1 (zeige SUMO1 Proteine) and SUM2 (zeige SUMO2 Proteine) together prevent salicylic acid accumulation in noninfected plants.
SUMO proteins, such as SUMO3, and ubiquitin (see MIM 191339) posttranslationally modify numerous cellular proteins and affect their metabolism and function. However, unlike ubiquitination, which targets proteins for degradation, sumoylation participates in a number of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability (Su and Li, 2002
SMT3 homolog 1
, SMT3 suppressor of mif two 3 homolog 1
, SMT3 suppressor of mif two 3 homolog 3
, small ubiquitin-related modifier 3
, ubiquitin-like protein SMT3A
, ubiquitin-like protein SMT3B
, SMT3 (supressor of mif two, 3) homolog 1
, SMT3 suppressor of mif two 3 homolog 2
, SMT3 suppressor of mif two 3 homolog 3, like
, small ubiquitin-related modifier 3-like
, SMT3 suppressor of mif two 3 homolog 3 (S. cerevisiae)
, small ubiquitin-related modifier 3 precursor (SMT3 homolog 1)
, Small ubiquitin-related modifier 3