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Human Polyclonal SUMO1 Primary Antibody pour FACS, IF - ABIN1882136
Yang, Sharrocks: SUMO promotes HDAC-mediated transcriptional repression. dans Molecular cell 2004
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Human Monoclonal SUMO1 Primary Antibody pour WB - ABIN1882054
Shanwell, Ringdén, Wiechel, Rumin, Akerblom: A study of the effect of ABO incompatible plasma in platelet concentrates transfused to bone marrow transplant recipients. dans Vox sanguinis 1991
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Human Polyclonal SUMO1 Primary Antibody pour FACS, IF - ABIN1882137
Bailey, OHare: Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1. dans The Journal of biological chemistry 2003
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Human Monoclonal SUMO1 Primary Antibody pour IF, IHC (p) - ABIN2452138
Saitoh, Uchimura, Tachibana, Sugahara, Saitoh, Nakao: In situ SUMOylation analysis reveals a modulatory role of RanBP2 in the nuclear rim and PML bodies. dans Experimental cell research 2006
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Human Monoclonal SUMO1 Primary Antibody pour IF, IHC (p) - ABIN2452136
Cheng, Bawa, Lee, Gong, Yeh: Role of desumoylation in the development of prostate cancer. dans Neoplasia (New York, N.Y.) 2006
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Human Monoclonal SUMO1 Primary Antibody pour IF, IHC (p) - ABIN2452137
Uchimura, Ichimura, Uwada, Tachibana, Sugahara, Nakao, Saitoh: Involvement of SUMO modification in MBD1- and MCAF1-mediated heterochromatin formation. dans The Journal of biological chemistry 2006
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Human Polyclonal SUMO1 Primary Antibody pour IHC (p), ELISA - ABIN542825
Ling, Sankpal, Robertson, McNally, Karpova, Robertson: Modification of de novo DNA methyltransferase 3a (Dnmt3a) by SUMO-1 modulates its interaction with histone deacetylases (HDACs) and its capacity to repress transcription. dans Nucleic acids research 2004
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Human Polyclonal SUMO1 Primary Antibody pour FACS, IHC (p) - ABIN388027
Laoong-u-thai, Zhao, Phongdara, Ako, Yang: Identifications of SUMO-1 cDNA and its expression patterns in Pacific white shrimp Litopeanaeus vannamei. dans International journal of biological sciences 2009
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Schistosoma japonicum Monoclonal SUMO1 Primary Antibody pour WB - ABIN387785
Jia, Li, Meng, Shi: Association between polymorphisms at small ubiquitin-like modifier 1 and nonsyndromic orofacial clefts in Western China. dans DNA and cell biology 2010
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Human Polyclonal SUMO1 Primary Antibody pour IF, IHC (p) - ABIN543364
Degerny, Monte, Beaudoin, Jaffray, Portois, Hay, de Launoit, Baert: SUMO modification of the Ets-related transcription factor ERM inhibits its transcriptional activity. dans The Journal of biological chemistry 2005
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SUMO1 expression results in a gain of PKR activity by increasing its activation. SUMO1 was able to activate PKR and eIF-2alpha in the absence of viral infection.
SPOP inhibits hepatocellular carcinoma (HCC) cell metastasis via ubiquitin-dependent SUMO1/SENP7 proteolysis and may thus serve as a new opinion for the prevention of HCC metastasis.
Study found a significant difference in the expression of Cx43 and SUMO1 between cancer stem cells and non-cancer stem cells in liver cancer. By the co-expression of Cx43 and SUMO1 in cancer stem cells, the gap junction intercellular communication of liver cancer stem cells was obviously improved.
Two SUMO modification sites existed in dopamine receptor D1, the phosphorylation of which, due to SUMO modification, can interact with PP2A, leading to the inhibition of D1 de-phosphorylation and normal function.
The SUMO1/UBC9 axis may regulate Nox1mediated diabetic retinopathy by inhibiting reactive oxygen species generation and apoptosis.
These results suggest that SUMO1 contributes to hepatocellular carcinoma progression by promoting p65 nuclear translocation
In summary, our study revealed a negative regulation of the UPR transducer ATF6 through post-translational SUMOylation. The information from this study will not only increase our understanding of the fine-tuning regulation of the UPR signaling but will also be informative to the modulation of the UPR for therapeutic benefits.
Molecular dynamics simulations showed that binding of the beta-grasp domain of SUMO1 induces significant conformational and dynamic changes in SENP1, including widening of the exosite cleft and quenching of nanosecond dynamics in all but a distal region.
Mutational analysis of functional sites showed that both peroxidase and PLA2 active sites were necessary for mutant Prdx6 function, and that Prdx6 phosphorylation (at T177 residue) was essential for optimum PLA2 activity.Mutant Prdx6 at its Sumo1 sites escapes and abates this adverse process by maintaining its integrity and gaining function
SUMO and p21Cip1 regulate the transit of proteins through the nucleolus; disruption of nucleolar export by DNA damage induces SUMO and p21Cip1 to act as hub proteins to form a multiprotein complex in the nucleolus.
This study reveals an essential role of SUMOylated FADD in Drp1- and caspase-10-dependent necrosis.
SUMO-1 gene silencing inhibits proliferation and promotes apoptosis of human gastric cancer cells.
the critical role of Cys52 in maintaining SUMO-1 conformation and function
Findings suggest SUMO-1 protein and PGE2 receptor subtype 4 (EP4) as two potential targets for new therapeutic or prevention strategies for endometrial cancers.
This study demonstrated that the rs12472035 polymorphism of SUMO1 was significantly associated with an increased risk of AD in male group.
FOXP2 can be modified with all three human SUMO proteins and that PIAS1 promotes this process.
Ang II-induced upregulation of ATF3 and SUMO1 in vitro and in vivo was blocked by Ang II type I receptor antagonist olmesartan. Moreover, Ang II induced ATF3 SUMOylation at lysine 42, which is SUMO1 dependent.
Data show that mutation of key residues in the binding site abolishes binding and that small ubiquitin-like modifier 1 (SUMO1) can simultaneously and non-cooperatively bind both the ZZ domain and a canonical SIM motif of CREB-binding protein (CBP/p300).
Roles for SUMO in pre-mRNA processing
SUMOylation at specific sites on PXR protein are involved in enhancement of transcription function of this receptor.
SUMO chain formation relies on the amino-terminal region of SCE1 and has dedicated substrates in plants.
Functionally similar to human SUMO2 and SUMO3, Arabidopsis SUMO1 and 2 can form chains, even though they do not possess a consensus SUMOylation motif. The surprising finding that plants have dedicated enzymes for chain synthesis implies a specific role for SUMO chains in plants
we provide evidence for the existence of a preferential conjugation of AtSUMO1/2 compared with AtSUMO3/5, which is determined by a role of the E1-activating enzyme in SUMO paralogue discrimination.
SUMO1 becomes conjugated with ubiquitin during heat stress, showing posttranslational modifications.
SUM3 promotes plant defense downstream of salicylic acid, while SUM1 and SUM2 together prevent salicylic acid accumulation in noninfected plants.
SIZ1-mediated conjugation of SUMO1 and SUMO2 to other intracellular proteins is essential in Arabidopsis, possibly through stress-induced modification of a potentially diverse pool of nuclear proteins.
results support the critical role of SUMO-1 in SERCA2a function and underline the therapeutic potential of SUMO-1 for HF patients
Analysis of protein interactions showed that K179A, K180A, and K221A substitutions of classical swine fever virus core protein disrupt core-SUMO-1 binding, while K220A substitution precludes core-UBC9 binding.
The gene knockout technique is important in xenotransplantation research; here we have described the molecular cloning of SUMO-1 gene that may be a candidates to overcome the poor rate of homologous recombination.
integrity is required for PLK1 localization with SUMO-1 but not with SUMO-2/3. Inhibition of SUMOylation disrupts proper meiotic bipolar spindle organization and spindle-kinetochore attachment.
These findings indicate that SUMO1-conjugation of synaptic proteins does not occur or is extremely rare and hence not detectable using current methodology.
Study found expression of several mutated forms of SOD1 in the NSC-34 motor neuronal cells induces the formation of cytosolic and sometimes nuclear aggregates containing the SUMO-1 protein and showed that the formation of these aggregates can be modulated by action on the K75 SUMOylation site
The LKB1 K178R SUMO mutant had defective AMPK signaling and mitochondrial function, inducing death in energy-deprived cells.
These findings point to a significant contribution of SUMO1 modification on neuronal function which may have implications for mechanisms involved in mental retardation and neurodegeneration.
PML IV/ARF interaction enhances p53 SUMO-1 conjugation, activation, and senescence.
SUMO1 accelerates the accumulation of autophagic vacuoles and promotes Abeta production.
The present study used immunohistochemical and immunoblot analysis with the different developmental stages of mice and demonstrated the developmentally regulated distribution of SUMO1.
The results of this study indicate that post-translational modifications of SERCA2a caused by the toxic environment of the hypertrophied and failing myocardium can be prevented by SUMO-1.
SUMO-1 plays crucial roles for spindle organization, chromosome congression, and chromosome segregation during mouse oocyte meiotic maturation.
Results indicate that a functional SUMO1-3 expression is essential for emotionality and cognition
Adult mice showed proportionately greater increases in SUMO-1 than the aged group.
Increasing SUMOylation in astrocytes, by over-expression of constitutively active SUMO-1, but not its inactive mutant, abrogated Abeta-induced increase in GFAP, suggesting astrocytes require SUMO-1 conjugation to remain non-reactive.
Sumo1 Heterozygosity Rescues Senp1 Mutant Defects.
SUMO-1 is elevated in the brain of Alzheimer disease model mice.
SUMOylation of pancreatic glucokinase regulates its cellular stability and activity
Mutant lamin A/C alters the dynamics of sumo1 and thus misregulation of sumoylation may be contributing to disease progression in laminopathies.
identification of SUMOylated proteins in the brain of His6-HA-SUMO1 knock-in mice
SUMO modification of Stra13 is required for repression of cyclin D1 expression and cellular growth arrest
SUMO1 covalently modifies Blimp-1 at lysine 816
This gene encodes a protein that is a member of the SUMO (small ubiquitin-like modifier) protein family. It functions in a manner similar to ubiquitin in that it is bound to target proteins as part of a post-translational modification system. However, unlike ubiquitin which targets proteins for degradation, this protein is involved in a variety of cellular processes, such as nuclear transport, transcriptional regulation, apoptosis, and protein stability. It is not active until the last four amino acids of the carboxy-terminus have been cleaved off. Several pseudogenes have been reported for this gene. Alternate transcriptional splice variants encoding different isoforms have been characterized.
SMT3 suppressor of mif two 3 homolog 1
, small ubiquitin-related modifier 1
, small ubiquitin-related modifier-1
, ubiquitin-like 1 (sentrin)
, GAP modifying protein 1
, SMT3 homolog 3
, ubiquitin-homology domain protein PIC1
, ubiquitin-like protein SMT3C
, ubiquitin-like protein UBL1
, SMT3 suppressor of mif two 3 homolog 1 (S. cerevisiae)
, SMT3 suppressor of mif two 3-like 1
, small ubiquitin-related modifier 1-B
, small ubiquitin-related protein 1
, smt3 suppressor of mif two 3 homolog 1
, SUMO-1 related peptidase
, ubiquitin-like 1
, small ubiquitin-like modifier 1