Publications by authors named "Magda Liczmanska"
The small ubiquitin-like modifier (SUMO) protease SENP6 disassembles SUMO chains from cellular substrate proteins. We use a proteomic method to identify putative SENP6 substrates based on increased apparent molecular weight after SENP6 depletion. Proteins of the lamin family of intermediate filaments show substantially increased SUMO modification after SENP6 depletion.
View Article and Find Full Text PDFAcute Promyelocytic Leukemia is caused by expression of the oncogenic Promyelocytic Leukemia (PML)-Retinoic Acid Receptor Alpha (RARA) fusion protein. Therapy with arsenic trioxide results in degradation of PML-RARA and PML and cures the disease. Modification of PML and PML-RARA with SUMO and ubiquitin precedes ubiquitin-mediated proteolysis.
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- Researchers studied how SUMO modification affects pluripotent stem cells using ML792, a SUMO Activating Enzyme inhibitor, which led to the loss of key pluripotency markers in these cells.
- Through engineering cells to express modified SUMO proteins, they identified 976 SUMO modification sites across 427 proteins, revealing networks involved in gene expression regulation, ribosome biogenesis, and RNA splicing.
- The study found that SUMO modification plays a significant role in maintaining the pluripotent state of human induced pluripotent stem cells, with a focus on chromatin-associated proteins as critical SUMO substrates.
In the class of polyene macrolides, there is a subgroup of aromatic heptaenes, which exhibit the highest antifungal activity within this type of antibiotics. Yet, due to their complex nature, aromatic heptaenes were not extensively studied and their potential as drugs is currently underexploited. Moreover, there are many inconsistencies in the literature regarding the composition and the structures of the individual components of the aromatic heptaene complexes.
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