Dr SEBASTIAAN WINKLER's Outputs (5)

A non-proteolytic role for ubiquitin in deadenylation by the RNA-binding E3 ligase MEX-3C (2015)
Journal Article
Cano, F., Rapiteanu, R., Winkler, G., & Lehner, P. J. (2015). A non-proteolytic role for ubiquitin in deadenylation by the RNA-binding E3 ligase MEX-3C. Nature Communications, 6, Article 8670. https://doi.org/10.1038/ncomms9670

The regulation of protein and mRNA turnover is essential for many cellular processes. We recently showed that ubiquitin—traditionally linked to protein degradation—directly regulates the degradation of mRNAs through the action of a newly identified f... Read More about A non-proteolytic role for ubiquitin in deadenylation by the RNA-binding E3 ligase MEX-3C.

Phosphonium polymethacrylates for siRNA delivery: effect of polymer and RNA structural parameters on polyplex assembly and gene knockdown (2015)
Journal Article
Loczenski Rose, V., Shubber, S., Sajeesh, S., Spain, S. G., Puri, S., Allen, S., Lee, D.-K., Winkler, G. S., & Mantovani, G. (2015). Phosphonium polymethacrylates for siRNA delivery: effect of polymer and RNA structural parameters on polyplex assembly and gene knockdown. Biomacromolecules, 16(11), https://doi.org/10.1021/acs.biomac.5b00898

Synthetic polymers containing quaternary phosphonium salts are an emerging class of materials for the delivery of oligo/polynucleotides. In this work, cationic phosphonium salt-containing polymethacrylates –and their corresponding ammonium analogues–... Read More about Phosphonium polymethacrylates for siRNA delivery: effect of polymer and RNA structural parameters on polyplex assembly and gene knockdown.

Structural basis of Lewis(b) antigen binding by the Helicobacter pylori adhesin BabA (2015)
Journal Article
Hage, N., Howard, T., Phillips, C., Brassington, C., Overman, R., Debreczeni, J., Gellert, P., Stolnik, S., Winkler, G. S., & Falcone, F. H. (2015). Structural basis of Lewis(b) antigen binding by the Helicobacter pylori adhesin BabA. Science Advances, 1(7), Article e1500315. https://doi.org/10.1126/sciadv.1500315

Helicobacter pylori is a leading cause of peptic ulceration and gastric cancer worldwide. To achieve colonization of the stomach, this Gram-negative bacterium adheres to Lewis(b) (Le(b)) antigens in the gastric mucosa using its outer membrane protein... Read More about Structural basis of Lewis(b) antigen binding by the Helicobacter pylori adhesin BabA.

Discovery, synthesis and biochemical profiling of purine-2,6-dione derivatives as inhibitors of the human poly(A)-selective ribonuclease Caf1 (2015)
Journal Article
Winkler, S., Jadhav, G. P., Kaur, I., Maryati, M., Airhihen, B., & Fischer, P. M. (2015). Discovery, synthesis and biochemical profiling of purine-2,6-dione derivatives as inhibitors of the human poly(A)-selective ribonuclease Caf1. Bioorganic and Medicinal Chemistry Letters, 25(19), 4219-4224. https://doi.org/10.1016/j.bmcl.2015.07.095

Eukaryotic mRNA contains a 3? poly(A) tail, which plays important roles in the regulation of mRNA stability and translation. Well-characterized enzymes involved in the shortening of the poly(A) tail include the multi-subunit Ccr4-Not deadenylase, whi... Read More about Discovery, synthesis and biochemical profiling of purine-2,6-dione derivatives as inhibitors of the human poly(A)-selective ribonuclease Caf1.

The enzyme activities of Caf1 and Ccr4 are both required for deadenylation by the human Ccr4-Not nuclease module (2015)
Journal Article
Maryati, M., Airhihen, B., & Winkler, G. S. (2015). The enzyme activities of Caf1 and Ccr4 are both required for deadenylation by the human Ccr4-Not nuclease module. Biochemical Journal, 469(1), https://doi.org/10.1042/BJ20150304

In eukaryotic cells, the shortening and removal of the poly(A) tail (deadenylation) of cytoplasmic mRNA is a key event in regulated mRNA degradation. A major enzyme involved in deadenylation is the Ccr4-Not deadenylase complex, which can be recruited... Read More about The enzyme activities of Caf1 and Ccr4 are both required for deadenylation by the human Ccr4-Not nuclease module.