444058-90-6Relevant academic research and scientific papers
Synthesis and Antibacterial Evaluation of Mannich Bases Derived from 1,2,4-Triazole
Paneth, Agata,Trotsko, Nazar,Popio?ek, ?ukasz,Grzegorczyk, Agnieszka,Krzanowski, Tomasz,Janowska, Sara,Malm, Anna,Wujec, Monika
, (2019)
The series of novel Mannich bases were synthesized and evaluated for their in vitro antibacterial activity against Gram-positive and Gram-negative bacterial strains. The results showed that all compounds were less active than the drugs used as reference, but some of them had moderate potency against Staphylococcus epidermidis ATCC 12228 and Bacillus subtilis ATCC 6633. The presence of a phenyl ring in the position 4 of piperazine seems to be necessary for antibacterial activity in this class of compounds.
Antibacterial activity of fluorobenzoylthiosemicarbazides and their cyclic analogues with 1,2,4-triazole scaffold
Kosikowska, Urszula,P?onka, Wojciech,Paneth, Agata,Paneth, Piotr,Trotsko, Nazar,Wujec, Monika
, (2021/05/28)
The development of drug-resistant bacteria is currently one of the major challenges in medicine. Therefore, the discovery of novel lead structures for the design of antibacterial drugs is urgently needed. In this structure–activity relationship study, a l
Discovery of protein-protein interaction inhibitors of replication protein A
Patrone, James D.,Kennedy, J. Phillip,Frank, Andreas O.,Feldkamp, Michael D.,Vangamudi, Bhavatarini,Pelz, Nicholas F.,Rossanese, Olivia W.,Waterson, Alex G.,Chazin, Walter J.,Fesik, Stephen W.
, p. 601 - 605 (2013/07/26)
Replication protein A (RPA) is a ssDNA binding protein that is essential for DNA replication and repair. The initiation of the DNA damage response by RPA is mediated by protein-protein interactions involving the N-terminal domain of the 70 kDa subunit with partner proteins. Inhibition of these interactions increases sensitivity toward DNA damage and replication stress and may therefore be a potential strategy for cancer drug discovery. Toward this end, we have discovered two lead series of compounds, derived from hits obtained from a fragment-based screen, that bind to RPA70N with low micromolar affinity and inhibit the binding of an ATRIP-derived peptide to RPA. These compounds may offer a promising starting point for the discovery of clinically useful RPA inhibitors.
