13283-92-6Relevant articles and documents
Seven new didemnins from the marine tunicate Trididemnum solidum
Sakai, Ryuichi,Stroh, Justin G.,Sullins, David W.,Rinehart, Kenneth L.
, p. 3734 - 3748 (1995)
Seven new didemnins-didemnins M (1), N (2), X (3) and Y (4), nordidemnin N (5), epididemnin A1 (6), and acyclodidemnin A (7)-were isolated from an extract of the Caribbean tunicate Trididemnum solidum. The structures of these compounds were assigned, based on FABMS, high-field NMR data, and chemical degradation studies. Biological activities of these peptides are also described.
Biosynthesis of 2-Alkyl-4(1H)-Quinolones in Pseudomonas aeruginosa: Potential for Therapeutic Interference with Pathogenicity
Pistorius, Dominik,Ullrich, Angelika,Lucas, Simon,Hartmann, Rolf W.,Kazmaier, Uli,Mueller, Rolf
, p. 850 - 853 (2011)
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MACROCYCLIC BROAD SPECTRUM ANTIBIOTICS
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, (2017/08/01)
Provided herein are antibacterial compounds, wherein the compounds in some embodiments have broad spectrum bioactivity. In various embodiments, the compounds act by inhibition of bacterial type 1 signal peptidase (SpsB), an essential protein in bacteria. Pharmaceutical compositions and methods for treatment using the compounds described herein are also provided.
A Continuous, Fluorogenic Sirtuin 2 Deacylase Assay: Substrate Screening and Inhibitor Evaluation
Galleano, Iacopo,Schiedel, Matthias,Jung, Manfred,Madsen, Andreas S.,Olsen, Christian A.
, p. 1021 - 1031 (2016/02/23)
Sirtuins are important regulators of lysine acylation, which is implicated in cellular metabolism and transcriptional control. This makes the sirtuin class of enzymes interesting targets for development of small molecule probes with pharmaceutical potential. To achieve detailed profiling and kinetic insight regarding sirtuin inhibitors, it is important to have access to efficient assays. In this work, we report readily synthesized fluorogenic substrates enabling enzyme-economical evaluation of SIRT2 inhibitors in a continuous assay format as well as evaluation of the properties of SIRT2 as a long chain deacylase enzyme. Novel enzymatic activities of SIRT2 were thus established in vitro, which warrant further investigation, and two known inhibitors, suramin and SirReal2, were profiled against substrates containing ε-N-acyllysine modifications of varying length.
