10562-83-1Relevant academic research and scientific papers
SAR of non-hydrolysable analogs of pyridoxal 5′-phosphate against low molecular weight protein tyrosine phosphatase isoforms
DeSouza, Shirin R.,Flynn, Rebecca S.,Jakubowski, Henry V.,Marshall, Quinlen F.,McIntee, Edward J.,Olson, Maxwell C.,Sinner, Erica K.,Tinucci, Samantha L.
, (2020)
Kinases and phosphatases are key enzymes in cell signal transduction pathways. Imbalances in these enzymes have been linked to numerous disease states ranging from cancer to diabetes to autoimmune disorders. The two isoforms (IFA and IFB) of Low Molecular Weight Protein Tyrosine Phosphatase (LMW-PTP) appear to play a role in these diseases. Pyridoxal 5′-phosphate (PLP) has been shown to act as a potent but, impractical micromolar inhibitor for both isoforms. In this study, a series of non-hydrolysable phosphonate analogs of PLP were designed, synthesized and tested against the two isoforms of LMW-PTP. Assay results demonstrated that the best inhibitor for both isoforms was compound 5 with a Kis of 1.84 μM (IFA) and 15.6 μM (IFB). The most selective inhibitor was compound 16, with a selectivity of roughly 370-fold for IFA over IFB.
Rhodium-catalyzed hydrophosphorylation of terminal alkynes leading to highly selective formation of (E)-alkenylphosphonates: Complete reversal of regioselectivity to the palladium-catalyzed counterpart
Zhao, Chang-Qiu,Han, Li-Biao,Goto, Midori,Tanaka, Masato
, p. 1929 - 1932 (2007/10/03)
Insights into the mechanism of the rhodium-catalyzed hydrophosphorylation of alkynes with the cylclic hydrogen phosphonate 1 are provided by isolable RhIII intermediates 2 and 3. The reactions proceed at room temperature and give high yields of exclusively (E)-alkenyl phosphonates 4, which are not readily, L = phosphane or hydrogen-phosphonic acid.
