53243-58-6Relevant academic research and scientific papers
Development of O-H insertion for the attachment of phosphonates to nucleosides; Synthesis of α-carboxy phosphononucleosides
Hladezuk, Isabelle,Chastagner, Veronique,Collins, Stuart G.,Plunkett, Stephen J.,Ford, Alan,Debarge, Sebastien,Maguire, Anita R.
experimental part, p. 1894 - 1909 (2012/03/26)
Development of rhodium catalysed O-H insertion reactions employing α-diazophosphonates with appropriately protected adenosine, uridine and thymidine derivatives is described. This synthetic methodology leads, following deprotection, to novel phosphononucl
N5-Phosphonoacetyl-l-ornithine (PALO): A convenient synthesis and investigation of influence on regulation of amino acid biosynthetic genes in Saccharomyces cerevisiae
Johnson, Brad,Steadman, Rachel,Patefield, Krista D.,Bunker, Jeffrey J.,Atkin, Audrey L.,Dussault, Patrick
supporting information; experimental part, p. 2351 - 2353 (2011/06/11)
A scalable four-step synthesis of the ornithine transcarbamylase inhibitor N5-phosphonoacetyl-l-ornithine (PALO) is achieved through boroxazolidinone protection of ornithine. Investigations in the model organism Saccharomyces cerevisiae found t
Inhibition of staphyloxanthin virulence factor biosynthesis in Staphylococcus aureus: In vitro, in vivo, and crystallographic results
Song, Yongcheng,Liu, Chia-I.,Lin, Fu-Yang,Joo, Hwan No,Hensler, Mary,Liu, Yi-Liang,Jeng, Wen-Yih,Low, Jennifer,Liu, George Y.,Nizet, Victor,Wang, Andrew H.-J.,Oldfield, Eric
scheme or table, p. 3869 - 3880 (2009/12/28)
The gold color of Staphylococcus aureus is derived from the carotenoid staphyloxanthin, a virulence factor for the organism. Here, we report the synthesis and activity of a broad variety of staphyloxanthin biosynthesis inhibitors that inhibit the first co
Design, synthesis and activity of bisubstrate, transition-state analogues and competitive inhibitors of aspartate transcarbamylase
Grison, Claude,Coutrot, Philippe,Comoy, Corinne,Balas, Laurence,Joliez, Stephane,Lavecchia, Guido,Oliger, Patrick,Penverne, Bernadette,Serre, Valerie,Herve, Guy
, p. 333 - 344 (2007/10/03)
Aspartate transcarbamylase initiates the de novo biosynthetic pathway for the production of the pyrimidine nucleotides, precursors of nucleic acids. This pathway is particularly active in rapidly growing cells and tissues. Thus, this enzyme has been tested as a potential target for antiproliferative drugs. In the present work, on the basis of its structural and mechanistic properties, a series of substrate analogues, including potential suicide-pseudosubstrates was synthesized and their putative inhibitory effects were tested using E. coli aspartate transcarbamylase as a model. Two of these compounds appear to be very efficient inhibitors of this enzyme.
