136516-64-8Relevant articles and documents
Efficient two-step synthesis of salicylaldehydes via directed ortho-lithiation of in situ N-silylated O-aryl N-isopropylcarbamates
Kauch, Matthias,Hoppe, Dieter
, p. 1575 - 1577 (2006)
O-Aryl N-isopropylcarbamates, conveniently prepared from phenols and isopropyl isocyanate, are subjected to an efficient ortho-lithiation protocol to afford the corresponding salicylaldehydes in a one-pot operation in high yields. Georg Thieme Verlag Stuttgart.
Compounds for treating spinal muscular atrophy
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Page/Page column 327; 328, (2017/05/02)
Provided herein are compounds, compositions thereof and uses therewith for treating spinal muscular atrophy. In a specific embodiment, provided herein are compounds of a form that may be used to modulate the inclusion of exon 7 of SMN2 into mRNA that is transcribed from the SMN2 gene. In another specific embodiment, provided herein are compounds of a form that may be used to modulate the inclusion of exon 7 of SMN1 into mRNA that is transcribed from the SMN1 gene. In yet another embodiment, provided herein are compounds of a form that may be used to modulate the inclusion of exon 7 of SMN1 and SMN2 into mRNA that is transcribed from the SMN1 and SMN2 genes, respectively.
Structure based drug design: Development of potent and selective factor IXa (FIXa) inhibitor
Wang, Shouming,Beck, Richard,Burd, Andrew,Blench, Toby,Marlin, Frederic,Ayele, Tenagne,Buxton, Stuart,Dagostin, Claudio,Malic, Maja,Joshi, Rina,Barry, John,Sajad, Mohammed,Cheung, Chiming,Shaikh, Shaheda,Chahwala, Suresh,Criandera, Chaman,Baumgartner, Christine,Holthoff, Hans-Peter,Murray, Elizabeth,Blackney, Michael,Giddings, Amanda
experimental part, p. 1473 - 1482 (2010/08/03)
On the basis of our understanding on the binding interactions of the benzothiophene template within the FIXa active site by X-ray crystallography and molecular modeling studies, we developed our SAR strategy by targeting the 4-position of the template to access the S1 β and S2-S4 sites. A number of highly selective and potent, factor Xa (FXa) and FIXa inhibitors were identified by simple switch of functional groups with conformational changes toward the S2-S4 sites.