Thioester derivatives of the natural product psammaplin A as potent histone deacetylase inhibitors

• Matthias G. J. Baud,
• Thomas Leiser,
• Vanessa Petrucci,
• Mekala Gunaratnam,
• Stephen Neidle,
• Franz-Josef Meyer-Almes and
• Matthew J. Fuchter

Beilstein J. Org. Chem. 2013, 9, 81–88, doi:10.3762/bjoc.9.11

• class IV. Despite their name, several HDACs are able to deacetylate a number of nonhistone protein substrates [10][11]. Sirtuins are structurally and mechanistically distinct enzymes. To date, only two compounds that inhibit HDACs have been FDA approved: suberoylanilide hydroxamic acid (SAHA, 1, trade

Approaches to α-amino acids via rearrangement to electron-deficient nitrogen: Beckmann and Hofmann rearrangements of appropriate carboxyl-protected substrates

• Sosale Chandrasekhar and
• V. Mohana Rao

Beilstein J. Org. Chem. 2012, 8, 1393–1399, doi:10.3762/bjoc.8.161

• complicated by competing deacylation, hydroxamic acid formation, etc. We are only aware of two reports [8][9] of the Beckmann rearrangement of β-keto ester oximes. A particular problem was the formation of isoxazolone byproducts, which apparently limited the synthesis to α,α-disubstituted derivatives