10098-40-5Relevant articles and documents
Design and Synthesis of a Highly Selective and in Vivo-Capable Inhibitor of the Second Bromodomain of the Bromodomain and Extra Terminal Domain Family of Proteins
Preston, Alex,Atkinson, Stephen,Bamborough, Paul,Chung, Chun-Wa,Craggs, Peter D.,Gordon, Laurie,Grandi, Paola,Gray, James R. J.,Jones, Emma J.,Lindon, Matthew,Michon, Anne-Marie,Mitchell, Darren J.,Prinjha, Rab K.,Rianjongdee, Francesco,Rioja, Inmaculada,Seal, Jonathan,Taylor, Simon,Wall, Ian,Watson, Robert J.,Woolven, James,Demont, Emmanuel H
, p. 9070 - 9092 (2020/10/19)
Pan-bromodomain and extra terminal domain (BET) inhibitors interact equipotently with the eight bromodomains of the BET family of proteins and have shown profound efficacy in a number of in vitro phenotypic assays and in vivo pre-clinical models in inflam
BENZAMIDE DERIVATIVES AS INHIBITORS OF HISTONE DEACETYLASE
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Page/Page column 109, (2008/06/13)
The invention relates to the inhibition of histone deacetylase. The invention provides compounds which are derivatives of benzamide and suitable in methods for inhibiting histone deacetylase enzymatic activity. The invention also provides compositions and methods for treating cell proliferative diseases and conditions .
Structure-Based Inhibitors of Influenza Virus Salidase. A Benzoic Acid Lead with Novel Interaction
Singh, Sangetta,Jedrzejas, Marek J.,Air, Gillian M.,Luo, Ming,Laver, W. Graeme,Brouillette, Wayne
, p. 3217 - 3225 (2007/10/03)
Influenza virus sialidase is a surface enzyme that is essential for infection of the virus.The catalytic site is highly conserved among all known influenza variants, suggesting that this protein is a suitable target for drug intervention.The most potent known inhibitors are analogs of 2-deoxy-2,3-didehydro-N-acetylneuraminic acid (Neu5Ac2en), particulary the 4-guanidino derivative (4-guanidino-Neu5Ac2en).We utilized the benzene ring of 4-(N-acetylamino)benzoic acids as a cyclic template to substitute for the dihydropyran ring of Neu5Ac2en.In this study several 3-(N-acylamino) derivatives were prepared as potential replacements for the glycerol side chain of Neu5Ac2en, and some were found to interact with the same binding subsite of sialidase.Of greater significance was the observation that the 3-guanidinobenzoic acid derivative (equivalent to the 4-guanidino grouping of 4-guanidino-Neu5Ac2en), the most potent benzoic acid inhibitor of influenza sialidase thus far identified (IC50 = 10 μM), occupied the glycerol-binding subsite on sialidase as opposed to the guanidino-binding subsite.This benzoic acid derivative thus provides a new compound that interacts in a novel manner with the catalytic site of influenza sialidase.