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Cover Picture: Studies on Cycloheptathiophene‐3‐carboxamide Derivatives as Allosteric HIV‐1 Ribonuclease H Inhibitors (ChemMedChem 16/2016)
Author(s) -
Corona Angela,
Desantis Jenny,
Massari Serena,
Distinto Simona,
Masaoka Takashi,
Sabatini Stefano,
Esposito Francesca,
Manfroni Giuseppe,
Maccioni Elias,
Cecchetti Violetta,
Pannecouque Christophe,
Le Grice Stuart F. J.,
Tramontano Enzo,
Tabarrini Oriana
Publication year - 2016
Publication title -
chemmedchem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 0.817
H-Index - 100
eISSN - 1860-7187
pISSN - 1860-7179
DOI - 10.1002/cmdc.201600392
Subject(s) - allosteric regulation , rnase h , rna , chemistry , dna , duplex (building) , reverse transcriptase , ribonuclease , rnase p , enzyme , carboxamide , stereochemistry , biochemistry , gene
The front cover picture shows the heterodimeric structure of the HIV‐1 reverse transcriptase (RT) complexed with the RNA:DNA duplex. RT is a multifunctional enzyme endowed with several different functions, including the ribonuclease H (RNase H) activity responsible for the RNA strand hydrolysis of the RNA:DNA replication intermediate. Compounds able to interfere with this pivotal RT‐associated function could represent an innovative anti‐HIV‐1 strategy. The cycloheptathiophene‐3‐carboxamide catechol derivative is a new RNase H nanomolar inhibitor, which is able to recognize an allosteric site (yellow) located below the catalytic site (light blue) as suggested by computational studies. More information can be found in the Full Paper by Oriana Tabarrini, et al. on page 1709 in Issue 16, 2016 (DOI: 10.1002/cmdc.201600015). Artwork by Serena Massari.