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Cover Picture: Probing Mercaptobenzamides as HIV Inactivators via Nucleocapsid Protein 7 (ChemMedChem 10/2017)
Author(s) -
Saha Mrinmoy,
Scerba Michael T.,
Shank Nathaniel I.,
Hartman Tracy L.,
Buchholz Caitlin A.,
Buckheit Robert W.,
Durell Stewart R.,
Appella Daniel H.
Publication year - 2017
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.201700283
Subject(s) - human immunodeficiency virus (hiv) , chemistry , zinc finger , cover (algebra) , front cover , small molecule , zinc , molecule , cysteine , function (biology) , virology , stereochemistry , computational biology , crystallography , biochemistry , biology , microbiology and biotechnology , organic chemistry , mechanical engineering , transcription factor , engineering , gene , enzyme
The front cover picture shows the C‐terminal domain of Nucleocapsid Protein 7 (NCp7) of the human immunodeficiency virus (HIV) and the likely mode by which an S ‐acetylmercaptobenzamide molecule reacts with the protein. Acetyl transfer from the mercaptobenzamide to the sulfur of a cysteine in NCp7 destabilizes the zinc coordination, which leads to protein unfolding and loss of function. These types of molecules are being developed as potential new treatments for HIV infection. More information can be found in the Communication by Daniel H. Appella et al. on page 714 in Issue 10, 2017 (DOI: 10.1002/cmdc.201700141).