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Inside Back Cover: Fluorescein Analogues Inhibit SecA ATPase: The First Sub‐micromolar Inhibitor of Bacterial Protein Translocation (ChemMedChem 4/2012)
Author(s) -
Huang YingJu,
Wang Hongyun,
Gao FenBiao,
Li Minyong,
Yang Hsiuchin,
Wang Binghe,
Tai Phang C.
Publication year - 2012
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.201290017
Subject(s) - chemistry , chromosomal translocation , atpase , secretion , fluorescein , enzyme , cover (algebra) , bacterial translocation , side chain , biochemistry , combinatorial chemistry , biophysics , stereochemistry , biology , fluorescence , organic chemistry , gene , mechanical engineering , physics , quantum mechanics , engineering , polymer
The back cover picture shows the inhibition of SecA, a key enzyme in the bacterial general secretion (Sec) pathway. SecA is essential for bacterial growth and as such represents an ideal target for antibacterial agents. The fluorescein derivatives shown represent the first sub‐micromolar inhibitors of SecA's ATPase activity. For more details, see the Full Paper by Binghe Wang, Phang C. Tai et al. on p. 571 ff.