作者: Daniel L Flynn , Norman A Abood , Barry C Holwerda
DOI: 10.1016/S1367-5931(97)80009-9
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摘要: Major advances have been reported in the last two years regarding molecular biology and structural properties of herpesvirus proteases. X-ray diffraction studies enabled several groups to solve structure human cytomegalovirus protease. Fluorescence-based substrate assays also recently reported. These substrates exhibit sufficient kinetic sensitivity enable high-throughput screening efforts dedicated toward discovery protease inhibitors. Three classes inhibitors recently: nonpeptidic aryl trifluoromethylketones; alternate (benzoxazinones/azalactones); thiol-modifying The class offers a unique opportunity discover specific protease, as this requires reduced cysteine residues for its enzymatic activity.