Coxsackievirus B3 is the main cause of human viral myocarditis and cardiomyopathy. Virally encoded Coxsackievirus 3C protease (3C<SUP>pro</SUP>) plays an essential role in viral proliferation. Here, benserazide was discovered as a novel in...
http://chineseinput.net/에서 pinyin(병음)방식으로 중국어를 변환할 수 있습니다.
변환된 중국어를 복사하여 사용하시면 됩니다.
https://www.riss.kr/link?id=A107549490
2015
-
SCOPUS,SCIE
학술저널
1795-1801(7쪽)
0
상세조회0
다운로드다국어 초록 (Multilingual Abstract)
Coxsackievirus B3 is the main cause of human viral myocarditis and cardiomyopathy. Virally encoded Coxsackievirus 3C protease (3C<SUP>pro</SUP>) plays an essential role in viral proliferation. Here, benserazide was discovered as a novel in...
Coxsackievirus B3 is the main cause of human viral myocarditis and cardiomyopathy. Virally encoded Coxsackievirus 3C protease (3C<SUP>pro</SUP>) plays an essential role in viral proliferation. Here, benserazide was discovered as a novel inhibitor from a drug library screen targeting Coxsackievirus 3C<SUP>pro</SUP> using a FRET-based enzyme assay. Benserazide, whose chemical structure has no electrophilic functional groups, was characterized as a non-competitive inhibitor by enzyme kinetic studies. A molecular docking study with benserazide and its analogs indicated that a novel putative allosteric binding site was involved. Specifically, a 2,3,4-trihydroxybenzyl moiety was determined to be a key pharmacophore for the enzyme's inhibitory activity. We suggest that the putative allosteric binding site may be a novel target for future therapeutic strategies.
Hyperproduction of IL-6 caused by aberrant TDP-43 overexpression in high-fat diet-induced obese mice