
IndraLab
Statements
Hydroxychloroquine inhibits Protease. 19 / 19
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"Overall, Chloroquine and its derivatives demonstrated a higher binding affinity for NSP3 viral protein when compared to other proteins included in this study, thereby signifying their potential as inhibitors of NSP3 function.The main protease is moderately inhibited by Hydroxychloroquine with the binding affinity (À4.8 kcal/mol) (Tables 5 and 5.1 supplementary)."
reach
"Overall, Chloroquine and its derivatives demonstrated a higher binding affinity for NSP3 viral protein when compared to other proteins included in this study, thereby signifying their potential as inhibitors of NSP3 function.The main protease is moderately inhibited by Hydroxychloroquine with the binding affinity (−4.8 kcal/mol) (Tables 5 and 5.1 supplementary)."
eidos
"The reduced acidification might also be the reason for prevention of SARS-CoV-2 invasion via the cathepsin L-dependent endocytic pathway : since cathepsin L has an acidic pH optimum ( around pH 5.5 ) and is unstable at higher pH ( Turk et al ., 1993 ) , CQ and HCQ could lower the activity of these proteases and block proteolytic activation of the S protein and thus block subsequent fusion between the viral envelope and lysosomal or endosomal membranes ."