Id |
Subject |
Object |
Predicate |
Lexical cue |
T33 |
0-220 |
Sentence |
denotes |
Another potential drug target for SARS-CoV-2 is RNA‐dependent RNA polymerase (RdRp) (Figure 1), which is a key component of the replication machinery of the virus to make multiple copies of the RNA genome (Elfiky 2020c). |
T34 |
221-274 |
Sentence |
denotes |
RdRp in various coronaviruses are remarkably similar. |
T35 |
275-367 |
Sentence |
denotes |
For example, the RdRp of SARS-CoV exhibits ∼97% sequence similarity with that of SARS-CoV-2. |
T36 |
368-705 |
Sentence |
denotes |
More importantly, there is no human polymerase counterpart that resembles the sequence/structural homology with RdRp from coronaviruses, and hence, the development of RdRp inhibitors could be a potential therapeutic strategy without risk of crosstalk with human polymerases (Borgio et al., 2020; Subissi et al., 2014; Zhai et al., 2005). |
T37 |
706-1086 |
Sentence |
denotes |
Very recently, Yin et al. reported the crystal structure RdRp of SARS-CoV-2 complexed with an antiviral drug, Remdesivir highlighting how the template-primer RNA is recognized by the polymerase enzyme and the chain elongation is inhibited by Remdesivir providing a basis for developing a wide range of effective inhibitors to overcome from SARS-CoV-2 infection (Yin et al., 2020). |
T38 |
1087-1280 |
Sentence |
denotes |
RdRp has been found to be an effective drug target for several other RNA viruses, spanning from the hepatitis C virus, zika virus to coronaviruses (Elfiky, 2017, 2019; Ganesan & Barakat, 2017). |
T39 |
1281-1445 |
Sentence |
denotes |
The active site of RdRp is highly conserved, and the catalytic domains contain two consecutive aspartate residues in a beta-turn joining β15 and β16 (Elfiky 2020c). |
T40 |
1446-1681 |
Sentence |
denotes |
The general structure of RdRp consists of 7 motifs (A to G) among them inner channel of catalytic sites represented by motif A to C, and they play a crucial role during the nucleotide addition cycle (Jia & Gong, 2019; Wu & Gong, 2018). |