Selected article for: "active form and replication inhibit"

Author: Jingyue Ju; Xiaoxu Li; Shiv Kumar; Steffen Jockusch; Minchen Chien; Chuanjuan Tao; Irina Morozova; Sergey Kalachikov; Robert N. Kirchdoerfer; James J. Russo
Title: Nucleotide Analogues as Inhibitors of SARS-CoV Polymerase
  • Document date: 2020_3_14
  • ID: hj675z1b_8
    Snippet: These results demonstrate that lower fidelity polymerases will have a high likelihood of incorporating 2'-F,Me-UTP and inhibit viral RNA replication, whereas high fidelity enzymes, more typical of the host DNA and RNA polymerases, will have a low likelihood of being inhibited by 2'-F,Me-UTP. Anti-viral drug design based on this principle may lead to potent viral polymerase inhibitors with fewer side effects. To provide further proof that SARS-CoV.....
    Document: These results demonstrate that lower fidelity polymerases will have a high likelihood of incorporating 2'-F,Me-UTP and inhibit viral RNA replication, whereas high fidelity enzymes, more typical of the host DNA and RNA polymerases, will have a low likelihood of being inhibited by 2'-F,Me-UTP. Anti-viral drug design based on this principle may lead to potent viral polymerase inhibitors with fewer side effects. To provide further proof that SARS-CoV-2 RdRp might be inhibited by 2'-F,Me-UTP, we next tested the ability of this molecule to be incorporated into an RNA primer to terminate the reaction catalyzed by the RdRp from SARS-CoV, using an RNA template. As shown in Fig. 4a , the active triphosphate form of the drug not only was incorporated by the RdRp, but prevented further incorporation, behaving as a terminator in the polymerase reaction.

    Search related documents:
    Co phrase search for related documents
    • active drug triphosphate form and polymerase reaction: 1, 2
    • active drug triphosphate form and RNA polymerase: 1, 2, 3, 4
    • active drug triphosphate form and RNA replication: 1
    • active drug triphosphate form and RNA template: 1
    • active drug triphosphate form and SARS RdRp inhibit: 1
    • active drug triphosphate form and triphosphate form: 1, 2, 3, 4, 5, 6
    • active drug triphosphate form and viral polymerase: 1, 2
    • drug design and RNA polymerase: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21, 22, 23, 24, 25, 26, 27, 28, 29, 30, 31, 32, 33, 34, 35, 36, 37, 38, 39, 40, 41, 42, 43, 44
    • drug design and RNA primer: 1, 2, 3
    • drug design and RNA replication: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11, 12, 13, 14, 15, 16, 17, 18, 19, 20, 21
    • drug design and RNA template: 1, 2, 3
    • drug design and triphosphate form: 1
    • drug design and viral polymerase: 1, 2, 3, 4, 5, 6, 7, 8, 9, 10, 11
    • drug design and viral RNA replication: 1, 2, 3, 4, 5, 6, 7, 8, 9
    • drug triphosphate form and polymerase reaction: 1, 2
    • drug triphosphate form and RNA polymerase: 1, 2, 3, 4
    • drug triphosphate form and RNA replication: 1
    • drug triphosphate form and RNA template: 1
    • drug triphosphate form and SARS RdRp inhibit: 1