Title : Molecular modeling study on the resistance mechanism of HCV NS3/4A serine protease mutants R155K, A156V and D168A to TMC435.

Pub. Date : 2012 Jan

PMID : 22127068






6 Functional Relationships(s)
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1 Molecular modeling study on the resistance mechanism of HCV NS3/4A serine protease mutants R155K, A156V and D168A to TMC435. Simeprevir KRAS proto-oncogene, GTPase Homo sapiens
2 Herein, based on the recently determined structure of NS3/4A-TMC435 complex, atomic-level models of the key residue mutated (R155K, A156V and D168A) NS3/4A-TMC435 complexes were constructed. Simeprevir KRAS proto-oncogene, GTPase Homo sapiens
3 Herein, based on the recently determined structure of NS3/4A-TMC435 complex, atomic-level models of the key residue mutated (R155K, A156V and D168A) NS3/4A-TMC435 complexes were constructed. Simeprevir KRAS proto-oncogene, GTPase Homo sapiens
4 Herein, based on the recently determined structure of NS3/4A-TMC435 complex, atomic-level models of the key residue mutated (R155K, A156V and D168A) NS3/4A-TMC435 complexes were constructed. Simeprevir KRAS proto-oncogene, GTPase Homo sapiens
5 Herein, based on the recently determined structure of NS3/4A-TMC435 complex, atomic-level models of the key residue mutated (R155K, A156V and D168A) NS3/4A-TMC435 complexes were constructed. Simeprevir KRAS proto-oncogene, GTPase Homo sapiens
6 These findings could provide some insights into the resistance mechanism of NS3/4A protease mutants to TMC435 and would be critical for the development of novel inhibitors that are less susceptible to drug resistance. Simeprevir KRAS proto-oncogene, GTPase Homo sapiens