156 related articles for article (PubMed ID: 27311576)
1. Biophysical Studies on HCV 1a NS3/4A Protease and Its Catalytic Triad in Wild Type and Mutants by the In Silico Approach.
Palanisamy N; Lennerstrand J
Interdiscip Sci; 2018 Mar; 10(1):143-156. PubMed ID: 27311576
[TBL] [Abstract][Full Text] [Related]
2. Low susceptibility of asunaprevir towards R155K and D168A point mutations in HCV NS3/4A protease: A molecular dynamics simulation.
Kammarabutr J; Mahalapbutr P; Nutho B; Kungwan N; Rungrotmongkol T
J Mol Graph Model; 2019 Jun; 89():122-130. PubMed ID: 30884449
[TBL] [Abstract][Full Text] [Related]
3. Computational study on the drug resistance mechanism against HCV NS3/4A protease inhibitors vaniprevir and MK-5172 by the combination use of molecular dynamics simulation, residue interaction network, and substrate envelope analysis.
Xue W; Ban Y; Liu H; Yao X
J Chem Inf Model; 2014 Feb; 54(2):621-33. PubMed ID: 23745769
[TBL] [Abstract][Full Text] [Related]
4. A comparative study of the efficiency of HCV NS3/4A protease drugs against different HCV genotypes using in silico approaches.
Ezat AA; Elshemey WM
Life Sci; 2019 Jan; 217():176-184. PubMed ID: 30528183
[TBL] [Abstract][Full Text] [Related]
5. Molecular docking investigation of the binding interactions of macrocyclic inhibitors with HCV NS3 protease and its mutants (R155K, D168A and A156V).
Ezat AA; El-Bialy NS; Mostafa HI; Ibrahim MA
Protein J; 2014 Feb; 33(1):32-47. PubMed ID: 24374429
[TBL] [Abstract][Full Text] [Related]
6. Exploring resistance mechanisms of HCV NS3/4A protease mutations to MK5172: insight from molecular dynamics simulations and free energy calculations.
Guan Y; Sun H; Pan P; Li Y; Li D; Hou T
Mol Biosyst; 2015 Sep; 11(9):2568-78. PubMed ID: 26219385
[TBL] [Abstract][Full Text] [Related]
7. [Molecular recognition mechanism and motion of HCV NS3/4A protease with Faldaprevir analogue].
Liang L; Hu J; Du W; Zuo K; Liu W; Gou X
Sheng Wu Gong Cheng Xue Bao; 2016 May; 32(5):669-682. PubMed ID: 29019204
[TBL] [Abstract][Full Text] [Related]
8. Molecular principles behind Boceprevir resistance due to mutations in hepatitis C NS3/4A protease.
Nagpal N; Goyal S; Wahi D; Jain R; Jamal S; Singh A; Rana P; Grover A
Gene; 2015 Oct; 570(1):115-21. PubMed ID: 26055089
[TBL] [Abstract][Full Text] [Related]
9. Exploring of paritaprevir and glecaprevir resistance due to A156T mutation of HCV NS3/4A protease: molecular dynamics simulation study.
Boonma T; Nutho B; Darai N; Rungrotmongkol T; Nunthaboot N
J Biomol Struct Dyn; 2022 Aug; 40(12):5283-5294. PubMed ID: 33430709
[TBL] [Abstract][Full Text] [Related]
10. Understanding the drug resistance mechanism of hepatitis C virus NS3/4A to ITMN-191 due to R155K, A156V, D168A/E mutations: a computational study.
Pan D; Xue W; Zhang W; Liu H; Yao X
Biochim Biophys Acta; 2012 Oct; 1820(10):1526-34. PubMed ID: 22698669
[TBL] [Abstract][Full Text] [Related]
11. Molecular modeling study on the resistance mechanism of HCV NS3/4A serine protease mutants R155K, A156V and D168A to TMC435.
Xue W; Pan D; Yang Y; Liu H; Yao X
Antiviral Res; 2012 Jan; 93(1):126-37. PubMed ID: 22127068
[TBL] [Abstract][Full Text] [Related]
12. Understanding the structural and energetic basis of inhibitor and substrate bound to the full-length NS3/4A: insights from molecular dynamics simulation, binding free energy calculation and network analysis.
Xue W; Wang M; Jin X; Liu H; Yao X
Mol Biosyst; 2012 Oct; 8(10):2753-65. PubMed ID: 22833015
[TBL] [Abstract][Full Text] [Related]
13. Computational study on the molecular mechanisms of drug resistance of Narlaprevir due to V36M, R155K, V36M+R155K, T54A, and A156T mutations of HCV NS3/4A protease.
Wang H; Geng L; Chen BZ; Ji M
Biochem Cell Biol; 2014 Oct; 92(5):357-69. PubMed ID: 25178998
[TBL] [Abstract][Full Text] [Related]
14. Avoiding Drug Resistance by Substrate Envelope-Guided Design: Toward Potent and Robust HCV NS3/4A Protease Inhibitors.
Matthew AN; Zephyr J; Nageswara Rao D; Henes M; Kamran W; Kosovrasti K; Hedger AK; Lockbaum GJ; Timm J; Ali A; Kurt Yilmaz N; Schiffer CA
mBio; 2020 Mar; 11(2):. PubMed ID: 32234812
[TBL] [Abstract][Full Text] [Related]
15. Unraveling the structural basis of grazoprevir potency against clinically relevant substitutions in hepatitis C virus NS3/4A protease from genotype 1a.
Guo Z; Black S; Hu Y; McMonagle P; Ingravallo P; Chase R; Curry S; Asante-Appiah E
J Biol Chem; 2017 Apr; 292(15):6202-6212. PubMed ID: 28228479
[TBL] [Abstract][Full Text] [Related]
16. The molecular basis of drug resistance against hepatitis C virus NS3/4A protease inhibitors.
Romano KP; Ali A; Aydin C; Soumana D; Ozen A; Deveau LM; Silver C; Cao H; Newton A; Petropoulos CJ; Huang W; Schiffer CA
PLoS Pathog; 2012; 8(7):e1002832. PubMed ID: 22910833
[TBL] [Abstract][Full Text] [Related]
17. Mapping natural polymorphisms of hepatitis C virus NS3/4A protease and antiviral resistance to inhibitors in worldwide isolates.
López-Labrador FX; Moya A; Gonzàlez-Candelas F
Antivir Ther; 2008; 13(4):481-94. PubMed ID: 18672527
[TBL] [Abstract][Full Text] [Related]
18. Comparative molecular dynamics simulation of Hepatitis C Virus NS3/4A protease (Genotypes 1b, 3a and 4b) predicts conformational instability of the catalytic triad in drug resistant strains.
Kramer M; Halleran D; Rahman M; Iqbal M; Anwar MI; Sabet S; Ackad E; Yousef MS
PLoS One; 2014; 9(8):e104425. PubMed ID: 25111232
[TBL] [Abstract][Full Text] [Related]
19. Relative replication capacity and selective advantage profiles of protease inhibitor-resistant hepatitis C virus (HCV) NS3 protease mutants in the HCV genotype 1b replicon system.
He Y; King MS; Kempf DJ; Lu L; Lim HB; Krishnan P; Kati W; Middleton T; Molla A
Antimicrob Agents Chemother; 2008 Mar; 52(3):1101-10. PubMed ID: 18086851
[TBL] [Abstract][Full Text] [Related]
20. Identification of potential inhibitors for HCV NS3 genotype 4a by combining protein-ligand interaction fingerprint, 3D pharmacophore, docking, and dynamic simulation.
El-Hasab MAE; El-Bastawissy EE; El-Moselhy TF
J Biomol Struct Dyn; 2018 May; 36(7):1713-1727. PubMed ID: 28531373
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]