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Exploring the Influence of EGCG on the β-Sheet-Rich Oligomers of Human Islet Amyloid Polypeptide (hIAPP1–37) and Identifying Its Possible Binding Sites from Molecular Dynamics Simulation
EGCG possesses the ability of disaggregating the existing amyloid fibrils which were associated with many age-related degenerative diseases. However, the molecular mechanism of EGCG to disaggregate… Expand
Molecular modeling and residue interaction network studies on the mechanism of binding and resistance of the HCV NS5B polymerase mutants to VX-222 and ANA598.
Hepatitis C virus (HCV) NS5B protein is an RNA-dependent RNA polymerase (RdRp) with essential functions in viral genome replication and represents a promising therapeutic target to develop… Expand
Stabilities and structures of islet amyloid polypeptide (IAPP22-28) oligomers: from dimer to 16-mer.
- Jingjing Guo, Y. Zhang, Lulu Ning, Pingzu Jiao, H. Liu, X. Yao
- Chemistry, Medicine
- Biochimica et biophysica acta
BACKGROUND The formation of amyloid fibrils is associated with many age-related degenerative diseases. Nevertheless, the molecular mechanism that directs the nucleation of these fibrils is not fully… Expand
Understanding the drug resistance mechanism of hepatitis C virus NS5B to PF-00868554 due to mutations of the 423 site: a computational study.
- Pingzu Jiao, Weiwei Xue, Yulin Shen, Nengzhi Jin, H. Liu
- Biology, Medicine
- Molecular bioSystems
- 4 March 2014
NS5B, a hepatitis C virus (HCV) RNA-dependent RNA polymerase (RdRp) that plays a key role in viral replication, is an important target in the discovery of antiviral agents. PF-00868554 is a potent… Expand