Plasticity of 150-loop in influenza neuraminidase explored by Hamiltonian replica exchange molecular dynamics simulations
Neuraminidase (NA) of influenza is a key target for antiviral inhibitors, and the 150-cavity in group-1 NA provides new insight in treating this disease. However, NA of 2009 pandemic influenza (09N1) was found lacking this cavity in a crystal structure. To address the issue of flexibility of the 1...
Saved in:
Main Authors: | Han, Nanyu, Mu, Yuguang |
---|---|
Other Authors: | School of Biological Sciences |
Format: | Article |
Language: | English |
Published: |
2013
|
Subjects: | |
Online Access: | https://hdl.handle.net/10356/96407 http://hdl.handle.net/10220/9875 |
Tags: |
Add Tag
No Tags, Be the first to tag this record!
|
Institution: | Nanyang Technological University |
Language: | English |
Similar Items
-
Locking the 150-cavity open : in silico design and verification of influenza neuraminidase inhibitors
by: Han, Nanyu, et al.
Published: (2013) -
Plasticity of the 340-loop in influenza neuraminidase offers new insight for antiviral drug development
by: Han, Nanyu, et al.
Published: (2021) -
Exploring the mechanism of Zanamivir resistance in a neuraminidase mutant : a molecular dynamics study
by: Han, Nanyu, et al.
Published: (2013) -
Glycan binding and specificity of viral influenza neuraminidases by classical molecular dynamics and replica exchange molecular dynamics simulations
by: Jiraphorn Phanich, et al.
Published: (2018) -
Resistant machanisms, dynamic properties and inhibitor development of neuraminidase in influenza virus : molecular dynamics simulations studies
by: Han, Nanyu
Published: (2014)