Outside-binding site mutations modify the active site's shapes in neuraminidase from influenza A H1N1.
about
Targeting a cluster of arginine residues of neuraminidase to avoid oseltamivir resistance in influenza A (H1N1): a theoretical study.An Amino Acid in the Stalk Domain of N1 Neuraminidase Is Critical for Enzymatic ActivityThe significance of naturally occurring neuraminidase quasispecies of H5N1 avian influenza virus on resistance to oseltamivir: a point of concernThree-dimensional structure and molecular dynamics studies of prorrenin/renin receptor: description of the active site.Molecular modeling studies demonstrate key mutations that could affect the ligand recognition by influenza AH1N1 neuraminidase.Identification of neuraminidase inhibitors against dual H274Y/I222R mutant strains.
P2860
Outside-binding site mutations modify the active site's shapes in neuraminidase from influenza A H1N1.
description
2013 nî lūn-bûn
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2013 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի հունվարին հրատարակված գիտական հոդված
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2013年の論文
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2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
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2013年论文
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name
Outside-binding site mutations ...... inidase from influenza A H1N1.
@ast
Outside-binding site mutations ...... inidase from influenza A H1N1.
@en
type
label
Outside-binding site mutations ...... inidase from influenza A H1N1.
@ast
Outside-binding site mutations ...... inidase from influenza A H1N1.
@en
prefLabel
Outside-binding site mutations ...... inidase from influenza A H1N1.
@ast
Outside-binding site mutations ...... inidase from influenza A H1N1.
@en
P2093
P2860
P50
P356
P1433
P1476
Outside-binding site mutations ...... minidase from influenza A H1N1
@en
P2093
Angeles Muñoz-Fernández
Jose Correa-Basurto
Luis Tolentino-Lopez
Mario Rodríguez-Pérez
Mirko Zimic
Paola Reyes-Loyola
P2860
P356
10.1002/BIP.22130
P577
2013-01-01T00:00:00Z