New binding site conformations of the dengue virus NS3 protease accessed by molecular dynamics simulation.
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NMR and MD Studies Reveal That the Isolated Dengue NS3 Protease Is an Intrinsically Disordered Chymotrypsin Fold Which Absolutely Requests NS2B for Correct Folding and Functional DynamicsMycobacterium tuberculosis Prolyl Oligopeptidase Induces In vitro Secretion of Proinflammatory Cytokines by Peritoneal Macrophages.Identification of new potent inhibitors of dengue virus NS3 protease from traditional Chinese medicine database.Molecular docking NS4B of DENV 1-4 with known bioactive phyto-chemicals.
P2860
New binding site conformations of the dengue virus NS3 protease accessed by molecular dynamics simulation.
description
2013 nî lūn-bûn
@nan
2013 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
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
@zh-tw
2013年论文
@wuu
name
New binding site conformations ...... molecular dynamics simulation.
@ast
New binding site conformations ...... molecular dynamics simulation.
@en
type
label
New binding site conformations ...... molecular dynamics simulation.
@ast
New binding site conformations ...... molecular dynamics simulation.
@en
prefLabel
New binding site conformations ...... molecular dynamics simulation.
@ast
New binding site conformations ...... molecular dynamics simulation.
@en
P2860
P50
P1433
P1476
New binding site conformations ...... molecular dynamics simulation
@en
P2093
Bernard Maigret
Jaime M Santana
P2860
P304
P356
10.1371/JOURNAL.PONE.0072402
P407
P577
2013-08-21T00:00:00Z