Enterovirus 71 VPg uridylation uses a two-molecular mechanism of 3D polymerase.
about
A Conserved Inhibitory Mechanism of a Lycorine Derivative against Enterovirus and Hepatitis C VirusRNA-Dependent RNA Polymerases of Picornaviruses: From the Structure to Regulatory MechanismsRecent developments in antiviral agents against enterovirus 71 infectionCrystal Structure of Enterovirus 71 RNA-Dependent RNA Polymerase Complexed with Its Protein Primer VPg: Implication for a trans Mechanism of VPg UridylylationCrystallization and preliminary crystallographic analysis of defective pollen wall (DPW) protein from Oryza sativa.Cyclophilin A associates with enterovirus-71 virus capsid and plays an essential role in viral infection as an uncoating regulatorBiochemical characterization of recombinant Enterovirus 71 3C protease with fluorogenic model peptide substrates and development of a biochemical assay.Peptidyl aldehyde NK-1.8k suppresses enterovirus 71 and enterovirus 68 infection by targeting protease 3CEnterovirus 71 Proteins 2A and 3D Antagonize the Antiviral Activity of Gamma Interferon via Signaling Attenuation.Amiloride inhibits the initiation of Coxsackievirus and poliovirus RNA replication by inhibiting VPg uridylylation.EV71 3D Protein Binds with NLRP3 and Enhances the Assembly of Inflammasome ComplexStudies on Inhibition of Proliferation of Enterovirus-71 by Compound YZ-LY-0.A comprehensive procedure for antiviral inhibitor discovery using EV71 as an example.Structure of the Enterovirus 71 3C Protease in Complex with NK-1.8k and Indications for the Development of Antienterovirus Protease Inhibitor.Picornaviral polymerase structure, function, and fidelity modulation.Sequence specificity for uridylylation of the viral peptide linked to the genome (VPg) of enteroviruses.Enterovirus A71 Proteins: Structure and Function.
P2860
Q26700115-C47E0F30-8903-4121-B619-125B91714C04Q26799887-8B803894-C179-40E5-9ED2-36729DB889D3Q26849627-69B120F4-99E3-47E7-A021-55EDB07BE66DQ27676806-A50F4391-CDE2-4988-93BD-5ACF4EAE8C6AQ33733691-DAB11BA8-2603-4338-9C14-DAD80B34FD0DQ34282430-4F79F00B-E406-4079-AD88-CD2B84A16BC7Q35168919-1B78C914-C3B8-419C-B82C-6D1D64493CC4Q35385360-34543F0B-F1DB-4D55-BE38-8C27A80D6BDFQ35758582-81991BED-8ADC-4284-9EF3-DEAECFC06EBDQ35972897-E84484A4-1E10-4A6F-8A01-DD265FFA4C98Q36242863-4D6A49F2-7FA1-4BA8-88B4-6721718B80F6Q36274964-87CD2C55-3261-459E-B5B9-B2BBAE940C6BQ36603072-F0E1DDAB-EAC5-4B3E-A81E-86B49B244D58Q38403369-56387ADE-700B-4151-9C7E-DF65C2E692FDQ39120524-D99109BB-1ABE-4F97-B096-848D1DFA2DB4Q41161438-0B82F8B7-EF6C-44E1-AEFE-139ABB8A4E84Q54260296-220D92DA-F104-4584-8215-083DF9C9E6D6
P2860
Enterovirus 71 VPg uridylation uses a two-molecular mechanism of 3D polymerase.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年学术文章
@wuu
2012年学术文章
@zh-cn
2012年学术文章
@zh-hans
2012年学术文章
@zh-my
2012年学术文章
@zh-sg
2012年學術文章
@yue
2012年學術文章
@zh
2012年學術文章
@zh-hant
name
Enterovirus 71 VPg uridylation uses a two-molecular mechanism of 3D polymerase.
@ast
Enterovirus 71 VPg uridylation uses a two-molecular mechanism of 3D polymerase.
@en
type
label
Enterovirus 71 VPg uridylation uses a two-molecular mechanism of 3D polymerase.
@ast
Enterovirus 71 VPg uridylation uses a two-molecular mechanism of 3D polymerase.
@en
prefLabel
Enterovirus 71 VPg uridylation uses a two-molecular mechanism of 3D polymerase.
@ast
Enterovirus 71 VPg uridylation uses a two-molecular mechanism of 3D polymerase.
@en
P2093
P2860
P356
P1433
P1476
Enterovirus 71 VPg uridylation uses a two-molecular mechanism of 3D polymerase.
@en
P2093
Cheng Chen
Cheng Yang
Honggang Zhou
Mohan Song
Yaxin Wang
Zhiyong Lou
P2860
P304
13662-13671
P356
10.1128/JVI.01712-12
P407
P577
2012-10-10T00:00:00Z