Structure and functionality in flavivirus NS-proteins: perspectives for drug design
about
The role of viral persistence in flavivirus biologyStructure-guided insights on the role of NS1 in flavivirus infectionZIKA-How fast does this virus mutate?Zika virus – emergence, evolution, pathology, diagnosis, and control: current global scenario and future perspectives – a comprehensive reviewTranscriptome Analysis Reveals a Signature Profile for Tick-Borne Flavivirus Persistence in HEK 293T CellsIdentification and Characterization of Novel Broad-Spectrum Inhibitors of the Flavivirus MethyltransferaseUnderstanding the dengue viruses and progress towards their controlSynergistic interactions between the NS3(hel) and E proteins contribute to the virulence of dengue virus type 1Illustrating and homology modeling the proteins of the Zika virus.A crystal structure of the Dengue virus NS5 protein reveals a novel inter-domain interface essential for protein flexibility and virus replicationVirtual Screening for Potential Inhibitors of NS3 Protein of Zika VirusSmall Molecule Inhibitors That Selectively Block Dengue Virus MethyltransferaseCrystal Structure and Functional Analysis of the SARS-Coronavirus RNA Cap 2′-O-Methyltransferase nsp10/nsp16 ComplexA macrocyclic HCV NS3/4A protease inhibitor interacts with protease and helicase residues in the complex with its full-length targetThe Zika virus methyltransferase: structure and functions for drug design perspectivesZika virus: from pathogenesis to disease controlIn vitro reconstitution of SARS-coronavirus mRNA cap methylationThe interface between methyltransferase and polymerase of NS5 is essential for flavivirus replicationNovel Broad Spectrum Inhibitors Targeting the Flavivirus MethyltransferaseDengue and Zika viruses: lessons learned from the similarities between these Aedes mosquito-vectored arbovirusesFuture developments in biosensors for field-ready Zika virus diagnosticsAnalysis of Ribonucleotide 5’ -Triphosphate Analogs as Potential Inhibitors of Zika Virus RNA-dependent RNA Polymerase Using Non-Radioactive Polymerase AssaysInhibitors compounds of the flavivirus replication processSelective Activation of Type II Interferon Signaling by Zika Virus NS5 Protein.Host-Virus Interaction of ZIKA Virus in Modulating Disease Pathogenesis.Zika virus: An emerging flavivirus.Biological and historical overview of Zika virusPotential Antivirals: Natural Products Targeting Replication Enzymes of Dengue and Chikungunya Viruses.Steady-state NTPase activity of Dengue virus NS3: number of catalytic sites, nucleotide specificity and activation by ssRNA.Flaviviruses, an expanding threat in public health: focus on dengue, West Nile, and Japanese encephalitis virus.Exploring of primate models of tick-borne flaviviruses infection for evaluation of vaccines and drugs efficacy.A tick-borne segmented RNA virus contains genome segments derived from unsegmented viral ancestorsInduction of a protective response in mice by the dengue virus NS3 protein using DNA vaccines.Biocrystallography: past, present, future.Ivermectin is a potent inhibitor of flavivirus replication specifically targeting NS3 helicase activity: new prospects for an old drug.Monomeric nature of dengue virus NS3 helicase and thermodynamic analysis of the interaction with single-stranded RNA.Molecular basis for nucleotide conservation at the ends of the dengue virus genome.Novel benzoxazole inhibitor of dengue virus replication that targets the NS3 helicase.The eukaryotic translation initiation factor 3 subunit L protein interacts with Flavivirus NS5 and may modulate yellow fever virus replication.The C-terminal 50 amino acid residues of dengue NS3 protein are important for NS3-NS5 interaction and viral replication
P2860
Q22809893-2217E6ED-FD70-451A-A08D-B73C7B4597FCQ24048592-67E30A1A-8FA9-4E2C-9A29-79FA1BD3C710Q24261172-27879742-1060-4FEA-862E-EC7404DE0F64Q24765944-1F07AEB3-BB8C-4FFC-A52F-3DB465BA37F4Q26700068-2A6B0D7B-85DA-4B4C-8CF5-F5868C7CB19BQ26700125-673015CD-4754-46D2-93D8-E954E6A1AF6AQ27011587-D5127C66-BEA9-4E9A-BCC0-51A2011AA5CDQ27305534-90F31840-2202-4D8B-9AD7-3FC0DB5969DCQ27313484-E331597A-9ECA-4E2C-AC45-FECA18743AFBQ27321114-6E107601-CE2B-4115-B3F1-F6B1878909C3Q27468584-88287B89-F6B0-4929-84B9-3C0C07C4D2E9Q27666321-3BA08769-67BA-41D5-AC25-E27D34D0D86DQ27668161-E8E488B0-85F9-43B1-B5D9-893C67F79E7AQ27676133-999E9F22-FEA0-44B3-8CF4-0535F0478214Q28114691-3879835C-213F-41FD-9E81-C69220A7520DQ28278045-26BD61EA-3FAF-4EDD-9284-8324B97B3E46Q28473757-C98628B8-3F8F-48D2-BE50-7D504E55FB06Q28539043-1894D280-BDC2-4B30-B3DF-E2ACE3607210Q28548514-CD037D4A-A125-4544-B5CE-672A76E183D0Q28577861-1421427E-0049-419D-BFBF-3C085738DF7CQ28577936-2FA53606-38AD-404C-888D-A8D906532062Q28581011-4EC43FF6-8092-4431-8D8E-D21FABD21AC8Q29994474-84A19204-6BCB-4243-AF00-0DE2DC31947EQ30145653-1BA4E23C-9EFA-4688-BAA9-A9152F00170EQ30235062-D23C60E3-7437-445D-B574-FB4C3D2B2C7DQ30235530-21080573-6201-45CF-A2ED-AC4504288229Q30235549-E9475998-0B13-4C3F-87E1-FE89A82BBD13Q30400192-6FB773CE-91D5-4DD7-8F3D-82F7D8C918DFQ30421795-0EAB29BA-AB1A-44CB-BDD1-70464A5195F4Q30857727-17626577-1040-412F-97AB-17F5BC0B352DQ33407061-8271763A-D6FD-4C3C-A5F9-F8717D24D8BEQ33606780-6A0BE40F-D0BC-48E8-9816-6BD01B8CF1DCQ34059579-0CB95F39-7FAB-4F91-ADE5-AEB734287628Q34089778-D8C7777A-F3C0-4F7B-8E17-82DBD905DB2CQ34246661-5209751F-572C-4DFE-963F-A70C8FB2FD3BQ34312992-745EB2E6-D580-4A17-9884-8C5883073676Q34426452-81F45E83-AF18-43E7-9250-F1C24875B7FDQ34583461-CB04463B-05FB-46C1-8B11-E88B7B7DAE47Q34783090-E435A2BF-9C56-440F-8567-2C6DDCD8CC03Q35002993-A5F08CF8-BB57-4088-9260-420ABC863C2E
P2860
Structure and functionality in flavivirus NS-proteins: perspectives for drug design
description
2010 nî lūn-bûn
@nan
2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
name
Structure and functionality in flavivirus NS-proteins: perspectives for drug design
@ast
Structure and functionality in flavivirus NS-proteins: perspectives for drug design
@en
Structure and functionality in flavivirus NS-proteins: perspectives for drug design
@en-gb
Structure and functionality in flavivirus NS-proteins: perspectives for drug design
@nl
type
label
Structure and functionality in flavivirus NS-proteins: perspectives for drug design
@ast
Structure and functionality in flavivirus NS-proteins: perspectives for drug design
@en
Structure and functionality in flavivirus NS-proteins: perspectives for drug design
@en-gb
Structure and functionality in flavivirus NS-proteins: perspectives for drug design
@nl
altLabel
Structure and functionality in flavivirus NS-proteins: Perspectives for drug design
@en
prefLabel
Structure and functionality in flavivirus NS-proteins: perspectives for drug design
@ast
Structure and functionality in flavivirus NS-proteins: perspectives for drug design
@en
Structure and functionality in flavivirus NS-proteins: perspectives for drug design
@en-gb
Structure and functionality in flavivirus NS-proteins: perspectives for drug design
@nl
P2093
P2860
P50
P921
P3181
P1433
P1476
Structure and functionality in flavivirus NS-proteins: perspectives for drug design
@en
P2093
Anna M Jansson
Cécile Baronti
Ernest A Gould
Grégory Moureau
Holger Steuber
Jonathan M Grimes
Karin Alvarez
Raymond J Owens
René Assenberg
Shelley Cook
P2860
P304
P3181
P356
10.1016/J.ANTIVIRAL.2009.11.009
P407
P50
P577
2010-08-01T00:00:00Z