Functional interplay among the flavivirus NS3 protease, helicase, and cofactors.
about
A crystal structure of the Dengue virus NS5 protein reveals a novel inter-domain interface essential for protein flexibility and virus replicationOrganization of the Flavivirus RNA replicase complex.Screening of FDA-Approved Drugs for Inhibitors against Japanese Encephalitis Virus Infection.Structural characterization of the linked NS2B-NS3 protease of Zika virus.Regulation of Flavivirus RNA synthesis and replicationStructural features of NS3 of Dengue virus serotypes 2 and 4 in solution and insight into RNA binding and the inhibitory role of quercetin.The methyltransferase domain of dengue virus protein NS5 ensures efficient RNA synthesis initiation and elongation by the polymerase domain.
P2860
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P2860
Functional interplay among the flavivirus NS3 protease, helicase, and cofactors.
description
article científic
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article scientifique
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articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
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artigo científico
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artikel ilmiah
@id
artikull shkencor
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artículo científico
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name
Functional interplay among the flavivirus NS3 protease, helicase, and cofactors.
@en
type
label
Functional interplay among the flavivirus NS3 protease, helicase, and cofactors.
@en
prefLabel
Functional interplay among the flavivirus NS3 protease, helicase, and cofactors.
@en
P2860
P1433
P1476
Functional interplay among the flavivirus NS3 protease, helicase, and cofactors.
@en
P2093
Wint Wint Phoo
P2860
P2888
P356
10.1007/S12250-014-3438-6
P50
P577
2014-03-26T00:00:00Z
P5875
P6179
1015966132