Functional domains of the influenza A virus PB2 protein: identification of NP- and PB1-binding sites.
about
New world bats harbor diverse influenza A virusesGenomic signatures of human versus avian influenza A virusesStructure-based discovery of the novel antiviral properties of naproxen against the nucleoprotein of influenza A virus.Evidence for a Novel Mechanism of Influenza Virus-Induced Type I Interferon Expression by a Defective RNA-Encoded ProteinStructural insight into the essential PB1–PB2 subunit contact of the influenza virus RNA polymeraseThe Influenza Virus Polymerase Complex: An Update on Its Structure, Functions, and Significance for Antiviral Drug DesignA Rab11- and microtubule-dependent mechanism for cytoplasmic transport of influenza A virus viral RNAHeat shock protein 70 inhibits the activity of Influenza A virus ribonucleoprotein and blocks the replication of virus in vitro and in vivoThe N-terminal fragment of a PB2 subunit from the influenza A virus (A/Hong Kong/156/1997 H5N1) effectively inhibits RNP activity and viral replicationConserved features of the PB2 627 domain impact influenza virus polymerase function and replicationPersistent host markers in pandemic and H5N1 influenza virusesMutations associated with severity of the pandemic influenza A(H1N1)pdm09 in humans: a systematic review and meta-analysis of epidemiological evidence.Identification of human-to-human transmissibility factors in PB2 proteins of influenza A by large-scale mutual information analysis.An inhibitory activity in human cells restricts the function of an avian-like influenza virus polymerase.Human HA and polymerase subunit PB2 proteins confer transmission of an avian influenza virus through the air.Nuclear import and assembly of influenza A virus RNA polymerase studied in live cells by fluorescence cross-correlation spectroscopy.Conservation and diversity of influenza A H1N1 HLA-restricted T cell epitope candidates for epitope-based vaccines.Complete-proteome mapping of human influenza A adaptive mutations: implications for human transmissibility of zoonotic strains.Pandemic Seasonal H1N1 Reassortants Recovered from Patient Material Display a Phenotype Similar to That of the Seasonal Parent.PB2 residue 158 is a pathogenic determinant of pandemic H1N1 and H5 influenza a viruses in mice.Atypical characteristics of nucleoprotein of pandemic influenza virus H1N1 and their roles in reassortment restriction.The RNA polymerase PB2 subunit of influenza A/HongKong/156/1997 (H5N1) restricts the replication of reassortant ribonucleoprotein complexes [corrected]Virulence determinants of pandemic A(H1N1)2009 influenza virus in a mouse model.Adaptation of avian influenza A virus polymerase in mammals to overcome the host species barrierGenetic trans-complementation establishes a new model for influenza virus RNA transcription and replication.Influenza A virus polymerase: structural insights into replication and host adaptation mechanismsInfluenza polymerase activity correlates with the strength of interaction between nucleoprotein and PB2 through the host-specific residue K/E627.Effectiveness of esterified whey proteins fractions against Egyptian Lethal Avian Influenza A (H5N1)Identification of human H1N2 and human-swine reassortant H1N2 and H1N1 influenza A viruses among pigs in Ontario, Canada (2003 to 2005).NP body domain and PB2 contribute to increased virulence of H5N1 highly pathogenic avian influenza viruses in chickens.Influenza A viruses with different amino acid residues at PB2-627 display distinct replication properties in vitro and in vivo: revealing the sequence plasticity of PB2-627 positionInteraction of the influenza A virus polymerase PB2 C-terminal region with importin alpha isoforms provides insights into host adaptation and polymerase assembly.Temperature sensitive influenza A virus genome replication results from low thermal stability of polymerase-cRNA complexes.Replication-coupled and host factor-mediated encapsidation of the influenza virus genome by viral nucleoprotein.Reversion of PB2-627E to -627K during replication of an H5N1 Clade 2.2 virus in mammalian hosts depends on the origin of the nucleoprotein.Pre-mRNA Processing Factor Prp18 Is a Stimulatory Factor of Influenza Virus RNA Synthesis and Possesses Nucleoprotein Chaperone Activity.In vivo inhibition of influenza A virus replication by RNA interference targeting the PB2 subunit via intratracheal delivery.Identification of a Novel Viral Protein Expressed from the PB2 Segment of Influenza A Virus.Microevolution of highly pathogenic avian influenza A(H5N1) viruses isolated from humans, Egypt, 2007-2011.Nucleozin targets cytoplasmic trafficking of viral ribonucleoprotein-Rab11 complexes in influenza A virus infection.
P2860
Q21090482-CC28B8B4-D3F0-486D-8419-D8D43B378049Q24623524-50314BD8-9DCD-4B5A-B5AD-717046AC5DC9Q24632337-7D12C861-EAD4-4243-B173-FFA29AE79771Q27319771-8B7C9E50-31A7-42FA-95A6-C5B1008957EBQ27655568-BBF1788F-B22A-458E-A8A0-CCEDD7B78FB3Q28071809-A27B8F41-23A4-4792-B562-658CBABCA181Q28305057-6F5CDA1E-F73B-4817-801D-BD0C32E56E53Q28477264-0FBCD28C-EDCD-425C-B192-77DD6BB3162EQ28542440-C5A60EB1-11CC-4CE4-9BC6-414901EEADAAQ30360137-CD6B03F7-C4AA-4252-A043-AE0893585FA2Q30363055-16E44644-1099-44CF-8D8B-DBA3DAEC4658Q30365296-88E52220-ED90-49AF-9B38-45A06B8A507DQ30368054-D0CDCFB6-91D5-4FD7-A692-85F90BAD5E1BQ30371316-4C7421C8-8756-46D6-A2BA-C1835111AAACQ30374897-BD72DB13-863D-43EB-BFB2-97B04C6B316AQ30382441-D214B490-9577-47CD-B2FB-6B520D577A19Q30384675-2ECA4BD6-FF26-4FF0-AF09-F7D7BF494506Q30385456-DFEAF529-0073-483C-80C1-05CB767697B6Q30389102-1E816517-F8E2-405B-BB77-5976D4708561Q30395091-7420984F-5672-4BDF-83DB-E8FFF96EE976Q30399937-18F91F39-5550-4308-A660-6F1D7CC80E70Q30413814-D78AFD60-A6F9-44C9-B41E-AB7A45FC67C2Q30424508-12D92339-126B-4FFE-AE36-5C2DEFD99EF3Q30429748-9665A417-5CFB-4E95-B5AF-8B1247B50E36Q33455562-CD3B75BC-D9DE-4520-AA28-CE50E3421F9BQ34121115-56FD0A00-5FA7-4177-A4C9-F4647B2623AAQ34263308-6F33EB65-36B3-436D-8FF0-81E62F6ED098Q34387936-B04843BA-99CD-41CE-933A-A341BF316D8EQ34431719-B69253C3-7748-45AA-943D-E324B1A173B5Q34529786-633BF5E3-CF23-444C-93D5-6758975C4D2BQ34615966-A01A62B2-9253-424D-B17A-AAE26A3C8D45Q34695795-A9BF05B3-52F5-47C6-834D-DF3EEF549558Q35037734-18AAF1FC-D5A4-4C89-A08B-EBD397BA7C96Q35077609-D7F82A7A-91AC-4F37-8623-F476BBC0B41CQ35275017-DEA80915-7221-4D28-A0F3-21798402DAA3Q36194662-B23700D8-6A01-4953-9B1C-BCC6F0F068F7Q36335944-8BCBDA0D-2B16-4704-A2B2-5E2BD6D84C44Q36433861-EF6E2368-3CDC-4BFB-B03D-304D0473FDA0Q36584392-5B45CD12-7F74-4FD8-94DE-8A7106A39021Q36760084-FD2AA713-AC92-49B7-A549-9F20067949E6
P2860
Functional domains of the influenza A virus PB2 protein: identification of NP- and PB1-binding sites.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年学术文章
@wuu
2004年学术文章
@zh
2004年学术文章
@zh-cn
2004年学术文章
@zh-hans
2004年学术文章
@zh-my
2004年学术文章
@zh-sg
2004年學術文章
@yue
2004年學術文章
@zh-hant
name
Functional domains of the infl ...... of NP- and PB1-binding sites.
@en
Functional domains of the infl ...... of NP- and PB1-binding sites.
@nl
type
label
Functional domains of the infl ...... of NP- and PB1-binding sites.
@en
Functional domains of the infl ...... of NP- and PB1-binding sites.
@nl
prefLabel
Functional domains of the infl ...... of NP- and PB1-binding sites.
@en
Functional domains of the infl ...... of NP- and PB1-binding sites.
@nl
P2093
P1433
P1476
Functional domains of the infl ...... of NP- and PB1-binding sites.
@en
P2093
Debra Elton
Emma Poole
Liz Medcalf
P304
P356
10.1016/J.VIROL.2003.12.022
P407
P50
P577
2004-03-01T00:00:00Z