Two aromatic residues in the PB2 subunit of influenza A RNA polymerase are crucial for cap binding.
about
Perspective of Use of Antiviral Peptides against Influenza VirusCrystal structure of the RNA-dependent RNA polymerase from influenza C virus.Structure and nuclear import function of the C-terminal domain of influenza virus polymerase PB2 subunitNucleoside Monophosphate Complex Structures of the Endonuclease Domain from the Influenza Virus Polymerase PA Subunit Reveal the Substrate Binding Site inside the Catalytic CenterThe structural basis for cap binding by influenza virus polymerase subunit PB2Structural Basis of the Influenza A Virus RNA Polymerase PB2 RNA-binding Domain Containing the Pathogenicity-determinant Lysine 627 ResidueConformational polymorphism of m7GTP in crystal structure of the PB2 middle domain from human influenza A virusModel suggesting that replication of influenza virus is regulated by stabilization of replicative intermediatesDifferent de novo initiation strategies are used by influenza virus RNA polymerase on its cRNA and viral RNA promoters during viral RNA replication.Upolu virus and Aransas Bay virus, two presumptive bunyaviruses, are novel members of the family OrthomyxoviridaeBiochemical characterization of enzyme fidelity of influenza A virus RNA polymerase complexIdentification of a PA-binding peptide with inhibitory activity against influenza A and B virus replicationHeat shock protein 70 inhibits the activity of Influenza A virus ribonucleoprotein and blocks the replication of virus in vitro and in vivoMutations 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.Identification of PB2 mutations responsible for the efficient replication of H5N1 influenza viruses in human lung epithelial cellsComplete-proteome mapping of human influenza A adaptive mutations: implications for human transmissibility of zoonotic strains.PB2 residue 271 plays a key role in enhanced polymerase activity of influenza A viruses in mammalian host cells.Postreassortment amino acid substitutions in influenza A viruses.Discovery of Novel, Orally Bioavailable β-Amino Acid Azaindole Inhibitors of Influenza PB2.Polymerase activity of hybrid ribonucleoprotein complexes generated from reassortment between 2009 pandemic H1N1 and seasonal H3N2 influenza A viruses.The RNA polymerase PB2 subunit of influenza A/HongKong/156/1997 (H5N1) restricts the replication of reassortant ribonucleoprotein complexes [corrected]Replication and transcription activities of ribonucleoprotein complexes reconstituted from avian H5N1, H1N1pdm09 and H3N2 influenza A virusesThe N-terminal region of the PA subunit of the RNA polymerase of influenza A/HongKong/156/97 (H5N1) influences promoter binding.Dynamical insight into Caenorhabditis elegans eIF4E recognition specificity for mono-and trimethylated structures of mRNA 5' cap.Influenza A virus-generated small RNAs regulate the switch from transcription to replication.Identification of BPR3P0128 as an inhibitor of cap-snatching activities of influenza virus.The splicing factor proline-glutamine rich (SFPQ/PSF) is involved in influenza virus transcription.Influenza A virus polymerase: structural insights into replication and host adaptation mechanismsStructural and functional characterization of an influenza virus RNA polymerase-genomic RNA complexEmerging antiviral resistant strains of influenza A and the potential therapeutic targets within the viral ribonucleoprotein (vRNP) complex.Cellular protein HAX1 interacts with the influenza A virus PA polymerase subunit and impedes its nuclear translocationNP body domain and PB2 contribute to increased virulence of H5N1 highly pathogenic avian influenza viruses in chickens.Preclinical activity of VX-787, a first-in-class, orally bioavailable inhibitor of the influenza virus polymerase PB2 subunit.Involvement of Hsp90 in assembly and nuclear import of influenza virus RNA polymerase subunitsFunctional Constraint Profiling of a Viral Protein Reveals Discordance of Evolutionary Conservation and FunctionalityHigher polymerase activity of a human influenza virus enhances activation of the hemagglutinin-induced Raf/MEK/ERK signal cascade.Compatibility among polymerase subunit proteins is a restricting factor in reassortment between equine H7N7 and human H3N2 influenza viruses.Structure-function studies of the influenza virus RNA polymerase PA subunit.Interspecies and intraspecies transmission of influenza A viruses: viral, host and environmental factors.
P2860
Q26780434-129456CB-4F3E-4517-9032-2FA55719E37DQ27315161-FDAF8603-DA93-4E2D-B392-F963E1AFAB0EQ27643860-CF639251-780E-4628-8452-565389D46EBBQ27646520-395C6136-6ADD-403B-93C6-A335B96BF97EQ27650520-35F4F5BA-13FF-4E33-909A-ECC5D6687238Q27653426-7F75F2CD-C959-40A7-9713-10D8A0309B5EQ27680799-1CB37650-0224-40F5-A08A-634CD106946EQ27863792-B6D7A83B-F3ED-4D0C-95E3-6EECE3C12FAEQ27863913-F8F4154E-067C-4359-A36E-881B165EEAA8Q28308081-FE0E1ED8-BDA0-48AD-AD3D-0AAD5AF1C79EQ28473796-496C7403-8D7B-4861-A3E9-35D2A17EDFBBQ28476315-25DDD145-D688-4DBC-BA63-14FE777E08B2Q28477264-8ABD244F-91CD-4A7D-875A-8C13198F1E09Q30365296-4A297751-2BBB-4C54-A2A2-A82A0602A7EFQ30368054-37AEA33E-6A56-4B0B-B54F-63AD4825AFE8Q30370990-75DE9910-BC6A-4144-AAFE-743A57CC8966Q30385456-C7EFC98D-8B03-4F9E-9C71-ED5472B9C7A9Q30385995-52ACF5B8-AF65-43C2-AE85-00C8C53A0FFBQ30388799-7504FFC4-EDA1-4D31-B935-381B568BFA66Q30398601-A1D152A8-28AE-4E1C-902A-DF83653EEC2EQ30410407-09300826-11E6-4116-AB97-420AB34DD8A2Q30413814-567E4F70-8852-4B1E-9FC7-1651D82F2B78Q30431677-1C4FFC53-E94E-48C9-AEC9-06365B15B5C0Q33440587-656ABD8D-28BF-45FD-A1A4-D29CA44EF556Q33599838-8BE18FBF-63B7-484D-AF58-7FF5D82AB9B2Q33953132-8A6895E5-BCA0-4801-B089-B8D6F9FBAABDQ34022729-BCAFCE5A-607F-4C19-95C1-6AD3B4089822Q34082693-CC0EA1AC-AACB-40C8-BEBC-B4CF9F7E1C86Q34121115-CBBE6CD3-E6BF-494F-89E8-B6B68F0EC781Q34178189-53790D51-3A3B-4B08-A17A-1C8FD867514EQ34269400-6AFC11A4-050D-453C-B9ED-2EB7847A1C39Q34440497-3CC755E3-3A56-437E-95E3-A19FD60C921CQ34529786-BF45539A-F377-4DB3-A1E5-8B34D59236A0Q35076802-194A69FC-4C4E-42BF-A7CB-018B1543AF28Q35635186-ACD7A694-5E2F-486A-A901-8BB288A727A9Q35680145-352EBE79-4F4B-43C7-AAE2-33901AA3E260Q36419847-19BF3136-88D2-48A9-BA74-8372D7E58757Q36974774-27E4D5EC-0AAB-4A3B-9BC2-2F8E58E72383Q37496812-9DDE3D37-DAD9-4493-B9A7-8D37079C0682Q37768935-9894D8EC-0C69-4C73-B2C9-0CE03150874F
P2860
Two aromatic residues in the PB2 subunit of influenza A RNA polymerase are crucial for cap binding.
description
2003 nî lūn-bûn
@nan
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
@yue
2003年學術文章
@zh
2003年學術文章
@zh-hant
name
Two aromatic residues in the P ...... e are crucial for cap binding.
@en
type
label
Two aromatic residues in the P ...... e are crucial for cap binding.
@en
prefLabel
Two aromatic residues in the P ...... e are crucial for cap binding.
@en
P2093
P2860
P356
P1476
Two aromatic residues in the P ...... e are crucial for cap binding.
@en
P2093
George G Brownlee
Jane Sharps
Louise Mingay
Pierre Fechter
P2860
P304
20381-20388
P356
10.1074/JBC.M300130200
P407
P577
2003-03-19T00:00:00Z