about
Sequence requirements for viral RNA replication and VPg uridylylation directed by the internal cis-acting replication element (cre) of human rhinovirus type 14.Molecular and biological characterization of deformed wing virus of honeybees (Apis mellifera L.)Molecular mechanisms for the conversion of zymogens to active proteolytic enzymesBiological function of Foot-and-mouth disease virus non-structural proteins and non-coding elementsSignal peptidase cleavage at the flavivirus C-prM junction: dependence on the viral NS2B-3 protease for efficient processing requires determinants in C, the signal peptide, and prM3C-like protease of rabbit hemorrhagic disease virus: identification of cleavage sites in the ORF1 polyprotein and analysis of cleavage specificityRNA-protein interactions in regulation of picornavirus RNA translationStructure of coronavirus main proteinase reveals combination of a chymotrypsin fold with an extra alpha-helical domain.Structural Basis for Antiviral Inhibition of the Main Protease, 3C, from Human Enterovirus 93Limits of Structural Plasticity in a Picornavirus Capsid Revealed by a Massively Expanded Equine Rhinitis A Virus ParticleThe refined crystal structure of the 3C gene product from hepatitis A virus: specific proteinase activity and RNA recognitionDual inhibition of human rhinovirus 2A and 3C proteases by homophthalimidesRole and mechanism of the maturation cleavage of VP0 in poliovirus assembly: structure of the empty capsid assembly intermediate at 2.9 A resolutionThe picornaviral 3C proteinases: cysteine nucleophiles in serine proteinase folds.Genetic selection of poliovirus 2Apro-binding peptidesParechovirusesStructural aspects of activation pathways of aspartic protease zymogens and viral 3C protease precursorsDifferential restriction patterns of mRNA decay factor AUF1 during picornavirus infections.AIM2 Co-immunization with VP1 Is Associated with Increased Memory CD8 T Cells and Mounts Long Lasting Protection against Coxsackievirus B3 Challenge.Cleavage of the feline calicivirus capsid precursor is mediated by a virus-encoded proteinase.Rapamycin and wortmannin enhance replication of a defective encephalomyocarditis virus5'-Terminal deletions occur in coxsackievirus B3 during replication in murine hearts and cardiac myocyte cultures and correlate with encapsidation of negative-strand viral RNA.The leader polypeptide of Theiler's murine encephalomyelitis virus is required for the assembly of virions in mouse L cells.A stable HeLa cell line that inducibly expresses poliovirus 2A(pro): effects on cellular and viral gene expression.Coxsackievirus expression of the murine secretory protein interleukin-4 induces increased synthesis of immunoglobulin G1 in mice.Hepatitis A virus capsid protein VP1 has a heterogeneous C terminus.Maturation of the hepatitis A virus capsid protein VP1 is not dependent on processing by the 3Cpro proteinase.Mapping of the feline calicivirus proteinase responsible for autocatalytic processing of the nonstructural polyprotein and identification of a stable proteinase-polymerase precursor protein.Deletion mapping of the encephalomyocarditis virus primary cleavage site.An emerging recombinant human enterovirus 71 responsible for the 2008 outbreak of hand foot and mouth disease in Fuyang city of ChinaMolecular characterization of a novel Ljungan virus (Parechovirus; Picornaviridae) reveals a fourth genotype and indicates ancestral recombination.Polyprotein processing in cis and in trans by hepatitis A virus 3C protease cloned and expressed in Escherichia coliAntisense RNA: function and fate of duplex RNA in cells of higher eukaryotes.Attenuated Mengo virus as a vector for immunogenic human immunodeficiency virus type 1 glycoprotein 120.Molecular analysis of three Ljungan virus isolates reveals a new, close-to-root lineage of the Picornaviridae with a cluster of two unrelated 2A proteinsProcessing of rabbit hemorrhagic disease virus polyprotein.Polyprotein processing in Southampton virus: identification of 3C-like protease cleavage sites by in vitro mutagenesis.Nucleoporin phosphorylation triggered by the encephalomyocarditis virus leader protein is mediated by mitogen-activated protein kinasesMutational analysis of the EMCV 2A protein identifies a nuclear localization signal and an eIF4E binding site.Foot-and-mouth disease.
P2860
Q24537790-8C09215F-B850-45E6-AF92-A1537A0E50ADQ24545875-EB158A6B-4925-424D-A60E-0D96B595FEA0Q24673104-2D6BE982-80F7-4088-A6F7-BA50DA3D7B8BQ26743377-89FD498D-A78B-4056-AE2E-B25593CFB443Q27469528-71642233-59DB-4CC1-9C6D-5280D46B429FQ27480312-4DC0AF82-8E34-4696-8BDA-71196C38F8CCQ27486105-2B4E42C8-70C9-4C46-91FF-A5735CBAB7B2Q27639290-D7FF9AB0-49CA-4C7E-9C21-750CE862A58FQ27671687-A0E33CE7-B162-4491-AD29-B006747FA35EQ27682315-298BB8A8-7FED-48D0-A31E-3CD8152544F7Q27734773-5B961372-AD96-425C-B500-65B0EC021908Q28379474-771CF9E6-6AB6-41BD-AB4B-07046D9ADD55Q28756233-0C5DC6A0-BAC2-4FEE-ACAA-0D0F73062048Q30423126-32F20539-436B-4642-A8A6-6FAE2E5C3F3DQ31957787-B5C0DE67-327B-4E24-A478-2762770633C0Q33655062-F7FCC1E4-F0AE-4B03-B26D-553B917D21C9Q33740132-9A1971B4-37F5-47E9-8C88-531D7B24EEE7Q33761818-2A0276F9-B83D-45E3-972E-25823FBF7F4FQ33774747-9D612829-609C-421A-91AF-345F08416AD1Q33783099-44B6BF0D-F4D5-4DCB-9A07-598C67E364D5Q33785626-1B59BE73-C383-48E5-8360-6EEEFB63A210Q33788804-ABF2E986-3C96-46C4-B380-04BF970C2375Q33796472-A2A4D03E-C789-4F8E-8607-4588C80F90F7Q33799106-AB7BC84A-696E-4527-B87D-081F95878F3FQ33810592-1ABED7D1-C70A-42B1-B0D4-3166C914040BQ33815879-D65B171A-556A-4669-B39C-DDA8543C4766Q33816313-9A627A87-4B83-4513-AFE2-798FDCDC0998Q33817321-F498EC67-F657-4941-9472-57BE6B39CFA7Q33844859-DFE49044-B96E-477C-812B-8C40D70AC86FQ33911890-A7A9607D-9E26-49E8-8C93-9F484C02F420Q33928915-5EDED7E3-5125-4742-8B71-FB48389EBFE6Q33934692-FDC77B74-E097-4868-AEB9-8D3F62EC3701Q34010093-0A277568-1A09-4544-B2F9-9F61399FBA0EQ34324295-01D95B41-538F-4D80-953E-2BB66B68DAC1Q34363105-C87CB5D8-9201-4274-AE17-71D9A7F446A9Q34370402-D9554ADE-711E-4FB2-BDFC-7D6FFACA68F8Q34381405-79EFCDBD-E87C-4002-8331-43EAB87D0A67Q34416478-47AEDA5F-AD65-4224-AC56-27864FCDF3BFQ34491180-2D5EF85D-09DF-4F54-9596-4A72B617D505Q34547126-2BE4F026-A16C-4844-90BB-51E6A0346139
P2860
description
article científic
@ca
article scientifique
@fr
articol științific
@ro
articolo scientifico
@it
artigo científico
@gl
artigo científico
@pt
artigo científico
@pt-br
artikel ilmiah
@id
artikull shkencor
@sq
artículo científico
@es
name
Proteolytic processing of picornaviral polyprotein.
@en
type
label
Proteolytic processing of picornaviral polyprotein.
@en
prefLabel
Proteolytic processing of picornaviral polyprotein.
@en
P1476
Proteolytic processing of picornaviral polyprotein.
@en
P2093
Palmenberg AC
P304
P356
10.1146/ANNUREV.MI.44.100190.003131
P577
1990-01-01T00:00:00Z