eIF2-dependent and eIF2-independent modes of initiation on the CSFV IRES: a common role of domain II
about
Insights into the role of yeast eIF2A in IRES-mediated translationActivities of Ligatin and MCT-1/DENR in eukaryotic translation initiation and ribosomal recyclingEnterovirus Control of Translation and RNA Granule Stress ResponsesCould the eIF2α-Independent Translation Be the Achilles Heel of Cancer?RAN translation and frameshifting as translational challenges at simple repeats of human neurodegenerative disordersAnimal virus schemes for translation dominanceRNA-Binding Protein hnRNP D Modulates Internal Ribosome Entry Site-Dependent Translation of Hepatitis C Virus RNAStructure and function of HCV IRES domainsConserved functional domains and a novel tertiary interaction near the pseudoknot drive translational activity of hepatitis C virus and hepatitis C virus-like internal ribosome entry sitesInhibitor-induced structural change in the HCV IRES domain IIa RNAHepatitis-C-virus-like internal ribosome entry sites displace eIF3 to gain access to the 40S subunitStructure of the mammalian 80S initiation complex with initiation factor 5B on HCV-IRES RNAStructural integrity of {alpha}-helix H12 in translation initiation factor eIF5B is critical for 80S complex stability.Regulation of translation initiation in eukaryotes: mechanisms and biological targetsFour translation initiation pathways employed by the leaderless mRNA in eukaryotesTranslation of 5' leaders is pervasive in genes resistant to eIF2 repressionDual mechanism for the translation of subgenomic mRNA from Sindbis virus in infected and uninfected cells.Initiation factor eIF2-independent mode of c-Src mRNA translation occurs via an internal ribosome entry site.The HCV IRES pseudoknot positions the initiation codon on the 40S ribosomal subunit.Toward a structural understanding of IRES RNA functionTranslation initiation on mammalian mRNAs with structured 5'UTRs requires DExH-box protein DHX29.eIF2A mediates translation of hepatitis C viral mRNA under stress conditions.Upregulation of eIF5B controls cell-cycle arrest and specific developmental stagesFunctional conservation despite structural divergence in ligand-responsive RNA switches.Ligand-responsive RNA mechanical switches.eIF5 and eIF5B together stimulate 48S initiation complex formation during ribosomal scanning.Cellular IRES-mediated translation: the war of ITAFs in pathophysiological states.HCV IRES domain IIb affects the configuration of coding RNA in the 40S subunit's decoding groove.DAZAP1, an RNA-binding protein required for development and spermatogenesis, can regulate mRNA translation.Widespread distribution and structural diversity of Type IV IRESs in members of Picornaviridae.Repeat-associated non-AUG translation and its impact in neurodegenerative disease.IRES-mediated translation of cellular messenger RNA operates in eIF2α- independent manner during stress.A distinct class of internal ribosomal entry site in members of the Kobuvirus and proposed Salivirus and Paraturdivirus genera of the Picornaviridae.A new framework for understanding IRES-mediated translation.Modulation of translation initiation efficiency in classical swine fever virus.Conformational flexibility of viral RNA switches studied by FRET.The current status of vertebrate cellular mRNA IRESsRibosomal Initiation Complex Assembly within the Wild-Strain of Coxsackievirus B3 and Live-Attenuated Sabin3-like IRESes during the Initiation of TranslationToward the mechanism of eIF4F-mediated ribosomal attachment to mammalian capped mRNAseIF1A/eIF5B interaction network and its functions in translation initiation complex assembly and remodeling.
P2860
Q21560926-1A1D169F-26AB-4F43-8274-03F51D8A2784Q24296405-B3E771B4-BD88-4A82-AB86-B35272F90C92Q26752604-79C6DFA6-D337-4332-9A67-3FEE0B1E6823Q26774488-5D874F94-EB92-4700-8C57-B906B90BBE99Q26823908-D3DCC160-CA91-4705-A972-40190DFD02A9Q26851527-64C28E81-3E60-412D-BE78-C3102102FD22Q27487410-9F3DE1E7-A22B-4EF4-9CBF-FECA783B3985Q27489322-B6B107DC-2A90-4EF7-9A87-A798F0AB414BQ27490136-132D180F-808F-4F10-994A-82AD93BD95D1Q27660398-04D0A48E-A06C-423A-B830-9FA76F31BF20Q27680505-62A98A47-7946-4F19-B481-3551B236855AQ27694629-7F4F49D8-7455-4326-9457-9BE57CC705E8Q27935687-3861DE7A-0D6E-4C8C-B1E3-CCF473A0E353Q28111696-57FA4C25-4F06-40EE-9512-C93755BB2C3CQ28592763-7A1B031D-61A3-4B2F-BD77-6F7D023509E3Q28771734-CA83ACD8-FB71-4621-B8F5-3E56BB5FDCECQ33416419-CC474CA6-63F3-479D-880D-0F305FE1B2C1Q33648488-4F583662-1BAE-4D22-AF74-CA4024D15755Q34002207-AB18A782-E551-4D7A-B92E-85005E3C906AQ34017026-7068CA6D-093F-4110-9C09-21FCFB6B0FCCQ34168375-031544EA-9F0F-4C4A-BA1B-BA9A80C41D95Q34183856-AEBF022A-40FC-432E-9E9D-F16A6EC4C737Q34384024-58398501-91DA-407D-B38F-0C3CAD820EA8Q34445182-D7683EEC-E9C1-4710-8FE5-6CE9F78A360DQ34484231-6BA2E852-5457-4A54-B91A-035212981FA9Q34510080-53F2EB24-1858-4D9C-B76D-781B85DE8133Q34624747-004F9B95-5DE8-4923-9EEA-4AC1576412ADQ35111836-71E6FD26-DE85-40A7-87CE-2EA17ADF2685Q35111839-8F77B1C6-E930-45B8-A693-40C2DFA1D237Q35223057-129DA62E-0395-468D-83D4-9961EBA4A36BQ35340115-141BD031-208E-4555-94F2-2C88DE13F252Q35672175-F8107C2B-336B-4DBD-89FA-BC56BE1357FDQ35689574-B7A88DBE-DE7C-4251-80B3-596B7FC21100Q35992360-4ACD4C89-2EAC-44B1-812F-548925D76A87Q36172109-4FF457A3-986F-4046-9420-BC822CDD62B8Q36386398-CEDCEC06-AE98-4976-BD4B-327FBE66C17AQ36555207-DE73DFEA-F15B-4DC7-86EA-1E2589D9EA93Q36790234-E491FCFD-9C11-4368-942D-C8B9E19186ADQ37104721-3F9EF9DC-1666-440C-A133-73C8E7C1E217Q37228876-D2B113F0-B8E9-4314-9ED0-2684855559CE
P2860
eIF2-dependent and eIF2-independent modes of initiation on the CSFV IRES: a common role of domain II
description
2008 nî lūn-bûn
@nan
2008 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2008 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
name
eIF2-dependent and eIF2-indepe ...... ES: a common role of domain II
@ast
eIF2-dependent and eIF2-indepe ...... ES: a common role of domain II
@en
eIF2-dependent and eIF2-indepe ...... ES: a common role of domain II
@nl
type
label
eIF2-dependent and eIF2-indepe ...... ES: a common role of domain II
@ast
eIF2-dependent and eIF2-indepe ...... ES: a common role of domain II
@en
eIF2-dependent and eIF2-indepe ...... ES: a common role of domain II
@nl
prefLabel
eIF2-dependent and eIF2-indepe ...... ES: a common role of domain II
@ast
eIF2-dependent and eIF2-indepe ...... ES: a common role of domain II
@en
eIF2-dependent and eIF2-indepe ...... ES: a common role of domain II
@nl
P2093
P2860
P3181
P356
P1433
P1476
eIF2-dependent and eIF2-indepe ...... ES: a common role of domain II
@en
P2093
Andrey V Pisarev
Christopher U T Hellen
Irina S Abaeva
Sylvain de Breyne
Tatyana V Pestova
P2860
P304
P3181
P356
10.1038/EMBOJ.2008.49
P407
P577
2008-04-09T00:00:00Z