Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP.
about
Structural characterization of the human eukaryotic initiation factor 3 protein complex by mass spectrometryMass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3Ribosomal position and contacts of mRNA in eukaryotic translation initiation complexesReconstitution reveals the functional core of mammalian eIF3RNA structure-based ribosome recruitment: lessons from the Dicistroviridae intergenic region IRESesLarge-scale mapping of human protein-protein interactions by mass spectrometryPosition of eukaryotic initiation factor eIF5B on the 80S ribosome mapped by directed hydroxyl radical probingPCI proteins eIF3e and eIF3m define distinct translation initiation factor 3 complexes'Ribozoomin'--translation initiation from the perspective of the ribosome-bound eukaryotic initiation factors (eIFs)The structure and function of the eukaryotic ribosomeLinking Α to Ω: diverse and dynamic RNA-based mechanisms to regulate gene expression by 5′-to-3′ communicationHCV and CSFV IRES domain II mediate eIF2 release during 80S ribosome assemblyFactor requirements for translation initiation on the Simian picornavirus internal ribosomal entry siteeIF2-dependent and eIF2-independent modes of initiation on the CSFV IRES: a common role of domain IIAnalysis of natural variants of the hepatitis C virus internal ribosome entry site reveals that primary sequence plays a key role in cap-independent translationThe pathway of hepatitis C virus mRNA recruitment to the human ribosomeStructure 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 sitesStructure of eIF3b RNA recognition motif and its interaction with eIF3j: structural insights into the recruitment of eIF3b to the 40 S ribosomal subunitStructure of the ternary initiation complex aIF2-GDPNP-methionylated initiator tRNAStructure of the mammalian 80S initiation complex with initiation factor 5B on HCV-IRES RNAeIF5 has GDI activity necessary for translational control by eIF2 phosphorylationEukaryotic translation initiation factor 3 (eIF3) and eIF2 can promote mRNA binding to 40S subunits independently of eIF4G in yeast.Coupled release of eukaryotic translation initiation factors 5B and 1A from 80S ribosomes following subunit joining.Review: Translational GTPasesThe mechanism of translation initiation on Type 1 picornavirus IRESsA mechanistic overview of translation initiation in eukaryotesThe mechanism of eukaryotic translation initiation and principles of its regulationCryo-EM study of start codon selection during archaeal translation initiationTranslation initiation factor eIF4G-1 binds to eIF3 through the eIF3e subunit.Regulatory elements in eIF1A control the fidelity of start codon selection by modulating tRNA(i)(Met) binding to the ribosomeThe central core region of yeast ribosomal protein L11 is important for subunit joining and translational fidelitySpecific functional interactions of nucleotides at key -3 and +4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex.A conserved structure within the HIV gag open reading frame that controls translation initiation directly recruits the 40S subunit and eIF3.Initiation on the divergent Type I cadicivirus IRES: factor requirements and interactions with the translation apparatusThe indispensable N-terminal half of eIF3j/HCR1 cooperates with its structurally conserved binding partner eIF3b/PRT1-RRM and with eIF1A in stringent AUG selectionRegulation of GTP hydrolysis prior to ribosomal AUG selection during eukaryotic translation initiation.The eukaryotic initiation factor (eIF) 5 HEAT domain mediates multifactor assembly and scanning with distinct interfaces to eIF1, eIF2, eIF3, and eIF4GTranslation initiation on mammalian mRNAs with structured 5'UTRs requires DExH-box protein DHX29.Functional reconstitution of human eukaryotic translation initiation factor 3 (eIF3).
P2860
Q24298332-3FAEBCAC-D918-4384-BEB7-AFFE3026E7FBQ24309617-009699B6-A9AC-4344-B1D5-79ACF3BDD3CCQ24310392-9FB97417-D7C0-4E4C-906A-AC1F4EEC2EDEQ24312641-3585A114-FDD8-4C25-89BF-FF0CAFA43873Q24649011-4CA00DF7-FFF7-4E70-B703-21AE84A865D9Q24670192-5FA63885-7E99-468D-8D3F-C291365215B1Q24676799-AF65C28B-A787-49AF-B096-3599BDC405E0Q24815484-343ED036-EDE2-4186-8066-AE5A1DD3A863Q26852951-218212A7-CBCC-4ABA-9050-C6858EB66706Q27022315-94B46470-6C48-4257-81EF-5C653E99DC35Q27468861-A094A87D-846E-43EE-BDE5-A0E1FB4B262FQ27478025-C4A12B72-21BB-466B-8177-3CB5E23CD90CQ27485197-BCD1788B-4AB9-4F28-90FA-B4ED0DB5EC58Q27485879-F3E18AA2-7425-4BBC-AEAF-C184BEFC6B38Q27487957-E4702375-6360-43F0-9CF8-22F6DEC3C9D7Q27488440-E4079A64-57FD-428C-91BE-E98CC5E3150EQ27489322-77F0AFD9-DEDD-498D-BA0E-748D3D317A3FQ27490136-F275FB3A-DED5-4E55-A39F-1925B3E87D07Q27643432-90549A38-C292-4D80-BE5B-EF65282115AFQ27678199-C2C49445-5F66-494C-B0BA-0E872965C6CFQ27694629-84D75640-9759-4950-996F-B4B0317D9C1FQ27931061-647A1587-917A-466A-BFA3-F932FDC5AF2AQ27936122-73AB1523-5F08-45F0-A813-C9FED65050C6Q27939079-3DAAF3F0-11A9-41B3-86E6-F3EA0BAC6041Q28077489-24B23969-3943-4571-AAA8-D5B52DC4AE0EQ28116162-9454438D-EA7D-4451-84F6-40B359F40487Q28268066-2981D2A9-3250-453E-9720-9BC430DF66A5Q29547270-8CDE3232-914A-4BE2-BA7A-911A1BCC569CQ30828138-F75DAA77-E531-46A3-AEF7-21C833C970B4Q33246406-B7DE9391-DC7A-4A59-9A67-4924A1E39C4DQ33573600-7CDE0EE5-02BA-4E1F-BBE5-48D5F30053D6Q33932898-47D44E6E-6195-4CF8-AD9F-1D8D3C0FC7D6Q33993880-14EF6116-BD2B-436F-B981-0D8CA78F3DB8Q34024695-51E24D8E-E886-4B73-8104-9B60FB65D4A3Q34046163-3E51DED3-2F49-450D-B9B3-4187342B3E13Q34091806-6BC1F0AA-F7FF-4BDA-A9DC-AAB94F6C4228Q34116930-A411AF07-77FC-4F85-994C-A4B13646E538Q34132377-26E879E5-A9F3-4C34-BBE0-A3FA533AB5CEQ34168375-6C199513-BDC2-4141-8757-89134C5AE9FEQ34237617-0C682174-FBAE-499D-93D2-3A7908257C0C
P2860
Release of initiation factors from 48S complexes during ribosomal subunit joining and the link between establishment of codon-anticodon base-pairing and hydrolysis of eIF2-bound GTP.
description
2004 nî lūn-bûn
@nan
2004 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Release of initiation factors ...... hydrolysis of eIF2-bound GTP.
@ast
Release of initiation factors ...... hydrolysis of eIF2-bound GTP.
@en
Release of initiation factors ...... hydrolysis of eIF2-bound GTP.
@nl
type
label
Release of initiation factors ...... hydrolysis of eIF2-bound GTP.
@ast
Release of initiation factors ...... hydrolysis of eIF2-bound GTP.
@en
Release of initiation factors ...... hydrolysis of eIF2-bound GTP.
@nl
prefLabel
Release of initiation factors ...... hydrolysis of eIF2-bound GTP.
@ast
Release of initiation factors ...... hydrolysis of eIF2-bound GTP.
@en
Release of initiation factors ...... hydrolysis of eIF2-bound GTP.
@nl
P2093
P2860
P356
P1433
P1476
Release of initiation factors ...... hydrolysis of eIF2-bound GTP.
@en
P2093
Anett Unbehaun
Christopher U T Hellen
Sergei I Borukhov
Tatyana V Pestova
P2860
P304
P356
10.1101/GAD.1255704
P577
2004-12-01T00:00:00Z