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‘Ribozoomin’ – Translation Initiation from the Perspective of the Ribosome-bound Eukaryotic Initiation Factors (eIFs)

https://doi.org/10.2174/138920312801619385
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Outgoing claims: the papers this work cites, builds on, or argues with.

inferredcites →https://doi.org/10.1002/j.1460-2075.1993.tb06077.xopenalex-snapshot
A Saccharomyces cerevisiae homologue of mammalian translation initiation factor 4B contributes to RNA helicase activity.
inferredcites →https://doi.org/10.1002/j.1460-2075.1993.tb06078.xopenalex-snapshot
A new yeast translation initiation factor suppresses a mutation in the eIF‐4A RNA helicase.
inferredcites →https://doi.org/10.1002/j.1460-2075.1994.tb06370.xopenalex-snapshot
Dominant negative mutants of mammalian translation initiation factor eIF‐4A define a critical role for eIF‐4F in cap‐dependent and cap‐independent initiation of translation.
inferredcites →https://doi.org/10.1002/j.1460-2075.1996.tb01021.xopenalex-snapshot
Ligand interactions with eukaryotic translation initiation factor 2: role of the gamma‐subunit.
inferredcites →https://doi.org/10.1002/j.1460-2075.1996.tb01108.xopenalex-snapshot
Association of the yeast poly(A) tail binding protein with translation initiation factor eIF‐4G.
inferredcites →https://doi.org/10.1016/0022-2836(91)90017-zopenalex-snapshot
A severely truncated form of translational initiation factor 2 supports growth of Escherichia coli
inferredcites →https://doi.org/10.1016/0092-8674(78)90039-9openalex-snapshot
How do eucaryotic ribosomes select initiation regions in messenger RNA?
inferredcites →https://doi.org/10.1016/0092-8674(86)90762-2openalex-snapshot
Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes
inferredcites →https://doi.org/10.1016/0092-8674(92)90193-gopenalex-snapshot
Phosphorylation of initiation factor 2α by protein kinase GCN2 mediates gene-specific translational control of GCN4 in yeast
inferredcites →https://doi.org/10.1016/b978-0-12-386497-0.00002-5openalex-snapshot
Termination and post-termination events in eukaryotic translation
inferredcites →https://doi.org/10.1016/j.bbagrm.2009.06.001openalex-snapshot
IRES-induced conformational changes in the ribosome and the mechanism of translation initiation by internal ribosomal entry
inferredcites →https://doi.org/10.1016/j.cell.2004.11.042openalex-snapshot
mRNA Helicase Activity of the Ribosome
inferredcites →https://doi.org/10.1016/j.cell.2005.03.023openalex-snapshot
The Cryo-EM Structure of a Translation Initiation Complex from Escherichia coli
inferredcites →https://doi.org/10.1016/j.cell.2005.10.024openalex-snapshot
mTOR and S6K1 Mediate Assembly of the Translation Preinitiation Complex through Dynamic Protein Interchange and Ordered Phosphorylation Events
inferredcites →https://doi.org/10.1016/j.cell.2007.08.041openalex-snapshot
Recycling of Eukaryotic Posttermination Ribosomal Complexes
inferredcites →https://doi.org/10.1016/j.cell.2008.02.030openalex-snapshot
Upf1 Phosphorylation Triggers Translational Repression during Nonsense-Mediated mRNA Decay
inferredcites →https://doi.org/10.1016/j.cell.2009.01.014openalex-snapshot
Topology and Regulation of the Human eIF4A/4G/4H Helicase Complex in Translation Initiation
inferredcites →https://doi.org/10.1016/j.cell.2009.01.042openalex-snapshot
Regulation of Translation Initiation in Eukaryotes: Mechanisms and Biological Targets
inferredcites →https://doi.org/10.1016/j.cell.2021.03.060openalex-snapshot
mTOR and S6K1 mediate assembly of the translation preinitiation complex through dynamic protein interchange and ordered phosphorylation events
inferredcites →https://doi.org/10.1016/j.gene.2005.06.037openalex-snapshot
Regulation of translation via mRNA structure in prokaryotes and eukaryotes
inferredcites →https://doi.org/10.1016/j.jmb.2003.09.045openalex-snapshot
The Crystal Structure of the N-terminal Region of the Alpha Subunit of Translation Initiation Factor 2 (eIF2α) from Saccharomyces cerevisiae Provides a View of the Loop Containing Serine 51, the Target of the eIF2α-specific Kinases
inferredcites →https://doi.org/10.1016/j.jmb.2003.10.049openalex-snapshot
Reinitiation and Recycling are Distinct Processes Occurring Downstream of Translation Termination in Yeast
inferredcites →https://doi.org/10.1016/j.jmb.2003.11.025openalex-snapshot
GTP-dependent Recognition of the Methionine Moiety on Initiator tRNA by Translation Factor eIF2
inferredcites →https://doi.org/10.1016/j.jmb.2005.11.083openalex-snapshot
Communication between Eukaryotic Translation Initiation Factors 5 and 1A within the Ribosomal Pre-initiation Complex Plays a Role in Start Site Selection
inferredcites →https://doi.org/10.1016/j.jmb.2006.03.037openalex-snapshot
Crystal Structure of the C-terminal Domain of S.cerevisiae eIF5
inferredcites →https://doi.org/10.1016/j.jmb.2006.05.021openalex-snapshot
The Crystal Structure of the Carboxy-Terminal Domain of Human Translation Initiation Factor eIF5
inferredcites →https://doi.org/10.1016/j.jmb.2008.07.039openalex-snapshot
Crystal Structure of the Intact Archaeal Translation Initiation Factor 2 Demonstrates Very High Conformational Flexibility in the α- and β-Subunits
inferredcites →https://doi.org/10.1016/j.jmb.2008.10.029openalex-snapshot
Kinetic Analysis of Late Steps of Eukaryotic Translation Initiation
inferredcites →https://doi.org/10.1016/j.jmb.2009.09.017openalex-snapshot
eIF1 Controls Multiple Steps in Start Codon Recognition during Eukaryotic Translation Initiation
inferredcites →https://doi.org/10.1016/j.jmb.2009.12.047openalex-snapshot
The Indispensable N-Terminal Half of eIF3j/HCR1 Cooperates with its Structurally Conserved Binding Partner eIF3b/PRT1-RRM and with eIF1A in Stringent AUG Selection
inferredcites →https://doi.org/10.1016/j.molcel.2004.11.051openalex-snapshot
A Conformational Change in the Eukaryotic Translation Preinitiation Complex and Release of eIF1 Signal Recognition of the Start Codon
inferredcites →https://doi.org/10.1016/j.molcel.2005.09.008openalex-snapshot
Pi Release from eIF2, Not GTP Hydrolysis, Is the Step Controlled by Start-Site Selection during Eukaryotic Translation Initiation
inferredcites →https://doi.org/10.1016/j.molcel.2007.03.018openalex-snapshot
The Eukaryotic Translation Initiation Factors eIF1 and eIF1A Induce an Open Conformation of the 40S Ribosome
inferredcites →https://doi.org/10.1016/j.molcel.2007.05.019openalex-snapshot
eIF3j Is Located in the Decoding Center of the Human 40S Ribosomal Subunit
inferredcites →https://doi.org/10.1016/j.molcel.2009.09.042openalex-snapshot
The SXL-UNR Corepressor Complex Uses a PABP-Mediated Mechanism to Inhibit Ribosome Recruitment to msl-2 mRNA
inferredcites →https://doi.org/10.1016/j.molcel.2009.12.034openalex-snapshot
The Role of ABCE1 in Eukaryotic Posttermination Ribosomal Recycling
inferredcites →https://doi.org/10.1016/j.molcel.2010.08.021openalex-snapshot
The 5′-7-Methylguanosine Cap on Eukaryotic mRNAs Serves Both to Stimulate Canonical Translation Initiation and to Block an Alternative Pathway
inferredcites →https://doi.org/10.1016/j.sbi.2010.11.007openalex-snapshot
Dynamics of the translational machinery
inferredcites →https://doi.org/10.1016/j.str.2004.07.010openalex-snapshot
Solution Structure of Human Initiation Factor eIF2α Reveals Homology to the Elongation Factor eEF1B
inferredcites →https://doi.org/10.1016/j.str.2005.09.020openalex-snapshot
Structural Switch of the γ Subunit in an Archaeal aIF2αγ Heterodimer
inferredcites →https://doi.org/10.1016/j.str.2006.03.012openalex-snapshot
Two Structurally Atypical HEAT Domains in the C-Terminal Portion of Human eIF4G Support Binding to eIF4A and Mnk1
inferredcites →https://doi.org/10.1016/j.str.2009.09.015openalex-snapshot
Comprehensive Molecular Structure of the Eukaryotic Ribosome
inferredcites →https://doi.org/10.1016/s0021-9258(18)50898-xopenalex-snapshot
eIF4G dramatically enhances the binding of eIF4E to the mRNA 5′-cap structure.
inferredcites →https://doi.org/10.1016/s0079-6603(02)72066-7openalex-snapshot
Viral strategies of translation initiation: Ribosomal shunt and reinitiation
inferredcites →https://doi.org/10.1016/s0092-8674(00)00181-1openalex-snapshot
X-Ray Structures of the Universal Translation Initiation Factor IF2/eIF5B
inferredcites →https://doi.org/10.1016/s0092-8674(00)80280-9openalex-snapshot
Cocrystal Structure of the Messenger RNA 5′ Cap-Binding Protein (eIF4E) Bound to 7-methyl-GDP
inferredcites →https://doi.org/10.1016/s0092-8674(00)81308-2openalex-snapshot
Site-Specific Ribose Methylation of Preribosomal RNA: A Novel Function for Small Nucleolar RNAs
inferredcites →https://doi.org/10.1016/s0092-8674(01)00487-1openalex-snapshot
A Plant Viral “Reinitiation” Factor Interacts with the Host Translational Machinery
inferredcites →https://doi.org/10.1016/s0092-8674(01)00539-6openalex-snapshot
Structure of the 80S Ribosome from Saccharomyces cerevisiae—tRNA-Ribosome and Subunit-Subunit Interactions
inferredcites →https://doi.org/10.1016/s0092-8674(02)01171-6openalex-snapshot
Uncoupling of Initiation Factor eIF5B/IF2 GTPase and Translational Activities by Mutations that Lower Ribosome Affinity
inferredcites →https://doi.org/10.1016/s0092-8674(03)00975-9openalex-snapshot
Ribosome Loading onto the mRNA Cap Is Driven by Conformational Coupling between eIF4G and eIF4E
inferredcites →https://doi.org/10.1016/s0092-8674(88)80006-0openalex-snapshot
Mutations at a Zn(II) finger motif in the yeast elF-2β gene alter ribosomal start-site selection during the scanning process
inferredcites →https://doi.org/10.1016/s0960-9822(00)00025-7openalex-snapshot
Eukaryotic translation initiation factor 5 (eIF5) acts as a classical GTPase-activator protein
inferredcites →https://doi.org/10.1016/s1097-2765(00)80407-4openalex-snapshot
The eIF1A Solution Structure Reveals a Large RNA-Binding Surface Important for Scanning Function
inferredcites →https://doi.org/10.1016/s1097-2765(01)00167-8openalex-snapshot
A Conserved HEAT Domain within eIF4G Directs Assembly of the Translation Initiation Machinery
inferredcites →https://doi.org/10.1016/s1097-2765(02)00555-5openalex-snapshot
Recognition of eIF4G by Rotavirus NSP3 Reveals a Basis for mRNA Circularization
inferredcites →https://doi.org/10.1017/s0033583505004026openalex-snapshot
Translation initiation: structures, mechanisms and evolution
inferredcites →https://doi.org/10.1017/s1355838298980487openalex-snapshot
The RNA recognition motif of yeast translation initiation factor Tif3/eIF4B is required but not sufficient for RNA strand-exchange and translational activity
inferredcites →https://doi.org/10.1021/bi011984nopenalex-snapshot
Structure of the β Subunit of Translation Initiation Factor 2 from the Archaeon Methanococcus jannaschii: A Representative of the eIF2β/eIF5 Family of Proteins,
inferredcites →https://doi.org/10.1021/bi047645mopenalex-snapshot
A Mutant of Eukaryotic Protein Synthesis Initiation Factor eIF4EK119A Has an Increased Binding Affinity for both m7G Cap Analogues and eIF4G Peptides
inferredcites →https://doi.org/10.1021/bi050373iopenalex-snapshot
Structure−Function Relationships of the Intact aIF2α Subunit from the Archaeon Pyrococcus abyssi,
inferredcites →https://doi.org/10.1021/bi052387uopenalex-snapshot
Structure of the Eukaryotic Initiation Factor (eIF) 5 Reveals a Fold Common to Several Translation Factors,
inferredcites →https://doi.org/10.1021/bi992322popenalex-snapshot
Wheat Germ Translation Initiation Factor eIF4B Affects eIF4A and eIFiso4F Helicase Activity by Increasing the ATP Binding Affinity of eIF4A
inferredcites →https://doi.org/10.1038/29703openalex-snapshot
Eukaryotic ribosomes require initiation factors 1 and 1A to locate initiation codons
inferredcites →https://doi.org/10.1038/35002118openalex-snapshot
The joining of ribosomal subunits in eukaryotes requires eIF5B
inferredcites →https://doi.org/10.1038/emboj.2008.259openalex-snapshot
General RNA‐binding proteins have a function in poly(A)‐binding protein‐dependent translation
inferredcites →https://doi.org/10.1038/emboj.2008.90openalex-snapshot
Ribosomal position and contacts of mRNA in eukaryotic translation initiation complexes
inferredcites →https://doi.org/10.1038/emboj.2010.312openalex-snapshot
Multiple elements in the eIF4G1 N‐terminus promote assembly of eIF4G1•PABP mRNPs in vivo
inferredcites →https://doi.org/10.1038/embor.2009.272openalex-snapshot
The iron–sulphur protein RNase L inhibitor functions in translation termination
inferredcites →https://doi.org/10.1038/nature02160openalex-snapshot
Release of eIF6 (p27BBP) from the 60S subunit allows 80S ribosome assembly
inferredcites →https://doi.org/10.1038/nature06974openalex-snapshot
Translation factors promote the formation of two states of the closed-loop mRNP
inferredcites →https://doi.org/10.1038/nature07192openalex-snapshot
Structure of the 30S translation initiation complex
inferredcites →https://doi.org/10.1038/nature08403openalex-snapshot
What recent ribosome structures have revealed about the mechanism of translation
inferredcites →https://doi.org/10.1038/nature09003openalex-snapshot
eIF5 has GDI activity necessary for translational control by eIF2 phosphorylation
inferredcites →https://doi.org/10.1038/nrm2838openalex-snapshot
The mechanism of eukaryotic translation initiation and principles of its regulation
inferredcites →https://doi.org/10.1038/nrm3154openalex-snapshot
From unwinding to clamping — the DEAD box RNA helicase family
inferredcites →https://doi.org/10.1038/nsb0997-717openalex-snapshot
Structure of translation factor elF4E bound to m7GDP and interaction with 4E-binding protein
inferredcites →https://doi.org/10.1038/nsmb.1445openalex-snapshot
Eukaryotic translation initiation machinery can operate in a bacterial-like mode without eIF2
inferredcites →https://doi.org/10.1038/nsmb.2133openalex-snapshot
Initiation factor eIF2γ promotes eIF2–GTP–Met-tRNAiMet ternary complex binding to the 40S ribosome
inferredcites →https://doi.org/10.1038/nsmb822openalex-snapshot
Identification of the versatile scaffold protein RACK1 on the eukaryotic ribosome by cryo-EM
inferredcites →https://doi.org/10.1038/sj.emboj.7600116openalex-snapshot
Functions of eIF3 downstream of 48S assembly impact AUG recognition and GCN4 translational control
inferredcites →https://doi.org/10.1038/sj.emboj.7600821openalex-snapshot
The eIF1A C‐terminal domain promotes initiation complex assembly, scanning and AUG selection in vivo
inferredcites →https://doi.org/10.1038/sj.emboj.7600844openalex-snapshot
Regulation of GTP hydrolysis prior to ribosomal AUG selection during eukaryotic translation initiation
inferredcites →https://doi.org/10.1038/sj.emboj.7600904openalex-snapshot
The fidelity of translation initiation: reciprocal activities of eIF1, IF3 and YciH
inferredcites →https://doi.org/10.1038/sj.emboj.7601047openalex-snapshot
mTOR‐dependent stimulation of the association of eIF4G and eIF3 by insulin
inferredcites →https://doi.org/10.1038/sj.emboj.7601339openalex-snapshot
An eIF5/eIF2 complex antagonizes guanine nucleotide exchange by eIF2B during translation initiation
inferredcites →https://doi.org/10.1038/sj.emboj.7601613openalex-snapshot
N‐ and C‐terminal residues of eIF1A have opposing effects on the fidelity of start codon selection
inferredcites →https://doi.org/10.1038/sj.emboj.7601751openalex-snapshot
Position of eukaryotic initiation factor eIF5B on the 80S ribosome mapped by directed hydroxyl radical probing
inferredcites →https://doi.org/10.1038/sj.emboj.7601765openalex-snapshot
Reconstitution reveals the functional core of mammalian eIF3
inferredcites →https://doi.org/10.1038/sj.embor.7400291openalex-snapshot
Regulation of eukaryotic translation by the RACK1 protein: a platform for signalling molecules on the ribosome
inferredcites →https://doi.org/10.1042/0264-6021:3470703openalex-snapshot
Conserved sequences in the β subunit of archaeal and eukaryal translation initiation factor 2 (eIF2), absent from eIF5, mediate interaction with eIF2γ
inferredcites →https://doi.org/10.1042/0264-6021:3550223openalex-snapshot
Structural and functional similarities between the central eukaryotic initiation factor (eIF)4A-binding domain of mammalian eIF4G and the eIF4A-binding domain of yeast eIF4G
inferredcites →https://doi.org/10.1042/bst0381558openalex-snapshot
Translational termination–reinitiation in RNA viruses
inferredcites →https://doi.org/10.1073/pnas.0400541101openalex-snapshot
Reinitiation involving upstream ORFs regulates ATF4 mRNA translation in mammalian cells
inferredcites →https://doi.org/10.1073/pnas.0507960102openalex-snapshot
The eukaryotic initiation factor (eIF) 5 HEAT domain mediates multifactor assembly and scanning with distinct interfaces to eIF1, eIF2, eIF3, and eIF4G
inferredcites →https://doi.org/10.1073/pnas.0706784104openalex-snapshot
Structure of an archaeal heterotrimeric initiation factor 2 reveals a nucleotide state between the GTP and the GDP states
inferredcites →https://doi.org/10.1073/pnas.0800418105openalex-snapshot
Crystal structure of the yeast eIF4A-eIF4G complex: An RNA-helicase controlled by protein–protein interactions
inferredcites →https://doi.org/10.1073/pnas.0801313105openalex-snapshot
Mass spectrometry reveals modularity and a complete subunit interaction map of the eukaryotic translation factor eIF3
inferredcites →https://doi.org/10.1073/pnas.0811115106openalex-snapshot
ATP hydrolysis is required for DEAD-box protein recycling but not for duplex unwinding
inferredcites →https://doi.org/10.1073/pnas.1009269107openalex-snapshot
Initiation context modulates autoregulation of eukaryotic translation initiation factor 1 (eIF1)
inferredcites →https://doi.org/10.1073/pnas.1116821108openalex-snapshot
Functional reconstitution of human eukaryotic translation initiation factor 3 (eIF3)
inferredcites →https://doi.org/10.1073/pnas.262569399openalex-snapshot
Initiation factor eIF5B catalyzes second GTP-dependent step in eukaryotic translation initiation
inferredcites →https://doi.org/10.1073/pnas.94.17.9046openalex-snapshot
Translation initiation factor eIF4G mediates in vitro poly(A) tail-dependent translation
inferredcites →https://doi.org/10.1073/pnas.97.24.13080openalex-snapshot
Crystal structure of yeast initiation factor 4A, a DEAD-box RNA helicase
inferredcites →https://doi.org/10.1074/jbc.270.37.21975openalex-snapshot
Mapping of Functional Domains in Eukaryotic Protein Synthesis Initiation Factor 4G (eIF4G) with Picornaviral Proteases
inferredcites →https://doi.org/10.1074/jbc.272.19.12359openalex-snapshot
Subunit Assembly and Guanine Nucleotide Exchange Activity of Eukaryotic Initiation Factor-2B Expressed in Sf9 Cells
inferredcites →https://doi.org/10.1074/jbc.272.2.1101openalex-snapshot
Conservation and Diversity of Eukaryotic Translation Initiation Factor eIF3
inferredcites →https://doi.org/10.1074/jbc.272.29.18333openalex-snapshot
Characterization of Translation Initiation Factor 5 (eIF5) fromSaccharomyces cerevisiae
inferredcites →https://doi.org/10.1074/jbc.272.35.21677openalex-snapshot
eIF4G Dramatically Enhances the Binding of eIF4E to the mRNA 5′-Cap Structure
inferredcites →https://doi.org/10.1074/jbc.272.50.31712openalex-snapshot
Specific Interaction of Eukaryotic Translation Initiation Factor 5 (eIF5) with the β-Subunit of eIF2
inferredcites →https://doi.org/10.1074/jbc.273.29.18573openalex-snapshot
Complex Formation by All Five Homologues of Mammalian Translation Initiation Factor 3 Subunits from Yeast Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1074/jbc.273.4.2379openalex-snapshot
Rack1, a Receptor for Activated Protein Kinase C, Interacts with Integrin β Subunit
inferredcites →https://doi.org/10.1074/jbc.273.48.31901openalex-snapshot
Characterization of cDNAs Encoding the p44 and p35 Subunits of Human Translation Initiation Factor eIF3
inferredcites →https://doi.org/10.1074/jbc.274.18.12236openalex-snapshot
Biochemical and Kinetic Characterization of the RNA Helicase Activity of Eukaryotic Initiation Factor 4A
inferredcites →https://doi.org/10.1074/jbc.274.30.21297openalex-snapshot
The Cap-binding Protein eIF4E Promotes Folding of a Functional Domain of Yeast Translation Initiation Factor eIF4G1
inferredcites →https://doi.org/10.1074/jbc.274.38.26720openalex-snapshot
Interaction of Translation Initiation Factor eIF4G with eIF4A in the Yeast Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1074/jbc.274.39.27567openalex-snapshot
The Saccharomyces cerevisiae HCR1 Gene Encoding a Homologue of the p35 Subunit of Human Translation Initiation Factor 3 (eIF3) Is a High Copy Suppressor of a Temperature-sensitive Mutation in the Rpg1p Subunit of Yeast eIF3
inferredcites →https://doi.org/10.1074/jbc.274.50.35415openalex-snapshot
Further Biochemical and Kinetic Characterization of Human Eukaryotic Initiation Factor 4H
inferredcites →https://doi.org/10.1074/jbc.c109.096057openalex-snapshot
Mechanism of eIF6-mediated Inhibition of Ribosomal Subunit Joining
inferredcites →https://doi.org/10.1074/jbc.m004565200openalex-snapshot
Stabilization of Eukaryotic Initiation Factor 4E Binding to the mRNA 5′-Cap by Domains of eIF4G
inferredcites →https://doi.org/10.1074/jbc.m006345200openalex-snapshot
Characterization of the Two eIF4A-binding Sites on Human eIF4G-1
inferredcites →https://doi.org/10.1074/jbc.m008863200openalex-snapshot
Eukaryotic Translation Initiation Factor 5 Functions as a GTPase-activating Protein
inferredcites →https://doi.org/10.1074/jbc.m100157200openalex-snapshot
Modulation of the Helicase Activity of eIF4A by eIF4B, eIF4H, and eIF4F
inferredcites →https://doi.org/10.1074/jbc.m109.007658openalex-snapshot
Phosphorylation of Plant Translation Initiation Factors by CK2 Enhances the in Vitro Interaction of Multifactor Complex Components
inferredcites →https://doi.org/10.1074/jbc.m111804200openalex-snapshot
Crystal Structure of the N-terminal Segment of Human Eukaryotic Translation Initiation Factor 2α
inferredcites →https://doi.org/10.1074/jbc.m210357200openalex-snapshot
Mammalian Translation Initiation Factor eIF1 Functions with eIF1A and eIF3 in the Formation of a Stable 40 S Preinitiation Complex
inferredcites →https://doi.org/10.1074/jbc.m310418200openalex-snapshot
X-ray Structure of Translation Initiation Factor eIF2γ
inferredcites →https://doi.org/10.1074/jbc.m311055200openalex-snapshot
Structure of the Catalytic Fragment of Translation Initiation Factor 2B and Identification of a Critically Important Catalytic Residue
inferredcites →https://doi.org/10.1074/jbc.m311561200openalex-snapshot
Functional Molecular Mapping of Archaeal Translation Initiation Factor 2
inferredcites →https://doi.org/10.1074/jbc.m312745200openalex-snapshot
The j-Subunit of Human Translation Initiation Factor eIF3 Is Required for the Stable Binding of eIF3 and Its Subcomplexes to 40 S Ribosomal Subunits in Vitro
inferredcites →https://doi.org/10.1074/jbc.m511700200openalex-snapshot
Direct Binding of Translation Initiation Factor eIF2γ-G Domain to Its GTPase-activating and GDP-GTP Exchange Factors eIF5 and eIF2Bϵ
inferredcites →https://doi.org/10.1074/jbc.m600210200openalex-snapshot
Interaction between Eukaryotic Initiation Factors 1A and 5B Is Required for Efficient Ribosomal Subunit Joining
inferredcites →https://doi.org/10.1074/jbc.m602780200openalex-snapshot
Functional Analysis of Individual Binding Activities of the Scaffold Protein eIF4G
inferredcites →https://doi.org/10.1074/jbc.m605418200openalex-snapshot
Translation Initiation Factor eIF4G-1 Binds to eIF3 through the eIF3e Subunit
inferredcites →https://doi.org/10.1074/jbc.m610860200openalex-snapshot
Structure of eIF3b RNA Recognition Motif and Its Interaction with eIF3j
inferredcites →https://doi.org/10.1074/jbc.m708530200openalex-snapshot
Phosphorylation of eIF2 Directs ATF5 Translational Control in Response to Diverse Stress Conditions
inferredcites →https://doi.org/10.1074/jbc.r900002200openalex-snapshot
eIF4E: New Family Members, New Binding Partners, New Roles
inferredcites →https://doi.org/10.1083/jcb.200710215openalex-snapshot
eIF4GI links nutrient sensing by mTOR to cell proliferation and inhibition of autophagy
inferredcites →https://doi.org/10.1093/emboj/16.22.6812openalex-snapshot
Identification of partners of TIF34, a component of the yeast eIF3 complex, required for cell proliferation and translation initiation
inferredcites →https://doi.org/10.1093/emboj/16.4.817openalex-snapshot
A new translational regulator with homology to eukaryotic translation initiation factor 4G
inferredcites →https://doi.org/10.1093/emboj/17.24.7480openalex-snapshot
A newly identified N‐terminal amino acid sequence of human eIF4G binds poly(A)‐binding protein and functions in poly(A)‐dependent translation
inferredcites →https://doi.org/10.1093/emboj/18.6.1673openalex-snapshot
Conserved bipartite motifs in yeast eIF5 and eIF2Bϵ, GTPase‐activating and GDP–GTP exchange factors in translation initiation, mediate binding to their common substrate eIF2
inferredcites →https://doi.org/10.1093/emboj/18.9.2631openalex-snapshot
Structure and interactions of the translation initiation factor eIF1
inferredcites →https://doi.org/10.1093/emboj/19.17.4723openalex-snapshot
Multiple portions of poly(A)‐binding protein stimulate translation in vivo
inferredcites →https://doi.org/10.1093/emboj/19.24.6891openalex-snapshot
A new pathway of translational regulation mediated by eukaryotic initiation factor 3
inferredcites →https://doi.org/10.1093/emboj/20.4.891openalex-snapshot
Related eIF3 subunits TIF32 and HCR1 interact with an RNA recognition motif in PRT1 required for eIF3 integrity and ribosome binding
inferredcites →https://doi.org/10.1093/emboj/20.9.2326openalex-snapshot
Multiple roles for the C‐terminal domain of eIF5 in translation initiation complex assembly and GTPase activation
inferredcites →https://doi.org/10.1093/emboj/21.7.1821openalex-snapshot
The large subunit of initiation factor aIF2 is a close structural homologue of elongation factors
inferredcites →https://doi.org/10.1093/emboj/cdf563openalex-snapshot
Direct eIF2–eIF3 contact in the multifactor complex is important for translation initiation in vivo
inferredcites →https://doi.org/10.1093/emboj/cdg030openalex-snapshot
Domains of eIF1A that mediate binding to eIF2, eIF3 and eIF5B and promote ternary complex recruitment in vivo
inferredcites →https://doi.org/10.1093/nar/26.5.1150openalex-snapshot
The yeast transcription factor genes YAP1 and YAP2 are subject to differential control at the levels of both translation and mRNA stability
inferredcites →https://doi.org/10.1093/nar/29.24.5226openalex-snapshot
Constraints on reinitiation of translation in mammals
inferredcites →https://doi.org/10.1093/nar/gkp1113openalex-snapshot
Yeast strains with N-terminally truncated ribosomal protein S5: implications for the evolution, structure and function of the Rps5/Rps7 proteins
inferredcites →https://doi.org/10.1093/nar/gkp519openalex-snapshot
Position of eukaryotic translation initiation factor eIF1A on the 40S ribosomal subunit mapped by directed hydroxyl radical probing
inferredcites →https://doi.org/10.1093/nar/gkq1206openalex-snapshot
Synergistic activation of eIF4A by eIF4B and eIF4G
inferredcites →https://doi.org/10.1093/nar/gkr045openalex-snapshot
Common conformational changes induced in type 2 picornavirus IRESs by cognate trans-acting factors
inferredcites →https://doi.org/10.1093/nar/gkr1083openalex-snapshot
The eIF3c/NIP1 PCI domain interacts with RNA and RACK1/ASC1 and promotes assembly of translation preinitiation complexes
inferredcites →https://doi.org/10.1093/nar/gkr1192openalex-snapshot
Stringency of start codon selection modulates autoregulation of translation initiation factor eIF5
inferredcites →https://doi.org/10.1093/nar/gkr765openalex-snapshot
Structural analysis of an eIF3 subcomplex reveals conserved interactions required for a stable and proper translation pre-initiation complex assembly
inferredcites →https://doi.org/10.1093/nar/gkr772openalex-snapshot
The human translation initiation multi-factor complex promotes methionyl-tRNA i binding to the 40S ribosomal subunit
inferredcites →https://doi.org/10.1101/087969767.48.225openalex-snapshot
9 Mechanism of Translation Initiation in the Yeast Saccharomyces cerevisiae
inferredcites →https://doi.org/10.1101/087969767.48.87openalex-snapshot
4 The Mechanism of Translation Initiation in Eukaryotes
inferredcites →https://doi.org/10.1101/gad.1020902openalex-snapshot
The roles of individual eukaryotic translation initiation factors in ribosomal scanning and initiation codon selection
inferredcites →https://doi.org/10.1101/gad.1065403openalex-snapshot
The yeast eIF3 subunits TIF32/a, NIP1/c, and eIF5 make critical connections with the 40S ribosome in vivo
inferredcites →https://doi.org/10.1101/gad.1141803openalex-snapshot
Position of eukaryotic initiation factor eIF1 on the 40S ribosomal subunit determined by directed hydroxyl radical probing
inferredcites →https://doi.org/10.1101/gad.12.4.514openalex-snapshot
eIF2 independently binds two distinct eIF2B subcomplexes that catalyze and regulate guanine-nucleotide exchange
inferredcites →https://doi.org/10.1101/gad.1255704openalex-snapshot
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
inferredcites →https://doi.org/10.1101/gad.1262905openalex-snapshot
Mammalian poly(A)-binding protein is a eukaryotic translation initiation factor, which acts via multiple mechanisms
inferredcites →https://doi.org/10.1101/gad.1335305openalex-snapshot
Structural basis for the enhancement of eIF4A helicase activity by eIF4G
inferredcites →https://doi.org/10.1101/gad.1397906openalex-snapshot
Specific functional interactions of nucleotides at key - 3 and + 4 positions flanking the initiation codon with components of the mammalian 48S translation initiation complex
inferredcites →https://doi.org/10.1101/gad.1528307openalex-snapshot
Dissociation of eIF1 from the 40S ribosomal subunit is a key step in start codon selection in vivo
inferredcites →https://doi.org/10.1101/gad.1696608openalex-snapshot
Genetic identification of yeast 18S rRNA residues required for efficient recruitment of initiator tRNAMet and AUG selection
inferredcites →https://doi.org/10.1101/gad.1871910openalex-snapshot
Regulatory elements in eIF1A control the fidelity of start codon selection by modulating tRNAiMet binding to the ribosome
inferredcites →https://doi.org/10.1101/gad.276504openalex-snapshot
What determines whether mammalian ribosomes resume scanning after translation of a short upstream open reading frame?
inferredcites →https://doi.org/10.1101/gad.439507openalex-snapshot
The mechanism of an exceptional case of reinitiation after translation of a long ORF reveals why such events do not generally occur in mammalian mRNA translation
inferredcites →https://doi.org/10.1101/gad.480508openalex-snapshot
eIF3a cooperates with sequences 5′ of uORF1 to promote resumption of scanning by post-termination ribosomes for reinitiation on GCN4 mRNA
inferredcites →https://doi.org/10.1101/gad.507609openalex-snapshot
The importance of inter- and intramolecular base pairing for translation reinitiation on a eukaryotic bicistronic mRNA
inferredcites →https://doi.org/10.1101/gad.831800openalex-snapshot
A multifactor complex of eukaryotic initiation factors, eIF1, eIF2, eIF3, eIF5, and initiator tRNAMet is an important translation initiation intermediate in vivo
inferredcites →https://doi.org/10.1101/gad.887201openalex-snapshot
Regulation of translation initiation by FRAP/mTOR
inferredcites →https://doi.org/10.1101/gad.912401openalex-snapshot
Hierarchical phosphorylation of the translation inhibitor 4E-BP1
inferredcites →https://doi.org/10.1107/s0108767302085288openalex-snapshot
X-ray structures of the universal translation initiation factor IF2/eIF5B: conformational changes on GDP and GTP binding
inferredcites →https://doi.org/10.1110/ps.03506604openalex-snapshot
Structure of the archaeal translation initiation factor aIF2β from Methanobacterium thermoautotrophicum: Implications for translation initiation
inferredcites →https://doi.org/10.1126/science.1057766openalex-snapshot
Crystal Structure of an Initiation Factor Bound to the 30 S Ribosomal Subunit
inferredcites →https://doi.org/10.1126/science.1118977openalex-snapshot
Structural Roles for Human Translation Factor eIF3 in Initiation of Protein Synthesis
inferredcites →https://doi.org/10.1126/science.1168978openalex-snapshot
Genome-Wide Analysis in Vivo of Translation with Nucleotide Resolution Using Ribosome Profiling
inferredcites →https://doi.org/10.1126/science.1194294openalex-snapshot
Crystal Structure of the Eukaryotic Ribosome
inferredcites →https://doi.org/10.1126/science.1198308openalex-snapshot
Crystal Structure of the Eukaryotic 40 S Ribosomal Subunit in Complex with Initiation Factor 1
inferredcites →https://doi.org/10.1126/science.1211204openalex-snapshot
Crystal Structure of the Eukaryotic 60 S Ribosomal Subunit in Complex with Initiation Factor 6
inferredcites →https://doi.org/10.1126/science.1212642openalex-snapshot
The Structure of the Eukaryotic Ribosome at 3.0 Å Resolution
inferredcites →https://doi.org/10.1126/science.280.5370.1757openalex-snapshot
Promotion of Met-tRNA i Met Binding to Ribosomes by yIF2, a Bacterial IF2 Homolog in Yeast
inferredcites →https://doi.org/10.1128/jvi.79.15.9651-9664.2005openalex-snapshot
mRNA Decay during Herpes Simplex Virus (HSV) Infections: Protein-Protein Interactions Involving the HSV Virion Host Shutoff Protein and Translation Factors eIF4H and eIF4A
inferredcites →https://doi.org/10.1128/mcb.00280-10openalex-snapshot
The C-Terminal Region of Eukaryotic Translation Initiation Factor 3a (eIF3a) Promotes mRNA Recruitment, Scanning, and, Together with eIF3j and the eIF3b RNA Recognition Motif, Selection of AUG Start Codons
inferredcites →https://doi.org/10.1128/mcb.00430-10openalex-snapshot
The RNA Recognition Motif of Eukaryotic Translation Initiation Factor 3g (eIF3g) Is Required for Resumption of Scanning of Posttermination Ribosomes for Reinitiation on GCN4 and Together with eIF3i Stimulates Linear Scanning
inferredcites →https://doi.org/10.1128/mcb.01147-08openalex-snapshot
Translation Initiation Factor 2γ Mutant Alters Start Codon Selection Independent of Met-tRNA Binding
inferredcites →https://doi.org/10.1128/mcb.01187-08openalex-snapshot
Requirement of RNA Binding of Mammalian Eukaryotic Translation Initiation Factor 4GI (eIF4GI) for Efficient Interaction of eIF4E with the mRNA Cap
inferredcites →https://doi.org/10.1128/mcb.02254-06openalex-snapshot
Coupled Release of Eukaryotic Translation Initiation Factors 5B and 1A from 80S Ribosomes following Subunit Joining
inferredcites →https://doi.org/10.1128/mcb.05819-11openalex-snapshot
Functional Elements in Initiation Factors 1, 1A, and 2β Discriminate against Poor AUG Context and Non-AUG Start Codons
inferredcites →https://doi.org/10.1128/mcb.10.3.1134openalex-snapshot
Bidirectional RNA Helicase Activity of Eucaryotic Translation Initiation Factors 4A and 4F
inferredcites →https://doi.org/10.1128/mcb.12.4.1432openalex-snapshot
Mutational analysis of conserved positions potentially important for initiator tRNA function in Saccharomyces cerevisiae.
inferredcites →https://doi.org/10.1128/mcb.14.1.606openalex-snapshot
Effect of sequence context at stop codons on efficiency of reinitiation in GCN4 translational control
showing the first 200 of 225

What points at this work

Incoming claims: where this work appears in other papers’ reference lists and arguments.

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Translation arrest as a protein quality control system for aberrant translation of the 3′‐UTR in mammalian cells
inferred← citeshttps://doi.org/10.1002/cbic.201300318openalex-snapshot
Ribosomal Protein S5e is Implicated in Translation Initiation through its Interaction with the N‐Terminal Domain of Initiation Factor eIF2α
inferred← citeshttps://doi.org/10.1002/wrna.1473openalex-snapshot
Translation initiation by cap‐dependent ribosome recruitment: Recent insights and open questions
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Plant Translational Machinery
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Cytoplasm: Translational Apparatus
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mRNA Translation: Fungal Variations on a Eukaryotic Theme
inferred← citeshttps://doi.org/10.1007/978-94-017-9078-9_8openalex-snapshot
eIF3
inferred← citeshttps://doi.org/10.1007/978-981-97-0176-6_21openalex-snapshot
Legume Seed: A Useful Platform for the Production of Medical Proteins/Peptides
inferred← citeshttps://doi.org/10.1007/s11010-017-3127-5openalex-snapshot
Knockdown of eukaryotic translation initiation factor 3 subunit D (eIF3D) inhibits proliferation of acute myeloid leukemia cells
inferred← citeshttps://doi.org/10.1016/b978-0-12-816364-1.00005-6openalex-snapshot
Ribosome cycle—Assembly, degradation, and recycling
inferred← citeshttps://doi.org/10.1016/b978-0-323-99283-1.00016-1openalex-snapshot
Decoding the functional role of extracellular vesicles in hepatocellular carcinoma: implications in clinical theranostics
inferred← citeshttps://doi.org/10.1016/j.bbagrm.2014.10.005openalex-snapshot
The role of eIF3 and its individual subunits in cancer
inferred← citeshttps://doi.org/10.1016/j.bbagrm.2019.194411openalex-snapshot
Tetrapeptide 60–63 of human ribosomal protein uS3 is crucial for translation initiation
inferred← citeshttps://doi.org/10.1016/j.bbapap.2016.06.011openalex-snapshot
Exploring accessibility of structural elements of the mammalian 40S ribosomal mRNA entry channel at various steps of translation initiation
inferred← citeshttps://doi.org/10.1016/j.biochi.2013.07.024openalex-snapshot
Mitochondrial translation initiation machinery: Conservation and diversification
inferred← citeshttps://doi.org/10.1016/j.biochi.2013.11.001openalex-snapshot
Eukaryotic ribosomal protein S3: A constituent of translational machinery and an extraribosomal player in various cellular processes
inferred← citeshttps://doi.org/10.1016/j.biochi.2014.11.016openalex-snapshot
Roles of ribosomal proteins in the functioning of translational machinery of eukaryotes
inferred← citeshttps://doi.org/10.1016/j.biochi.2014.12.008openalex-snapshot
mRNAs that specifically interact with eukaryotic ribosomal subunits
inferred← citeshttps://doi.org/10.1016/j.canlet.2020.12.009openalex-snapshot
eIF3i regulation of protein synthesis, cell proliferation, cell cycle progression, and tumorigenesis
inferred← citeshttps://doi.org/10.1016/j.cbpb.2022.110785openalex-snapshot
RPS6 transcriptional modulation in neural tissues of Nauphoeta cinerea during streptozotocin-associated sugar metabolism impairment.
inferred← citeshttps://doi.org/10.1016/j.cell.2013.04.036openalex-snapshot
Structure of the Mammalian Ribosomal 43S Preinitiation Complex Bound to the Scanning Factor DHX29
inferred← citeshttps://doi.org/10.1016/j.cell.2014.07.044openalex-snapshot
Molecular Architecture of the 40S⋅eIF1⋅eIF3 Translation Initiation Complex
inferred← citeshttps://doi.org/10.1016/j.celrep.2020.108534openalex-snapshot
Structural Differences in Translation Initiation between Pathogenic Trypanosomatids and Their Mammalian Hosts
inferred← citeshttps://doi.org/10.1016/j.celrep.2024.113976openalex-snapshot
Stem-loop-induced ribosome queuing in the uORF2/ATF4 overlap fine-tunes stress-induced human ATF4 translational control
inferred← citeshttps://doi.org/10.1016/j.exphem.2019.05.004openalex-snapshot
Translational regulation and deregulation in erythropoiesis
inferred← citeshttps://doi.org/10.1016/j.exppara.2015.04.002openalex-snapshot
Molecular characterization and functional analysis of subunit 7 of eukaryotic initiation factor 3 from Eimeria tenella
inferred← citeshttps://doi.org/10.1016/j.jbc.2021.100578openalex-snapshot
eIF3 interacts with histone H4 messenger RNA to regulate its translation
inferred← citeshttps://doi.org/10.1016/j.jdermsci.2026.03.008openalex-snapshot
Inhibition of eukaryotic translation initiation factor 1 A (eIF1A) and 3B (eIF3B) diminishes the psoriatic phenotype in two mouse models and human 3D model samples
inferred← citeshttps://doi.org/10.1016/j.jmb.2020.03.006openalex-snapshot
Long-Lost Cousins? eIF3 Recognition of the HCV IRES and Cellular mRNAs
inferred← citeshttps://doi.org/10.1016/j.molcel.2015.06.033openalex-snapshot
Conformational Differences between Open and Closed States of the Eukaryotic Translation Initiation Complex
inferred← citeshttps://doi.org/10.1016/j.molcel.2020.06.004openalex-snapshot
Selective Translation Complex Profiling Reveals Staged Initiation and Co-translational Assembly of Initiation Factor Complexes
inferred← citeshttps://doi.org/10.1016/j.plaphy.2019.10.015openalex-snapshot
The role of eukaryotic initiation factor 3 in plant translation regulation
inferred← citeshttps://doi.org/10.1016/j.sbi.2026.103246openalex-snapshot
Toward a unifying mechanistic model of eukaryotic translation initiation through integrative single-molecule, structural, and computational insights
inferred← citeshttps://doi.org/10.1016/j.str.2014.03.010openalex-snapshot
Translation Initiation Factor eIF3b Contains a Nine-Bladed β-Propeller and Interacts with the 40S Ribosomal Subunit
inferred← citeshttps://doi.org/10.1016/j.str.2025.05.008openalex-snapshot
Antimalarial drug artemisinin stabilizes PfRACK1 binding to the ribosome
inferred← citeshttps://doi.org/10.1016/j.tibs.2017.03.004openalex-snapshot
Structural Insights into the Mechanism of Scanning and Start Codon Recognition in Eukaryotic Translation Initiation
inferred← citeshttps://doi.org/10.1016/j.virol.2013.06.008openalex-snapshot
Translation of viral mRNAs that do not require eIF4E is blocked by the inhibitor 4EGI-1
inferred← citeshttps://doi.org/10.1016/j.ymben.2020.02.001openalex-snapshot
Engineered transient and stable overexpression of translation factors eIF3i and eIF3c in CHOK1 and HEK293 cells gives enhanced cell growth associated with increased c-Myc expression and increased recombinant protein synthesis
inferred← citeshttps://doi.org/10.1017/s0033583516000056openalex-snapshot
The molecular choreography of protein synthesis: translational control, regulation, and pathways
inferred← citeshttps://doi.org/10.1021/acs.jproteome.0c00160openalex-snapshot
Proteomic Profiling of Fast Neutron-Induced Soybean Mutant Unveiled Pathways Associated with Increased Seed Protein Content
inferred← citeshttps://doi.org/10.1021/acsinfecdis.3c00127openalex-snapshot
Plasmodium falciparum Eukaryotic Translation Initiation Factor 3 is Stabilized by Quinazoline-Quinoline Bisubstrate Inhibitors
inferred← citeshttps://doi.org/10.1038/nature13401openalex-snapshot
DENR–MCT-1 promotes translation re-initiation downstream of uORFs to control tissue growth
inferred← citeshttps://doi.org/10.1038/nature14891openalex-snapshot
Structure of mammalian eIF3 in the context of the 43S preinitiation complex
inferred← citeshttps://doi.org/10.1038/s41467-024-51027-zopenalex-snapshot
eIF4E-independent translation is largely eIF3d-dependent
inferred← citeshttps://doi.org/10.1038/s42003-024-06761-xopenalex-snapshot
Differential effects of 40S ribosome recycling factors on reinitiation at regulatory uORFs in GCN4 mRNA are not dictated by their roles in bulk 40S recycling
inferred← citeshttps://doi.org/10.1038/s44318-026-00826-9openalex-snapshot
The identity crisis of cryptic lncRNAs: when non-coding RNAs translate into small peptides
inferred← citeshttps://doi.org/10.1042/bsr20140078openalex-snapshot
Lentivirus-mediated knockdown of eukaryotic translation initiation factor 3 subunit D inhibits proliferation of HCT116 colon cancer cells
inferred← citeshttps://doi.org/10.1042/bst20253069openalex-snapshot
eIF3: a critical player in mRNA recruitment to the ribosome with emerging roles across translation
inferred← citeshttps://doi.org/10.1073/pnas.1620569114openalex-snapshot
Rps3/uS3 promotes mRNA binding at the 40S ribosome entry channel and stabilizes preinitiation complexes at start codons
inferred← citeshttps://doi.org/10.1074/jbc.m112.386656openalex-snapshot
Functional Characterization of the Role of the N-terminal Domain of the c/Nip1 Subunit of Eukaryotic Initiation Factor 3 (eIF3) in AUG Recognition
inferred← citeshttps://doi.org/10.1080/15476286.2015.1017233openalex-snapshot
Two related trypanosomatid eIF4G homologues have functional differences compatible with distinct roles during translation initiation
inferred← citeshttps://doi.org/10.1080/15476286.2015.1086865openalex-snapshot
The unique Leishmania EIF4E4 N-terminus is a target for multiple phosphorylation events and participates in critical interactions required for translation initiation
inferred← citeshttps://doi.org/10.1080/15476286.2016.1269993openalex-snapshot
ABCE1: A special factor that orchestrates translation at the crossroad between recycling and initiation
inferred← citeshttps://doi.org/10.1080/15476286.2017.1353863openalex-snapshot
Does eIF3 promote reinitiation after translation of short upstream ORFs also in mammalian cells?
inferred← citeshttps://doi.org/10.1080/15476286.2017.1391437openalex-snapshot
eIF3: a factor for human health and disease
inferred← citeshttps://doi.org/10.1080/21655979.2021.2017567openalex-snapshot
Eukaryotic translation initiation factor 3 subunit B could serve as a potential prognostic predictor for breast cancer
inferred← citeshttps://doi.org/10.1080/21690731.2014.999576openalex-snapshot
Eukaryote-specific extensions in ribosomal proteins of the small subunit: Structure and function
inferred← citeshttps://doi.org/10.1080/21690731.2016.1257408openalex-snapshot
Fusion proteins of Arabidopsis cap-binding proteins: Cautionary “tails” of woe
inferred← citeshttps://doi.org/10.1093/femsre/fuw041openalex-snapshot
Non-canonical transcription initiation: the expanding universe of transcription initiating substrates
inferred← citeshttps://doi.org/10.1093/femsre/fux059openalex-snapshot
Please do not recycle! Translation reinitiation in microbes and higher eukaryotes
inferred← citeshttps://doi.org/10.1093/nar/gkab652openalex-snapshot
eIF4G is retained on ribosomes elongating and terminating on short upstream ORFs to control reinitiation in yeast
inferred← citeshttps://doi.org/10.1093/nar/gkag627openalex-snapshot
Elongationless start–stop elements are stress-resilient translation gates that are more repressive than uTranslons
inferred← citeshttps://doi.org/10.1093/nar/gkt1369openalex-snapshot
Structural integrity of the PCI domain of eIF3a/TIF32 is required for mRNA recruitment to the 43S pre-initiation complexes
inferred← citeshttps://doi.org/10.1093/nar/gku204openalex-snapshot
Fail-safe mechanism of GCN4 translational control—uORF2 promotes reinitiation by analogous mechanism to uORF1 and thus secures its key role in GCN4 expression
inferred← citeshttps://doi.org/10.1093/nar/gkv1325openalex-snapshot
LOOP IIId of the HCV IRES is essential for the structural rearrangement of the 40S-HCV IRES complex
inferred← citeshttps://doi.org/10.1093/nar/gkv421openalex-snapshot
Translation initiation factor eIF3 promotes programmed stop codon readthrough
inferred← citeshttps://doi.org/10.1093/nar/gkw972openalex-snapshot
Human eIF3b and eIF3a serve as the nucleation core for the assembly of eIF3 into two interconnected modules: the yeast-like core and the octamer
inferred← citeshttps://doi.org/10.1093/nar/gkx049openalex-snapshot
In vivoevidence that eIF3 stays bound to ribosomes elongating and terminating on short upstream ORFs to promote reinitiation
inferred← citeshttps://doi.org/10.1093/nar/gkx1050openalex-snapshot
Fluorescently-tagged human eIF3 for single-molecule spectroscopy
inferred← citeshttps://doi.org/10.1093/nar/gkx805openalex-snapshot
Embraced by eIF3: structural and functional insights into the roles of eIF3 across the translation cycle
inferred← citeshttps://doi.org/10.1093/nar/gky054openalex-snapshot
Structure of a human cap-dependent 48S translation pre-initiation complex
inferred← citeshttps://doi.org/10.1093/nar/gkz570openalex-snapshot
Binding of eIF3 in complex with eIF5 and eIF1 to the 40S ribosomal subunit is accompanied by dramatic structural changes
inferred← citeshttps://doi.org/10.1093/nar/gkz929openalex-snapshot
uS3/Rps3 controls fidelity of translation termination and programmed stop codon readthrough in co-operation with eIF3
inferred← citeshttps://doi.org/10.1098/rstb.2016.0177openalex-snapshot
Dynamics of IRES-mediated translation
inferred← citeshttps://doi.org/10.1098/rstb.2016.0186openalex-snapshot
Eukaryotic aspects of translation initiation brought into focus
inferred← citeshttps://doi.org/10.1101/072702openalex-snapshot
Eukaryotic translation initiation factor 3 plays distinct roles at the mRNA entry and exit channels of the ribosomal preinitiation complex
inferred← citeshttps://doi.org/10.1101/2021.07.26.453809openalex-snapshot
Regulatory Start-Stop Elements in 5’ Untranslated Regions Pervasively Modulate Translation
inferred← citeshttps://doi.org/10.1101/2022.12.10.519887openalex-snapshot
Quinazoline-quinoline bisubstrate inhibitors target eukaryotic translation initiation factor 3 in Plasmodium falciparum
inferred← citeshttps://doi.org/10.1101/2024.03.06.583729openalex-snapshot
Impacts of yeast Tma20/MCTS1, Tma22/DENR and Tma64/eIF2D on translation reinitiation and ribosome recycling
inferred← citeshttps://doi.org/10.1101/2024.04.25.581977openalex-snapshot
The eIF3a subunit drives RNA binding within the eIF3 complex
inferred← citeshttps://doi.org/10.1101/cshperspect.a033092openalex-snapshot
Protein Synthesis Initiation in Eukaryotic Cells
inferred← citeshttps://doi.org/10.1103/physreve.100.022106openalex-snapshot
Biologically motivated three-species exclusion model: Effects of leaky scanning and overlapping genes on initiation of protein synthesis
inferred← citeshttps://doi.org/10.1104/pp.16.00435openalex-snapshot
eIF4A RNA Helicase Associates with Cyclin-Dependent Protein Kinase A in Proliferating Cells and Is Modulated by Phosphorylation
inferred← citeshttps://doi.org/10.1104/pp.18.00648openalex-snapshot
Dynamics of the Pollen Sequestrome Defined by Subcellular Coupled Omics
inferred← citeshttps://doi.org/10.1104/pp.19.00557openalex-snapshot
eIFiso4G Augments the Synthesis of Specific Plant Proteins Involved in Normal Chloroplast Function
inferred← citeshttps://doi.org/10.1111/cmi.12149openalex-snapshot
Participation of eIF4F complex in Junin virus infection: blockage of eIF4E does not impair virus replication
inferred← citeshttps://doi.org/10.1111/mmi.12379openalex-snapshot
A molecular switch in the efficiency of translation reinitiation controls expression of var2csa , a gene implicated in pregnancy‐associated malaria
inferred← citeshttps://doi.org/10.1128/mcb.00663-14openalex-snapshot
Functional and Biochemical Characterization of Human Eukaryotic Translation Initiation Factor 3 in Living Cells
inferred← citeshttps://doi.org/10.1134/s0006297920030013openalex-snapshot
Protein Biosynthesis in Mitochondria: Past Simple, Present Perfect, Future Indefinite
inferred← citeshttps://doi.org/10.1146/annurev-biophys-070816-034034openalex-snapshot
The Jigsaw Puzzle of mRNA Translation Initiation in Eukaryotes: A Decade of Structures Unraveling the Mechanics of the Process
inferred← citeshttps://doi.org/10.11606/d.11.2021.tde-31032021-150358openalex-snapshot
Caracterização do proteoma de folhas, caules e raízes de plantas de >i /i
inferred← citeshttps://doi.org/10.1177/1010428317709805openalex-snapshot
Eukaryotic translation initiation factors and cancer
inferred← citeshttps://doi.org/10.1186/1471-2164-15-1175openalex-snapshot
The translation initiation complex eIF3 in trypanosomatids and other pathogenic excavates – identification of conserved and divergent features based on orthologue analysis
inferred← citeshttps://doi.org/10.1199/tab.0176openalex-snapshot
Mechanism of Cytoplasmic mRNA Translation
inferred← citeshttps://doi.org/10.1261/rna.047084.114openalex-snapshot
Initiation codon selection is accomplished by a scanning mechanism without crucial initiation factors in Sindbis virus subgenomic mRNA
inferred← citeshttps://doi.org/10.1261/rna.054452.115openalex-snapshot
Rules of UGA-N decoding by near-cognate tRNAs and analysis of readthrough on short uORFs in yeast
inferred← citeshttps://doi.org/10.1261/rna.055046.115openalex-snapshot
In-depth analysis of cis-determinants that either promote or inhibit reinitiation on GCN4 mRNA after translation of its four short uORFs
inferred← citeshttps://doi.org/10.1261/rna.069823.118openalex-snapshot
Does functional specialization of ribosomes really exist?
inferred← citeshttps://doi.org/10.1371/journal.pgen.1003962openalex-snapshot
Translation Initiation Factors eIF3 and HCR1 Control Translation Termination and Stop Codon Read-Through in Yeast Cells
inferred← citeshttps://doi.org/10.1371/journal.pgen.1005233openalex-snapshot
The 4E-BP Caf20p Mediates Both eIF4E-Dependent and Independent Repression of Translation
inferred← citeshttps://doi.org/10.1371/journal.pone.0040464openalex-snapshot
Small Ribosomal Protein RPS0 Stimulates Translation Initiation by Mediating 40S-Binding of eIF3 via Its Direct Contact with the eIF3a/TIF32 Subunit
inferred← citeshttps://doi.org/10.1371/journal.pone.0095396openalex-snapshot
Translational Control of Arabidopsis Meristem Stability and Organogenesis by the Eukaryotic Translation Factor eIF3h
inferred← citeshttps://doi.org/10.1371/journal.pone.0114390openalex-snapshot
SILAC-Based Quantitative Proteomic Analysis of Human Lung Cell Response to Copper Oxide Nanoparticles
inferred← citeshttps://doi.org/10.1534/genetics.115.186221openalex-snapshot
Mechanism and Regulation of Protein Synthesis in Saccharomyces cerevisiae
inferred← citeshttps://doi.org/10.21203/rs.3.rs-1655304/v2openalex-snapshot
The oncogene EIF3c promotes esophageal squamous cell carcinoma tumorigenesis by inhibiting cell proliferation and inducing cell apoptosis
inferred← citeshttps://doi.org/10.2147/ott.s193480openalex-snapshot
Androgen upregulates the palmitoylation of eIF3L in human prostate LNCaP cells
inferred← citeshttps://doi.org/10.3389/fmicb.2022.898884openalex-snapshot
Non-homologous End Joining-Mediated Insertional Mutagenesis Reveals a Novel Target for Enhancing Fatty Alcohols Production in Yarrowia lipolytica
inferred← citeshttps://doi.org/10.3389/fmolb.2021.787664openalex-snapshot
eIF3 and Its mRNA-Entry-Channel Arm Contribute to the Recruitment of mRNAs With Long 5′-Untranslated Regions
inferred← citeshttps://doi.org/10.3389/fpls.2017.00810openalex-snapshot
Salinity-Induced Palmella Formation Mechanism in Halotolerant Algae Dunaliella salina Revealed by Quantitative Proteomics and Phosphoproteomics
inferred← citeshttps://doi.org/10.3389/fpls.2021.748120openalex-snapshot
eIF3k Domain-Containing Protein Regulates Conidiogenesis, Appressorium Turgor, Virulence, Stress Tolerance, and Physiological and Pathogenic Development of Magnaporthe oryzae Oryzae
inferred← citeshttps://doi.org/10.3390/ijms20164043openalex-snapshot
Control of Translation at the Initiation Phase During Glucose Starvation in Yeast
inferred← citeshttps://doi.org/10.3390/ijms27010462openalex-snapshot
RNA-Binding Proteins in Dinoflagellates
inferred← citeshttps://doi.org/10.3390/microorganisms6020030openalex-snapshot
Translation and Translational Control in Dinoflagellates
inferred← citeshttps://doi.org/10.3390/v10020070openalex-snapshot
The Regulation of Translation in Alphavirus-Infected Cells
inferred← citeshttps://doi.org/10.3390/v7072778openalex-snapshot
Plant Translation Factors and Virus Resistance
inferred← citeshttps://doi.org/10.3410/f.732604689.793545498openalex-snapshot
Faculty Opinions recommendation of Structure of a human cap-dependent 48S translation pre-initiation complex.
inferred← citeshttps://doi.org/10.53846/goediss-7434openalex-snapshot
Structural Characterization of the Eukaryotic Translation Initiation by Electron Cryo-Microscopy
inferred← citeshttps://doi.org/10.53846/goediss-8411openalex-snapshot
Kinetic Analysis of Mammalian Translation Initiation
inferred← citeshttps://doi.org/10.70675/07d08744z485bz418dzad0az2a77205306d8openalex-snapshot
Effet des microARNs sur la traduction cellulaire et virale
inferred← citeshttps://doi.org/10.70675/19918f3azade0z4d4fz8194z3eef58ec9e94openalex-snapshot
Druggability of kinetoplastid-specific mRNA translation-related proteins : Structural investigation by cryo-Electron Microscopy
inferred← citeshttps://doi.org/10.70675/864962c8zeda0z44c2z8f93zea827ffd8cd9openalex-snapshot
Élargissement du spectre de résistance aux potyvirus : utilisation de la plante modèle Arabidopsis thaliana
inferred← citeshttps://doi.org/10.70675/99113a96zb45cz47efzb5f2z52eb15be3fe5openalex-snapshot
Étude de l'effet des microARN sur l'initiation de la traduction dirigée par l'IRES du Virus de l'Hépatite C
inferred← citeshttps://doi.org/10.70675/b34f5d54z11cfz46c1zae6ezf5128736d001openalex-snapshot
Rôle du facteur d'initiation eIF3 dans la traduction de l'ARNm de l'histone H4
inferred← citeshttps://doi.org/10.70675/c49589fazfc73z47d7z9ab8zca0524c65317openalex-snapshot
Le piratage de l'appareil de traduction de la cellule hôte par le virus de la paralysie du criquet (CrPV)
inferred← citeshttps://doi.org/10.70675/c6c84d2ez1844z4ce2z8e9cz814164ecbf34openalex-snapshot
Spécificités et différences structurales des complexes de l’initiation de la traduction de l’ARNm entre les trypanosomes et leurs hôtes
inferred← citeshttps://doi.org/10.7554/elife.102977openalex-snapshot
eIF3 engages with 3’-UTR termini of highly translated mRNAs
inferred← citeshttps://doi.org/10.7554/elife.102977.1openalex-snapshot
eIF3 engages with 3’-UTR termini of highly translated mRNAs
inferred← citeshttps://doi.org/10.7554/elife.102977.2openalex-snapshot
eIF3 engages with 3’-UTR termini of highly translated mRNAs
inferred← citeshttps://doi.org/10.7554/elife.102977.3openalex-snapshot
eIF3 engages with 3’-UTR termini of highly translated mRNAs
inferred← citeshttps://doi.org/10.7554/elife.20934openalex-snapshot
Eukaryotic translation initiation factor 3 plays distinct roles at the mRNA entry and exit channels of the ribosomal preinitiation complex
inferred← citeshttps://doi.org/10.7554/elife.31476openalex-snapshot
Yeast eIF4A enhances recruitment of mRNAs regardless of their structural complexity
inferred← citeshttps://doi.org/10.7554/elife.95846openalex-snapshot
Perturbations in eIF3 subunit stoichiometry alter expression of ribosomal proteins and key components of the MAPK signaling pathways
inferred← citeshttps://doi.org/10.7554/elife.95846.1openalex-snapshot
Perturbations in eIF3 subunit stoichiometry alter expression of ribosomal proteins and key components of the MAPK signaling pathway
inferred← citeshttps://doi.org/10.7554/elife.95846.2openalex-snapshot
Perturbations in eIF3 subunit stoichiometry alter expression of ribosomal proteins and key components of the MAPK signaling pathways
inferred← citeshttps://doi.org/10.7554/elife.95846.3openalex-snapshot
Perturbations in eIF3 subunit stoichiometry alter expression of ribosomal proteins and key components of the MAPK signaling pathways
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