Affinage

EEFSEC

Selenocysteine-specific elongation factor · UniProt P57772

Round 2 corrected
Length
596 aa
Mass
65.3 kDa
Annotated
2026-04-28
77 papers in source corpus 26 papers cited in narrative 26 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

EEFSEC (eEFSec) is a selenocysteine-specific translational elongation factor and GTPase that delivers Sec-tRNA(Sec) to the ribosomal A site during UGA codon recoding, enabling co-translational selenocysteine incorporation into selenoproteins (PMID:2140572, PMID:10970870). The protein adopts a chalice-like architecture with three N-terminal EF-Tu-homologous domains that bind GTP and Sec-tRNA(Sec) with extraordinary affinity (Kd ~0.2 pM in the GTP-bound state), and a C-terminal domain 4 that engages SBP2 upon SECIS-induced conformational change; codon recognition triggers GTPase activation via docking on the sarcin–ricin loop, accelerating tRNA release by more than 10⁶-fold (PMID:19940162, PMID:27842381, PMID:29555379). In eukaryotes, eEFSec does not directly bind the SECIS element but is recruited through SBP2, with ribosomal protein eS31 bridging Sec-tRNA(Sec) and SBP2 to stabilize the decoding complex (PMID:18948268, PMID:35709277). Bi-allelic loss-of-function variants in EEFSEC cause autosomal recessive progressive neurodegeneration due to global selenoprotein deficiency (PMID:39753114).

Mechanistic history

Synthesis pass · year-by-year structured walk · 13 steps
  1. 1990 High

    The discovery that prokaryotic SelB is a ribosome-associated elongation factor that specifically binds selenocysteyl-tRNA(Sec) established the first dedicated translational machinery for selenocysteine insertion at UGA codons.

    Evidence Protein purification, limited proteolysis, immunological analysis, and ribosome fractionation from E. coli

    PMID:2140572

    Open questions at the time
    • Eukaryotic ortholog not yet identified
    • GTPase mechanism not characterized
    • No structural information
  2. 1991 High

    Identification of the tRNA structural determinants—the 8-bp acceptor helix and the selenocysteinyl moiety—that confer exclusive SelB binding explained how Sec-tRNA(Sec) is discriminated from all other aminoacyl-tRNAs and excluded from EF-Tu.

    Evidence In vitro binding assays with defined tRNA mutants and kinetic analysis of aminoacylation

    PMID:1839607 PMID:1939093

    Open questions at the time
    • Thermodynamic coupling between aminoacyl identity and nucleotide state not quantified
    • Structural basis of tRNA recognition unknown
  3. 1993 High

    Demonstration that SelB directly binds the mRNA SECIS hairpin and forms a ternary complex with Sec-tRNA(Sec) and mRNA revealed how selenocysteine insertion is spatially coupled to the UGA codon in bacteria.

    Evidence Gel shift assays, nuclease and iodine footprinting, and toeprint assays on fdhF and fdnG mRNAs

    PMID:8314089 PMID:8483932

    Open questions at the time
    • Unknown whether eukaryotic SelB orthologs also bind SECIS directly
    • Ribosomal context of the complex not visualized
  4. 1996 High

    Domain dissection and GTPase assays established that SelB's N-terminal EF-Tu-like domains bind GTP and tRNA while a distinct C-terminal domain binds SECIS mRNA, and that SECIS binding stimulates ribosome-dependent GTP hydrolysis, providing a conformational switch linking mRNA recognition to catalytic activation.

    Evidence Truncation analysis with functional binding assays, in vitro GTPase activity measurements with ribosome stimulation, and in vivo UGA readthrough quantification

    PMID:8893853 PMID:8898393 PMID:9454578

    Open questions at the time
    • Atomic structure of the full-length protein not available
    • Mechanism of ribosome-stimulated GTPase activation unresolved
  5. 2000 High

    Quantitative kinetics revealed that SelB binds GTP preferentially over GDP with fast GDP release (obviating an exchange factor), and characterization of the mammalian ortholog mSelB/eEFSec showed it retains GTP and Sec-tRNA(Sec) binding but cannot bind the SECIS alone, establishing that eukaryotic selenocysteine incorporation requires additional trans-acting factors.

    Evidence Stopped-flow fluorescence kinetics with fluorescent nucleotide analogs for prokaryotic SelB; GTP binding, tRNA binding, in vivo translation, and HeLa extract complementation for mouse eEFSec; archaeal SelB biochemical characterization

    PMID:10781605 PMID:10860743 PMID:10970870

    Open questions at the time
    • Identity of the eukaryotic factor(s) bridging eEFSec to the SECIS unknown
    • Eukaryotic eEFSec structure not determined
  6. 2002 High

    Crystal and NMR structures of the SelB C-terminal domain and its cognate SECIS RNA revealed a novel winged-helix RNA-binding mode and defined the critical RNA features (GpU tetraloop, bulge uracil) required for recognition, providing the first atomic view of how the mRNA-binding domain works.

    Evidence X-ray crystallography at 2.12 Å (M. thermoacetica WH domains) and NMR spectroscopy of the SECIS hairpin with mutational analysis

    PMID:12145214 PMID:12421564

    Open questions at the time
    • No co-crystal of WH domain with SECIS RNA yet
    • Communication between mRNA-binding and tRNA-binding halves of SelB not structurally resolved
  7. 2005 High

    Co-crystal structures of the SelB WH domains bound to SECIS RNA demonstrated that RNA binding does not induce major protein conformational change but disrupts a salt bridge between WH2 and WH3, providing a molecular switch that communicates mRNA binding to the tRNA-binding N-terminal domains.

    Evidence X-ray crystallography of E. coli WH3/4 and M. thermoacetica WH1-4 bound to SECIS at 2.3–2.6 Å with site-directed mutagenesis

    PMID:15665870 PMID:17537456

    Open questions at the time
    • Full-length SelB structure not available
    • Mechanism of signal relay to GTPase domain unresolved
  8. 2008 High

    In the eukaryotic system, SBP2 was shown to undergo a SECIS-induced conformational change that recruits eEFSec, establishing SBP2 as the obligate adaptor between the SECIS element and eEFSec and explaining why eEFSec itself cannot bind SECIS.

    Evidence Alanine scanning mutagenesis of SBP2, in vitro Sec incorporation assay, and trans-complementation of SBP2 domains

    PMID:18948268

    Open questions at the time
    • Structural basis of the SBP2–eEFSec interface unknown
    • Whether additional factors stabilize the complex in vivo unresolved
  9. 2009 High

    Quantitative thermodynamic analysis revealed that SelB·GTP binds Sec-tRNA(Sec) with picomolar affinity (Kd ~0.2 pM) and that GTP hydrolysis accelerates tRNA release by >10⁶-fold, establishing the energetic basis for high-fidelity selenocysteine delivery and discriminating Sec- from Ser-tRNA(Sec) through thermodynamic coupling.

    Evidence Stopped-flow fluorescence kinetics and isothermal titration calorimetry with purified components

    PMID:19940162

    Open questions at the time
    • Whether eukaryotic eEFSec achieves similar affinities not measured
    • On-ribosome kinetics of tRNA release not directly captured
  10. 2015 High

    The first full-length SelB crystal structure revealed the chalice-like seven-domain architecture (D1–D3 plus WHD1–4) and showed that the Sec-binding site at the D1–D2 interface is smaller and more exposed than EF-Tu's aminoacyl pocket, explaining selective accommodation of the unique tRNA(Sec) secondary structure.

    Evidence X-ray crystallography of A. aeolicus SelB with GTP analog at 3.2 Å and structural modeling of tRNA docking

    PMID:26304550

    Open questions at the time
    • No structure of the full-length SelB–tRNA complex
    • Eukaryotic eEFSec full-length structure still missing
  11. 2016 High

    Cryo-EM visualization of six intermediates on the bacterial UGA recoding pathway resolved the complete GTPase activation mechanism: codon recognition causes 30S closure that repositions Sec-tRNA(Sec) away from the sarcin–ricin loop and docks SelB onto it, triggering GTP hydrolysis.

    Evidence Single-particle cryo-EM of six structural intermediates of the E. coli ribosome–SelB complex with molecular dynamics

    PMID:27842381

    Open questions at the time
    • Eukaryotic ribosome recoding mechanism not yet visualized
    • Post-GTP-hydrolysis accommodation steps not captured
  12. 2022 High

    Cryo-EM of the mammalian ribosome decoding a Sec UGA codon revealed a fundamentally distinct eukaryotic mechanism: eEFSec and SBP2 do not contact each other directly but engage opposite ends of the SECIS, while ribosomal protein eS31 bridges Sec-tRNA(Sec) and SBP2; eEFSec was found to be indiscriminate toward L-serine, revealing a fidelity challenge in eukaryotic selenocysteine incorporation.

    Evidence Cryo-EM structural determination of the mammalian ribosome·eEFSec·SBP2·SECIS complex

    PMID:35709277

    Open questions at the time
    • Mechanism preventing serine misincorporation in vivo not identified
    • Dynamics of SECIS delivery and factor recycling on the ribosome unknown
  13. 2025 High

    Identification of bi-allelic EEFSEC loss-of-function variants in patients with progressive neurodegeneration established EEFSEC as essential for selenoprotein homeostasis in humans and defined a new Mendelian disease of selenoprotein deficiency.

    Evidence Exome/genome sequencing, in vitro functional assay of variants, selenoprotein Western blot in patient fibroblasts, and Drosophila eEFSec-RNAi motor/synaptic phenotyping

    PMID:39753114

    Open questions at the time
    • Tissue-specific consequences of partial EEFSEC loss not characterized
    • Genotype–phenotype correlations across variants not established
    • Whether neurodegeneration is driven by loss of specific selenoproteins versus global deficiency unknown

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key open questions include: (1) how eukaryotic cells prevent eEFSec-mediated serine misincorporation at Sec UGA codons in vivo; (2) the structural basis of the SBP2–SECIS conformational change that recruits eEFSec domain 4; and (3) whether eEFSec has non-translational functions relevant to cancer cell proliferation.
  • No mechanism identified for fidelity proofreading of Sec versus Ser in eukaryotes
  • No high-resolution structure of the SBP2 conformational switch
  • Cancer cell phenotypes upon EEFSEC knockdown are correlative and from a single study

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 5 GO:0003924 GTPase activity 5 GO:0045182 translation regulator activity 4
Localization
GO:0005840 ribosome 4 GO:0005829 cytosol 2
Pathway
R-HSA-392499 Metabolism of proteins 5
Partners
ES31SBP2SEC-TRNA(SEC)SECIS RNA
Complex memberships
Ribosome·eEFSec·SBP2·SECIS decoding complexeEFSec·Sec-tRNA(Sec)·GTP ternary complex

Evidence

Reading pass · 26 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1990 SELB (prokaryotic ortholog of EEFSEC) was purified from E. coli and shown to be an elongation factor-like protein that specifically binds selenocysteyl-tRNA(Sec). It is partially associated with ribosomes and is required for co-translational selenocysteine insertion at UGA codons. Protein purification, limited proteolysis, immunological analysis, ribosome fractionation The Journal of biological chemistry High 2140572
1991 The 8-base-pair aminoacyl-acceptor helix of tRNA(Sec) is the primary determinant for binding to SELB (prokaryotic EEFSEC ortholog); reduction to 7 base pairs prevents SELB binding but allows EF-Tu binding. This structural feature exclusively directs selenocysteyl-tRNA(Sec) to SELB and precludes interaction with EF-Tu. In vitro binding assays with purified mutant tRNA variants, kinetic analysis of seryl-tRNA synthetase and selenocysteine synthase The Journal of biological chemistry High 1939093
1991 SELB (EEFSEC ortholog) specifically complexes selenocysteyl-tRNA(Sec); interaction with the selenol group of the aminoacylated selenocysteine residue is required for stable SELB·tRNA complex formation, providing the biochemical basis for exclusive selection of selenocysteyl-tRNA(Sec). Biochemical characterization, in vitro binding assays Biochimie High 1839607
1993 SELB (EEFSEC ortholog) directly and specifically binds the mRNA SECIS hairpin loop region via gel-shift and footprinting assays. In the presence of selenocysteinyl-tRNA, SELB forms a ternary complex with charged tRNA and mRNA, positioning the tRNA at the UGA codon. Gel shift assays, nuclease and iodine footprinting Proceedings of the National Academy of Sciences of the United States of America High 8483932
1994 The SELB-GTP-Sec-tRNA(Sec) ternary complex binds selenoprotein mRNAs (fdhF and fdnG) and toeprint experiments show SELB recognizes ribosome-bound message, with the complex extending toward the large ribosomal subunit, increasing local concentration of Sec-tRNA(Sec) at the UGA codon. Boundary experiments, toeprint assays Genes & development High 8314089
1996 SELB (EEFSEC ortholog) domain structure was elucidated: the N-terminal three domains are homologous to EF-Tu (binding GTP and selenocysteyl-tRNA(Sec)), while a distinct C-terminal ~17 kDa domain specifically binds the mRNA SECIS hairpin. Truncated SelB lacking the C-terminal domain retains tRNA binding but loses mRNA binding. Cloning of selB from multiple bacteria, sequence alignment, expression and biochemical analysis of truncated SelB fragments Journal of molecular biology High 8893853
1996 SELB GTPase activity is stimulated ~3-4 fold by the SECIS mRNA hairpin in a ribosome-dependent manner. mRNA binding to SELB induces a conformational switch promoting increased ribosome-mediated GTP hydrolysis; the minimal stimulatory region maps to the upper half of the hairpin. GTPase activity assays, ribosome stimulation, truncated mRNA hairpin titration Biochemistry High 9454578
1996 Overproduction of SelB (EEFSEC ortholog) in vivo reduces UGA readthrough to <1%, reversed by co-overexpression of tRNA(Sec), demonstrating that balanced stoichiometry between SelB, selenocysteyl-tRNA(Sec), and mRNA is essential for selenocysteine insertion. The mRNA-binding and tRNA-binding domains are physically separable. Genetic overexpression, in vivo UGA readthrough assay (lacZ fusion), truncation analysis Molecular microbiology High 8898393
1998 Evolutionary analysis established that SELB/eEFSec belongs to a GTPase superfamily ancestral to both bacterial SELB and eukaryotic/archaeal eIF2γ, indicating these translation factors share a common evolutionary origin and that change of function occurred within this GTPase subfamily. Phylogenetic analysis, sequence comparison across diplomonads, parabasalia, microsporidia, and archaebacteria Journal of molecular evolution Medium 9847405
2000 The kinetics of SELB (EEFSEC ortholog) interaction with GTP (Kd = 0.74 µM) and GDP (Kd = 13.4 µM) were determined; rapid GDP release (15 s⁻¹) obviates the need for a nucleotide exchange factor. SECIS RNA binds with ~1 nM affinity, further increased by selenocysteyl-tRNA(Sec) binding, suggesting SELB forms a tight quaternary complex on the SECIS that loosens after GTP hydrolysis. Stopped-flow fluorescence kinetics using intrinsic tryptophan fluorescence and methylanthraniloyl nucleotide derivatives The Journal of biological chemistry High 10781605
2000 mSelB (mouse EEFSEC, the mammalian ortholog of bacterial SelB) was characterized: it binds GTP, recognizes Sec-tRNA(Sec) in vitro and in vivo, and is required for efficient selenoprotein translation in vivo. Unlike bacterial SelB, mSelB alone cannot bind the eukaryotic SECIS RNA; complementation with cell extracts yields a SECIS-dependent complex containing mSelB and at least one additional factor. Database cloning, GTP binding assay, in vitro Sec-tRNA(Sec) binding, in vivo selenoprotein translation assay, HeLa cell extract complementation The EMBO journal High 10970870
2000 Archaeal SelB (from Methanococcus jannaschii, aSelB) binds guanine nucleotides and preferentially binds selenocysteyl-tRNA(Sec) like bacterial SelB, but does not bind the SECIS element, lacking the bacterial C-terminal mRNA-binding domain. This suggests that in archaea and eukaryotes, functions of bacterial SelB are distributed over at least two proteins. Genome database search, protein purification, guanine nucleotide binding assay, tRNA binding assay Journal of molecular biology High 10860743
2002 Crystal structure of the C-terminal mRNA-binding fragment of SelB from Moorella thermoacetica (SelB-C) determined at 2.12 Å resolution, revealing four tandem winged-helix (WH) domains arranged in an L-shape. This was the first structure showing winged-helix domains involved in RNA binding; conserved basic residues define the mRNA-binding site. X-ray crystallography (multiwavelength anomalous dispersion), structural analysis The EMBO journal High 12145214
2002 NMR structure of the prokaryotic SECIS mRNA hairpin revealed conserved structural features critical for SelB (EEFSEC ortholog) binding. A GpU sequence at the tip of the capping tetraloop and a bulge uracil five base-pairs away are essential for SelB interaction; SelB binding stabilizes RNA secondary structure. NMR spectroscopy, mutational analysis of SECIS binding Journal of molecular biology High 12421564
2004 In mammalian systems, eEFSec (EEFSEC), Sec-tRNA(Sec), and SBP2 are all required for selenocysteine incorporation. SBP2 is the only limiting factor in rabbit reticulocyte lysate; selenocysteine incorporation efficiency into a luciferase reporter is 5-8% in vitro and ~1% in transfected cells, demonstrating the reconstituted system and quantifying factor contributions. In vitro translation assay, transfected cell Sec incorporation efficiency measurement, factor depletion and reconstitution The Journal of biological chemistry High 15229221
2005 Crystal structure of the mRNA-binding domain of SelB (EEFSEC ortholog) in complex with SECIS RNA at 2.3 Å resolution revealed the first example of a winged-helix (WH) domain binding RNA. RNA binding does not induce major conformational change in the WH motif; the structure suggests the complex wraps around the small ribosomal subunit. X-ray crystallography Nature structural & molecular biology High 15665870
2007 Crystal structures of E. coli SelB WH3/4 domains and M. thermoacetica WH1-4 domains each bound to SECIS mRNA revealed that both WH modules use the same structural elements to bind RNA. A salt bridge connecting WH2 to WH3 is disrupted upon mRNA binding, providing a molecular switch allowing communication between tRNA- and mRNA-binding sites, with RNA acting as an activator. X-ray crystallography (2.3 Å for E. coli WH3/4; 2.6 Å for M. thermoacetica WH1-4), site-directed mutagenesis Journal of molecular biology High 17537456
2008 SBP2's Sec incorporation domain (SID) promotes high-affinity SECIS binding and eEFSec (EEFSEC) recruitment to the SBP2 RNA-binding domain. SECIS binding induces a conformational change in SBP2 that recruits eEFSec; the SID and RNA-binding domain can function in trans, establishing eEFSec as a downstream effector of SBP2·SECIS complex formation. Alanine scanning mutagenesis, in vitro Sec incorporation assay, binding domain separation experiments The Journal of biological chemistry High 18948268
2009 Sec-tRNA(Sec) binds SelB (EEFSEC ortholog)·GTP with extraordinary affinity (Kd = 0.2 pM); GTP hydrolysis accelerates tRNA release by >10⁶-fold (from 0.3 h⁻¹ to 240 s⁻¹). Thermodynamic coupling between Sec-tRNA(Sec) and GTP binding ensures specificity of Sec vs. Ser-tRNA(Sec) selection. This mechanism is reminiscent of eIF2 rather than EF-Tu. Stopped-flow fluorescence kinetics, thermodynamic binding measurements, isothermal titration calorimetry The Journal of biological chemistry High 19940162
2015 Crystal structure of the full-length SelB from Aquifex aeolicus in complex with a GTP analog at 3.2 Å resolution revealed: three EF-Tu-like domains (D1-3) followed by four winged-helix domains (WHD1-4) connected by a spacer region. The Sec-binding site is at the D1-D2 interface (smaller and more exposed than EF-Tu's aminoacyl site). Structural modeling suggests tRNA(Sec)'s unique secondary structure allows SelB to specifically recognize it and place it at the ribosomal A-site. X-ray crystallography at 3.2 Å, structural modeling Nucleic acids research High 26304550
2016 Cryo-EM structures of six intermediates on the UGA recoding pathway revealed the mechanism of SelB (EEFSEC ortholog) GTPase activation: initial SelB·Sec-tRNA(Sec) binding causes the 30S subunit to adopt an open conformation with Sec-tRNA(Sec) covering the sarcin-ricin loop (SRL). Codon recognition triggers local decoding-site closure, moving Sec-tRNA(Sec) away from the SRL and causing global 30S shoulder domain closure, which docks SelB on the SRL to activate GTPase. Single-particle cryo-electron microscopy (six structural intermediates), molecular dynamics Nature High 27842381
2018 Mammalian eEFSec (EEFSEC) folds into a chalice-like structure with three N-terminal EF-Tu-like domains and a C-terminal domain 4 that binds Sec-tRNA(Sec) and SBP2. GTP hydrolysis does not induce a canonical conformational change but instead promotes a slight ratchet of domains 1 and 2 and a lever-like movement of domain 4, which may be critical for Sec-tRNA(Sec) release on the ribosome. A non-canonical mechanism for Sec UGA recoding elongation is proposed. Structural analysis, crystal structure review, domain function mapping, GTP hydrolysis assays Biochimica et biophysica acta. General subjects Medium 29555379
2022 Cryo-EM structure of the mammalian ribosome decoding the Sec UGA codon revealed: (1) eEFSec (EEFSEC) and SBP2 do not interact directly but deploy their C-terminal domains to engage opposite ends of the SECIS; (2) ribosomal protein eS31 simultaneously contacts Sec-tRNA(Sec) and SBP2 via its Lys-rich and C-terminal segments to stabilize the assembly; (3) eEFSec is indiscriminate toward L-serine and can misincorporate it at Sec UGA codons. This reveals a fundamentally distinct mechanism of Sec UGA recoding in eukaryotes versus bacteria. Cryo-electron microscopy structural determination of mammalian ribosome·eEFSec·SBP2·SECIS complex Science High 35709277
2025 Bi-allelic loss-of-function variants in EEFSEC cause autosomal recessive selenoprotein deficiency in humans, leading to progressive neurodegeneration (EEFSEC deficiency). Pathogenic EEFSEC variants showed reduced EEFSEC function in vitro and lower selenoprotein levels in patient fibroblasts. A Drosophila eEFSec-RNAi model displayed progressive motor impairment and synaptic defects, confirming the in vivo requirement of EEFSEC for normal neuronal function. Exome/genome sequencing, in vitro functional assay of variants, Western blot of selenoproteins in fibroblasts, Drosophila RNAi motor function assay, synaptic morphology analysis American journal of human genetics High 39753114
2025 In yellow catfish, the eefsec gene promoter contains a functional FOXO1 binding site (-1070 to -1080 bp) and a STAT3 binding site (-428 to -436 bp). These transcription factors directly regulate eefsec transcriptional activity in a selenium (selenomethionine)-dependent manner, as confirmed by EMSA and chromatin immunoprecipitation. Promoter deletion analysis, EMSA, chromatin immunoprecipitation Biochimica et biophysica acta. Gene regulatory mechanisms Medium 40618995
2021 EEFSEC knockdown in human prostate cancer 22Rv1 cells suppressed proliferation, migration, and invasion, caused G0/G1 cell cycle arrest, downregulated C-myc and CCNB1, and upregulated p15, suggesting EEFSEC expression modulates cell cycle progression through C-myc-related pathways. Lentiviral shRNA knockdown, XTT proliferation assay, Transwell migration/invasion assay, flow cytometry cell cycle analysis, qRT-PCR, Western blot Nan fang yi ke da xue xue bao Medium 35012909

Source papers

Stage 0 corpus · 77 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2012 Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 1718 22658674
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
2015 A human interactome in three quantitative dimensions organized by stoichiometries and abundances. Cell 1015 26496610
2021 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. Cell 705 33961781
2012 A census of human soluble protein complexes. Cell 689 22939629
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
2014 Parent-of-origin-specific allelic associations among 106 genomic loci for age at menarche. Nature 445 25231870
2015 Panorama of ancient metazoan macromolecular complexes. Nature 407 26344197
2010 Thirty new loci for age at menarche identified by a meta-analysis of genome-wide association studies. Nature genetics 392 21102462
2017 Genetic Associations with Gestational Duration and Spontaneous Preterm Birth. The New England journal of medicine 294 28877031
2009 Genome-wide association and replication studies identify four variants associated with prostate cancer susceptibility. Nature genetics 284 19767754
2000 Characterization of mSelB, a novel mammalian elongation factor for selenoprotein translation. The EMBO journal 226 10970870
1999 High-level expression in Escherichia coli of selenocysteine-containing rat thioredoxin reductase utilizing gene fusions with engineered bacterial-type SECIS elements and co-expression with the selA, selB and selC genes. Journal of molecular biology 193 10512699
2014 Global mapping of herpesvirus-host protein complexes reveals a transcription strategy for late genes. Molecular cell 173 25544563
2020 UFMylation maintains tumour suppressor p53 stability by antagonizing its ubiquitination. Nature cell biology 168 32807901
2010 Personalized smoking cessation: interactions between nicotine dose, dependence and quit-success genotype score. Molecular medicine (Cambridge, Mass.) 108 20379614
2021 FBW7 suppresses ovarian cancer development by targeting the N6-methyladenosine binding protein YTHDF2. Molecular cancer 106 33658012
2022 EZH2 depletion potentiates MYC degradation inhibiting neuroblastoma and small cell carcinoma tumor formation. Nature communications 99 35013218
1996 Domain structure of the prokaryotic selenocysteine-specific elongation factor SelB. Journal of molecular biology 96 8893853
2014 Genome-wide association analyses identify variants in developmental genes associated with hypospadias. Nature genetics 93 25108383
2016 The pathway to GTPase activation of elongation factor SelB on the ribosome. Nature 92 27842381
1993 Interaction of translation factor SELB with the formate dehydrogenase H selenopolypeptide mRNA. Proceedings of the National Academy of Sciences of the United States of America 92 8483932
1991 The length of the aminoacyl-acceptor stem of the selenocysteine-specific tRNA(Sec) of Escherichia coli is the determinant for binding to elongation factors SELB or Tu. The Journal of biological chemistry 89 1939093
2000 Identification and characterisation of the selenocysteine-specific translation factor SelB from the archaeon Methanococcus jannaschii. Journal of molecular biology 78 10860743
2004 Efficiency of mammalian selenocysteine incorporation. The Journal of biological chemistry 77 15229221
2022 SARS-CoV-2 N Protein Antagonizes Stress Granule Assembly and IFN Production by Interacting with G3BPs to Facilitate Viral Replication. Journal of virology 75 35652658
2021 Histone deacetylase inhibitors inhibit cervical cancer growth through Parkin acetylation-mediated mitophagy. Acta pharmaceutica Sinica. B 66 35256949
1996 Solution structure of mRNA hairpins promoting selenocysteine incorporation in Escherichia coli and their base-specific interaction with special elongation factor SELB. RNA (New York, N.Y.) 66 8634916
2022 Scalable multiplex co-fractionation/mass spectrometry platform for accelerated protein interactome discovery. Nature communications 65 35831314
2018 RNA-binding proteins with basic-acidic dipeptide (BAD) domains self-assemble and aggregate in Alzheimer's disease. The Journal of biological chemistry 65 29802200
2017 A Role for Mitochondrial Translation in Promotion of Viability in K-Ras Mutant Cells. Cell reports 64 28700943
2005 Structural basis for mRNA recognition by elongation factor SelB. Nature structural & molecular biology 64 15665870
1990 Purification and biochemical characterization of SELB, a translation factor involved in selenoprotein synthesis. The Journal of biological chemistry 58 2140572
2022 Structure of the mammalian ribosome as it decodes the selenocysteine UGA codon. Science (New York, N.Y.) 56 35709277
1997 In vitro and in vivo characterization of novel mRNA motifs that bind special elongation factor SelB. Proceedings of the National Academy of Sciences of the United States of America 56 9192624
2010 The protein network surrounding the human telomere repeat binding factors TRF1, TRF2, and POT1. PloS one 51 20811636
2008 A novel protein domain induces high affinity selenocysteine insertion sequence binding and elongation factor recruitment. The Journal of biological chemistry 48 18948268
2022 NUDT21 limits CD19 levels through alternative mRNA polyadenylation in B cell acute lymphoblastic leukemia. Nature immunology 46 36138187
1994 Recognition of the mRNA selenocysteine insertion sequence by the specialized translational elongation factor SELB. Genes & development 45 8314089
2019 LncRNAs-directed PTEN enzymatic switch governs epithelial-mesenchymal transition. Cell research 44 30631154
2000 Kinetics of the interaction of translation factor SelB from Escherichia coli with guanosine nucleotides and selenocysteine insertion sequence RNA. The Journal of biological chemistry 44 10781605
2018 ATG5 is required for B cell polarization and presentation of particulate antigens. Autophagy 42 30196744
1996 Role of stoichiometry between mRNA, translation factor SelB and selenocysteyl-tRNA in selenoprotein synthesis. Molecular microbiology 42 8898393
2002 Crystal structure of an mRNA-binding fragment of Moorella thermoacetica elongation factor SelB. The EMBO journal 40 12145214
2002 Structure of prokaryotic SECIS mRNA hairpin and its interaction with elongation factor SelB. Journal of molecular biology 39 12421564
2003 Inactivation of the selB gene in Methanococcus maripaludis: effect on synthesis of selenoproteins and their sulfur-containing homologs. Journal of bacteriology 38 12486046
2009 Thermodynamic and kinetic framework of selenocysteyl-tRNASec recognition by elongation factor SelB. The Journal of biological chemistry 36 19940162
1998 Selenocysteine inserting RNA elements modulate GTP hydrolysis of elongation factor SelB. Biochemistry 35 9454578
1998 Evolutionary relationship between translation initiation factor eIF-2gamma and selenocysteine-specific elongation factor SELB: change of function in translation factors. Journal of molecular evolution 35 9847405
1991 The function of selenocysteine synthase and SELB in the synthesis and incorporation of selenocysteine. Biochimie 31 1839607
1999 In vitro selection of RNA aptamers that bind special elongation factor SelB, a protein with multiple RNA-binding sites, reveals one major interaction domain at the carboxyl terminus. RNA (New York, N.Y.) 24 10496219
2000 The bulged nucleotide in the Escherichia coli minimal selenocysteine insertion sequence participates in interaction with SelB: a genetic approach. Journal of bacteriology 22 11053373
2007 Structural insight into a molecular switch in tandem winged-helix motifs from elongation factor SelB. Journal of molecular biology 20 17537456
2018 On elongation factor eEFSec, its role and mechanism during selenium incorporation into nascent selenoproteins. Biochimica et biophysica acta. General subjects 18 29555379
2007 Structural basis for dynamic interdomain movement and RNA recognition of the selenocysteine-specific elongation factor SelB. Structure (London, England : 1993) 17 17502103
2001 Functional analysis of prokaryotic SELB proteins. BioFactors (Oxford, England) 17 11568440
1999 Genetic probing of the interaction between the translation factor SelB and its mRNA binding element in Escherichia coli. Molecular & general genetics : MGG 17 10628863
2015 Crystal structure of the full-length bacterial selenocysteine-specific elongation factor SelB. Nucleic acids research 15 26304550
2011 An ancient family of SelB elongation factor-like proteins with a broad but disjunct distribution across archaea. BMC evolutionary biology 10 21255425
2001 Distinctive features in the SelB family of elongation factors for selenoprotein synthesis. A glimpse of an evolutionary complexified translation apparatus. BioFactors (Oxford, England) 10 11568434
2003 Purification and characterization of hexahistidine-tagged elongation factor SelB. Protein expression and purification 6 14550646
2025 EEFSEC deficiency: A selenopathy with early-onset neurodegeneration. American journal of human genetics 4 39753114
2007 The three-dimensional structure of the Moorella thermoacetica selenocysteine insertion sequence RNA hairpin and its interaction with the elongation factor SelB. RNA (New York, N.Y.) 4 17901155
1997 Domain structure of the selenocysteine-specific translation factor SelB in prokaryotes. Biomedical and environmental sciences : BES 4 9315303
2021 [EEFSEC knockdown inhibits proliferation, migration and invasion of prostate cancer cells in vitro]. Nan fang yi ke da xue xue bao = Journal of Southern Medical University 3 35012909
2011 The involvement of SelB in the expression of cytotoxic necrotizing factor 1 in Escherichia coli. FEBS letters 3 21570972
2007 Molecular switch in tandem winged-helix motifs of elongation factor SelB. Nucleic acids symposium series (2004) 3 18029744
2024 Selagibenzophenone B and Its Derivatives: SelB-1, a Dual Topoisomerase I/II Inhibitor Identified through In Vitro and In Silico Analyses. ACS bio & med chem Au 2 39184056
2021 Bioinformatic Prediction of an tRNASec Gene Nested inside an Elongation Factor SelB Gene in Alphaproteobacteria. International journal of molecular sciences 2 33925673
2005 Crystallization and preliminary X-ray analysis of the mRNA-binding domain of elongation factor SelB in complex with RNA. Acta crystallographica. Section F, Structural biology and crystallization communications 2 16511023
2025 Directed Evolution of a SelB Variant that Does Not Require a Selenocysteine Insertion Sequence Element for Function. ACS synthetic biology 1 40536028
2025 Identifying compound heterozygous variants in the EEFSEC gene linked to progressive cerebellar atrophy. Journal of neurodevelopmental disorders 1 40652205
2023 Association of rs142548867 (EEFSEC) and periodontitis Grade C in a young Brazilian population. Journal of applied oral science : revista FOB 1 37466550
2015 A SelB/EF-Tu/aIF2γ-like protein from Methanosarcina mazei in the GTP-bound form binds cysteinyl-tRNA(Cys.). Journal of structural and functional genomics 1 25618148
2007 Crystallization and preliminary X-ray analysis of the mRNA-binding domain of elongation factor SelB from Escherichia coli in complex with RNA. Acta crystallographica. Section F, Structural biology and crystallization communications 1 17565186
2007 Conformational switches in winged-helix domains 1 and 2 of bacterial translation elongation factor SelB. Acta crystallographica. Section D, Biological crystallography 1 17881825
2025 Functional characterization of promoter regions in selenoprotein synthesis-relevant genes (sbp2, eefsec and sepsecs) and their selenium-dependent regulation in yellow catfish Pelteobagrus fulvidraco. Biochimica et biophysica acta. Gene regulatory mechanisms 0 40618995