Affinage

EEFSEC

Selenocysteine-specific elongation factor · UniProt P57772

Length
596 aa
Mass
65.3 kDa
Annotated
2026-06-09
47 papers in source corpus 27 papers cited in narrative 27 extracted findings
Cross-family judge vs UniProt: Affinage preferred faithfulness: 6/6 claims corpus-supported (100%)

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

EEFSEC (eEFSec/SELB) is a specialized GTPase translation elongation factor dedicated to selenocysteine incorporation, delivering selenocysteinyl-tRNA(Sec) to the ribosomal A site for decoding of in-frame UGA codons (PMID:2140572, PMID:8483932). It was the first elongation factor shown to recognize a single charged tRNA species: it binds Sec-tRNA(Sec) with extraordinary affinity (Kd ~0.2 pM) in a complex requiring contact with the selenol group of the aminoacylated residue, while the 8-bp acceptor stem of tRNA(Sec) is the determinant that selects this tRNA and excludes it from EF-Tu (PMID:1939093, PMID:1839607, PMID:19940162). Architecturally, the protein combines three N-terminal EF-Tu-like GTP/tRNA-binding domains with C-terminal tandem winged-helix domains that constitute a separable mRNA-binding module recognizing the SECIS hairpin located 3' of the UGA codon, producing a quaternary SELB·GTP·Sec-tRNA(Sec)·mRNA complex that positions the charged tRNA at the recoding codon (PMID:8483932, PMID:8893853, PMID:12145214, PMID:26304550). Unlike canonical elongation factors, SELB has low GTP/GDP affinity and very rapid GDP release, dispensing with a dedicated nucleotide-exchange factor; SECIS binding and ribosome engagement stimulate its GTPase activity, and GTP hydrolysis accelerates Sec-tRNA(Sec) release by more than a million-fold to drive insertion (PMID:9454578, PMID:10781605, PMID:19940162). Cryo-EM of recoding intermediates shows that initial binding holds the 30S in an open state with Sec-tRNA(Sec) over the sarcin-ricin loop, and codon recognition triggers 30S closure, SELB docking on the sarcin-ricin loop, and GTPase activation (PMID:27842381). Genetic ablation of the archaeal ortholog abolishes synthesis of all selenoproteins, confirming its essential, pathway-defining role (PMID:12486046), and bi-allelic loss-of-function variants in human EEFSEC reduce selenoprotein levels in patient fibroblasts and cause progressive motor and synaptic defects in a Drosophila model, linking the factor to selenoprotein deficiency and neurodegeneration (PMID:39753114).

Mechanistic history

Synthesis pass · year-by-year structured walk · 10 steps
  1. 1990 High

    Established that selenocysteine insertion requires a dedicated elongation factor distinct from EF-Tu, answering whether Sec delivery uses the canonical translation machinery.

    Evidence Protein purification and ribosome fractionation of bacterial SELB binding selenocysteyl-tRNA(Sec)

    PMID:2140572

    Open questions at the time
    • Did not define the structural basis for tRNA(Sec) discrimination
    • Mechanism of UGA codon recognition unresolved
  2. 1991 High

    Identified the tRNA features that route Sec-tRNA(Sec) to SELB and away from EF-Tu, explaining specificity at the level of the charged tRNA.

    Evidence In vitro binding with tRNA(Sec) stem mutants plus in vivo selenoprotein assay; biochemical characterization of selenol-group dependence

    PMID:1839607 PMID:1939093

    Open questions at the time
    • Did not localize the tRNA-contact residues on SELB
    • Did not address mRNA recognition
  3. 1993 High

    Showed SELB directly reads the SECIS mRNA hairpin and forms a quaternary complex, establishing how Sec delivery is targeted to specific codons.

    Evidence Gel shift, RNA footprinting, and quaternary complex reconstitution on fdhF/fdnG mRNAs; toeprinting on ribosome-bound mRNA

    PMID:8314089 PMID:8483932

    Open questions at the time
    • Did not separate tRNA- and mRNA-binding functions structurally
    • Did not define SECIS nucleotide contacts
  4. 1996 High

    Mapped the mRNA-binding function to a separable C-terminal domain and defined the SECIS nucleotides contacted, dissecting the bifunctional architecture.

    Evidence Domain truncation with RNA-binding assays, chemical probing/NMR with quantitative binding, in vivo competition and stoichiometry experiments

    PMID:8634916 PMID:8893853 PMID:8898393

    Open questions at the time
    • Atomic structure of the domain still unknown
    • Did not explain how mRNA binding affects GTPase
  5. 1998 High

    Connected SECIS binding to catalytic activation, showing the mRNA element conformationally licenses GTP hydrolysis rather than merely tethering the factor.

    Evidence In vitro GTPase kinetics with ribosomes and SECIS hairpin (kcat analysis); SELEX plus in vivo readthrough indicating SECIS roles beyond tethering

    PMID:9192624 PMID:9454578

    Open questions at the time
    • Structural basis of the conformational switch not yet resolved
    • Coupling to codon recognition unknown
  6. 2000 High

    Quantified the unusual nucleotide and RNA binding properties, explaining why SELB needs no exchange factor and how cooperative RNA binding occurs.

    Evidence Stopped-flow kinetics and FRET; archaeal ortholog binding assays; genetic suppressor mapping of SECIS contact residues

    PMID:10781605 PMID:10860743 PMID:11053373

    Open questions at the time
    • Did not capture full-length structure
    • Pico-molar tRNA affinity and its release mechanism not yet measured
  7. 2005 High

    Determined the winged-helix fold and its RNA-recognition mode, revealing the first WH domain used for RNA binding and how the complex could wrap the small subunit.

    Evidence X-ray crystallography of SelB C-terminal domain alone and bound to SECIS RNA; further WH structures with molecular-switch mutagenesis

    PMID:12145214 PMID:12421564 PMID:15665870 PMID:17502103 PMID:17537456

    Open questions at the time
    • Did not show coupling to GTPase domains in full-length context
    • Functional consequence of sequence-independent backbone contacts inferred only
  8. 2009 High

    Defined the thermodynamic logic of Sec-tRNA(Sec) selection and GTP-driven release, showing hydrolysis is the switch for releasing the charged tRNA.

    Evidence Thermodynamic and stopped-flow kinetic measurements with fluorescent tRNA analogs

    PMID:19940162

    Open questions at the time
    • Did not place these steps in the ribosomal recoding pathway
  9. 2016 High

    Visualized the full UGA recoding cascade, establishing how codon recognition mechanically triggers SELB GTPase activation on the ribosome.

    Evidence Single-particle cryo-EM of six recoding intermediates; full-length crystal structure with GTP analog defining the Sec-binding site

    PMID:26304550 PMID:27842381

    Open questions at the time
    • Mammalian eEFSec-specific conformational details only partly resolved
    • Role of SBP2 in human system not structurally captured here
  10. 2025 High

    Established the physiological and disease relevance of human EEFSEC, linking loss of function to selenoprotein deficiency and neurodegeneration.

    Evidence Patient fibroblast selenoprotein quantification, in vitro variant assays, Drosophila RNAi motor/synaptic phenotyping; promoter analysis of transcriptional control by FOXO1/STAT3 in fish

    PMID:39753114 PMID:40618995

    Open questions at the time
    • Which selenoproteins drive neuronal phenotype not defined
    • Human transcriptional regulation not directly tested

Open questions

Synthesis pass · forward-looking unresolved questions
  • How the human eEFSec·SBP2 system and SECIS recognition differ mechanistically from the bacterial SELB single-protein paradigm, and which selenoproteins mediate neuronal maintenance, remain to be resolved.
  • No ribosome-bound structure of the mammalian eEFSec·SBP2 complex in the corpus
  • Tissue-specific selenoprotein requirements unknown

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 6 GO:0003924 GTPase activity 4 GO:0045182 translation regulator activity 4 GO:0140110 transcription regulator activity 1
Localization
GO:0005840 ribosome 3 GO:0005829 cytosol 1
Pathway
R-HSA-392499 Metabolism of proteins 3
Partners
SBP2

Evidence

Reading pass · 27 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
1990 SELB (bacterial ortholog) was purified and shown to be an EF-Tu-like protein that specifically binds selenocysteyl-tRNA(Sec); it was found partially associated with ribosomes by cell fractionation, establishing it as the first elongation factor with specificity for a particular charged tRNA. Protein purification, limited proteolysis, immunological analysis, ribosome fractionation The Journal of biological chemistry High 2140572
1991 The 8-bp aminoacyl-acceptor stem of tRNA(Sec) is the key determinant for binding to SELB and for exclusion from EF-Tu; reducing the stem to 7 bp (canonical length) abolished SELB binding but allowed EF-Tu binding, irrespective of the charged amino acid. In vitro binding assays with purified SELB, EF-Tu, and tRNA(Sec) mutants; in vivo selenoprotein synthesis assay The Journal of biological chemistry High 1939093
1991 SELB specifically complexes selenocysteyl-tRNA(Sec); interaction with the selenol group of the aminoacylated residue is required for stable SELB·tRNA complex formation, providing the biochemical basis for exclusive selection of Sec-tRNA(Sec) during UGA decoding. Biochemical characterization of purified SELB with charged tRNA variants Biochimie Medium 1839607
1993 Bacterial SELB directly and specifically binds the mRNA hairpin SECIS element (located 3' of the UGA codon) via its loop region; in the presence of selenocysteinyl-tRNA, SELB forms a quaternary complex with charged tRNA and mRNA, positioning Sec-tRNA(Sec) at the UGA codon. Gel shift assays, RNA footprinting with nucleases and iodine, complex formation assays 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 to selenoprotein mRNAs fdhF and fdnG; toeprint experiments showed SELB recognizes ribosome-bound mRNA and may protrude toward the large subunit, placing the ternary complex at the selenocysteine codon. Boundary experiments, toeprinting assays Genes & development High 8314089
1996 The C-terminal domain of bacterial SELB (a ~17 kDa subdomain) specifically binds the mRNA SECIS hairpin; a truncated SELB lacking this domain still binds selenocysteyl-tRNA(Sec) but cannot bind mRNA, demonstrating that the tRNA- and mRNA-binding functions are physically separable. Domain truncation, expression of isolated fragments, RNA-binding assays, in vivo competition experiments Journal of molecular biology High 8893853
1996 Bases G23, U24, and bulge residues U17/U18 in the SECIS mRNA hairpin apical loop are directly involved in binding to SELB in both fdhF and fdnG mRNAs; SELB binding affinity for the fdhF hairpin is ~30 nM (apparent Kd). Chemical probing, NMR-based structure determination, computer modeling, binding studies RNA (New York, N.Y.) High 8634916
1996 Overproduction of SELB reduces selenocysteine UGA readthrough; co-overexpression of tRNA(Sec) reverses inhibition, establishing that a correct stoichiometric quaternary complex (SELB·GTP·Sec-tRNA(Sec)·mRNA) is required for selenocysteine insertion in vivo. In vivo overexpression, UGA readthrough assay (lacZ fusion), genetic complementation Molecular microbiology Medium 8898393
1997 In vitro selection (SELEX) identified novel RNA aptamers binding SELB; in vivo analysis showed that mRNA hairpin binding to SELB is necessary but not sufficient for UGA readthrough, implying SECIS element functions beyond mere tethering of Sec-tRNA(Sec) to UGA. In vitro SELEX, domain-mapping with truncated SELB, in vivo lacZ UGA readthrough assay Proceedings of the National Academy of Sciences of the United States of America Medium 9192624
1998 SELB possesses low intrinsic GTPase activity stimulated by 70S ribosomes; the SECIS mRNA hairpin further increases ribosome-stimulated GTPase activity 3–4 fold (via increased kcat), showing mRNA binding induces a conformational switch that promotes GTP hydrolysis. GTPase activity assays in vitro with ribosomes and mRNA hairpin, kinetic analysis Biochemistry High 9454578
1999 The C-terminus of SELB is the primary interaction domain for mRNA hairpin binding; the vast majority of SELEX-derived aptamers from a random pool bound specifically to the C-terminal domain of SELB. In vitro SELEX with full-length and truncated SELB, domain mapping RNA (New York, N.Y.) Medium 10496219
2000 SelB GTP affinity (Kd = 0.74 µM) and GDP affinity (Kd = 13.4 µM) are much lower than other translation factors; GDP release is very rapid (15 s⁻¹), explaining why no GDP/GTP exchange factor is needed. The SECIS RNA minihelix binds with Kd ~1 nM, affinity increasing further when Sec-tRNA(Sec) is bound to SelB. Stopped-flow kinetics using intrinsic tryptophan fluorescence and fluorescent nucleotide analogs; fluorescence resonance energy transfer The Journal of biological chemistry High 10781605
2000 The archaeal SelB homolog (MJ0495/aSelB) from Methanococcus jannaschii binds guanine nucleotides and preferentially binds selenocysteyl-tRNA(Sec), but unlike bacterial SelB, does not bind the SECIS element, correlating with its lack of the bacterial C-terminal mRNA-binding domain. Purification of recombinant MJ0495, GTP binding assay, tRNA binding assay, SECIS binding assay Journal of molecular biology High 10860743
2002 Crystal structure of the C-terminal mRNA-binding fragment of Moorella thermoacetica SelB (SelB-C) at 2.12 Å reveals four tandem winged-helix (WH) domains arranged in an L-shape; this is the first example of WH domains in RNA binding, with conserved basic residues defining the mRNA-binding site. X-ray crystallography with multiwavelength anomalous dispersion phasing The EMBO journal High 12145214
2002 NMR structure of the prokaryotic SECIS mRNA hairpin shows conserved nucleotides exposed for SelB recognition; binding of the SelB C-terminal domain stabilizes RNA secondary structure; a GpU sequence at the tetraloop tip and a bulge uracil 5 base pairs away are essential for SelB interaction. NMR spectroscopy, mutagenesis of RNA, SelB binding assays Journal of molecular biology High 12421564
2003 Inactivation of selB in Methanococcus maripaludis abolishes synthesis of all selenoproteins, proving aSelB is the archaeal translation factor specialized for selenocysteine insertion; the mutation also derepresses expression of cysteine-containing homologs and impairs growth on formate. Targeted gene knockout, metabolic labeling, proteomics Journal of bacteriology High 12486046
2005 Crystal structure of the SelB mRNA-binding domain in complex with SECIS RNA at 2.3 Å reveals the first RNA-binding winged-helix (WH) domain; RNA recognition occurs without major conformational change in the WH motif, and the geometry allows the complex to wrap around the small ribosomal subunit. X-ray crystallography Nature structural & molecular biology High 15665870
2007 Crystal structures of E. coli WH3/4 domains and M. thermoacetica WH1-4 domains each bound to SECIS RNA reveal that both WH motifs use the same structural elements for RNA binding; a salt bridge connecting WH2 to WH3 is disrupted upon mRNA binding, providing a molecular switch that may communicate between tRNA and mRNA binding sites. X-ray crystallography at 2.3 Å (E. coli WH3/4) and 2.6 Å (M. thermoacetica WH1-4), mutagenesis Journal of molecular biology High 17537456
2007 Crystal structure of SelB C-terminal domain complexed with RNA reveals large domain rearrangement; an interdomain region forms new interactions with phosphate backbone of a neighboring RNA in a sequence-independent manner, potentially reflecting SelB interactions with tRNA or rRNA during ribosome engagement. X-ray crystallography Structure (London, England : 1993) Medium 17502103
2009 Sec-tRNA(Sec) binds SelB·GTP with extraordinarily high affinity (Kd = 0.2 pM); binding is enthalpically driven with ~4 ion pairs. GTP hydrolysis accelerates release of Sec-tRNA(Sec) by >10⁶-fold (from 0.3 h⁻¹ to 240 s⁻¹). Ser-tRNA(Sec) and uncharged tRNA(Sec) bind with much lower affinity (~0.5 µM) to any nucleotide-bound form. Thermodynamic and kinetic stopped-flow measurements, fluorescent tRNA analogs The Journal of biological chemistry High 19940162
2015 Crystal structure of full-length bacterial SelB from Aquifex aeolicus in complex with GTP analog at 3.2 Å shows three EF-Tu-like domains (D1-3) followed by four WH domains; the Sec-binding site is located at the D1-D2 interface with Arg residues coordinating the Sec moiety, and is smaller and more exposed than EF-Tu's aminoacyl binding site. X-ray crystallography at 3.2 Å Nucleic acids research High 26304550
2016 Cryo-EM structures of six intermediates on the UGA recoding pathway reveal that: initial SelB-Sec-tRNA(Sec) binding induces 30S open conformation with Sec-tRNA(Sec) covering the sarcin-ricin loop (SRL); codon recognition in the decoding site causes local closure moving Sec-tRNA(Sec) away from the SRL and global 30S shoulder closure; this triggers SelB docking on the SRL, activating its GTPase. Single-particle cryo-electron microscopy, six structural intermediates Nature High 27842381
2018 Mammalian 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 promotes a slight ratchet of domains 1-2 and a lever-like movement of domain 4, which may be critical for Sec-tRNA(Sec) release on the ribosome. Structural analysis, biochemical characterization of domain functions (summary/review of published experimental work) Biochimica et biophysica acta. General subjects Medium 29555379
2025 Bi-allelic loss-of-function variants in EEFSEC cause reduced EEFSEC function in vitro, leading to lower selenoprotein levels in patient fibroblasts; an eEFSec-RNAi Drosophila model shows progressive motor impairment and synaptic defects, establishing that EEFSEC function is required for selenoprotein synthesis and neuronal maintenance in vivo. Patient fibroblast selenoprotein quantification, in vitro functional assays of variants, Drosophila RNAi model with motor and synaptic phenotyping American journal of human genetics High 39753114
2000 The bulged nucleotide U17 in the E. coli SECIS upper stem-loop participates in interaction with SelB; suppressor mutations in selB that rescue SECIS bulge mutations map to a 28-amino acid stretch in SelB C-terminal subdomain 4b, identifying this region as the contact interface. Genetic suppressor analysis, in vivo UGA readthrough assay, selB sequencing Journal of bacteriology Medium 11053373
1999 Genetic analysis of SelB-SECIS interaction identified suppressor mutations in selB that counteract SECIS mutations; four suppressor amino acid exchanges cluster in a 23-amino acid stretch in domain 4b (direct RNA contact sites), and a fifth mutation in domain 4a promotes allele-nonspecific readthrough, suggesting domain 4a modulates communication between tRNA- and mRNA-binding regions. In vivo suppressor selection, UGA readthrough assay, selenium incorporation, sequencing Molecular & general genetics : MGG Medium 10628863
2025 FOXO1 and STAT3 transcription factors directly bind functional sites in the eefsec promoter (-1070 bp FOXO1 site; -428 bp STAT3 site) and regulate eefsec transcriptional activity in a selenium-dependent manner in yellow catfish. Sequential promoter deletion analysis, EMSA, chromatin immunoprecipitation Biochimica et biophysica acta. Gene regulatory mechanisms Medium 40618995

Source papers

Stage 0 corpus · 47 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
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
1996 Domain structure of the prokaryotic selenocysteine-specific elongation factor SelB. Journal of molecular biology 96 8893853
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 93 8483932
2016 The pathway to GTPase activation of elongation factor SelB on the ribosome. Nature 92 27842381
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
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
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
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
1994 Recognition of the mRNA selenocysteine insertion sequence by the specialized translational elongation factor SELB. Genes & development 45 8314089
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
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
2003 Inactivation of the selB gene in Methanococcus maripaludis: effect on synthesis of selenoproteins and their sulfur-containing homologs. Journal of bacteriology 39 12486046
2002 Structure of prokaryotic SECIS mRNA hairpin and its interaction with elongation factor SelB. Journal of molecular biology 39 12421564
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 21 17537456
2018 On elongation factor eEFSec, its role and mechanism during selenium incorporation into nascent selenoproteins. Biochimica et biophysica acta. General subjects 19 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 5 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
2025 Directed Evolution of a SelB Variant that Does Not Require a Selenocysteine Insertion Sequence Element for Function. ACS synthetic biology 3 40536028
2021 Bioinformatic Prediction of an tRNASec Gene Nested inside an Elongation Factor SelB Gene in Alphaproteobacteria. International journal of molecular sciences 3 33925673
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
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 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

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