2023
DOI: 10.1007/s12104-023-10141-7
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Backbone resonance assignments of the C-terminal region of human translation initiation factor eIF4B

Abstract: Translation initiation in eukaryotes is an early step in protein synthesis, requiring multiple factors to recruit the ribosomal small subunit to the mRNA 5' untranslated region. One such protein factor is the eukaryotic translation initiation factor 4B (eIF4B), which increases the activity of the eIF4A RNA helicase, and is linked to cell survival and proliferation. We report here the protein backbone chemical shift assignments corresponding to the C-terminal 279 residues of human eIF4B. Analysis of the chemica… Show more

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Cited by 3 publications
(4 citation statements)
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“…To return to the DRYG-CTR construct at moderate ionic strength, the number and position of observed amide crosspeaks is remarkably similar to the pattern observed for the isolated CTR 29 . An overlay of the DRYG-CTR and CTR spectra at 150 mM NaCl highlights this similarity (Fig.…”
Section: Eif4b Idr Is Largely Devoid Of Stable Secondary Structuresupporting
confidence: 62%
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“…To return to the DRYG-CTR construct at moderate ionic strength, the number and position of observed amide crosspeaks is remarkably similar to the pattern observed for the isolated CTR 29 . An overlay of the DRYG-CTR and CTR spectra at 150 mM NaCl highlights this similarity (Fig.…”
Section: Eif4b Idr Is Largely Devoid Of Stable Secondary Structuresupporting
confidence: 62%
“…The CD spectrum shows a large minimum at 202 nm and small ellipticity signal at 220 nm, which is consistent with low secondary structure content as expected for disordered proteins. The small contribution of ellipticity at 220 nm is likely originating from transient short helical motifs at the CTR suggested by our previous NMR data 29 (Supplementary Fig. 1).…”
Section: Eif4b Idr Is Largely Devoid Of Stable Secondary Structurementioning
confidence: 58%
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