Structural basis for mRNA recognition by elongation factor SelB (Q81308492)

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7 January 2020

title

Structural basis for mRNA recognition by elongation factor SelB (English)

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1

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Daisuke Kohda

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Dominique Fourmy

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author name string

Linda Rasubala

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Toyoyuki Ose

3

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Katsumi Maenaka

6

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publication date

23 January 2005

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Nature Structural & Molecular Biology

7 January 2020

published in

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volume

12

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issue

2

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page(s)

198-203

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https://scigraph.springernature.com/pub.10.1038/nsmb890

7 January 2020

exact match

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cites work

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Crystal structure of formate dehydrogenase H: catalysis involving Mo, molybdopterin, selenocysteine, and an Fe4S4 cluster

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Identification of a novel translation factor necessary for the incorporation of selenocysteine into protein

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Selection of tRNA by the ribosome requires a transition from an open to a closed form

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Domain structure of the prokaryotic selenocysteine-specific elongation factor SelB.

31 March 2020

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Kinetics of the Interaction of Translation Factor SelB fromEscherichia coliwith Guanosine Nucleotides and Selenocysteine Insertion Sequence RNA

31 March 2020

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The bulged nucleotide in the Escherichia coli minimal selenocysteine insertion sequence participates in interaction with SelB: a genetic approach

31 March 2020

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Structure of prokaryotic SECIS mRNA hairpin and its interaction with elongation factor SelB

31 March 2020

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Revised Escherichia coli selenocysteine insertion requirements determined by in vivo screening of combinatorial libraries of SECIS variants

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Crystal structure of an mRNA-binding fragment of Moorella thermoacetica elongation factor SelB.

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tRNA(Pro) anticodon recognition by Thermus thermophilus prolyl-tRNA synthetase

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Genetic probing of the interaction between the translation factor SelB and its mRNA binding element in Escherichia coli

31 March 2020

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In vitro and in vivo characterization of novel mRNA motifs that bind special elongation factor SelB

31 March 2020

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31 March 2020

Identifiers

DOI

10.1038/NSMB890

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7 January 2020

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