(Q41470071)

1 October 2017

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title

The ternary complex of aminoacylated tRNA and EF-Tu-GTP. Recognition of a bond and a fold (English)

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1 October 2017

1

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1 October 2017

Kjeldgaard M

2

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1 October 2017

Thirup S

series ordinal

3

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1 October 2017

Clark BF

series ordinal

4

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1 October 2017

Nyborg J

series ordinal

5

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1 October 2017

publication date

1 January 1996

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1 October 2017

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1 October 2017

volume

78

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1 October 2017

issue

11-12

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1 October 2017

page(s)

921-933

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Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog

1 October 2017

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Why do two EF-Tu molecules act in the elongation cycle of protein biosynthesis?

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Two GTPs are consumed on EF-Tu per peptide bond in poly(Phe) synthesis, in spite of switching stoichiometry of the EF-Tu.aminoacyl-tRNA complex with temperature

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Minimalist aminoacylated RNAs as efficient substrates for elongation factor Tu

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Differences between transfer RNA molecules.

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Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase

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Mammalian valyl-tRNA synthetase forms a complex with the first elongation factor

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The crystal structure of elongation factor EF-Tu from Thermus aquaticus in the GTP conformation

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CH/pi interaction in the packing of the adenine ring in protein structures

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The influence of different modifications of elongation factor Tu from Escherichia coli on ternary complex formation investigated by fluorescence spectroscopy

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7 January 2021

Mutation of the conserved Gly83 and Gly94 in Escherichia coli elongation factor Tu. Indication of structural pivots

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7 January 2021

Mapping Escherichia coli elongation factor Tu residues involved in binding of aminoacyl-tRNA.

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7 January 2021

Recruiting proteins to the RNA world.

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Mutations to kirromycin resistance occur in the interface of domains I and III of EF-Tu.GTP.

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Phosphorylation of elongation factor Tu prevents ternary complex formation.

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7 January 2021

Three-Dimensional Tertiary Structure of Yeast Phenylalanine Transfer RNA

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7 January 2021

Structure of yeast phenylalanine tRNA at 3 Å resolution

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7 January 2021

Crystal structure of active elongation factor Tu reveals major domain rearrangements

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7 January 2021

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7 January 2021

Aminoacyl-tRNAs. Diversity before and unity after interaction with EF-Tu:GTP

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7 January 2021

Fluorescence characterization of the interaction of various transfer RNA species with elongation factor Tu.GTP: evidence for a new functional role for elongation factor Tu in protein biosynthesis.

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7 January 2021

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The role of N-formyl-methionyl-sRNA in protein biosynthesis

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

Antideterminants present in minihelix(Sec) hinder its recognition by prokaryotic elongation factor Tu.

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7 January 2021

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

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7 January 2021

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7 January 2021

MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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7 January 2021

Systematic analysis of structural data as a research technique in organic chemistry

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COCI

https://opencitations.net/index/coci/api/v1/citations/10.1021/AR00089A001

10.1016/S0300-9084(97)86714-4

5 March 2023

Identifiers

DOI

1 reference

1 October 2017

1 reference