An intact conformation at the tip of elongation factor G domain IV is functionally important (Q77301717)

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4 December 2019

title

An intact conformation at the tip of elongation factor G domain IV is functionally important (English)

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4 December 2019

author name string

K A Martemyanov

1

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4 December 2019

A S Yarunin

2

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4 December 2019

A Liljas

3

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4 December 2019

A T Gudkov

4

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4 December 2019

publication date

1 August 1998

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4 December 2019

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4 December 2019

volume

434

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4 December 2019

issue

1-2

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4 December 2019

page(s)

205-208

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A complex profile of protein elongation: translating chemical energy into molecular movement

4 December 2019

cites work

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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Elongation factor Tu can reduce translation errors in poly(U)-directed cell-free systems

21 January 2018

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Analysis of orthophosphate-pyrophosphate mixtures resulting from weak pyrophosphatase activities

21 January 2018

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Initiation of protein synthesis II a convenient assay for the ribosome-dependent synthesis of N-formyl-C14-methionylpuromycin

21 January 2018

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Cloning and sequencing of the gene encoding thermostable elongation factor 2 in Sulfolobus solfataricus

21 January 2018

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Amino acid sequence of mammalian elongation factor 2 deduced from the cDNA sequence: homology with GTP-binding proteins

21 January 2018

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The histidine residue of codon 715 is essential for function of elongation factor 2

21 January 2018

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Conserved motifs in prokaryotic and eukaryotic polypeptide release factors: tRNA-protein mimicry hypothesis

21 January 2018

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The crystal structure of elongation factor G complexed with GDP, at 2.7 A resolution

21 January 2018

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Ribosomal translocation: facts and models

7 January 2021

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inferred from DOI database lookup

7 January 2021

based on heuristic

Identifiers

DOI

10.1016/S0014-5793(98)00982-X

1 reference

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4 December 2019

1 reference