Mutant species of EF-Tu, altered at position 375, exhibit a reduced affinity for aminoacylated transfer-RNAs (Q44932635)

7 December 2017

Mutant species of EF-Tu, altered at position 375, exhibit a reduced affinity for aminoacylated transfer-RNAs (English)

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7 December 2017

Sam T

1

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7 December 2017

Pingoud A

series ordinal

2

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7 December 2017

Bosch L

series ordinal

3

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7 December 2017

language of work or name

English

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publication date

1 June 1985

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7 December 2017

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7 December 2017

185

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1

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7 December 2017

51-56

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The role of guanosine 5′-triphosphate in polypeptide chain elongation

7 December 2017

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2885%2980739-0

RNA Replication: Function and Structure of QBeta-Replicase

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2885%2980739-0

Primary structure of elongation factor Tu from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2885%2980739-0

A kirromycin resistant elongation factor EF-Tu from Escherichia coli contains a threonine instead of an alanine residue in position 375.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2885%2980739-0

Allosteric changes of the guanine nucleotide site of elongation factor EF-Tu: a comparative study of two kirromycin-resistant EF-Tu species.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2885%2980739-0

Ternary Complex Formation between Elongation Factor Tu, GTP and Aminoacyl-tRNA: an Equilibrium Study

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2885%2980739-0

The determination of binding parameters from protection experiments. A quantitative assay for ternary complex formation of elongation factor Tu, GTP, and aminoacyl-tRNA.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2885%2980739-0

Specificity of Elongation Factor Tu from Escherichia coli with Respect to Attachment of the Amino Acid to the 2' or 3'-Hydroxyl Group of the Terminal Adenosine of tRNA

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2885%2980739-0

Identification of a histidine residue near the aminoacyl transfer ribonucleic acid binding site of elongation factor Tu.

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2885%2980739-0

A simplified procedure for the isolation of bacterial polypeptide elongation factor EF-Tu

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2885%2980739-0

Aminoacyl transfer ribonucleic acid binding site of the bacterial elongation factor Tu

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2885%2980739-0

Interaction of Escherichia coli EF-Tu.GTP and EF-Tu.GDP with analogues of the 3' terminus of aminoacyl-tRNA

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2885%2980739-0

Isolation, characterization and structural implications of a nuclease-digested complex of aminoacyl transfer RNA and Escherichia coli elongation factor Tu

21 January 2018

1 reference

https://api.crossref.org/works/10.1016%2F0014-5793%2885%2980739-0

10.1016/0014-5793(85)80739-0

21 January 2018

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DOI

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7 December 2017

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