(Q54008053)

23 May 2018

title

Phosphorylation of elongation factor Tu prevents ternary complex formation. (English)

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23 May 2018

0 references

7

Erdmann VA

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23 May 2018

author name string

Alexander C

1

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23 May 2018

Bilgin N

2

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23 May 2018

Lindschau C

3

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23 May 2018

Mesters JR

4

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23 May 2018

Kraal B

5

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23 May 2018

Hilgenfeld R

6

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23 May 2018

Lippmann C

8

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23 May 2018

language of work or name

English

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publication date

1 June 1995

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23 May 2018

Journal of Biological Chemistry

published in

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23 May 2018

volume

270

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23 May 2018

issue

24

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23 May 2018

page(s)

14541-14547

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23 May 2018

Zone-interference gel electrophoresis: a new method for studying weak protein-nucleic acid complexes under native equilibrium conditions

cites work

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.24.14541

Primary structure of elongation factor Tu from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.24.14541

Crystal structure of active elongation factor Tu reveals major domain rearrangements

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.24.14541

Structure investigation of Phe-tRNAphefromE.colibound to the ribosomal A-site

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.24.14541

The GTPase superfamily: conserved structure and molecular mechanism

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.24.14541

Novel data on interactions of elongation factor Ts.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.24.14541

How many EF-Tu molecules participate in aminoacyl-tRNA binding and peptide bond formation in Escherichia coli translation?

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.24.14541

Refined structure of elongation factor EF-Tu from Escherichia coli

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.24.14541

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

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.24.14541

Nucleotide binding and GTP hydrolysis by elongation factor Tu from Thermus thermophilus as monitored by proton NMR

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.24.14541

Location of the site of methylation in elongation factor Tu

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.24.14541

Interaction of the isolated domain II/III of Thermus thermophilus elongation factor Tu with the nucleotide exchange factor EF-Ts

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.24.14541

Two GTPs are hydrolysed on two molecules of EF-Tu for each elongation cycle during code translation.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.24.14541

Toward a model for the interaction between elongation factor Tu and the ribosome.

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.24.14541

Kirromycin, an inhibitor of protein biosynthesis that acts on elongation factor Tu

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.24.14541

Mechanism of the Inhibition of Protein Synthesis by Kirromycin. Role of Elongation Factor Tu and Ribosomes

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.24.14541

Kirromycin drastically reduces the affinity of Escherichia coli elongation factor Tu for aminoacyl-tRNA

21 January 2018

1 reference

https://api.crossref.org/works/10.1074%2FJBC.270.24.14541

21 January 2018

Identifiers

DOI

10.1074/JBC.270.24.14541

1 reference

23 May 2018

PubMed ID

7782317

1 reference

23 May 2018