Literature DB >> 7030387

Spectroscopic studies of the nucleotide binding site of elongation factor Tu from Escherichia coli. An approach to characterizing the elementary steps of the elongation cycle of protein biosynthesis.

J F Eccleston.   

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Year:  1981        PMID： 7030387     DOI： 10.1021/bi00524a055

Source DB:  PubMed          Journal:  Biochemistry        ISSN： 0006-2960            Impact factor:   3.162


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  5 in total

1.  Hydrolysis of GTP by p21NRAS, the NRAS protooncogene product, is accompanied by a conformational change in the wild-type protein: use of a single fluorescent probe at the catalytic site.

Authors:  S E Neal; J F Eccleston; M R Webb
Journal:  Proc Natl Acad Sci U S A       Date:  1990-05       Impact factor: 11.205

2.  A continuous spectrophotometric assay for inorganic phosphate and for measuring phosphate release kinetics in biological systems.

Authors:  M R Webb
Journal:  Proc Natl Acad Sci U S A       Date:  1992-06-01       Impact factor: 11.205

3.  Expression of p21 proteins in Escherichia coli and stereochemistry of the nucleotide-binding site.

Authors:  J Tucker; G Sczakiel; J Feuerstein; J John; R S Goody; A Wittinghofer
Journal:  EMBO J       Date:  1986-06       Impact factor: 11.598

4.  The structural and functional basis for the kirromycin resistance of mutant EF-Tu species in Escherichia coli.

Authors:  J R Mesters; L A Zeef; R Hilgenfeld; J M de Graaf; B Kraal; L Bosch
Journal:  EMBO J       Date:  1994-10-17       Impact factor: 11.598

5.  Structural details of the binding of guanosine diphosphate to elongation factor Tu from E. coli as studied by X-ray crystallography.

Authors:  T F la Cour; J Nyborg; S Thirup; B F Clark
Journal:  EMBO J       Date:  1985-09       Impact factor: 11.598
  5 in total

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