Literature DB >> 6112171

The GTPase activity of elongation factor Tu and the 3'-terminal end of aminoacyl-tRNA.

G Parlato, J Guesnet, J B Crechet, A Parmeggiani.   

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Year:  1981        PMID： 6112171     DOI： 10.1016/0014-5793(81)80733-8

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


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  5 in total

1.  GTPase center of elongation factor Tu is activated by occupation of the second tRNA binding site.

Authors:  J M Van Noort; B Kraal; L Bosch
Journal:  Proc Natl Acad Sci U S A       Date:  1986-07       Impact factor: 11.205

2.  Functional assay of tRNA molecules transcribed from a purified gene.

Authors:  L Corbo; G Ciliberto; C Traboni; R Santamaria; F Cimino; R Cortese; F Salvatore
Journal:  Nucleic Acids Res       Date:  1982-11-25       Impact factor: 16.971

3.  Enacyloxin IIa, an inhibitor of protein biosynthesis that acts on elongation factor Tu and the ribosome.

Authors:  R Cetin; I M Krab; P H Anborgh; R H Cool; T Watanabe; T Sugiyama; K Izaki; A Parmeggiani
Journal:  EMBO J       Date:  1996-05-15       Impact factor: 11.598

4.  New antibiotic that acts specifically on the GTP-bound form of elongation factor Tu.

Authors:  P H Anborgh; A Parmeggiani
Journal:  EMBO J       Date:  1991-04       Impact factor: 11.598

5.  Many of the conserved nucleotides of tRNA(Phe) are not essential for ternary complex formation and peptide elongation.

Authors:  I A Nazarenko; K M Harrington; O C Uhlenbeck
Journal:  EMBO J       Date:  1994-05-15       Impact factor: 11.598
  5 in total

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