Translation elongation factor-3 (EF-3): an evolving eukaryotic ribosomal protein? (Q54605424)

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English	Translation elongation factor-3 (EF-3): an evolving eukaryotic ribosomal protein?	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

7563124

retrieved

1 June 2018

reference URL

http://europepmc.org/abstract/MED/7563124

title

Translation elongation factor-3 (EF-3): an evolving eukaryotic ribosomal protein? (English)

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Europe PubMed Central

PubMed publication ID

7563124

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1 June 2018

reference URL

http://europepmc.org/abstract/MED/7563124

author

Mick F. Tuite

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3

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PubMed publication ID

7563124

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1 June 2018

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http://europepmc.org/abstract/MED/7563124

author name string

G P Belfield

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1

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Europe PubMed Central

PubMed publication ID

7563124

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1 June 2018

reference URL

http://europepmc.org/abstract/MED/7563124

N J Ross-Smith

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2

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Europe PubMed Central

PubMed publication ID

7563124

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1 June 2018

reference URL

http://europepmc.org/abstract/MED/7563124

publication date

1 September 1995

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Europe PubMed Central

PubMed publication ID

7563124

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1 June 2018

reference URL

http://europepmc.org/abstract/MED/7563124

published in

Journal of Molecular Evolution

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Europe PubMed Central

PubMed publication ID

7563124

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1 June 2018

reference URL

http://europepmc.org/abstract/MED/7563124

volume

41

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Europe PubMed Central

PubMed publication ID

7563124

retrieved

1 June 2018

reference URL

http://europepmc.org/abstract/MED/7563124

issue

3

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stated in

Europe PubMed Central

PubMed publication ID

7563124

retrieved

1 June 2018

reference URL

http://europepmc.org/abstract/MED/7563124

page(s)

376-387

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Europe PubMed Central

PubMed publication ID

7563124

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1 June 2018

reference URL

http://europepmc.org/abstract/MED/7563124

cites work

Role of yeast elongation factor 3 in the elongation cycle.

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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The ribosome returns

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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An accuracy center in the ribosome conserved over 2 billion years

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Isolation of the yeast gene encoding elongation factor 3 for protein synthesis

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

based on heuristic

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Mechanism and regulation of eukaryotic protein synthesis

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Mutations in ribosomal proteins S4 and S12 influence the higher order structure of 16 S ribosomal RNA.

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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The yeast peptide elongation factor 3 (EF-3) carries an active site for ATP hydrolysis which can interact with various nucleoside triphosphates in the absence of ribosomes

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Sequence analysis of the translational elongation factor 3 from Saccharomyces cerevisiae.

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Characterization of the ATPase and GTPase activities of elongation factor 3 (EF-3) purified from yeasts

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Elongation factor 3 (EF-3) from Candida albicans shows both structural and functional similarity to EF-3 from Saccharomyces cerevisiae

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Interaction of tRNA with 23S rRNA in the ribosomal A, P, and E sites

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Amphiphilic Secondary Structure: Design of Peptide Hormones

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Expression of the gene encoding a translational elongation factor 3 homolog of Chlorella virus CVK2.

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https://pubmed.ncbi.nlm.nih.gov/7563124

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61 Separation and characterization of yeast elongation factors

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https://pubmed.ncbi.nlm.nih.gov/7563124

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The yeast omnipotent suppressor SUP46 encodes a ribosomal protein which is a functional and structural homolog of the Escherichia coli S4 ram protein

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Mutants of elongation factor Tu promote ribosomal frameshifting and nonsense readthrough.

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Sequence and functional similarity between a yeast ribosomal protein and the Escherichia coli S5 ram protein

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Effect of different mutaions in ribosomal protein S5 of Escherichia coli on translational fidelity

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Altered S5 and S20 ribosomal proteins in revertants of an alanyl-tRNA synthetase mutant of Escherichia coli.

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Nucleotide sequence of the SUP2 (SUP35) gene of Saccharomyces cerevisiae

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Soluble factor requirements for the Tetrahymena peptide elongation system and the ribosomal ATPase as a counterpart of yeast elongation factor 3 (EF-3)

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https://pubmed.ncbi.nlm.nih.gov/7563124

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Suppressors in yeast

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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The structure of ribosomal protein S5 reveals sites of interaction with 16S rRNA

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Molecular genetics of myosin

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Cloning, nucleotide sequence, and expression of one of two genes coding for yeast elongation factor 1 alpha

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Protein synthesis in yeast. Structural and functional analysis of the gene encoding elongation factor 3.

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Ribosomal protein S4 is an internal protein: Localization by immunoelectron microscopy on protein-deficient subribosomal particles

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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GCN1, a translational activator of GCN4 in Saccharomyces cerevisiae, is required for phosphorylation of eukaryotic translation initiation factor 2 by protein kinase GCN2.

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https://pubmed.ncbi.nlm.nih.gov/7563124

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Isolation of a Soluble Factor Needed for Protein Synthesis with Various Messenger Ribonucleic Acids Other Than Poly(U)

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Translation elongation factor 3: a fungus-specific translation factor?

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12 December 2020

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A comprehensive set of sequence analysis programs for the VAX

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Polypeptide chain termination in Saccharomyces cerevisiae

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Testing an alternative model for the ribosomal peptide elongation cycle

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Monoclonal antibody specific for yeast elongation factor 3.

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Elongation factor EF-1 alpha gene dosage alters translational fidelity in Saccharomyces cerevisiae

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Candida albicans and three other Candida species contain an elongation factor structurally and functionally analogous to elongation factor 3

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Protein synthesis in yeast. Purification of elongation factor 3 from temperature-sensitive mutant 13-06 of the yeast Saccharomyces cerevisiae

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Constraints on the accuracy of messenger RNA movement

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Polypeptide chain elongation factor 1 alpha (EF-1 alpha) from yeast: nucleotide sequence of one of the two genes for EF-1 alpha from Saccharomyces cerevisiae

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Protein synthesis in yeast. I. Purification and properties of elongation factor 3 from Saccharomyces cerevisiae

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Protein synthesis in yeast

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Role of yeast peptide elongation factor 3 (EF-3) at the AA-tRNA binding step

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Ribosomal proteins. XIX. Altered S5 ribosomal protein in an Escherichia coli revertant from strptomycin dependence to independence

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https://pubmed.ncbi.nlm.nih.gov/7563124

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54 Isolation of the protein synthesis elongation factors EF-Tu, EF-Ts, and EF-G from Escherichia coli

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The yeast MYO1 gene encoding a myosin-like protein required for cell division.

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Isolation and sequence analysis of the gene for translation elongation factor 3 from Candida albicans

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Solution of the ribosome riddle: how the ribosome selects the correct aminoacyl‐tRNA out of 41 similar contestants

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PubMed

reference URL

https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Sequence analysis and expression of the two genes for elongation factor 1 alpha from the dimorphic yeast Candida albicans

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PubMed

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Synthetic peptide model of an essential region of an aminoacyl-tRNA synthetase

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A ribosome-dependent GTPase from yeast distinct from elongation factor 2

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12 December 2020

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Structural model of ATP-binding proteins associated with cystic fibrosis, multidrug resistance and bacterial transport

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Identification of an altered elongation factor in temperature-sensitive mutant ts 7'-14 of Saccharomyces cerevisiae

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https://pubmed.ncbi.nlm.nih.gov/7563124

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12 December 2020

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Ribosomal association of the yeast SAL4 (SUP45) gene product: implications for its role in translation fidelity and termination

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https://pubmed.ncbi.nlm.nih.gov/7563124

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Identifiers

DOI

10.1007/BF00186550

1 reference

stated in

Europe PubMed Central

PubMed publication ID

7563124

retrieved

1 June 2018

reference URL

http://europepmc.org/abstract/MED/7563124

PubMed publication ID

7563124

1 reference

stated in

Europe PubMed Central

PubMed publication ID

7563124

retrieved

1 June 2018

reference URL

http://europepmc.org/abstract/MED/7563124

 

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