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EEF2 gene
Known as:
EEF2
, POLYPEPTIDYL-tRNA TRANSLOCASE
, EUKARYOTIC TRANSLATION ELONGATION FACTOR 2
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This gene plays a role in nucleotide binding and protein biosynthesis.
National Institutes of Health
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Related topics
Related topics
4 relations
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EEF2 wt Allele
Genetic Translation Process
Peptide Elongation Factor 2
protein protein interaction
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
1999
Highly Cited
1999
Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic subunit favors association with the alpha 4 subunit which promotes dephosphorylation of elongation factor-2.
H. Chung
,
A. Nairn
,
K. Murata
,
D. Brautigan
Biochemistry
1999
Corpus ID: 21452025
The cellular location and substrate specificity of the catalytic subunit (C) of protein phosphatase 2A (PP2A) depend on its…
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Highly Cited
1995
Highly Cited
1995
Decreased polysomal HSP-70 may slow polypeptide elongation during skeletal muscle atrophy.
Z. Ku
,
Jiwei Yang
,
Vandana Menon
,
Donald B. Thomason
American Journal of Physiology
1995
Corpus ID: 29753701
Slowed elongation rate is the apparent cause of the rapid decrease in rat soleus muscle protein synthesis rate during non-weight…
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Highly Cited
1989
Highly Cited
1989
Effect of alpha-sarcin and ribosome-inactivating proteins on the interaction of elongation factors with ribosomes.
M. Brigotti
,
Fioretta Rambelli
,
Mariacristina Zamboni
,
L. Montanaro
,
S. Sperti
Biochemical Journal
1989
Corpus ID: 23966159
alpha-Sarcin from Aspergillus giganteus and the ribosome-inactivating proteins (RIPs) from higher plants inactivate the 60 S…
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Highly Cited
1989
Highly Cited
1989
The tumour promoter okadaic acid inhibits reticulocyte-lysate protein synthesis by increasing the net phosphorylation of elongation factor 2.
N. Redpath
,
C. Proud
Biochemical Journal
1989
Corpus ID: 26545594
Okadaic acid, a tumour promoter which potently inhibits protein phosphatases, inhibited translation in the reticulocyte-lysate…
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Highly Cited
1984
Highly Cited
1984
In vitro biosynthesis of diphthamide, studied with mutant Chinese hamster ovary cells resistant to diphtheria toxin
T. Moehring
,
D. Danley
,
J. Moehring
Molecular and Cellular Biology
1984
Corpus ID: 25035318
Diphthamide, a unique amino acid, is a post-translational derivative of histidine that exists in protein synthesis elongation…
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Highly Cited
1983
Highly Cited
1983
Strains of CHO-K1 cells resistant to Pseudomonas exotoxin A and cross-resistant to diphtheria toxin and viruses
J. Moehring
,
T. Moehring
Infection and Immunity
1983
Corpus ID: 28258884
We have investigated two phenotypically distinct types of mutants of CHO-K1 cells that are resistant to Pseudomonas exotoxin A…
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Highly Cited
1980
Highly Cited
1980
Posttranslational modification of elongation factor 2 in diphtheria-toxin-resistant mutants of CHO-K1 cells.
J. Moehring
,
T. Moehring
,
D. Danley
Proceedings of the National Academy of Sciences…
1980
Corpus ID: 939512
We have identified two types of mutants of Chinese hamster ovary cells in which the unique ADP-ribose attachment site in…
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Highly Cited
1978
Highly Cited
1978
Chimeric toxins: toxic, disulfide-linked conjugate of concanavalin A with fragment A from diphtheria toxin.
D. Gilliland
,
R. Collier
,
Joan M. MOEHRINGt
,
Thomas J. MOEHRINGt
Proceedings of the National Academy of Sciences…
1978
Corpus ID: 28393568
A disulfide-linked conjugate of concanavalin A (Con A) and fragment A from diphtheria toxin has been synthesized and shown to be…
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Highly Cited
1973
Highly Cited
1973
The elongation factor 2 content of mammalian cells. Assay method and relation to ribosome number.
D. Gill
,
L. L. Dinius
Journal of Biological Chemistry
1973
Corpus ID: 29623222
Abstract A method is described for quantitatively assaying elongation factor 2 (EF-2), the enzyme that catalyses the…
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Highly Cited
1960
Highly Cited
1960
Studies on the chemical basis of the antigenicity of proteins. 1. Antigenicity of polypeptidyl gelatins.
Michael Sela
,
Ruth Arnon
Biochemical Journal
1960
Corpus ID: 37221694
In the preceding paper it was shown that the attachment of tyrosine, tryptophan or phenylalanine peptides to gelatin converts it…
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