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EIF1B gene

Known as: EIF1B, GC20, eukaryotic translation initiation factor 1B 
This gene is involved in the initiation of protein translation.
National Institutes of Health

Related topics

Related topics

4 relations
Eukaryotic Translation Initiation Factor 1b, humanGenetic Translation ProcessTranslation InitiationTranslational Activation

Papers overview

Semantic Scholar uses AI to extract papers important to this topic.
2019
2019
Pharmacokinetics and Tissue Distribution of a Novel Bis-Chelated Gold(I) Diphosphine Compound, Bis(2,3-bis(tert-butylmethylphosphino)Quinoxaline)Aurate(I), in Rats
GC20, a novel soluble bis-chelated gold(I)−diphosphine compound, has been reported as a promising anticancer candidate. Assessing… 
2013
2013
A soluble bis-chelated gold(I) diphosphine compound with strong anticancer activity and low toxicity.
Gold-containing compounds have shown anticancer potential, but their clinical applications have been severely limited by poor… 
2013
2013
Tissue-Based Microarray Expression of Genes Predictive of Metastasis in Uveal Melanoma and Differentially Expressed in Metastatic Uveal Melanoma
Purpose To screen the microarray expression of CDH1, ECM1, EIF1B, FXR1, HTR2B, ID2, LMCD1, LTA4H, MTUS1, RAB31, ROBO1, and SATB1… 
2012
2012
Molecular Cloning and Identification of Genes Encoding Eukaryotic Initiation Factor Family 1 (LceIF1, LceIF1A, and LceIF1B) in Leymus chinensis
Soil salinity has become the most significant a biotic stress, resulting in inhibition of plant growth and even death. To search… 
2004
2004
Wettability between Glass-Like Carbon and Optical Glasses
To apply glass-like carbon (GC) to precision die for press-molding of optical glass lens, the wettability between optical glasses… 
Highly Cited
1989
Highly Cited
1989
Recruitment of a penicillin-binding protein gene from Neisseria flavescens during the emergence of penicillin resistance in Neisseria meningitidis.
Non-beta-lactamase-producing, penicillin-resistant strains of Neisseria meningitidis produce altered forms of penicillin-binding… 
1984
1984
High resolution NMR study of CAP binding site 22mer in H2O solution.
High resolution proton NMR were measured for the deoxyoligonucleotide 22mer duplex corresponding to the CAP (catabolite gene… 
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