A few notes on science in Ukraine

As a person who has had a long scientific career in Ukraine, both before and after its re-acquisition of independence thirty years ago, I would like to share my observations with the readership of this Special Issue. By no means are these observations meant to provide a systematic presentation, which requires a different format. Rather, they are highly personal notes, providing snippets of the past and present and a discussion of the future of Ukrainian science. They also allow me to acknowledge my wonderful colleagues and bright students. I am delighted to see that many of them have contributed excellent reviews and original manuscripts to this Special Issue. (I am also keenly aware of the fact that because of the brutal invasion and bombardments by our imperial neighbor, many of my colleagues have been unable to share their latest work). It will be up to this next generation of Ukrainian scientists to develop Biological Sciences in Ukraine in the future

A2 isoform of mammalian translation factor eEF1A displays increased tyrosine phosphorylation and ability to interact with different signalling molecules

The eEF1A1 and eEF1A2 isoforms of translation elongation factor 1A have 98% similarity and perform the same protein synthesis function catalyzing codon-dependent binding of aminoacyl-tRNA to 80S ribosome. However, the isoforms apparently play different non-canonical roles in apoptosis and cancer development which are awaiting further investigations. We hypothesize that the difference in non-translational functions could be caused, in particular, by differential ability of the isoforms to be involved in phosphotyrosine-mediated signalling

Evidence for the formation of an unusual ternary complex of rabbit liver EF-1α with GDP and deacylated tRNA

AbstractEukaryotic translation elongation factor1α is known to interact in GTP-bound form with aminoacyl-tRNA promoting its binding to the ribosome. In this paper another ternary complex [EF-1α*GDP*deacylated tRNA], never considered in widely accepted elongation schemes, is reported for the first time. The formation of this unusual complex, postulated earlier (FEBS Lett. (1996) 382, 18–20), has been detected by four independent methods. [EF-1α*GDP]-interacting sites are located in the acceptor stem, TψC stem and TψC loop of tRNAPhe and tRNALeu molecules. Both tRNA and EF-1α are found to undergo certain conformational changes during their interaction. The ability of EF-1α to form a complex with deacylated tRNA indicates that the factor may perform an important role in tRNA and aminoacyl-tRNA channeling in higher eukaryotic cells

Conservation of exposed residues in putative calmodulin binding domain of the eEF1A homologues

<p><b>Copyright information:</b></p><p>Taken from "Multiple molecular dynamics simulation of the isoforms of human translation elongation factor 1A reveals reversible fluctuations between "open" and "closed" conformations and suggests specific for eEF1A1 affinity for Ca-calmodulin"</p><p>http://www.biomedcentral.com/1472-6807/8/4</p><p>BMC Structural Biology 2008;8():4-4.</p><p>Published online 25 Jan 2008</p><p>PMCID:PMC2275276.</p><p></p

Multiple molecular dynamics simulation of the isoforms of human translation elongation factor 1A reveals reversible fluctuations between "open" and "closed" conformations and suggests specific for eEF1A1 affinity for Ca-calmodulin-1

Ctory 9, cyan – trajectory 10, magenta – trajectory 11, yellow – trajectory 12, orange – trajectory 13. Black – average curves.<p><b>Copyright information:</b></p><p>Taken from "Multiple molecular dynamics simulation of the isoforms of human translation elongation factor 1A reveals reversible fluctuations between "open" and "closed" conformations and suggests specific for eEF1A1 affinity for Ca-calmodulin"</p><p>http://www.biomedcentral.com/1472-6807/8/4</p><p>BMC Structural Biology 2008;8():4-4.</p><p>Published online 25 Jan 2008</p><p>PMCID:PMC2275276.</p><p></p

Multiple molecular dynamics simulation of the isoforms of human translation elongation factor 1A reveals reversible fluctuations between "open" and "closed" conformations and suggests specific for eEF1A1 affinity for Ca-calmodulin-5

<p><b>Copyright information:</b></p><p>Taken from "Multiple molecular dynamics simulation of the isoforms of human translation elongation factor 1A reveals reversible fluctuations between "open" and "closed" conformations and suggests specific for eEF1A1 affinity for Ca-calmodulin"</p><p>http://www.biomedcentral.com/1472-6807/8/4</p><p>BMC Structural Biology 2008;8():4-4.</p><p>Published online 25 Jan 2008</p><p>PMCID:PMC2275276.</p><p></p

Multiple molecular dynamics simulation of the isoforms of human translation elongation factor 1A reveals reversible fluctuations between "open" and "closed" conformations and suggests specific for eEF1A1 affinity for Ca-calmodulin-2

<p><b>Copyright information:</b></p><p>Taken from "Multiple molecular dynamics simulation of the isoforms of human translation elongation factor 1A reveals reversible fluctuations between "open" and "closed" conformations and suggests specific for eEF1A1 affinity for Ca-calmodulin"</p><p>http://www.biomedcentral.com/1472-6807/8/4</p><p>BMC Structural Biology 2008;8():4-4.</p><p>Published online 25 Jan 2008</p><p>PMCID:PMC2275276.</p><p></p