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1.  Protein Tyrosine Kinase Panel As a Tool for Anticancer Drug Design 
Acta Naturae  2009;1(3):84-88.
The discovery of the pharmaceutical potential of small molecule inhibitors of oncogenic protein tyrosine kinases is one of the directions in target therapy in oncology. Presently, investigations aiming at developing new therapeutically important inhibitors have to be based on a combination of computational and experimental approaches including biochitalicical, cell-based or in silico screening and the study of the three-dimensional structure of the kinase active center, in complex with an inhibitor, using crystallography and X-ray analysis or molecular modeling. This work is an example of a combination of inhibitor experimental search with the computational analysis of the potential mechanism of the inhibitors' action, which allowed to propose the 2-hydroxyphenol group as a scaffold for the design of new tyrosine kinase inhibitors.
PMCID: PMC3347529  PMID: 22649618
2.  PEDF – A Noninhibitory Serpin with Neurotrophic Activity  
Acta Naturae  2010;2(3):62-71.
The pigment epithelium-derived factor (PEDF) is a glycoprotein with a molecular weight of 50 kDa belonging to the noninhibitory serpin family. It regulates several physiological processes, such as stimulation of retinoblastoma cell differentiation into neuron cells, and facilitation of the growth and viability of photoreceptor cells and neurons of the central nervous system. Moreover, this factor protects neuronal cells against apoptosis. PEDF is not only a neurotrophic factor, but also a natural angiogenesis inhibitor. This protein, as well as its biologically active fragments, possesses significant neuroprotective, neurotrophic, and antiangiogenic capabilities. The precise molecular mechanisms underpinning the effects of PEDF are still not quite clear. However, this protein generates great interest as a promising drug for the therapy of a wide range of neurodegenerative, ophthalmological, and oncological diseases. This review is a summary of what is known today about the structural features, biochemical properties, and multimodal functions of PEDF.
PMCID: PMC3347567  PMID: 22649652
PEDF (pigment epithelium-derived factor); serpin; neurotrophic factor; angiogenesis
3.  The primary structure of E. coli RNA polymerase, Nucleotide sequence of the rpoC gene and amino acid sequence of the beta'-subunit. 
Nucleic Acids Research  1982;10(13):4035-4044.
The primary structure of the E. coli rpoC gene (5321 base pairs) coding the beta'-subunit of RNA polymerase as well as its adjacent segment have been determined. The structure analysis of the peptides obtained by cleavage of the protein with cyanogen bromide and trypsin has confirmed the amino acid sequence of the beta'-subunit deduced from the nucleotide sequence analysis. The beta'-subunit of E. coli RNA polymerase contains 1407 amino acid residues. Its translation is initiated by codon GUG and terminated by codon TAA. It has been detected that the sequence following the terminating codon is strikingly homologous to known sequences of rho-independent terminators.
PMCID: PMC320776  PMID: 6287430

Results 1-3 (3)