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V P Almazov

Publications and source records attributed to V P Almazov.

4 recordsLinked to original sources
PubMedDate not supplied

[Construction of chimeric tumor suppressor p53 resistant to the dominant-negative interaction with p53 mutants].

A chimeric p53 cDNA was constructed so that the fragment coding for 39 residues of the chicken p53 tetramerization domain replaced the corresponding region of human p53. The chimeric cDNA substantially inhibited the colony-forming ability of transfected human and mouse cells, suggesting a suppressory potential for its product. The chimeric p53 activated promoters containing p53-responsive elements. In contrast to wild-type human p53, the chimeric p53 remained capable of transcription activation in the presence of dominant-negative mutant p53-His175. This makes the chimeric p53 a convenient model for elaborating gene therapy protocols for tumors with dominant-negative p53 forms. The chimeric p53 may be used to study the role of transdominance of p53 mutants in carcinogenesis and the interactions of p53 with related transcription factors (p73, p63).

Amino Acid Sequence↗
PubMedDate not supplied

[Dominant-negative inactivation of p53: the effect of the proportion between trans-dominant inhibitor and its target].

Dominant-negative mutations of the p53 tumor suppressor gene and oligomerization of the mutant and wild-type p53 are considered responsible for functional inactivation of the p53 tetramer. Although dominant-negative inactivation of p53 is well reproducible in experimental systems, its contribution to processes occurring in tumor cells heterozygous at p53 is still unclear. To study the effect of dominant-negative inhibitor GSE22 on the p53 activity, cultures coexpressing GSE22 and tetracycline-suppressible p53 were derived from p53-negative cell lines. Transcriptional activity and expression of p53 proved to depend on the proportion between p53 and GSE22. The dominant-negative effect was observed only when GSE22 was in a multifold excess to p53. GSE22 was shown to be suitable for complete reversible inactivation of p53.

Animals↗
PubMedDate not supplied

[A model of enzymatic decarboxylation of glutamic acid].

Interaction of glutamate decarboxylase with its adequate substrate and some quasi-substrates was studied by spectrokinetic, quantum-chemical and some other approaches. It was shown that in the course of decarboxylation an abortive transamination of pyridoxal-5'-phosphate leading to the enzyme inactivation does occur. Identification of intermediate coenzyme-substrate complexes allowed to formulate a model of enzymatic decarboxylation taking into account both the main and abortive reactions. The analysis of electronic structure of the intermediates revealed some of the factors determining the functional specificity of the reaction under study.

Circular Dichroism↗