Publications by authors named "E A Riazanova"

Oligonucleotides with 1,2-diol grouping were prepared from 2'-O-[2-(2,3-dihydroxypropyl)amino-2-oxo-ethyl]uridine 3'-phosphoramidite. The thermal stability of modified DNA duplexes and their ability to form complexes with the p50 subunit of the NF-kappaB transcription factor and (cytosine-5)-DNA methyltransferase SsoII were studied. The periodate oxidation of the l,2-diol grouping of the oligonucleotides resulted in reactive 2'-aldehyde derivatives.

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To study the age-related features of growth areas and to detect the x-ray background of recurrent deformities in patients with rickets-like diseases, the investigators analyzed knee arthrograms in 74 patients aged 4 to 16 years (28 and 46 patients with vitamin D-deficiency or vitamin D-resistant rickets (phosphate diabetes), respectively) prior to treatment and in the late period.

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The study is concerned with proapoptotic properties of chimera peptides which incorporate sequences of inhibitors of cyclin kinases p161NK4a and p21CIP/WAF1 as well as internalized sequences (Antp and tat). Sequences of the p16 type appeared to be more cytotoxic than the p21 one. Cytotoxic effect proved dependent on orientation with respect to the C or N terminal point of a polypeptide chain rather than on chimera sequence extent.

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Effects of calpain inhibitors on thyroid follicle conversion into monolayer was investigated. Human and rat primary thyroid cultures require the follicular structure after enzyme disaggregation of native tissue fragments. Removal of thyroid-stimulating hormone (TSH) from the culture medium causes migration of thyrocytes from follicles into monolayer, some differences were noted in conversion of rat and human thyroid follicles.

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A procedure for quantitatively estimating the activity of calpains involved chromatography on the hydrophobic sorbent octyl-Sepharose CL-4B, which enabled one to measure the true proteinase activity unmasked by the inhibitors calpastatins. After binding with the sorbent and removal of the contaminating proteins the calpains were eluted using 0.5% sodium cholate as well as by an increase of pH value from 7.

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