[Inhibition of herpes simplex virus helicase UL9 by netropsin derivatives and antiviral activities of bis-netropsins].

Data obtained show that antiviral activities of bis-linked netropsin derivatives are targeted by specific complexes formed by helicase UL9 of herpes simplex virus type 1 with viral DNA replication origins, represented by two OriS sites and one OriL site. According to the results of footprinting studies bis-netropsins get bound selectively to an A+T-cluster which separates interaction sites I and II for helicase UL9 in OriS. Upon binding to DNA bis-netropsins stabilize a structure of the A+T-cluster and inhibit thermal fluctuation-induced opening of AT- base pairs which is needed for local unwinding of DNA by helicase UL9.

[Complex of the herpes simplex virus initiator protein UL9 with DNA as a platform for the design of a new type of antiviral drugs].

The protein binding to the origin of replication of the herpes simplex virus type 1 (HSV-1) is DNA helicase encoded by the UL9 gene of the herpes virus. The protein specifically binds to two binding sites in the viral DNA replication origins OriS or OriL. In order to determine the role of the UL9 protein in the initiation of replication and find efficient inhibitors of the UL9 activity, we have synthesized a recombinant UL9 protein expressed in E.

[Surgical treatment policy using recombinant prourokinase for submacular hemorrhages].

An immunofluorescence technique was used to study the transretinal penetration of intravitreal fibrinolytic agent Hemase (a recombinant urokinase) in an experiment on 4 rabbit eyes. Hemase (54 kD) was proved to be able to penetrate across all retinal layers 2 hours after intravitreal administration. The efficacy of Hemase was tested in the treatment of submacular hemorrhages (SMH) of various etiology.

[Urokinase induces adhesion of monocytes to fibrinogen].

Urokinase activates adhesion of monocytic U937 cells to fibrinogen-coated surface. This effect is due to urokinase proteolytic activity and does not depend on the urokinase binding to its receptor.

[The effect of intracellular concentrations of tRNA, corresponding to the rare arginine codons AGG and AGA, on the gene expression in Escherichia coli].

Influence of increased arginine concentrations of tRNA's corresponding to rare codons AGG and AGA was studied in the model system constructed earlier. The model system is a chimeric gene consisting of CAT gene fragment, part of the gene encoding for alpha-domain of beta-galactosidase E. coli and a series of synthetic inserts enriched with codons AGG and AGA.

[Rare codons and gene expression in Escherichia coli].

Influence of rare codons upon gene expression in E. coli was investigated. The chimeric gene was created combining CAT gene and a fragment of the gene, encoding for alpha-domain of beta-galactosidase.