Search Results - "RECHINSKY, V. O"

Mutants of T7 RNA polymerase that are able to synthesize both RNA and DNA by Kostyuk, D.A., Dragan, S.M., Lyakhov, D.L., Rechinsky, V.O., Tunitskaya, V.L., Chernov, B.K., Kochetkov, S.N.

“…A mutant T7 RNA polymerase (T7 RNAP) having two amino-acid substitutions (Y639F and S641A) is altered in its specificity towards nucleotide substrates, but is…”
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Suppression of nonsense mutations in the Dystrophin gene by a suppressor tRNA gene by Kiselev, A V, Ostapenko, O V, Rogozhkina, E V, Kholod, N S, Seit Nebi, A S, Baranov, A N, Lesina, E A, Ivashchenko, T E, Sabetskiĭ, V A, Shavlovskiĭ, M M, Rechinskiĭ, V O, Kiselev, L L, Baranov, V C

“…Nonsense mutations in the dystrophin gene are the cause of Duchenne muscular dystrophy (DMD) in 10-15% of patients. In such an event, one approach to gene…”
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On the functional role of the Tyr-639 residue of bacteriophage T7 RNA polymerase by Rechinsky, V.O., Kostyuk, D.A., Tunitskaya, V.L., Kochetkov, S.N.

“…Substitution or Asp for a Tyr residue normally present at position 639 of the bacteriophage T7 RNA polymerase leads to a drastic drop in the enzymatic…”
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Tyr-571 is involved in the T7 RNA polymerase binding to its promoter by Rechinsky, V.O., Tunitskaya, V.L., Dragan, S.M., Kostyuk, D.A., Kochetkov, S.N.

“…The in vitro studies of three T7 RNA polymerase point mutants suggest that substitutions of Ala and Thr for Pro-563 and of Ser for Tyr-571 have little effect…”
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The mechanism of pyrophosphorolysis of RNA by RNA polymerase. Endowment of RNA polymerase with artificial exonuclease activity by Rozovskaya, T A, Rechinsky, V O, Bibilashvili, R S, Karpeisky MYa, Tarusova, N B, Khomutov, R M, Dixon, H B

“…DNA-directed RNA polymerase from Escherichia coli can break down RNA by catalysing the reverse of the reaction: NTP + (RNA)n = (RNA)n+1 + PPi where n indicates…”
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Lys631 residue in the active site of the bacteriophage T7 RNA polymerase : affinity labeling and site-directed mutagenesis by MAKSIMOVA, T. G, MUSTAYEV, A. A, ZAYCHIKOV, E. F, LYAKHOV, D. L, TUNITSKAYA, V. L, AKBAROV, A. K, LUCHIN, S. V, RECHINSKY, V. O, CHERNOV, B. K, KOCHETKOV, S. N

“…A highly selective affinity labeling of T7 RNA polymerase with the o-formylphenyl ester of GMP and [alpha-32P]UTP was carried out. The site of the labeling was…”
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Functional expression of eukaryotic polypeptide chain release factors 1 and 3 by means of baculovirus/insect cells and complex formation between the factors by Frolova, L.Y, Simonsen, J.L, Merkulova, T.I, Litvinov, D.Y, Martensen, P.M, Rechinsky, V.O, Camonis, J.H, Kisselev, L.L, Justesen, J

“…Translation termination in eukaryotes is governed by termination codons in mRNA and two release factors, eRF1 and eRF3. In this work, human eRF1 and eRF3 have…”
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Interactions of the HIV-1 reverse transcriptase ‘AZT-resistant’ mutant with substrates and AZT-TP by Pokholok, Dmitry K., Gudima, Severin O., Yesipov, Dmitry S., Dobrynin, Vladimir N., Rechinsky, Vladimir O., Kochetkov, Sergey N.

“…To investigate the biochemical basis of the HIV-1 resistance to AZT we obtained the RT mutant containing four amino acid substitutions by an…”
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Inactivation of bacteriophage T7 DNA-dependent RNA polymerase by 5'-p-fluorosulfonylbenzoyladenosine : identification of the modification site and the effect of the modification on enzyme action by TUNITSKAYA, V. L, AKBAROV, A. K, LUCHIN, S. V, MEMELOVA, L. V, RECHINSKY, V. O, KOCHETKOV, S. N

“…Bacteriophage T7 RNA polymerase was covalently modified by 5'-[4-fluorosulfonyl)benzoyl]adenosine (4-FSO2BzAdo). The modified enzyme lacks the ability to…”
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Targeted mutagenesis identifies Asp-569 as a catalytically critical residue in T7 RNA polymerase by Rechinsky, V O, Chernov, B K, Dragan, S M, Kostyuk, D A, Tunitskaya, V L, Kochetkov, S N

“…In order to look more closely at a well-conserved region in T7 RNA polymerase (T7 RNAP) containing, as shown earlier, the functionally essential residues…”
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Development of the system ensuring a high-level expression of hepatitis C virus nonstructural NS5B and NS5A proteins by Ivanov, Alexander V., Korovina, Anna N., Tunitskaya, Vera L., Kostyuk, Dmitry A., Rechinsky, Vladimir O., Kukhanova, Marina K., Kochetkov, Sergey N.

“…The plasmid pET-21d-2c-5BΔ55 effectively expressing a C-terminally truncated form (NS5BΔ55) of the hepatitis C virus (HCV) RNA-dependent RNA polymerase (RdRp)…”
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Random mutagenesis of the gene for bacteriophage T7 RNA polymerase by Rechinsky, V O, Kostyuk, D A, Lyakhov, D L, Chernov, B K, Kochetkov, S N

“…Random mutagenesis of the gene for bacteriophage T7 RNA polymerase was used to identify functionally essential amino acid residues of the enzyme. A two-plasmid…”
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Extracellular ribonuclease from Bacillus thuringiensis by Chepurnova, N K, Liakhov, D L, Rechinskiĭ, V O, Karpeĭskiĭ, M Ia

“…The ability of the strain Bacillus thuringiensis var. subtoxicus to produce extracellular ribonuclease (ribonuclease Bt) was studied. It was found that the…”
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Reverse transcriptase-based DNA vaccines against drug-resistant HIV-1 tested in a mouse model by Isaguliants, Maria G., Zuber, Bartek, Boberg, Andreas, Sjöstrand, Dan, Belikov, Sergey V., Rollman, Erik, Zuber, Anne Kjerrström, Rechinsky, Vladimir O., Rytting, Ann-Sofie, Källander, Clas F.R., Hinkula, Jorma, Kochetkov, Sergey N., Liu, Margaret, Wahren, Britta

“…Drug resistance is becoming a problem in the treatment of the human immunodeficiency virus type one (HIV-1). To obtain therapeutic DNA vaccines that would…”
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Tyr-571 is involved in the T7 RNA polymerase binding to its promoter by RECHINSKY, V. O, TUNITSKAYA, V. L, DRAGAN, S. M, KOSTYUK, D. A, KOCHETKOV, S. N

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Interactions of the HIV-1 reverse transcriptase AZT-resistant mutant with substrates and AZT-TP by POKHOLOK, D. K, GUDIMA, S. O, YESIPOV, D. S, DOBRYNIN, V. N, RECHINSKY, V. O, KOCHETKOV, S. N

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Inactivation of bacteriophage T7 DNA-dependent RNA polymerase by 5'-p-fluorosulfonyl-benzoyladenosine. Identification of the modification site and the effect of the modification on enzyme action by Tunitskaya, V L, Akbarov, A K, Luchin, S V, Memelova, LV, Rechinsky, VO, Kochetkov, S N

“…Bacteriophage T7 RNA polymerase was covalently modified by 5'-(4-fluorosulfonyl)-benzoyl)adenosine (4-FSO sub(2)BzAdo). The modified enzyme lacks the ability…”
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