Search

Your search keyword '"Venyaminova AG"' showing total 4 results
Start Over Author "Venyaminova AG" Journal febs letters
4 results on '"Venyaminova AG"'

1. Nuclease-resistant 63-bp trimeric siRNAs simultaneously silence three different genes in tumor cells.

Author

Gvozdeva OV, Gladkih DV, Chernikov IV, Meschaninova MI, Venyaminova AG, Zenkova MA, Vlassov VV, and Chernolovskaya EL

Subjects
ATP Binding Cassette Transporter, Subfamily B antagonists & inhibitors, ATP Binding Cassette Transporter, Subfamily B genetics, Base Sequence, Cell Line, Tumor, Cysteine Endopeptidases genetics, DEAD-box RNA Helicases metabolism, Drug Design, Humans, Kinetics, Proteasome Endopeptidase Complex genetics, RNA Processing, Post-Transcriptional, RNA Stability, RNA, Small Interfering chemical synthesis, Ribonuclease III metabolism, Ribonucleases metabolism, Gene Silencing, RNA, Small Interfering genetics, RNA, Small Interfering therapeutic use
Abstract

We designed a multimeric nuclease-resistant 63-bp trimeric small-interfering RNA (tsiRNA) comprising in one duplex the sequence of siRNAs targeting mRNAs of MDR1, LMP2, and LMP7 genes. We show that such tsiRNA is able to suppress the expression of all the target genes independently and with high efficiency, acting via a Dicer-dependent mechanism. tsiRNA is diced into 42- and 21-bp duplexes inside the cell. tsiRNA-induced gene silencing is characterized by kinetics similar to that of canonical siRNA, while the silencing efficiency is significantly higher than that of canonical siRNA with the same sequence., (© 2017 Federation of European Biochemical Societies.)

Published
2018
Full Text
View/download PDF

2. 42- and 63-bp anti-MDR1-siRNAs bearing 2'-OMe modifications in nuclease-sensitive sites induce specific and potent gene silencing.

Author

Gvozdeva OV, Dovydenko IS, Venyaminova AG, Zenkova MA, Vlassov VV, and Chernolovskaya EL

Subjects
ATP Binding Cassette Transporter, Subfamily B, ATP Binding Cassette Transporter, Subfamily B, Member 1 metabolism, Antineoplastic Agents, Phytogenic pharmacology, Cell Line, Tumor, Cell Survival drug effects, Gene Expression, Gene Knockdown Techniques, Humans, RNA Processing, Post-Transcriptional, RNA, Small Interfering chemistry, RNA, Small Interfering metabolism, Ribose analogs & derivatives, Ribose chemistry, Vinblastine pharmacology, ATP Binding Cassette Transporter, Subfamily B, Member 1 genetics, Drug Resistance, Neoplasm, RNA Interference, RNA, Small Interfering genetics
Abstract

DsRNAs longer than 30bp induce interferon response and global changes in gene expression profile in mammalians. 21bp siRNA and 25/27bp dsiRNA acting via RNA interference mechanism are used for specific gene silencing in this class of organisms. We designed selectively 2'-O-methyl-modified 42 and 63bp anti-MDR1-siRNAs that silence the expression of P-glycoprotein and restore the sensitivity of drug-resistant cancer cells to cytostatic more efficiently than canonical 21bp siRNAs. We also show that they act in a Dicer-independent mode and are devoid of immunostimulating properties. Our findings suggest that 42 and 63bp siRNAs could be used as potential therapeutics., (Copyright © 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)

Published
2014
Full Text
View/download PDF

3. Silencing activity of 2'-O-methyl modified anti-MDR1 siRNAs with mismatches in the central part of the duplexes.

Author

Petrova NS, Meschaninova MI, Venyaminova AG, Zenkova MA, Vlassov VV, and Chernolovskaya EL

Subjects
ATP Binding Cassette Transporter, Subfamily B, Animals, HEK293 Cells, Humans, Nucleotides genetics, RNA, Small Interfering chemistry, Thermodynamics, ATP Binding Cassette Transporter, Subfamily B, Member 1 genetics, ATP Binding Cassette Transporter, Subfamily B, Member 1 metabolism, Base Pair Mismatch, Gene Silencing, RNA, Small Interfering genetics, RNA, Small Interfering metabolism
Abstract

The thermodynamic properties of siRNA duplexes are important for their silencing activity. siRNAs with high thermodynamic stability of both the central part of the duplex and in the whole, usually display low silencing activity. Destabilization of the central part of the siRNA duplex could increase its silencing activity. However, mismatches located in the central part of the duplex could substantially decrease the amount of RNAi efficacy, hindering active RISC formation and function. In this study, we examined the impact of duplex destabilization by nucleotide substitutions in the central part (7-10 nt counting from the 5'-end of the antisense strand) of the nuclease-resistant siRNA on its silencing activity., (Copyright © 2011 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.)

Published
2011
Full Text
View/download PDF

4. Interaction of primer tRNA(Lys3) with the p51 subunit of human immunodeficiency virus type 1 reverse transcriptase: a possible role in enzyme activation.

Author

Zakharova OD, Tarrago-Litvak L, Fournier M, Andreola ML, Repkova MN, Venyaminova AG, Litvak S, and Nevinsky GA

Subjects
Anticodon, Base Sequence, Enzyme Activation, HIV Reverse Transcriptase, HIV-1 enzymology, Kinetics, Macromolecular Substances, Molecular Sequence Data, Protein Binding, RNA, Transfer, Amino Acyl chemistry, RNA-Directed DNA Polymerase chemistry, Spectrometry, Fluorescence, Structure-Activity Relationship, Time Factors, RNA, Transfer, Amino Acyl metabolism, RNA-Directed DNA Polymerase metabolism
Abstract

In the interaction between HIV-1 RT and tRNA(Lys3) each subunit of the heterodimer interacts with tRNA showing a different affinity: Kd (p66) = 23 nM, Kd (p51) = 140 nM. Preincubation of heterodimeric RT with tRNA, at concentrations similar to that of the Kd value for p51, leads to an increase of the catalytic activity on poly(A)-oligo(dT). These results were compared to those using different tRNA analogs: oxidized tRNA, tRNAs lacking one, two or three nucleotides from the 3'-end, or ribo- and deoxyribonucleotides mimicking the anticodon loop sequence. In all cases, tRNA analogs were weaker activators of HIV-1 RT than natural tRNA. A possible mechanism of RT p66/p51 activation by tRNA and its analogs, mediated through the p51 subunit, is discussed.

Published
1995
Full Text
View/download PDF

Catalog

Books, media, physical & digital resources
See catalog results