Výsledky vyhledávání - "I N Shatskiĭ"

Internal ribosome entry sites of viral and cellular RNAs

Autor: I N Shatskiĭ, Daria Sizova

Publikováno v: Molecular Biology. 34:157-167

In recent years mechanism of internal initation of translation in eukaryotic cells commands the attention of molecular biologists in increasing frequency. Ten years ago, experiments with picornaviruses demonstrated the ability of 40S ribosomal subuni

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::e9e6806e79d6e6d2db87c0a9d9cdf989
https://doi.org/10.1007/bf02759634

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[Binding of the IRES of hepatitis C virus RNA to the 40S ribosomal subunit: role of protein p40]

Autor: A A, Malygin, Z V, Bochkaeva, E I, Bondarenko, O A, Kosinova, V B, Loktev, I N, Shatskiĭ, G G, Karpova

Publikováno v: Molekuliarnaia biologiia. 43(6)

Ribosomal protein p40 is a structural component of the 40S ribosomal subunit, which is partially homologuos to prokaryotic ribosomal protein S2 and has a long eukaryote-specific C-terminal region. In the present work, we have studied the binding of t

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::4739bd937e5993a63fb0fbfb0d8da5e2
https://pubmed.ncbi.nlm.nih.gov/20088384

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[Molecular environment of the IIId subdomain of the IRES element of hepatitits C virus RNA on the human 40S ribosomal subunit]

Autor: E S, Babaĭlova, D M, Graĭfer, A A, Malygin, I N, Shatskiĭ, I, Shtal, G G, Karpova

Publikováno v: Bioorganicheskaia khimiia. 35(1)

The molecular environment of the key subdomain IIId of the internal ribosome entry site (IRES) element of hepatitis C virus (HCV) RNA in the binary complex with the human 40S ribosomal subunit was studied. To this end, HCV IRES derivatives bearing pe

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::5debaf5c0b7d6a2d9da003bcf65225bc
https://pubmed.ncbi.nlm.nih.gov/19377528

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[Approach to identifying the functionally important segments of RNA, based on complementation-addressed modification]

Autor: A A, Malygin, D M, Graĭfer, E S, Laletina, I N, Shatskiĭ, G G, Karpova

Publikováno v: Molekuliarnaia biologiia. 37(6)

An approach based on complementation-addressed modification of nucleic acids by oligodeoxyribonucleotide derivatives was proposed for changing the spatial structure of particular RNA sites in order to study their role in the biological activity of th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::908808f80b28a58a38da8c409a1fcb1c
https://pubmed.ncbi.nlm.nih.gov/14714498

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[Study of molecular mechanisms of translation initiation in mammals using in vitro reconstruction of initiation complexes]

Autor: I N, Shatskiĭ

Publikováno v: Molekuliarnaia biologiia. 35(4)

Papers on the mechanisms of translation initiation in mammals studied by reconstruction of initiation complexes from individual components are reviewed. The author points to the constraints of this approach and to the pitfalls ignoring which one migh

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::0a83ea47c325242fb357afafb63d1c18
https://pubmed.ncbi.nlm.nih.gov/11524949

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[Internal ribosome entry sites in viral and cellular RNA]

Autor: D V, Sizova, I N, Shatskiĭ

Publikováno v: Molekuliarnaia biologiia. 34(2)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c713e1574f7f1d56da95f00266ab0bd7
https://pubmed.ncbi.nlm.nih.gov/10779943

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[Internal initiation of translation in eukaryotes. Chemical probing of the encephalomyocarditis virus RNA IRES-element in the 48S preinitiation complex]

Autor: A V, Boroviagin, M V, Ezrokhi, I N, Shatskiĭ

Publikováno v: Molekuliarnaia biologiia. 29(3)

Using in vitro T7 polymerase system, the transcript containing the IRES-element (nts 315-833), and the initial part of the coding sequence of encephalomyocarditis virus (EMCV) RNA (nts 834-1155) was prepared. Its complex with the 40S ribosomal subuni

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::cf258a629ff77ea7cd82445c3dfb81ce
https://pubmed.ncbi.nlm.nih.gov/8552069

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[Measurement of the distance between the 3'- and 5'-ends of ribosome-bound template polynucleotide by using the singlet-singlet energy transfer method]

Autor: A B, Bakin, A G, Evstaf'eva, O F, Borisova, I N, Shatskiĭ, A A, Bogdanov

Publikováno v: Doklady Akademii nauk SSSR. 294(4)

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::73975d035f1eebb90b7f2cd43b1c0f12
https://pubmed.ncbi.nlm.nih.gov/2441942

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[Availability of DNP-modified 5'- and 3'-ends of the poly(U) fragment bound to the 30S ribosomal subunit for interaction with antibodies]

Autor: A G, Evstaf'eva, I N, Shatskiĭ

Publikováno v: Biokhimiia (Moscow, Russia). 49(7)

Modification of the 5'- or 3'-terminal nucleotide residues of poly(U) by dinitrophenyl haptens was carried out. The accessibility of the modified ends of short poly(U) (20-70 nucleotide residues) bound to the 30S subunit of E. coli ribosomes for the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::caaebe1ad4c447d4fd3231f835b67de1
https://pubmed.ncbi.nlm.nih.gov/6566578

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[Modification of sulfhydryl groups in ribosomal proteins by a dinitrophenyl hapten]

Autor: M S, Kozhukharova, T F, Bystrova, I N, Shatskiĭ

Publikováno v: Bioorganicheskaia khimiia. 9(7)

A dinitrophenyl hapten capable of protein SH-group modification was synthesized and the specificity of its reaction with SH-groups of the E. coli ribosomal proteins was studied. The possibility of incorporation of the Dnp-modified protein into riboso

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::e68f744ebf91abe638eacfe16780e6e2
https://pubmed.ncbi.nlm.nih.gov/6207845

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