Публикации

Публикации за последние 5 лет, ключевые публикации, патенты.

Conformation transitions of eukaryotic polyribosomes during multi-round translation.

Afonina Z.A, Myasnikov A.G, Shirokov V.A, Klaholz B.P, Spirin A.S.

Nucleic Acids Res. Jan 9;43(1):618-28.
Лаборатория механизмов биосинтеза белка
2015
pdf
Nonhydrolyzable ATP analog 5'-adenylyl-imidodiphosphate (AMP-PNP) does not inhibit ATP-dependent scanning of leader sequence of mRNA.

Sakharov P.A., Sokolov A.S., Agalarov S.Ch.

Biochemistry (Mosc). Jan;80(1):45-9.
Лаборатория механизмов биосинтеза белка
2015
pdf
Formation of new polysomes on free mRNAs in a cell-free translation systems is accompanied by partial disassembly of previously formed polysomes.

Sogorin EA, Agalarov SCh, Spirin AS.

Biochemistry (Mosc) Oct;80(10):1605-1608
Лаборатория механизмов биосинтеза белка
2015
Springer
Identifying RNA recombination events and non-covalent RNA-RNA interactions with the molecular colony technique.

Chetverina HV, Chetverin AB.

Methods Mol Biol. 2015;1240:1-25
Лаборатория биохимии вирусных РНК
2015
PubMed
Structural basis for RNA-genome recognition during bacteriophage Qβ replication.

Gytz H., Mohr D., Seweryn P., Yoshimura Y., Kutlubaeva Z., Dolman F., Chelchessa B., Chetverin A.B., Mulder F.A., Brodersen D.E., Knudsen C.R.

Nucleic Acids Res. 43(22):10893-906
Лаборатория биохимии вирусных РНК
2015
PubMed
Crystallographic analysis of archaeal ribosomal protein L11.

Mitroshin I., Garber M., Gabdulkhakov A.

Acta Cryst., F71, 1083-7
Лаборатория структурных исследований аппарата трансляции
2015
PubMed
Binding of the 5'-triphosphate end of mRNA to the γ-subunit of translation initiation factor 2 of the crenarchaeon Sulfolobus solfataricus.

Arkhipova V., Stolboushkina E., Kravchenko O., Kljashtorny V., Gabdulkhakov A., Garber M., Nikonov S., Märtens B., Bläsi U., Nikonov O.

J Mol Biol., 427, 3086-95.
Лаборатория структурных исследований аппарата трансляции
2015
PubMed
Crystallization and X-ray diffraction studies of a two-domain laccase from Streptomyces griseoflavus.

Tishchenko S., Gabdulkhakov A., Trubitsina L., Zakharova M., Leontievsky A.

Acta Cryst., F71, 1200–1204
Лаборатория структурных исследований аппарата трансляции
2015
PubMed
Structural studies of component of lysoamidase bacteriolytic complex from Lysobacter sp. XL1.

Tishchenko S, Gabdulkhakov A, Melnik B, Kudryakova I, Latypov O, Vasilyeva N, Leontievsky A.

Protein J. pp 1-7
Лаборатория структурных исследований аппарата трансляции
2015
PubMed
Protein–RNA affinity of ribosomal protein L1 mutants does not correlate with the number of intermolecular interactions.

Tishchenko S., Kostareva O., Gabdulkhakov A., Mikhaylina A., Nikonova E., Nevskaya N., Sarskikh A., Piendl W., Garber M. and Nikonov S.

Acta Cryst. D71, 376–386.
Лаборатория структурных исследований аппарата трансляции
2015
PubMed
Structural and functional characterization of two-domain laccase from Streptomyces viridochromogenes.

Trubitsina L.I., Tishchenko S.V., Gabdulkhakov A.G., Lisov A.V., Zakharova M.V., Leontievsky A.A.

Biochimie, 112, 151-159.
Лаборатория структурных исследований аппарата трансляции
2015
PubMed
The activation mechanism of 20-50-Oligoadenylate Synthetase gives new insights into OAS/cGAS triggers of innate immunity.

Lohofener J., Steinke N., Kay-Fedorov P., Baruch P., Nikulin A., Tishchenko S., Manstein D.J. and Fedorov R.

Structure, 23, 1–12.
Лаборатория структурных исследований аппарата трансляции
2015
PubMed
The heptameric SmAP1 and SmAP2 proteins of the crenarchaeon Sulfolobus Solfataricus bind to common and distinct RNA targets.

Märtens B., Bezerra G.A., Kreuter M.J., Grishkovskaya I., Manica A., Arkhipova V., Djinovic-Carugo K. and Bläsi U.

Life, 5, 1264-1281.
Лаборатория структурных исследований аппарата трансляции
2015
PubMed
Studying the properties of domain I of the ribosomal protein L1: incorporation into ribosome and regulation of the L1 operon expression.

Korepanov A.P., Kostareva O.S., Bazhenova M.V., Bubunenko M.G., Garber M.B. and Tishchenko S.V.

Protein J, 34,103-110.
Лаборатория структурных исследований аппарата трансляции
2015
PubMed
Strict experimental evidence that apo-chaperonin GroEL does not accelerate protein folding, although it does accelerate one of its steps.

Marchenko N.Y., Marchenkov V.V., Semisotnov G.V., Finkelstein A V.

Proc Natl Acad Sci USA; 112(50):E6831-2.
Лаборатория физики белка
2015
PubMed

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