Search Results - "Lekontseva, N V"

The Structure of the Hfq Protein from Chromobacterium haemolyticum Revealed a New Variant of Regulation of RNA Binding with the Protein by Lekontseva, N. V., Nikulin, A. D.

“…The structure of the Hfq protein from the bacterium Chromobacterium haemolyticum , which forms crystals in two different spatial groups, has been determined…”
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Crystal‐packing analysis of translation initiation factor 2 reveals new details of its function by Nikonov, O. S., Nikonova, E. Y., Lekontseva, N. V., Nevskaya, N. A., Nikonov, S. V.

“…Eukaryotic and archaeal translation initiation factor 2 in complex with GTP delivers the initiator methionyl‐tRNA to the small ribosomal subunit. Over the past…”
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Structure of a Mutant Form of Translation Regulator Hfq with the Extended Loop L4 by Alipov, A. A., Lekontseva, N. V., Mikhailina, A. O., Fando, M. S., Tishchenko, S. V., Nikulin, A. D.

“…The bacterial protein Hfq is a member of a large family of Lsm proteins, which are characterized by a conserved tertiary structure and form a stable…”
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Erratum to:Structural Investigations of RNA–Protein Complexes in Post-Ribosomal Era by Tishchenko, S. V., Mikhailina, A. O., Lekontseva, N. V., Stolboushkina, E. A., Nikonova, E. Yu, Nikonov, O. S., Nikulin, A. D.

“…An Erratum to this paper has been published: https://doi.org/10.1134/S1063774521340095…”
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Structural Investigations of RNA–Protein Complexes in Post-Ribosomal Era by Tishchenko, S. V., Mikhailina, A. O., Lekontseva, N. V., Stolboushkina, E. A., Nikonova, E. Yu, Nikonov, O. S., Nikulin, A. D.

“…Structural studies of RNA–protein complexes are important for understanding many molecular mechanisms occurring in cells (e.g., regulation of protein synthesis…”
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Supramolecular organization of Hfq-like proteins by Murina, V. N., Selivanova, O. M., Mikhaylina, A. O., Kazakov, A. S., Nikonova, E. Yu, Lekontseva, N. V., Tishchenko, S. V., Nikulin, A. D.

“…Bacterial Hfq proteins are structural homologs of archaeal and eukaryotic Sm/Lsm proteins, which are characterized by a 5-stranded β-sheet and an N-terminal…”
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Determination of the Minimal Fragment of the Poliovirus IRES Necessary for the Formation of a Specific Complex with the Human Glycyl-tRNA Synthetase by Nikonova, E Yu, Mihaylina, A O, Lekontseva, N V, Nikonov, O S, Klyashtorny, V G, Kravchenko, O V, Andreev, D E, Shatsky, I N, Garber, M B

“…Aminoacyl-tRNA synthetases are an ancient enzyme family that specifically charge a tRNA molecule with a cognate amino acid required for protein synthesis…”
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Determination of the minimal fragment of the poliovirus IRES that is necessary for the formation of a specific complex with the human glycyl-tRNA synthetase by Nikonova, E. Yu, Mihaylina, A. O., Lekontseva, N. V., Nikonov, O. S., Klyashtorny, V. G., Kravchenko, O. V., Andreev, D. E., Shatsky, I. N., Garber, M. B.

“…Aminoacyl-tRNA synthetases are an ancient enzyme family that specifically charge a tRNA molecule with a cognate amino acid that is required for protein…”
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