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29 results on '"Baratova, L.A."'

1. Soil saprophages as an emerging global source of micronutrients

Author

Gongalsky, K.B., primary, Korobushkin, D.I., additional, Baratova, L.A., additional, Bastrakov, A.I., additional, Degtyarev, M.I., additional, Gorbunova, A.Yu., additional, Ksenofontov, A.L., additional, Lapa, S.A., additional, Lebedev, I.M., additional, and Zaitsev, A.S., additional

Published
2023
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2. Structures of Helical Plant Virus Ribonucleoproteins as Assessed by Tritium Planigraphy and Theoretical Modeling

Author

Dobrov, E.N., Efimov, A.V., and Baratova, L.A.

Subjects
Plant viruses -- Research, Virus diseases of plants -- Research, Ribonucleoproteins -- Research, Tritium -- Research, Proteins -- Structure, Proteins -- Research, Science and technology
Abstract

Byline: E. N. Dobrov (1), A. V. Efimov (2), L. A. Baratova (3) Keywords: ribonucleoproteins; helical plant viruses; tritium planigraphy; spatial structure of proteins; modeling Abstract: This review considers the results of probing the structure of ribonucleoprotein particles of helical plant viruses by tritium planigraphy (TP). This method works by exposing macromolecular targets to a beam of tritium atoms and analyzing the tritium label distribution along the macromolecule length. The TP data combined with theoretical predictions made it possible to propose a structural model of the coat protein for the virions of potato viruses X (the type representative of potexviruses) and A (a potyvirus), which eluded X-ray diffraction analysis so far. TP revealed fine structural differences between the wild-type tobacco mosaic virus (strain U1) and its temperature-sensitive mutant with an altered coat protein and host specificity. The possibilities of using TP for studying the RNA--protein interactions in helical virus particles are discussed. Author Affiliation: (1) Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, 119992, Russia (2) Institute of Protein Research, Russian Academy of Sciences, Pushchino, Moscow Region, 142290, Russia (3) Belozersky Institute of Physico-Chemical Biology, Moscow State University, Moscow, 119992, Russia Article History: Registration Date: 11/12/2004

Published
2004

9. Modified model of the structure of the potato virus X coat protein.

Author

Dobrov, E.N., Nemykh, M.A., Lukashina, E.V., Baratova, L.A., Drachev, V.A., and Efimov, A.V.

Subjects
POTATO virus X, PROTEINS, MOLECULES, MOSAIC viruses, MICROORGANISMS
Abstract

A modified model was proposed for the tertiary structure of the coat protein (CP) molecules in potato virus X (PVX) virions, similar to the original model of 2001 describing the structure of CP of potato virus A, a member of another group of filamentous viruses. According to the new model, CP comprises two main structural domains, namely, a bundle of α-helices, located near the long axis of the virion, and the socalled RNP fold (or abCd fold), located in the vicinity of its surface. The model made it possible to suggest a possible mechanism of the PVX virion structural rearrangement (remodeling) resulting from translational activation of virions by the TGB1 movement protein according to Atabekov and colleagues. [ABSTRACT FROM AUTHOR]

Published
2007
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11. Partial N-terminal amino acid sequences of polypeptides p14 and p12 of encephalomyocarditis virus are identical and correspond to the N-terminus of the viral polyprotein

Author

Ugarova, T.Yu., Siyanova, E.Yu., Svitkin, Yu.V., Kazachkov, Yu.A., Baratova, L.A., and Agol, V.I.

Abstract

Our previous data suggested that translation in an EMC virus RNA-programmed cell-free system from Krebs-2 cells is initiated predominantly at a single site and that the earliest amino acid sequences synthesized correspond to non-structural ‘leader’ polypeptides p14 and p12 [(1982) FEBS Lett. 141, 153–156]. Here, polypeptides p14 and p12 were labelled in vitro by tritiated amino acids, isolated and subjected to automated Edman degradation. Both polypeptides (after the loss of the N-terminal methionine) were shown to contain alanine in position 1 and glutamic acid in positions 5 and 7. These and other data demonstrate that p14 and p12 share a common N-terminal sequence. This sequence coincides precisely with the N-terminus of EMC virus polyprotein sequence deduced from the primary structure of the viral genome [(1984) Nucleic Acids Res., in press]. Thus, the single initiation site operating in our translation system corresponds to the start of the polyprotein molecule.

Published
1984
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13. Investigation of the complex antibiotic INA-5812

Author

Lapchinskaya O.A., Katrukha G.S., Gladkikh E.G., Kulyaeva V.V., Coodan P.V., Topolyan A.P., Alferova V.A., Pogozheva V.V., Sukonnikov M.A., Rogozhin E.A., Prokhorenko I.A., Brylev V.A., Korolev A.M., Slyundina M.S., Borisov R.S., Serebryakova M.V., Shuvalov M.V., Ksenofontov A.L., Stoyanova L.G., Osterman I.A., Formanovsky A.A., Tashlitsky V.N., Baratova L.A., Timofeeva A.V., Tyurin A.P., Lapchinskaya O.A., Katrukha G.S., Gladkikh E.G., Kulyaeva V.V., Coodan P.V., Topolyan A.P., Alferova V.A., Pogozheva V.V., Sukonnikov M.A., Rogozhin E.A., Prokhorenko I.A., Brylev V.A., Korolev A.M., Slyundina M.S., Borisov R.S., Serebryakova M.V., Shuvalov M.V., Ksenofontov A.L., Stoyanova L.G., Osterman I.A., Formanovsky A.A., Tashlitsky V.N., Baratova L.A., Timofeeva A.V., and Tyurin A.P.

Abstract

A concentrate with the antimicrobial activity has been isolated from the culture broth of Streptomyces roseoflavus INA-Ac-5812. Its further fractionation by reversed-phase HPLC has resulted in six fractions. It has been established by MALDI-TOF and ESI-MSn precision mass-spectrometry methods that the main components of the complex antibiotic are several closely related compounds, presumably of a glycopeptide nature. The fraction containing an individual component with a mass of 1845.788 Da has been characterized by UV/Vis absorbance and fluorescence spectra, amino acid analysis, and derivatization with tris(2,6-dimethoxyphenyl)methyl cation. The activity of fractions against pathogenic microbes has been studied. The results allow the supposition that the INA-5812 antibiotic complex is a glyco- or lipoglycopeptide antibiotic of a new type, which is very promising for further study. © 2016, Pleiades Publishing, Ltd.

23. On the activation of pepsinogen

Author

Stepanov, V.M., primary, Timokhina, E.A., additional, Baratova, L.A., additional, Belyanova, L.P., additional, Korzhenko, V.P., additional, and Zhukova, I.G., additional

Published
1971
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