Search Results - "Kashparov, I.A"

Dataset concerning GroEL chaperonin interaction with proteins by Marchenkov, V.V., Marchenko, N.Yu, Kaysheva, A.L., Kotova, N.V., Kashparov, I.A., Semisotnov, G.V.

“…GroEL chaperonin is well-known to interact with a wide variety of polypeptide chains. Here we show the data related to our previous work…”
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Affinity chromatography of chaperones based on denatured proteins: Analysis of cell lysates of different origin by Marchenko, N. Yu, Sikorskaya, E.V., Marchenkov, V.V., Kashparov, I.A., Semisotnov, G.V.

“…Molecular chaperones are involved in folding, oligomerization, transport, and degradation of numerous cellular proteins. Most of chaperones are heat-shock…”
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Modeling and Integral X-Ray, Optical, and MRI Visualization of Multiorgan Metastases of Orthotopic 4T1 Breast Carcinoma in BALB/c Mice by Baklaushev, V. P., Grinenko, N. F., Yusubalieva, G. M., Abakumov, M. A., Gubskii, I. L., Cherepanov, S. A., Kashparov, I. A., Burenkov, M. S., Rabinovich, E. Z., Ivanova, N. V., Antonova, O. M., Chekhonin, V. P.

“…A model of highly metastasizing orthotopic allogeneic breast carcinoma was reproduced and standardized in experiments on BALB/c mice. 4T1 cells characterized…”
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Apomyoglobin mutants with single point mutations at Val10 can form amyloid structures at permissive temperature by Katina, N. S., Ilyina, N. B., Kashparov, I. A., Balobanov, V. A., Vasiliev, V. D., Bychkova, V. E.

“…Formation of amyloid-like protein aggregates in human organs and tissues underlies many serious diseases, therefore being in the focus of numerous biochemical,…”
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Ligands regulate GroEL thermostability by Surin, A.K, Kotova, N.V, Kashparov, I.A, Marchenkov, V.V, Marchenkova, S.Yu, Semisotnov, G.V

“…Escherichia coli heat-shock proteins GroEL and GroES stimulate (in an ATP-dependent manner) the folding of various proteins. In this study scanning…”
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Proteins of the Thermus thermophilus ribosome. Purification of proteins from the large ribosomal subunit by Sedelnikova, S E, Shikaeva, O S, Avlijakulov, N K, Muranova, T A, Markova, L F, Kashparov, I A, Garber, M B

“…Special procedures have been developed to isolate and purify 26 of the 30 individual proteins of the large ribosomal subunit from Thermus thermophilus. Sixteen…”
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Tyrosine residues in the C-terminal domain of the elongation factor G are essential for its interaction with the ribosome [Escherichia coli] by ALAKHOV, Yuly B., ZALITE, Indulis K., KASHPAROV, Ivan A.

“…Chemical modification of the elongation factor G (EF‐G) with tetranitromethane and iodine has been studied. It has been shown by spectrophotometric titration…”
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