Balobanov V - Search Results

1

Under Conditions of Amyloid Formation Bovine Carbonic Anhydrase B Undergoes Fragmentation by Acid Hydrolysis.

Marchenkov V, Ryabova N, Balobanov V, Glukhov A, Ilyina N, Katina N. Marchenkov V, et al. Among authors: balobanov v. Biomolecules. 2021 Oct 30;11(11):1608. doi: 10.3390/biom11111608. Biomolecules. 2021. PMID: 34827606 Free PMC article.

2

The presence of cross-β-structure as a key determinant of carbonic anhydrase amyloid fibrils cytotoxicity.

Fakhranurova L, Balobanov V, Ryabova N, Glukhov A, Ilyina N, Markelova N, Marchenkov V, Katina N. Fakhranurova L, et al. Among authors: balobanov v. Biochem Biophys Res Commun. 2020 Apr 2;524(2):453-458. doi: 10.1016/j.bbrc.2020.01.113. Epub 2020 Jan 29. Biochem Biophys Res Commun. 2020. PMID: 32007272

3

Carbonic anhydrase amyloid fibrils composed of laterally associated protofilaments show reduced cytotoxicity.

Ryabova N, Fakhranurova L, Balobanov V, Marchenkov V, Glukhov A, Ilyina N, Kochetov A, Suvorina M, Surin A, Katina N. Ryabova N, et al. Among authors: balobanov v. Biochem Biophys Res Commun. 2022 Feb 19;593:46-51. doi: 10.1016/j.bbrc.2022.01.040. Epub 2022 Jan 13. Biochem Biophys Res Commun. 2022. PMID: 35051782

4

Folding intermediate and folding nucleus for I-->N and U-->I-->N transitions in apomyoglobin: contributions by conserved and nonconserved residues.

Samatova EN, Melnik BS, Balobanov VA, Katina NS, Dolgikh DA, Semisotnov GV, Finkelstein AV, Bychkova VE. Samatova EN, et al. Among authors: balobanov va. Biophys J. 2010 Apr 21;98(8):1694-702. doi: 10.1016/j.bpj.2009.12.4326. Biophys J. 2010. PMID: 20409491 Free PMC article.

5

Loops linking secondary structure elements affect the stability of the molten globule intermediate state of apomyoglobin.

Majorina MA, Balobanov VA, Uversky VN, Melnik BS. Majorina MA, et al. Among authors: balobanov va. FEBS Lett. 2020 Oct;594(20):3293-3304. doi: 10.1002/1873-3468.13905. Epub 2020 Sep 2. FEBS Lett. 2020. PMID: 32770670 Free article.

6

How strong are side chain interactions in the folding intermediate?

Samatova EN, Katina NS, Balobanov VA, Melnik BS, Dolgikh DA, Bychkova VE, Finkelstein AV. Samatova EN, et al. Among authors: balobanov va. Protein Sci. 2009 Oct;18(10):2152-9. doi: 10.1002/pro.229. Protein Sci. 2009. PMID: 19693934 Free PMC article.

7

Use of Fluorescent Nucleotides to Map RNA-Binding Sites on Protein Surface.

Balobanov V, Lekontseva N, Mikhaylina A, Nikulin A. Balobanov V, et al. Methods Mol Biol. 2020;2113:251-262. doi: 10.1007/978-1-0716-0278-2_17. Methods Mol Biol. 2020. PMID: 32006319

8

Crystal structures and RNA-binding properties of Lsm proteins from archaea Sulfolobus acidocaldarius and Methanococcus vannielii: Similarity and difference of the U-binding mode.

Lekontseva N, Mikhailina A, Fando M, Kravchenko O, Balobanov V, Tishchenko S, Nikulin A. Lekontseva N, et al. Among authors: balobanov v. Biochimie. 2020 Aug;175:1-12. doi: 10.1016/j.biochi.2020.05.001. Epub 2020 May 15. Biochimie. 2020. PMID: 32422160

9

An Experimental Tool to Estimate the Probability of a Nucleotide Presence in the Crystal Structures of the Nucleotide-Protein Complexes.

Nemchinova M, Balobanov V, Nikonova E, Lekontseva N, Mikhaylina A, Tishchenko S, Nikulin A. Nemchinova M, et al. Among authors: balobanov v. Protein J. 2017 Jun;36(3):157-165. doi: 10.1007/s10930-017-9709-y. Protein J. 2017. PMID: 28317076

10

Dimerization of long hibernation promoting factor from Staphylococcus aureus: Structural analysis and biochemical characterization.

Usachev KS, Fatkhullin BF, Klochkova EA, Miftakhov AK, Golubev AA, Bikmullin AG, Nurullina LI, Garaeva NS, Islamov DR, Gabdulkhakov AG, Lekontseva NV, Tishchenko SV, Balobanov VA, Khusainov IS, Yusupov MM, Validov SZ. Usachev KS, et al. Among authors: balobanov va. J Struct Biol. 2020 Jan 1;209(1):107408. doi: 10.1016/j.jsb.2019.107408. Epub 2019 Oct 25. J Struct Biol. 2020. PMID: 31669310

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