Timchenko AA - Search Results

1

Myosin Binding Protein-C Forms Amyloid-Like Aggregates In Vitro.

Bobyleva LG, Shumeyko SA, Yakupova EI, Surin AK, Galzitskaya OV, Kihara H, Timchenko AA, Timchenko MA, Penkov NV, Nikulin AD, Suvorina MY, Molochkov NV, Lobanov MY, Fadeev RS, Vikhlyantsev IM, Bobylev AG. Bobyleva LG, et al. Among authors: timchenko aa. Int J Mol Sci. 2021 Jan 13;22(2):731. doi: 10.3390/ijms22020731. Int J Mol Sci. 2021. PMID: 33450960 Free PMC article.

2

Effect of Single Amino Acid Substitutions by Asn and Gln on Aggregation Properties of Bence-Jones Protein BIF.

Timchenko M, Abdullatypov A, Kihara H, Timchenko A. Timchenko M, et al. Int J Mol Sci. 2019 Oct 20;20(20):5197. doi: 10.3390/ijms20205197. Int J Mol Sci. 2019. PMID: 31635169 Free PMC article.

3

Different amyloid aggregation of smooth muscles titin in vitro.

Yakupova EI, Vikhlyantsev IM, Bobyleva LG, Penkov NV, Timchenko AA, Timchenko MA, Enin GA, Khutzian SS, Selivanova OM, Bobylev AG. Yakupova EI, et al. Among authors: timchenko aa. J Biomol Struct Dyn. 2018 Jul;36(9):2237-2248. doi: 10.1080/07391102.2017.1348988. Epub 2017 Jul 10. J Biomol Struct Dyn. 2018. PMID: 28661225

4

Influence of a Single Point Mutation in the Constant Domain of the Bence-Jones Protein bif on Its Aggregation Properties.

Timchenko MA, Timchenko AA. Timchenko MA, et al. Among authors: timchenko aa. Biochemistry (Mosc). 2018 Feb;83(2):107-118. doi: 10.1134/S0006297918020037. Biochemistry (Mosc). 2018. PMID: 29618297 Free article.

5

Roughness of the globular protein surface: analysis of high resolution X-ray data.

Timchenko AA, Galzitskaya OV, Serdyuk IN. Timchenko AA, et al. Proteins. 1997 Jun;28(2):194-201. Proteins. 1997. PMID: 9188737

6

Dynamics of oligomer formation by denatured carbonic anhydrase II.

Prokhorov DA, Timchenko AA, Uversky VN, Khristoforov VS, Kihara H, Kimura K, Kutyshenko VP. Prokhorov DA, et al. Among authors: timchenko aa. Biochim Biophys Acta. 2008 May;1784(5):834-42. doi: 10.1016/j.bbapap.2008.02.012. Epub 2008 Mar 4. Biochim Biophys Acta. 2008. PMID: 18359304

7

GroES co-chaperonin small-angle X-ray scattering study shows ring orifice increase in solution.

Timchenko AA, Melnik BS, Kihara H, Kimura K, Semisotnov GV. Timchenko AA, et al. FEBS Lett. 2000 Apr 14;471(2-3):211-4. doi: 10.1016/s0014-5793(00)01402-2. FEBS Lett. 2000. PMID: 10767425 Free article.

8

The effect of hepatopancreas homogenate of the Red king crab on HA-based filler.

Ponomareva T, Sliadovskii D, Timchenko M, Molchanov M, Timchenko A, Sogorin E. Ponomareva T, et al. PeerJ. 2020 Feb 12;8:e8579. doi: 10.7717/peerj.8579. eCollection 2020. PeerJ. 2020. PMID: 32095375 Free PMC article.

9

The major mRNP protein YB-1: structural and association properties in solution.

Guryanov SG, Filimonov VV, Timchenko AA, Melnik BS, Kihara H, Kutyshenko VP, Ovchinnikov LP, Semisotnov GV. Guryanov SG, et al. Among authors: timchenko aa. Biochim Biophys Acta. 2013 Feb;1834(2):559-67. doi: 10.1016/j.bbapap.2012.11.007. Epub 2012 Dec 5. Biochim Biophys Acta. 2013. PMID: 23220387

10

Protein globularization during folding. A study by synchrotron small-angle X-ray scattering.

Semisotnov GV, Kihara H, Kotova NV, Kimura K, Amemiya Y, Wakabayashi K, Serdyuk IN, Timchenko AA, Chiba K, Nikaido K, Ikura T, Kuwajima K. Semisotnov GV, et al. Among authors: timchenko aa. J Mol Biol. 1996 Oct 4;262(4):559-74. doi: 10.1006/jmbi.1996.0535. J Mol Biol. 1996. PMID: 8893863

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