Dovidchenko NV - Search Results

1

Insulin and Lispro Insulin: What is Common and Different in their Behavior?

Selivanova OM, Suvorina MY, Surin AK, Dovidchenko NV, Galzitskaya OV. Selivanova OM, et al. Among authors: dovidchenko nv. Curr Protein Pept Sci. 2017;18(1):57-64. doi: 10.2174/1389203717666160526122421. Curr Protein Pept Sci. 2017. PMID: 27226198 Review.

2

Prediction of number and position of domain boundaries in multi-domain proteins by use of amino acid sequence alone.

Dovidchenko NV, Lobanov MY, Galzitskaya OV. Dovidchenko NV, et al. Curr Protein Pept Sci. 2007 Apr;8(2):189-95. doi: 10.2174/138920307780363460. Curr Protein Pept Sci. 2007. PMID: 17430200 Review.

3

Prediction of loop regions in protein sequence.

Dovidchenko NV, Bogatyreva NS, Galzitskaya OV. Dovidchenko NV, et al. J Bioinform Comput Biol. 2008 Oct;6(5):1035-47. doi: 10.1142/s0219720008003758. J Bioinform Comput Biol. 2008. PMID: 18942165

4

Modeling amyloid fibril formation.

Dovidchenko NV, Galzitskaya OV. Dovidchenko NV, et al. Biochemistry (Mosc). 2011 Mar;76(3):366-73. doi: 10.1134/s0006297911030114. Biochemistry (Mosc). 2011. PMID: 21568873

5

How to determine the size of folding nuclei of protofibrils from the concentration dependence of the rate and lag-time of aggregation. I. Modeling the amyloid protofibril formation.

Dovidchenko NV, Finkelstein AV, Galzitskaya OV. Dovidchenko NV, et al. J Phys Chem B. 2014 Feb 6;118(5):1189-97. doi: 10.1021/jp4083294. Epub 2014 Jan 24. J Phys Chem B. 2014. PMID: 24404849

6

How to determine the size of folding nuclei of protofibrils from the concentration dependence of the rate and lag-time of aggregation. II. Experimental application for insulin and LysPro insulin: aggregation morphology, kinetics, and sizes of nuclei.

Selivanova OM, Suvorina MY, Dovidchenko NV, Eliseeva IA, Surin AK, Finkelstein AV, Schmatchenko VV, Galzitskaya OV. Selivanova OM, et al. Among authors: dovidchenko nv. J Phys Chem B. 2014 Feb 6;118(5):1198-206. doi: 10.1021/jp4083568. Epub 2014 Jan 24. J Phys Chem B. 2014. PMID: 24428561

7

What handedness and angles between helices has the studied three-helical protein domain?

Pereyaslavets LB, Glyakina AV, Dovidchenko NV, Sokolovskiy IV, Galzitskaya OV. Pereyaslavets LB, et al. Among authors: dovidchenko nv. Bioinformatics. 2015 Mar 15;31(6):963-5. doi: 10.1093/bioinformatics/btu737. Epub 2014 Nov 10. Bioinformatics. 2015. PMID: 25388147

8

Mechanisms of amyloid fibril formation.

Dovidchenko NV, Leonova EI, Galzitskaya OV. Dovidchenko NV, et al. Biochemistry (Mosc). 2014 Dec;79(13):1515-27. doi: 10.1134/S0006297914130057. Biochemistry (Mosc). 2014. PMID: 25749162 Free article. Review.

9

Computational Approaches to Identification of Aggregation Sites and the Mechanism of Amyloid Growth.

Dovidchenko NV, Galzitskaya OV. Dovidchenko NV, et al. Adv Exp Med Biol. 2015;855:213-39. doi: 10.1007/978-3-319-17344-3_9. Adv Exp Med Biol. 2015. PMID: 26149932 Review.

10

One of the possible mechanisms of amyloid fibrils formation based on the sizes of primary and secondary folding nuclei of Aβ40 and Aβ42.

Dovidchenko NV, Glyakina AV, Selivanova OM, Grigorashvili EI, Suvorina MY, Dzhus UF, Mikhailina AO, Shiliaev NG, Marchenkov VV, Surin AK, Galzitskaya OV. Dovidchenko NV, et al. J Struct Biol. 2016 Jun;194(3):404-14. doi: 10.1016/j.jsb.2016.03.020. Epub 2016 Mar 22. J Struct Biol. 2016. PMID: 27016282

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