Kopylov K - Search Results

1

The visualCMAT: A web-server to select and interpret correlated mutations/co-evolving residues in protein families.

Suplatov D, Sharapova Y, Timonina D, Kopylov K, Švedas V. Suplatov D, et al. Among authors: kopylov k. J Bioinform Comput Biol. 2018 Apr;16(2):1840005. doi: 10.1142/S021972001840005X. Epub 2017 Dec 28. J Bioinform Comput Biol. 2018. PMID: 29361894

2

Mustguseal: a server for multiple structure-guided sequence alignment of protein families.

Suplatov DA, Kopylov KE, Popova NN, Voevodin VV, Švedas VK. Suplatov DA, et al. Among authors: kopylov ke. Bioinformatics. 2018 May 1;34(9):1583-1585. doi: 10.1093/bioinformatics/btx831. Bioinformatics. 2018. PMID: 29309510

3

Human p38α mitogen-activated protein kinase in the Asp168-Phe169-Gly170-in (DFG-in) state can bind allosteric inhibitor Doramapimod.

Suplatov D, Kopylov K, Sharapova Y, Švedas V. Suplatov D, et al. Among authors: kopylov k. J Biomol Struct Dyn. 2019 May;37(8):2049-2060. doi: 10.1080/07391102.2018.1475260. Epub 2018 Dec 5. J Biomol Struct Dyn. 2019. PMID: 29749295

4

CASBench: A Benchmarking Set of Proteins with Annotated Catalytic and Allosteric Sites in Their Structures.

Zlobin A, Suplatov D, Kopylov K, Švedas V. Zlobin A, et al. Among authors: kopylov k. Acta Naturae. 2019 Jan-Mar;11(1):74-80. Acta Naturae. 2019. PMID: 31024751 Free PMC article.

5

Conformational transitions induced by NADH binding promote reduction half-reaction in 2-hydroxybiphenyl-3-monooxygenase catalytic cycle.

Kopylov K, Kirilin E, Švedas V. Kopylov K, et al. Biochem Biophys Res Commun. 2023 Jan 8;639:77-83. doi: 10.1016/j.bbrc.2022.11.066. Epub 2022 Nov 26. Biochem Biophys Res Commun. 2023. PMID: 36470075

6

Fe(III)-TAML activator: a potent peroxidase mimic for chemiluminescent determination of hydrogen peroxide.

Vdovenko MM, Demiyanova AS, Kopylov KE, Sakharov IY. Vdovenko MM, et al. Among authors: kopylov ke. Talanta. 2014 Jul;125:361-5. doi: 10.1016/j.talanta.2014.03.040. Epub 2014 Mar 21. Talanta. 2014. PMID: 24840457

7

Drug-drug interaction of the anti-TFPI aptamer BAX499 and factor VIII: studies of spatial dynamics of fibrin clot formation in hemophilia A.

Parunov LA, Soshitova NP, Fadeeva OA, Balandina AN, Kopylov KG, Kumskova MA, Gilbert JC, Schaub RG, McGinness KE, Ataullakhanov FI, Panteleev MA. Parunov LA, et al. Among authors: kopylov kg. Thromb Res. 2014 Jan;133(1):112-9. doi: 10.1016/j.thromres.2013.10.036. Epub 2013 Nov 1. Thromb Res. 2014. PMID: 24263002

8

Investigation of the phenotype heterogeneity in severe hemophilia A using thromboelastography, thrombin generation, and thrombodynamics.

Tarandovskiy ID, Balandina AN, Kopylov KG, Konyashina NI, Kumskova MA, Panteleev MA, Ataullakhanov FI. Tarandovskiy ID, et al. Among authors: kopylov kg. Thromb Res. 2013 Jun;131(6):e274-80. doi: 10.1016/j.thromres.2013.04.004. Epub 2013 Apr 20. Thromb Res. 2013. PMID: 23611257

9

Improvement of spatial fibrin formation by the anti-TFPI aptamer BAX499: changing clot size by targeting extrinsic pathway initiation.

Parunov LA, Fadeeva OA, Balandina AN, Soshitova NP, Kopylov KG, Kumskova MA, Gilbert JC, Schaub RG, McGinness KE, Ataullakhanov FI, Panteleev MA. Parunov LA, et al. Among authors: kopylov kg. J Thromb Haemost. 2011 Sep;9(9):1825-34. doi: 10.1111/j.1538-7836.2011.04412.x. J Thromb Haemost. 2011. PMID: 21696535 Free article.

10

Mechanisms of action of recombinant activated factor VII in the context of tissue factor concentration and distribution.

Ovanesov MV, Panteleev MA, Sinauridze EI, Kireev DA, Plyushch OP, Kopylov KG, Lopatina EG, Saenko EL, Ataullakhanov FI. Ovanesov MV, et al. Among authors: kopylov kg. Blood Coagul Fibrinolysis. 2008 Dec;19(8):743-55. doi: 10.1097/MBC.0b013e3283104093. Blood Coagul Fibrinolysis. 2008. PMID: 19002040

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