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Dynamics and Conformational Changes in Human NEIL2 DNA Glycosylase Analyzed by Hydrogen/Deuterium Exchange Mass Spectrometry.

Journal of molecular biology

Zhdanova PV, Ishchenko AA, Chernonosov AA, Zharkov DO, Koval VV.
PMID: 34757057
J Mol Biol. 2022 Jan 30;434(2):167334. doi: 10.1016/j.jmb.2021.167334. Epub 2021 Oct 29.

Base excision DNA repair (BER) is necessary for removal of damaged nucleobases from the genome and their replacement with normal nucleobases. BER is initiated by DNA glycosylases, the enzymes that cleave the N-glycosidic bonds of damaged deoxynucleotides. Human endonuclease...

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Zhdanova PV, Ishchenko AA, Chernonosov AA, et al. Dynamics and Conformational Changes in Human NEIL2 DNA Glycosylase Analyzed by Hydrogen/Deuterium Exchange Mass Spectrometry. J Mol Biol. 2021;434(2):167334doi: 10.1016/j.jmb.2021.167334.
Zhdanova, P. V., Ishchenko, A. A., Chernonosov, A. A., Zharkov, D. O., & Koval, V. V. (2022). Dynamics and Conformational Changes in Human NEIL2 DNA Glycosylase Analyzed by Hydrogen/Deuterium Exchange Mass Spectrometry. Journal of molecular biology, 434(2), 167334. https://doi.org/10.1016/j.jmb.2021.167334
Zhdanova, Polina V, et al. "Dynamics and Conformational Changes in Human NEIL2 DNA Glycosylase Analyzed by Hydrogen/Deuterium Exchange Mass Spectrometry." Journal of molecular biology vol. 434,2 (2022): 167334. doi: https://doi.org/10.1016/j.jmb.2021.167334
Zhdanova PV, Ishchenko AA, Chernonosov AA, Zharkov DO, Koval VV. Dynamics and Conformational Changes in Human NEIL2 DNA Glycosylase Analyzed by Hydrogen/Deuterium Exchange Mass Spectrometry. J Mol Biol. 2022 Jan 30;434(2):167334. doi: 10.1016/j.jmb.2021.167334. Epub 2021 Oct 29. PMID: 34757057.
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Flame atomic absorption determination of manganese(II) in natural water after cloud point extraction.

Talanta

Doroschuk VO, Lelyushok SO, Ishchenko VB, Kulichenko SA.
PMID: 18969680
Talanta. 2004 Nov 15;64(4):853-6. doi: 10.1016/j.talanta.2004.03.056.

The possibility to use 4-(2-pyridylazo)resorcinol (PAR) and 1-(2-pyridylazo)-2-naphthol (PAN) for manganese(II) concentrating by the micellar extraction at cloud point (CP) temperature and subsequent atomic absorption spectrometry (AAS) determination was investigated. Under the optimum conditions, preconcentration of 100ml of water...

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Doroschuk VO, Lelyushok SO, Ishchenko VB, et al. Flame atomic absorption determination of manganese(II) in natural water after cloud point extraction. Talanta. 2004;64(4):853-6doi: 10.1016/j.talanta.2004.03.056.
Doroschuk, V. O., Lelyushok, S. O., Ishchenko, V. B., & Kulichenko, S. A. (2004). Flame atomic absorption determination of manganese(II) in natural water after cloud point extraction. Talanta, 64(4), 853-6. https://doi.org/10.1016/j.talanta.2004.03.056
Doroschuk, V O, et al. "Flame atomic absorption determination of manganese(II) in natural water after cloud point extraction." Talanta vol. 64,4 (2004): 853-6. doi: https://doi.org/10.1016/j.talanta.2004.03.056
Doroschuk VO, Lelyushok SO, Ishchenko VB, Kulichenko SA. Flame atomic absorption determination of manganese(II) in natural water after cloud point extraction. Talanta. 2004 Nov 15;64(4):853-6. doi: 10.1016/j.talanta.2004.03.056. PMID: 18969680.
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UV-Vis absorption spectra and electronic structure of merocyanines in the gas phase.

Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy

Ishchenko AA, Kulinich AV, Bondarev SL, Raichenok TF.
PMID: 28941887
Spectrochim Acta A Mol Biomol Spectrosc. 2018 Feb 05;190:332-335. doi: 10.1016/j.saa.2017.09.054. Epub 2017 Sep 21.

Gas-phase absorption spectra of a merocyanine vinylogous series have been studied for the first time. In vapour, their long-wavelength absorption bands were found to be considerably shifted hypsochromically, broader, more symmetrical, less intense, and their vinylene shift much smaller...

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Ishchenko AA, Kulinich AV, Bondarev SL, et al. UV-Vis absorption spectra and electronic structure of merocyanines in the gas phase. Spectrochim Acta A Mol Biomol Spectrosc. 2017;190:332-335doi: 10.1016/j.saa.2017.09.054.
Ishchenko, A. A., Kulinich, A. V., Bondarev, S. L., & Raichenok, T. F. (2018). UV-Vis absorption spectra and electronic structure of merocyanines in the gas phase. Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy, 190332-335. https://doi.org/10.1016/j.saa.2017.09.054
Ishchenko, Alexander A, et al. "UV-Vis absorption spectra and electronic structure of merocyanines in the gas phase." Spectrochimica acta. Part A, Molecular and biomolecular spectroscopy vol. 190 (2018): 332-335. doi: https://doi.org/10.1016/j.saa.2017.09.054
Ishchenko AA, Kulinich AV, Bondarev SL, Raichenok TF. UV-Vis absorption spectra and electronic structure of merocyanines in the gas phase. Spectrochim Acta A Mol Biomol Spectrosc. 2018 Feb 05;190:332-335. doi: 10.1016/j.saa.2017.09.054. Epub 2017 Sep 21. PMID: 28941887.
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Interaction of Polymethine Dyes with Detonation Nanodiamonds.

Chemphyschem : a European journal of chemical physics and physical chemistry

Ishchenko AA, Mchedlov-Petrossyan NO, Kriklya NN, Kryshtal AP, Ōsawa E, Kulinich AV.
PMID: 30848540
Chemphyschem. 2019 Apr 16;20(8):1028-1035. doi: 10.1002/cphc.201900083. Epub 2019 Mar 28.

Among cationic, anionic, and merocyanine polymethine dyes, the binding to detonation nanodiamond (DND) colloid particles in hydrosol occurs only for negatively charged dye species. This, in view of the positive ζ-potential of the DND used in this study, suggests...

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Ishchenko AA, Mchedlov-Petrossyan NO, Kriklya NN, et al. Interaction of Polymethine Dyes with Detonation Nanodiamonds. Chemphyschem. 2019;20(8):1028-1035doi: 10.1002/cphc.201900083.
Ishchenko, A. A., Mchedlov-Petrossyan, N. O., Kriklya, N. N., Kryshtal, A. P., Ōsawa, E., & Kulinich, A. V. (2019). Interaction of Polymethine Dyes with Detonation Nanodiamonds. Chemphyschem : a European journal of chemical physics and physical chemistry, 20(8), 1028-1035. https://doi.org/10.1002/cphc.201900083
Ishchenko, Alexander A, et al. "Interaction of Polymethine Dyes with Detonation Nanodiamonds." Chemphyschem : a European journal of chemical physics and physical chemistry vol. 20,8 (2019): 1028-1035. doi: https://doi.org/10.1002/cphc.201900083
Ishchenko AA, Mchedlov-Petrossyan NO, Kriklya NN, Kryshtal AP, Ōsawa E, Kulinich AV. Interaction of Polymethine Dyes with Detonation Nanodiamonds. Chemphyschem. 2019 Apr 16;20(8):1028-1035. doi: 10.1002/cphc.201900083. Epub 2019 Mar 28. PMID: 30848540.
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The Enigma of Substrate Recognition and Catalytic Efficiency of APE1-Like Enzymes.

Frontiers in cell and developmental biology

Davletgildeeva AT, Ishchenko AA, Saparbaev M, Fedorova OS, Kuznetsov NA.
PMID: 33842455
Front Cell Dev Biol. 2021 Mar 26;9:617161. doi: 10.3389/fcell.2021.617161. eCollection 2021.

Despite significant achievements in the elucidation of the nature of protein-DNA contacts that control the specificity of nucleotide incision repair (NIR) by apurinic/apyrimidinic (AP) endonucleases, the question on how a given nucleotide is accommodated by the active site of...

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Davletgildeeva AT, Ishchenko AA, Saparbaev M, et al. The Enigma of Substrate Recognition and Catalytic Efficiency of APE1-Like Enzymes. Front Cell Dev Biol. 2021;9:617161doi: 10.3389/fcell.2021.617161.
Davletgildeeva, A. T., Ishchenko, A. A., Saparbaev, M., Fedorova, O. S., & Kuznetsov, N. A. (2021). The Enigma of Substrate Recognition and Catalytic Efficiency of APE1-Like Enzymes. Frontiers in cell and developmental biology, 9617161. https://doi.org/10.3389/fcell.2021.617161
Davletgildeeva, Anastasiia T, et al. "The Enigma of Substrate Recognition and Catalytic Efficiency of APE1-Like Enzymes." Frontiers in cell and developmental biology vol. 9 (2021): 617161. doi: https://doi.org/10.3389/fcell.2021.617161
Davletgildeeva AT, Ishchenko AA, Saparbaev M, Fedorova OS, Kuznetsov NA. The Enigma of Substrate Recognition and Catalytic Efficiency of APE1-Like Enzymes. Front Cell Dev Biol. 2021 Mar 26;9:617161. doi: 10.3389/fcell.2021.617161. eCollection 2021. PMID: 33842455; PMCID: PMC8033172.
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Role of PARP-catalyzed ADP-ribosylation in the Crosstalk Between DNA Strand Breaks and Epigenetic Regulation.

Journal of molecular biology

Sutcu HH, Matta E, Ishchenko AA.
PMID: 31866292
J Mol Biol. 2019 Dec 20; doi: 10.1016/j.jmb.2019.12.019. Epub 2019 Dec 20.

Covalent linkage of ADP-ribose units to proteins catalyzed by poly(ADP-ribose) polymerases (PARPs) plays important signaling functions in a plethora of cellular processes including DNA damage response, chromatin organization, and gene transcription. Poly- and mono-ADP-ribosylation of target macromolecules are often...

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Sutcu HH, Matta E, Ishchenko AA. Role of PARP-catalyzed ADP-ribosylation in the Crosstalk Between DNA Strand Breaks and Epigenetic Regulation. J Mol Biol. 2019;doi: 10.1016/j.jmb.2019.12.019.
Sutcu, H. H., Matta, E., & Ishchenko, A. A. (2019). Role of PARP-catalyzed ADP-ribosylation in the Crosstalk Between DNA Strand Breaks and Epigenetic Regulation. Journal of molecular biology, . https://doi.org/10.1016/j.jmb.2019.12.019
Sutcu, Haser H, et al. "Role of PARP-catalyzed ADP-ribosylation in the Crosstalk Between DNA Strand Breaks and Epigenetic Regulation." Journal of molecular biology vol. (2019). doi: https://doi.org/10.1016/j.jmb.2019.12.019
Sutcu HH, Matta E, Ishchenko AA. Role of PARP-catalyzed ADP-ribosylation in the Crosstalk Between DNA Strand Breaks and Epigenetic Regulation. J Mol Biol. 2019 Dec 20; doi: 10.1016/j.jmb.2019.12.019. Epub 2019 Dec 20. PMID: 31866292.
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Harnessing the power of an X-ray laser for serial crystallography of membrane proteins crystallized in lipidic cubic phase.

IUCrJ

Lee MY, Geiger J, Ishchenko A, Han GW, Barty A, White TA, Gati C, Batyuk A, Hunter MS, Aquila A, Boutet S, Weierstall U, Cherezov V, Liu W.
PMID: 33209312
IUCrJ. 2020 Oct 15;7:976-984. doi: 10.1107/S2052252520012701. eCollection 2020 Nov 01.

Serial femtosecond crystallography (SFX) with X-ray free-electron lasers (XFELs) has proven highly successful for structure determination of challenging membrane proteins crystallized in lipidic cubic phase; however, like most techniques, it has limitations. Here we attempt to address some of...

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Lee MY, Geiger J, Ishchenko A, et al. Harnessing the power of an X-ray laser for serial crystallography of membrane proteins crystallized in lipidic cubic phase. IUCrJ. 2020;7:976-984doi: 10.1107/S2052252520012701.
Lee, M. Y., Geiger, J., Ishchenko, A., Han, G. W., Barty, A., White, T. A., Gati, C., Batyuk, A., Hunter, M. S., Aquila, A., Boutet, S., Weierstall, U., Cherezov, V., & Liu, W. (2020). Harnessing the power of an X-ray laser for serial crystallography of membrane proteins crystallized in lipidic cubic phase. IUCrJ, 7976-984. https://doi.org/10.1107/S2052252520012701
Lee, Ming-Yue, et al. "Harnessing the power of an X-ray laser for serial crystallography of membrane proteins crystallized in lipidic cubic phase." IUCrJ vol. 7 (2020): 976-984. doi: https://doi.org/10.1107/S2052252520012701
Lee MY, Geiger J, Ishchenko A, Han GW, Barty A, White TA, Gati C, Batyuk A, Hunter MS, Aquila A, Boutet S, Weierstall U, Cherezov V, Liu W. Harnessing the power of an X-ray laser for serial crystallography of membrane proteins crystallized in lipidic cubic phase. IUCrJ. 2020 Oct 15;7:976-984. doi: 10.1107/S2052252520012701. eCollection 2020 Nov 01. PMID: 33209312; PMCID: PMC7642783.
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[On biological characteristics of pathogenic serological types of Escherichia coli].

Meditsinskii zhurnal Uzbekistana

SHEVCHENKO FI, AKHTAMOV MA, ISHCHENKO GN, KAZAKOVA AN, EL'TEKOVA NI.
PMID: 13911776
Med Zh Uzb. 1962 Feb;2:22-5.

No abstract available.

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SHEVCHENKO FI, AKHTAMOV MA, ISHCHENKO GN, et al. [On biological characteristics of pathogenic serological types of Escherichia coli]. Med Zh Uzb. 1962;2:22-5
SHEVCHENKO, F. I., AKHTAMOV, M. A., ISHCHENKO, G. N., KAZAKOVA, A. N., & EL'TEKOVA, N. I. (1962). [On biological characteristics of pathogenic serological types of Escherichia coli]. Meditsinskii zhurnal Uzbekistana, 222-5.
SHEVCHENKO, F I, et al. "[On biological characteristics of pathogenic serological types of Escherichia coli]." Meditsinskii zhurnal Uzbekistana vol. 2 (1962): 22-5.
SHEVCHENKO FI, AKHTAMOV MA, ISHCHENKO GN, KAZAKOVA AN, EL'TEKOVA NI. [On biological characteristics of pathogenic serological types of Escherichia coli]. Med Zh Uzb. 1962 Feb;2:22-5. Russian. PMID: 13911776.
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Serial millisecond crystallography of membrane and soluble protein microcrystals using synchrotron radiation.

IUCrJ

Martin-Garcia JM, Conrad CE, Nelson G, Stander N, Zatsepin NA, Zook J, Zhu L, Geiger J, Chun E, Kissick D, Hilgart MC, Ogata C, Ishchenko A, Nagaratnam N, Roy-Chowdhury S, Coe J, Subramanian G, Schaffer A, James D, Ketwala G, Venugopalan N, Xu S, Corcoran S, Ferguson D, Weierstall U, Spence JCH, Cherezov V, Fromme P, Fischetti RF, Liu W.
PMID: 28875031
IUCrJ. 2017 May 24;4:439-454. doi: 10.1107/S205225251700570X. eCollection 2017 Jul 01.

Crystal structure determination of biological macromolecules using the novel technique of serial femtosecond crystallography (SFX) is severely limited by the scarcity of X-ray free-electron laser (XFEL) sources. However, recent and future upgrades render microfocus beamlines at synchrotron-radiation sources suitable...

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Martin-Garcia JM, Conrad CE, Nelson G, et al. Serial millisecond crystallography of membrane and soluble protein microcrystals using synchrotron radiation. IUCrJ. 2017;4:439-454doi: 10.1107/S205225251700570X.
Martin-Garcia, J. M., Conrad, C. E., Nelson, G., Stander, N., Zatsepin, N. A., Zook, J., Zhu, L., Geiger, J., Chun, E., Kissick, D., Hilgart, M. C., Ogata, C., Ishchenko, A., Nagaratnam, N., Roy-Chowdhury, S., Coe, J., Subramanian, G., Schaffer, A., James, D., Ketwala, G., Venugopalan, N., Xu, S., Corcoran, S., Ferguson, D., Weierstall, U., Spence, J. C. H., Cherezov, V., Fromme, P., Fischetti, R. F., & Liu, W. (2017). Serial millisecond crystallography of membrane and soluble protein microcrystals using synchrotron radiation. IUCrJ, 4439-454. https://doi.org/10.1107/S205225251700570X
Martin-Garcia, Jose M, et al. "Serial millisecond crystallography of membrane and soluble protein microcrystals using synchrotron radiation." IUCrJ vol. 4 (2017): 439-454. doi: https://doi.org/10.1107/S205225251700570X
Martin-Garcia JM, Conrad CE, Nelson G, Stander N, Zatsepin NA, Zook J, Zhu L, Geiger J, Chun E, Kissick D, Hilgart MC, Ogata C, Ishchenko A, Nagaratnam N, Roy-Chowdhury S, Coe J, Subramanian G, Schaffer A, James D, Ketwala G, Venugopalan N, Xu S, Corcoran S, Ferguson D, Weierstall U, Spence JCH, Cherezov V, Fromme P, Fischetti RF, Liu W. Serial millisecond crystallography of membrane and soluble protein microcrystals using synchrotron radiation. IUCrJ. 2017 May 24;4:439-454. doi: 10.1107/S205225251700570X. eCollection 2017 Jul 01. PMID: 28875031; PMCID: PMC5571807.
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Scope of negative solvatochromism and solvatofluorochromism of merocyanines.

Physical chemistry chemical physics : PCCP

Kulinich AV, Mikitenko EK, Ishchenko AA.
PMID: 26743674
Phys Chem Chem Phys. 2016 Feb 07;18(5):3444-53. doi: 10.1039/c5cp06653k.

A vinylogous series of highly dipolar merocyanines were designed to study their solvatochromism in a wide range of solvents including low-polarity alkanes. It has been revealed that the lower vinylogues indeed have negative solvatochromism in the full range of...

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Kulinich AV, Mikitenko EK, Ishchenko AA. Scope of negative solvatochromism and solvatofluorochromism of merocyanines. Phys Chem Chem Phys. 2016;18(5):3444-53doi: 10.1039/c5cp06653k.
Kulinich, A. V., Mikitenko, E. K., & Ishchenko, A. A. (2016). Scope of negative solvatochromism and solvatofluorochromism of merocyanines. Physical chemistry chemical physics : PCCP, 18(5), 3444-53. https://doi.org/10.1039/c5cp06653k
Kulinich, A V, et al. "Scope of negative solvatochromism and solvatofluorochromism of merocyanines." Physical chemistry chemical physics : PCCP vol. 18,5 (2016): 3444-53. doi: https://doi.org/10.1039/c5cp06653k
Kulinich AV, Mikitenko EK, Ishchenko AA. Scope of negative solvatochromism and solvatofluorochromism of merocyanines. Phys Chem Chem Phys. 2016 Feb 07;18(5):3444-53. doi: 10.1039/c5cp06653k. PMID: 26743674.
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Superparamagnetic behaviour of metallic Co nanoparticles according to variable temperature magnetic resonance.

Physical chemistry chemical physics : PCCP

Yakovlev IV, Yakushkin SS, Kazakova MA, Trukhan SN, Volkova ZN, Gerashchenko AP, Andreev AS, Ishchenko AV, Martyanov ON, Lapina OB, d'Espinose de Lacaillerie JB.
PMID: 33492314
Phys Chem Chem Phys. 2021 Feb 04;23(4):2723-2730. doi: 10.1039/d0cp05963c.

Investigating the size distributions of Co nanoparticle ensembles is an important problem, which has no straightforward solution. In this work, we use the combination of 59Co internal field nuclear magnetic resonance (59Co IF NMR) and ferromagnetic resonance (FMR) spectroscopies...

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Yakovlev IV, Yakushkin SS, Kazakova MA, et al. Superparamagnetic behaviour of metallic Co nanoparticles according to variable temperature magnetic resonance. Phys Chem Chem Phys. 2021;23(4):2723-2730doi: 10.1039/d0cp05963c.
Yakovlev, I. V., Yakushkin, S. S., Kazakova, M. A., Trukhan, S. N., Volkova, Z. N., Gerashchenko, A. P., Andreev, A. S., Ishchenko, A. V., Martyanov, O. N., Lapina, O. B., & d'Espinose de Lacaillerie, J. B. (2021). Superparamagnetic behaviour of metallic Co nanoparticles according to variable temperature magnetic resonance. Physical chemistry chemical physics : PCCP, 23(4), 2723-2730. https://doi.org/10.1039/d0cp05963c
Yakovlev, Ilya V, et al. "Superparamagnetic behaviour of metallic Co nanoparticles according to variable temperature magnetic resonance." Physical chemistry chemical physics : PCCP vol. 23,4 (2021): 2723-2730. doi: https://doi.org/10.1039/d0cp05963c
Yakovlev IV, Yakushkin SS, Kazakova MA, Trukhan SN, Volkova ZN, Gerashchenko AP, Andreev AS, Ishchenko AV, Martyanov ON, Lapina OB, d'Espinose de Lacaillerie JB. Superparamagnetic behaviour of metallic Co nanoparticles according to variable temperature magnetic resonance. Phys Chem Chem Phys. 2021 Feb 04;23(4):2723-2730. doi: 10.1039/d0cp05963c. PMID: 33492314.
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The .

Frontiers in cell and developmental biology

Taipakova S, Kuanbay A, Saint-Pierre C, Gasparutto D, Baiken Y, Groisman R, Ishchenko AA, Saparbaev M, Bissenbaev AK.
PMID: 33324653
Front Cell Dev Biol. 2020 Nov 26;8:606596. doi: 10.3389/fcell.2020.606596. eCollection 2020.

Proteins from the poly(ADP-ribose) polymerase (PARP) family, such as PARP1 and PARP2, use NAD

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Taipakova S, Kuanbay A, Saint-Pierre C, et al. The . Front Cell Dev Biol. 2020;8:606596doi: 10.3389/fcell.2020.606596.
Taipakova, S., Kuanbay, A., Saint-Pierre, C., Gasparutto, D., Baiken, Y., Groisman, R., Ishchenko, A. A., Saparbaev, M., & Bissenbaev, A. K. (2020). The . Frontiers in cell and developmental biology, 8606596. https://doi.org/10.3389/fcell.2020.606596
Taipakova, Sabira, et al. "The ." Frontiers in cell and developmental biology vol. 8 (2020): 606596. doi: https://doi.org/10.3389/fcell.2020.606596
Taipakova S, Kuanbay A, Saint-Pierre C, Gasparutto D, Baiken Y, Groisman R, Ishchenko AA, Saparbaev M, Bissenbaev AK. The . Front Cell Dev Biol. 2020 Nov 26;8:606596. doi: 10.3389/fcell.2020.606596. eCollection 2020. PMID: 33324653; PMCID: PMC7726343.
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