Effect of low-intensity electromagnetic field on dehydration self-assembly of core histones H 3.2 and H4

G.E. Brill; A.V. Egorova; I.O. Bugaeva; S.A. Dubovitsky; S.V. Vlaskin; D.E. Postnov

Effect of low-intensity electromagnetic field on dehydration self-assembly of core histones H 3.2 and H4

G.E. Brill¹, A.V. Egorova², I.O. Bugaeva³, S.A. Dubovitsky⁴, S.V. Vlaskin⁵, D.E. Postnov⁶

research article Pages: 36-41

¹ д.м.н., профессор, кафедра патологической физиологии, ГБОУ ВПО Саратовский ГМУ им. В.И. Разумовского Минздрава России
² к.м.н., доцент, кафедра гистологии, ГБОУ ВПО Саратовский ГМУ им. В.И. Разумовского Минздрава России. E-mail: AV_Egorova @BK.RU
³ д.м.н., профессор, кафедра гистологии, ГБОУ ВПО Саратовский ГМУ им. В.И. Разумовского Минздрава России
⁴ ген. директор, НПП «Телемак» (г. Саратов)
⁵ к.ф.-м.н., техн. директор, НПП «Телемак»
⁶ д.ф.-м.н., профессор, кафедра оптики и биофотоники, ФГБОУ ВПО «Саратовский государственный университет им. Н.Г. Чернышевского»

Keywords: core histones self-organization low-intensity electromagnetic field

Abstract

The analysis of influence of low-intensity electromagnetic field on the processes of self-assembly of core histones H3.2 and H4 was performed.

How to cite

Брилль Г.Е., Егорова А.В., Бугаева И.О., Дубовицкий С.А., Власкин С.В., Постнов Д.Э. Влияние низкоинтенсивного электромагнитного поля на структурообразование коровых гистонов Н3.2 и Н4 // Биомедицинская радиоэлектроника. 2013. № 5. С. 36–41.

References

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[1] Brill G.E., Panina N.P., Nevskaja E.JU. Dejjstvie ehlektromagnitnogo izluchenija millimetrovogo diapazona na politennye khromosomy Chironomusplumosus // Millimetrovye volny v biologii i medicine. 2000. T.17. № 1. S. 3 - 7.

[2] SHabalin V.N., SHatokhina S.N. Morfologija biologicheskikh zhidkostejj cheloveka. M.: KHrizostom. 2001. 303 s.

[3] Ammollo C.T., Semeraro F., Xu J. et al. Extracellularhistonesincreaseplasmathrombingenerationbyimpairingthrombomodulin-dependent protein C activation // J. Thromb. Haemost. 2011. V. 9. P. 1795 - 1803.

[4] Avvakumov N., Nourani A., Côté J. Histone chaperones: modulators of chromatin marks // Molecular. Cell. 2011. V. 41. P. 502 - 514.

[5] Bannister A.J., Kouzarides T. Regulation of chromatin by histone modifications // Cell Research. 2011. V. 21. P. 381 - 395.

[6] Khorasanizadeh S. The nucleosome: from genomic organization to genomic regulation // Cell. 2004. V. 116. R. 259 - 272.

[7] Kleine T.J., Lewis P.N., Lewis S.A. Histone-induced damage of a mammalian epithelium: the role of protein and membrane structure // Amer. J. Physiol. 1997. V. 273. P. 1925 - 1936.

[8] Lukas J., Lukas C., Bartek J. More than justa focus: The chromatin response toDNA damage and its role in genome integrity maintenance // Nature Cell Biol. 2011. V. 13. № 10. P. 1161 - 1169.

[9] Pemberton A.D., Brown J.K., Inglis N.F.Proteomic identification of interactions between histones and plasma proteins: Implications for cytoprotection // Proteomics. 2010. V. 10. P. 1484 - 1493.

[10] Sinitsyn N.I., Petrosyan V.I., Yolkin V.A. et al. Special function of the «millimeter wavelength waves-aqueous medium» system in nature // Crit. Rev. Biomed. Eng. 2000. V.28. P. 269 - 305.

[11] Suganuma T., Workman J.L. Signal and combinatorial functions of histone modifications // Annu. Rev. Biochem. 2011. V. 80. P. 473 - 499.