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Functional diversity of non-histone chromosomal protein hmgb1. / Chikhirzhina, Elena; Starkova, Tatyana; Beljajev, Anton; Polyanichko, Alexander; Tomilin, Alexey.

In: International Journal of Molecular Sciences, Vol. 21, No. 21, 7948, 01.11.2020, p. 1-29.

Research output: Contribution to journalReview articlepeer-review

Harvard

Chikhirzhina, E, Starkova, T, Beljajev, A, Polyanichko, A & Tomilin, A 2020, 'Functional diversity of non-histone chromosomal protein hmgb1', International Journal of Molecular Sciences, vol. 21, no. 21, 7948, pp. 1-29. https://doi.org/10.3390/ijms21217948

APA

Chikhirzhina, E., Starkova, T., Beljajev, A., Polyanichko, A., & Tomilin, A. (2020). Functional diversity of non-histone chromosomal protein hmgb1. International Journal of Molecular Sciences, 21(21), 1-29. [7948]. https://doi.org/10.3390/ijms21217948

Vancouver

Chikhirzhina E, Starkova T, Beljajev A, Polyanichko A, Tomilin A. Functional diversity of non-histone chromosomal protein hmgb1. International Journal of Molecular Sciences. 2020 Nov 1;21(21):1-29. 7948. https://doi.org/10.3390/ijms21217948

Author

Chikhirzhina, Elena ; Starkova, Tatyana ; Beljajev, Anton ; Polyanichko, Alexander ; Tomilin, Alexey. / Functional diversity of non-histone chromosomal protein hmgb1. In: International Journal of Molecular Sciences. 2020 ; Vol. 21, No. 21. pp. 1-29.

BibTeX

@article{e30920ac282942d9b6dc5f30423947d1,
title = "Functional diversity of non-histone chromosomal protein hmgb1",
abstract = "The functioning of DNA in the cell nucleus is ensured by a multitude of proteins, whose interactions with DNA as well as with other proteins lead to the formation of a complicated, organized, and quite dynamic system known as chromatin. This review is devoted to the description of properties and structure of the progenitors of the most abundant non-histone protein of the HMGB family—the HmgB1 protein. The proteins of the HMGB family are also known as “architectural factors” of chromatin, which play an important role in gene expression, transcription, DNA replication, and repair. However, as soon as HmgB1 goes outside the nucleus, it acquires completely different functions, post-translational modifications, and change of its redox state. Despite a lot of evidence of the functional activity of HmgB1, there are still many issues to be solved related to the mechanisms of the influence of HmgB1 on the development and treatment of different diseases—from oncological and cardiovascular diseases to pathologies during pregnancy and childbirth. Here, we describe molecular structure of the HmgB1 protein and discuss general mechanisms of its interactions with other proteins and DNA in cell.",
keywords = "DNA-protein, Extranuclear functions of HmgB1, Nuclear, Protein HmgB1, Protein–protein interactions",
author = "Elena Chikhirzhina and Tatyana Starkova and Anton Beljajev and Alexander Polyanichko and Alexey Tomilin",
note = "Publisher Copyright: {\textcopyright} 2020 by the authors. Licensee MDPI, Basel, Switzerland.",
year = "2020",
month = nov,
day = "1",
doi = "10.3390/ijms21217948",
language = "English",
volume = "21",
pages = "1--29",
journal = "International Journal of Molecular Sciences",
issn = "1422-0067",
publisher = "MDPI AG",
number = "21",

}

RIS

TY - JOUR

T1 - Functional diversity of non-histone chromosomal protein hmgb1

AU - Chikhirzhina, Elena

AU - Starkova, Tatyana

AU - Beljajev, Anton

AU - Polyanichko, Alexander

AU - Tomilin, Alexey

N1 - Publisher Copyright: © 2020 by the authors. Licensee MDPI, Basel, Switzerland.

PY - 2020/11/1

Y1 - 2020/11/1

N2 - The functioning of DNA in the cell nucleus is ensured by a multitude of proteins, whose interactions with DNA as well as with other proteins lead to the formation of a complicated, organized, and quite dynamic system known as chromatin. This review is devoted to the description of properties and structure of the progenitors of the most abundant non-histone protein of the HMGB family—the HmgB1 protein. The proteins of the HMGB family are also known as “architectural factors” of chromatin, which play an important role in gene expression, transcription, DNA replication, and repair. However, as soon as HmgB1 goes outside the nucleus, it acquires completely different functions, post-translational modifications, and change of its redox state. Despite a lot of evidence of the functional activity of HmgB1, there are still many issues to be solved related to the mechanisms of the influence of HmgB1 on the development and treatment of different diseases—from oncological and cardiovascular diseases to pathologies during pregnancy and childbirth. Here, we describe molecular structure of the HmgB1 protein and discuss general mechanisms of its interactions with other proteins and DNA in cell.

AB - The functioning of DNA in the cell nucleus is ensured by a multitude of proteins, whose interactions with DNA as well as with other proteins lead to the formation of a complicated, organized, and quite dynamic system known as chromatin. This review is devoted to the description of properties and structure of the progenitors of the most abundant non-histone protein of the HMGB family—the HmgB1 protein. The proteins of the HMGB family are also known as “architectural factors” of chromatin, which play an important role in gene expression, transcription, DNA replication, and repair. However, as soon as HmgB1 goes outside the nucleus, it acquires completely different functions, post-translational modifications, and change of its redox state. Despite a lot of evidence of the functional activity of HmgB1, there are still many issues to be solved related to the mechanisms of the influence of HmgB1 on the development and treatment of different diseases—from oncological and cardiovascular diseases to pathologies during pregnancy and childbirth. Here, we describe molecular structure of the HmgB1 protein and discuss general mechanisms of its interactions with other proteins and DNA in cell.

KW - DNA-protein

KW - Extranuclear functions of HmgB1

KW - Nuclear

KW - Protein HmgB1

KW - Protein–protein interactions

UR - http://www.scopus.com/inward/record.url?scp=85094126117&partnerID=8YFLogxK

U2 - 10.3390/ijms21217948

DO - 10.3390/ijms21217948

M3 - Review article

C2 - 33114717

AN - SCOPUS:85094126117

VL - 21

SP - 1

EP - 29

JO - International Journal of Molecular Sciences

JF - International Journal of Molecular Sciences

SN - 1422-0067

IS - 21

M1 - 7948

ER -

ID: 87708701