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Hydroxylation of protein constituents of the human translation system : Structural aspects and functional assignments. / Graifer, Dmitri; Malygin, Alexey; Karpova, Galina.

In: Future Medicinal Chemistry, Vol. 11, No. 4, 01.02.2019, p. 357-369.

Research output: Contribution to journal › Review article › peer-review

Harvard

Graifer, D, Malygin, A & Karpova, G 2019, 'Hydroxylation of protein constituents of the human translation system: Structural aspects and functional assignments', Future Medicinal Chemistry, vol. 11, no. 4, pp. 357-369. https://doi.org/10.4155/fmc-2018-0317

APA

Graifer, D., Malygin, A., & Karpova, G. (2019). Hydroxylation of protein constituents of the human translation system: Structural aspects and functional assignments. Future Medicinal Chemistry, 11(4), 357-369. https://doi.org/10.4155/fmc-2018-0317

Vancouver

Graifer D, Malygin A, Karpova G. Hydroxylation of protein constituents of the human translation system: Structural aspects and functional assignments. Future Medicinal Chemistry. 2019 Feb 1;11(4):357-369. doi: 10.4155/fmc-2018-0317

Author

Graifer, Dmitri ; Malygin, Alexey ; Karpova, Galina. / Hydroxylation of protein constituents of the human translation system : Structural aspects and functional assignments. In: Future Medicinal Chemistry. 2019 ; Vol. 11, No. 4. pp. 357-369.

BibTeX

@article{60eb95988e054af3884a762a90ca3750,
title = "Hydroxylation of protein constituents of the human translation system: Structural aspects and functional assignments",
abstract = "During the current decade, data on the post-translational hydroxylation of specific amino acid residues of some ribosomal proteins and translation factors in both eukaryotes and eubacteria have accumulated. The reaction is catalyzed by dedicated oxygenases (so-called ribosomal oxygenases), whose action is impaired under hypoxia conditions. The modification occurs at amino acid residues directly involved in the formation of the main functional sites of ribosomes and factors. This review summarizes currently available data on the specific hydroxylation of protein constituents of eukaryotic and eubacterial translation systems with a special emphasis on the human system, as well as on the links between hypoxia impacts on the operation of ribosomal oxygenases, the functioning of the translational apparatus and human health problems.",
keywords = "health disorders, hypoxia, ribosomal proteins, ribosome oxygenases, specific hydroxylation of proteins, translation factors, translation regulation dysfunctions",
author = "Dmitri Graifer and Alexey Malygin and Galina Karpova",
year = "2019",
month = feb,
day = "1",
doi = "10.4155/fmc-2018-0317",
language = "English",
volume = "11",
pages = "357--369",
journal = "Future Medicinal Chemistry",
issn = "1756-8919",
publisher = "Future Science",
number = "4",

}

RIS

TY - JOUR

T1 - Hydroxylation of protein constituents of the human translation system

T2 - Structural aspects and functional assignments

AU - Graifer, Dmitri

AU - Malygin, Alexey

AU - Karpova, Galina

PY - 2019/2/1

Y1 - 2019/2/1

N2 - During the current decade, data on the post-translational hydroxylation of specific amino acid residues of some ribosomal proteins and translation factors in both eukaryotes and eubacteria have accumulated. The reaction is catalyzed by dedicated oxygenases (so-called ribosomal oxygenases), whose action is impaired under hypoxia conditions. The modification occurs at amino acid residues directly involved in the formation of the main functional sites of ribosomes and factors. This review summarizes currently available data on the specific hydroxylation of protein constituents of eukaryotic and eubacterial translation systems with a special emphasis on the human system, as well as on the links between hypoxia impacts on the operation of ribosomal oxygenases, the functioning of the translational apparatus and human health problems.

AB - During the current decade, data on the post-translational hydroxylation of specific amino acid residues of some ribosomal proteins and translation factors in both eukaryotes and eubacteria have accumulated. The reaction is catalyzed by dedicated oxygenases (so-called ribosomal oxygenases), whose action is impaired under hypoxia conditions. The modification occurs at amino acid residues directly involved in the formation of the main functional sites of ribosomes and factors. This review summarizes currently available data on the specific hydroxylation of protein constituents of eukaryotic and eubacterial translation systems with a special emphasis on the human system, as well as on the links between hypoxia impacts on the operation of ribosomal oxygenases, the functioning of the translational apparatus and human health problems.

KW - health disorders

KW - hypoxia

KW - ribosomal proteins

KW - ribosome oxygenases

KW - specific hydroxylation of proteins

KW - translation factors

KW - translation regulation dysfunctions

UR - http://www.scopus.com/inward/record.url?scp=85063639412&partnerID=8YFLogxK

U2 - 10.4155/fmc-2018-0317

DO - 10.4155/fmc-2018-0317

M3 - Review article

C2 - 30802140

AN - SCOPUS:85063639412

VL - 11

SP - 357

EP - 369

JO - Future Medicinal Chemistry

JF - Future Medicinal Chemistry

SN - 1756-8919

IS - 4

ER -

ID: 19035297