Doklady Biochemistry and Biophysics, том 433, издание 1, номера страниц: 152-154

In vitro Dimerization of Telomerase Protein Est3p is Stimulated by Magnesium Cations

Тип документаJournal Article
Дата публикации2010-08-17
ИздательPleiades Publishing
Название журналаDoklady Biochemistry and Biophysics
Квартиль по SCImagoQ3
Квартиль по Web of ScienceQ4
Импакт-фактор 20210.83
ISSN16076729, 16083091
General Chemistry
General Medicine
Краткое описание
Telomeres are the special DNA protein structures at the end of the linear chromosomes of eukaryotic organisms. Telomeres maintain chromosome stability, protect them from degradation and fusion, participate in the regulation of transcription of genes in the subte lomeric regions and play an important role in cell aging [1]. Telomere DNA consists of repeated nucle otide sequences (telomeric repeats) and has a 3' pro truding single strand end. Each cell division results in under replication and telomere shortening. At a cer tain critical length of telomeres, cells can not divide and enter senescence and finally dies. However in most of the cells with unlimited division potential, such as unicellular organisms or germinal, stem or tumor cells, the telomeres are maintained by telom erase, which contain telomerase RNA, reverse tran scriptase and some other proteins [1].
Пристатейные ссылки: 15
Цитируется в публикациях: 1
Saccharomyces cerevisiae telomerase subunit Est3p binds DNA and RNA and stimulates unwinding of RNA/DNA heteroduplexes
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Saccharomyces cerevisiae Est3p dimerizes in vitro and dimerization contributes to efficient telomere replication in vivo
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N-terminal Domain of Yeast Telomerase Reverse Transcriptase: Recruitment of Est3p to the Telomerase Complex
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Q1 Molecular Biology of the Cell 2003 цитирований: 55
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Q1 Current Biology 1997 цитирований: 70
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Q1 Genes and Development 1997 цитирований: 106
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Three Ever Shorter Telomere (EST) genes are dispensable for in vitro yeast telomerase activity
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Q1 Proceedings of the National Academy of Sciences of the United States of America 1997 цитирований: 178
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1. Malyavko A.G. и др. In vitro dimerization of telomerase protein Est3p is stimulated by magnesium cations // Doklady Biochemistry and Biophysics. 2010. Т. 433. № 1. С. 152–154.


DO - 10.1134/s1607672910040034

UR -

TI - In vitro dimerization of telomerase protein Est3p is stimulated by magnesium cations

T2 - Doklady Biochemistry and Biophysics

AU - Malyavko, A. G.

AU - Logvina, N. A.

AU - Zvereva, M. E.

AU - Dontsova, O. A.

PY - 2010

DA - 2010/08

PB - Pleiades Publishing Ltd

SP - 152-154

IS - 1

VL - 433

SN - 1607-6729

SN - 1608-3091

ER -

BibTex |


doi = {10.1134/s1607672910040034},

url = {},

year = 2010,

month = {aug},

publisher = {Pleiades Publishing Ltd},

volume = {433},

number = {1},

pages = {152--154},

author = {A. G. Malyavko and N. A. Logvina and M. E. Zvereva and O. A. Dontsova},

title = {In vitro dimerization of telomerase protein Est3p is stimulated by magnesium cations}


Malyavko, A. G. et al. “In Vitro Dimerization of Telomerase Protein Est3p Is Stimulated by Magnesium Cations.” Doklady Biochemistry and Biophysics 433.1 (2010): 152–154. Crossref. Web.