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Russian Chemical Reviews, 2005, Volume 74, Issue 1, Pages 77–95
DOI: https://doi.org/10.1070/RC2005v074n01ABEH000882
(Mi rcr385)
 

This article is cited in 11 scientific papers (total in 11 papers)

Covalent binding of modified nucleic acids to proteins as a method for investigation of specific protein–nucleic acid interactions

T. S. Zatsepina, N. G. Dolinnayaa, E. A. Kubarevab, M. G. Ivanovskayab, V. G. Meteleva, T. S. Oretskayaa

a Lomonosov Moscow State University, Faculty of Chemistry
b Lomonosov Moscow State University, Belozersky Research Institute of Physico-Chemical Biology
English full-text Citations (11)
Abstract: Methods for specific covalent binding of modified nucleic acids to proteins and enzymes with conservation of their native structures are discussed. Possible applications of synthetic nucleic acids containing reactive (nucleophilic and electrophilic) groups and groups that can be photoactivated for testing protein–nucleic acid contacts and studying protein functioning are considered. The structures of protein–nucleic acid conjugates formed in the enzymatic reactions are described. Methods for the isolation and analysis of covalently bound protein–nucleic acid complexes are generalised. The main attention is given to methods for determination of protein sites attached to nucleic acids.
Received: 12.11.2003
Russian version:
Uspekhi Khimii, 2005, Volume 74, Issue 1, Pages 84–103
DOI: https://doi.org/10.1070/RC2005v074n01ABEH000882
Bibliographic databases:
Document Type: Article
Language: English
Original paper language: Russian


Citation: T. S. Zatsepin, N. G. Dolinnaya, E. A. Kubareva, M. G. Ivanovskaya, V. G. Metelev, T. S. Oretskaya, “Covalent binding of modified nucleic acids to proteins as a method for investigation of specific protein–nucleic acid interactions”, Usp. Khim., 74:1 (2005), 84–103; Russian Chem. Reviews, 74:1 (2005), 77–95
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  • https://doi.org/10.1070/RC2005v074n01ABEH000882
  • https://www.mathnet.ru/eng/rcr/v74/i1/p84
  • This publication is cited in the following 11 articles:
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