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Olga I. Lavrik

Researcher at Russian Academy of Sciences

Publications -  395
Citations -  7353

Olga I. Lavrik is an academic researcher from Russian Academy of Sciences. The author has contributed to research in topics: DNA & DNA polymerase. The author has an hindex of 38, co-authored 365 publications receiving 6085 citations. Previous affiliations of Olga I. Lavrik include Novosibirsk State University & Altai State University.

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Journal ArticleDOI

Poly(ADP-ribosyl)ation by PARP1: reaction mechanism and regulatory proteins.

Elizaveta E. Alemasova, +1 more
- 07 May 2019 - 
TL;DR: Old and up-to-date literature is summarized to clarify several points concerning PARylation mechanism and discuss different ways for regulation of PAR synthesis by accessory proteins reported thus far.
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DNA Polymerase β-mediated Long Patch Base Excision Repair POLY(ADP-RIBOSE) POLYMERASE-1 STIMULATES STRAND DISPLACEMENT DNA SYNTHESIS

Rajendra Prasad, +6 more
- 31 Aug 2001 - 
TL;DR: The DNA synthesis and flap excision steps in long patch BER are examined using a reconstituted system containing a 34-base pair BER substrate and five purified human enzymes: uracil-DNA glycosylase, apurinic/apyrimidinic endonuclease, DNA polymerase beta, flap end onuclease-1 (FEN-1), and PARP-1.
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The crystal structure of phenylalanyl-tRNA synthetase from Thermus thermophilus complexed with cognate tRNAPhe

Yehuda Goldgur, +6 more
- 15 Jan 1997 - 
TL;DR: The mode of interactions with tRNA explains the absolute necessity for the (alphabeta)2 architecture of PheRS and a new type of anticodon-binding domain emerges in the aaRS family.
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Photoaffinity labeling of mouse fibroblast enzymes by a base excision repair intermediate. Evidence for the role of poly(ADP-ribose) polymerase-1 in DNA repair.

Olga I. Lavrik, +6 more
- 06 Jul 2001 - 
TL;DR: It is shown that proteins interacting preferentially with a photoreactive BER intermediate can be selected from the crude cellular extract and the specificity of PARP-1 labeling was stronger with a DNA representing a B ER intermediate than with a nick in double-stranded DNA.
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Human replication protein A unfolds telomeric G-quadruplexes.

Tonatiuh Romero Salas, +6 more
- 01 Oct 2006 - 
TL;DR: It is shown that under near-physiological in vitro conditions, human RPA is able to bind and unfold G-quadruplex structures formed from a 21mer human telomeric sequence, pointing to the involvement of hRPA in regulation of telomere maintenance.