Olga I Lavrik

Ontology type: schema:Person     

Person Info


Olga I



Publications in SciGraph latest 50 shown

  • 2018-12 Dna is a New Target of Parp3 in SCIENTIFIC REPORTS
  • 2018-11 Excision of Carbohydrate-Modified dNMP Analogues from DNA 3' end by Human Apurinic/Apyrimidinic Endonuclease 1 (APE1) and Tyrosyl-DNA Phosphodiesterase 1 (TDP1) in MOLECULAR BIOLOGY
  • 2018-09 A New DNA Break Repair Pathway Involving PARP3 and Base Excision Repair Proteins in DOKLADY BIOCHEMISTRY AND BIOPHYSICS
  • 2018-07 Synthesis and Inhibitory Properties of Imines Containing Monoterpenoid and Adamantane Fragments Against DNA Repair Enzyme Tyrosyl-DNA Phosphodiesterase 1 (Tdp1) in CHEMISTRY OF NATURAL COMPOUNDS
  • 2018-04 Protein–Protein Interactions in DNA Base Excision Repair in BIOCHEMISTRY (MOSCOW)
  • 2018-03 DNA Bearing Bulky Fluorescent and Photoreactive Damage in Both Strands as Substrates of the Nucleotide Excision Repair System in MOLECULAR BIOLOGY
  • 2018-02 2,5-Diketopiperazines: A New Class of Poly(ADP-ribose)polymerase Inhibitors in BIOCHEMISTRY (MOSCOW)
  • 2018-01 DNA Repair Enzymes as Promising Targets in Oncotherapy in RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY
  • 2017-12 The genome-wide transcription response to telomerase deficiency in the thermotolerant yeast Hansenula polymorpha DL-1 in BMC GENOMICS
  • 2017-12 Y-box-binding protein 1 stimulates abasic site cleavage in BIOCHEMISTRY (MOSCOW)
  • 2017-06 Role of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) in DNA repair in BIOCHEMISTRY (MOSCOW)
  • 2017-02 A versatile strategy for the design and synthesis of novel ADP conjugates and their evaluation as potential poly(ADP-ribose) polymerase 1 inhibitors in MOLECULAR DIVERSITY
  • 2017-01 Usnic acid derivatives are effective inhibitors of tyrosyl-DNA phosphodiesterase 1 in RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY
  • 2017-01 Synthesis of a series of NAD+ analogues, potential inhibitors of PARP 1, using ADP conjugates functionalized at the terminal phosphate group in RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY
  • 2016-09 Replication protein A as a major eukaryotic single-stranded DNA-binding protein and its role in DNA repair in MOLECULAR BIOLOGY
  • 2016-09 AP endonuclease 1 as a key enzyme in repair of apurinic/apyrimidinic sites in BIOCHEMISTRY (MOSCOW)
  • 2016-07 Poly(ADP-Ribose) polymerase 1 as a key regulator of DNA repair in MOLECULAR BIOLOGY
  • 2016-03 DNA with damage in both strands as affinity probes and nucleotide excision repair substrates in BIOCHEMISTRY (MOSCOW)
  • 2016-03 Interaction of nucleotide excision repair protein XPC—RAD23B with DNA containing benzo[a]pyrene-derived adduct and apurinic/apyrimidinic site within a cluster in BIOCHEMISTRY (MOSCOW)
  • 2015-11 Inhibitory properties of nitrogen-containing adamantane derivatives with monoterpenoid fragments against tyrosyl-DNA phosphodiesterase 1 in RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY
  • 2015-09 Tyrosyl-DNA phosphodiesterase 1 is a new player in repair of apurinic/apyrimidinic sites in RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY
  • 2015-08 Repair of clustered damage and DNA polymerase iota in BIOCHEMISTRY (MOSCOW)
  • 2015-05 Expression of genes involved in DNA repair and telomere maintenance in the yeast Hansenula polymorpha DL1 under heat stress in DOKLADY BIOCHEMISTRY AND BIOPHYSICS
  • 2015-02 Y-box binding protein 1 (YB-1) promotes detection of DNA bulky lesions by XPC-HR23B factor in BIOCHEMISTRY (MOSCOW)
  • 2015-01 Role of Ku antigen in the repair of apurinic/apyrimidinic sites in DNA in MOLECULAR BIOLOGY
  • 2015-01 Nucleotide excision repair factor XPC-RAD23B is poly(ADP-ribosylated) by the poly(ADP-ribose) polymerase 1 in DOKLADY BIOCHEMISTRY AND BIOPHYSICS
  • 2014-07 Role of PARP2 in DNA repair in MOLECULAR BIOLOGY
  • 2014-06 Effect of point substitutions within the minimal DNA-binding domain of xeroderma pigmentosum group a protein on interaction with DNA intermediates of nucleotide excision repair in BIOCHEMISTRY (MOSCOW)
  • 2014-03 Repair of apurinic/apyrimidinic sites in single-stranded DNA initiated by tyrosyl-DNA phosphodiesterase 1 in DOKLADY BIOCHEMISTRY AND BIOPHYSICS
  • 2013-09 Repair of bulky DNA lesions deriving from polycyclic aromatic hydrocarbons in MOLECULAR BIOLOGY
  • 2012-06 Hit clustering can improve virtual fragment screening: CDK2 and PARP1 case studies in JOURNAL OF MOLECULAR MODELING
  • 2012-05 Interaction of nucleotide excision repair proteins with DNA containing bulky lesion and apurinic/apyrimidinic site in BIOCHEMISTRY (MOSCOW)
  • 2012-04 Influence of centrin 2 on the interaction of nucleotide excision repair factors with damaged DNA in BIOCHEMISTRY (MOSCOW)
  • 2011-06 Improved procedure of the search for poly(ADP-Ribose) polymerase-1 potential inhibitors with the use of the molecular docking approach in MOLECULAR BIOLOGY
  • 2011-01 Photoactivated DNA analogs of substrates of the nucleotide excision repair system and their interaction with proteins of NER-competent extract of HeLa cells. Synthesis and application of long model DNA in BIOCHEMISTRY (MOSCOW)
  • 2011-01 Affinity modification in a proteomic study of DNA repair ensembles in RUSSIAN JOURNAL OF BIOORGANIC CHEMISTRY
  • 2011-01 Interaction of poly(ADP-ribose) polymerase 1 with apurinic/apyrimidinic sites within clustered DNA damage in BIOCHEMISTRY (MOSCOW)
  • 2011-01 Nucleotide excision repair: DNA damage recognition and preincision complex assembly in BIOCHEMISTRY (MOSCOW)
  • 2010-12 DNA polymerases β and λ and their roles in DNA replication and repair in MOLECULAR BIOLOGY
  • 2010-04 Poly(ADP-ribose) polymerase 1 interaction with apurinic/apyrimidinic sites in DOKLADY BIOCHEMISTRY AND BIOPHYSICS
  • 2009-12-04 Nucleotide Excision Repair in Higher Eukaryotes: Mechanism of Primary Damage Recognition in Global Genome Repair in GENOME STABILITY AND HUMAN DISEASES
  • 2009-11 Interaction of DNA topoisomerase 1 with DNA intermediates and proteins of base excision repair in BIOCHEMISTRY (MOSCOW)
  • 2009-05 Photoactivated DNA analogs of substrates of the nucleotide excision repair system and their interaction with proteins of NER-competent HeLa cell extract in BIOCHEMISTRY (MOSCOW)
  • 2009-02 Identification of Ku80 subunit of Ku antigen as a protein reactive to apurinic/apyrimidinic sites in DOKLADY BIOCHEMISTRY AND BIOPHYSICS
  • 2009-01 Replication protein A modulates the activity of human telomerase in vitro in BIOCHEMISTRY (MOSCOW)
  • 2008-12 Mechanisms of single-stranded DNA-binding protein functioning in cellular DNA metabolism in BIOCHEMISTRY (MOSCOW)
  • 2008-11 DNA polymerases β and λ as potential participants of TLS during genomic DNA replication on the lagging strand in BIOCHEMISTRY (MOSCOW)
  • 2008-09 Interaction between DNA polymerase λ and RPA during translesion synthesis in BIOCHEMISTRY (MOSCOW)
  • 2008-08 Interaction of nucleotide excision repair factors XPC-HR23B, XPA, and RPA with damaged DNA in BIOCHEMISTRY (MOSCOW)
  • 2008-06 Flap endonuclease 1 and its role in eukaryotic DNA metabolism in MOLECULAR BIOLOGY
  • JSON-LD is the canonical representation for SciGraph data.

    TIP: You can open this SciGraph record using an external JSON-LD service: JSON-LD Playground Google SDTT

        "@context": "https://springernature.github.io/scigraph/jsonld/sgcontext.json", 
        "affiliation": [
            "affiliation": {
              "id": "https://www.grid.ac/institutes/grid.4605.7", 
              "type": "Organization"
            "isCurrent": true, 
            "type": "OrganizationRole"
            "id": "https://www.grid.ac/institutes/grid.4886.2", 
            "type": "Organization"
            "id": "https://www.grid.ac/institutes/grid.48336.3a", 
            "type": "Organization"
            "id": "https://www.grid.ac/institutes/grid.280664.e", 
            "type": "Organization"
            "id": "https://www.grid.ac/institutes/grid.77225.35", 
            "type": "Organization"
            "id": "https://www.grid.ac/institutes/grid.418910.5", 
            "type": "Organization"
            "id": "https://www.grid.ac/institutes/grid.419817.2", 
            "type": "Organization"
            "id": "https://www.grid.ac/institutes/grid.14476.30", 
            "type": "Organization"
            "id": "https://www.grid.ac/institutes/grid.418853.3", 
            "type": "Organization"
            "id": "https://www.grid.ac/institutes/grid.214572.7", 
            "type": "Organization"
            "id": "https://www.grid.ac/institutes/grid.464621.3", 
            "type": "Organization"
            "id": "https://www.grid.ac/institutes/grid.415877.8", 
            "type": "Organization"
        "familyName": "Lavrik", 
        "givenName": "Olga I", 
        "id": "sg:person.014141015537.37", 
        "sameAs": [
        "sdDataset": "persons", 
        "sdDatePublished": "2019-03-07T13:34", 
        "sdLicense": "https://scigraph.springernature.com/explorer/license/", 
        "sdPublisher": {
          "name": "Springer Nature - SN SciGraph project", 
          "type": "Organization"
        "sdSource": "s3://com-uberresearch-data-dimensions-researchers-20181010/20181011/dim_researchers/base/researchers_1360.json", 
        "type": "Person"

    Download the RDF metadata as:  json-ld nt turtle xml License info


    JSON-LD is a popular format for linked data which is fully compatible with JSON.

    curl -H 'Accept: application/ld+json' 'https://scigraph.springernature.com/person.014141015537.37'

    N-Triples is a line-based linked data format ideal for batch operations.

    curl -H 'Accept: application/n-triples' 'https://scigraph.springernature.com/person.014141015537.37'

    Turtle is a human-readable linked data format.

    curl -H 'Accept: text/turtle' 'https://scigraph.springernature.com/person.014141015537.37'

    RDF/XML is a standard XML format for linked data.

    curl -H 'Accept: application/rdf+xml' 'https://scigraph.springernature.com/person.014141015537.37'


    This table displays all metadata directly associated to this object as RDF triples.

    38 TRIPLES      10 PREDICATES      22 URIs      7 LITERALS      2 BLANK NODES

    Subject Predicate Object
    1 sg:person.014141015537.37 schema:affiliation N48ecf3a71c2a44b2a5078b02988c6cca
    2 https://www.grid.ac/institutes/grid.14476.30
    3 https://www.grid.ac/institutes/grid.214572.7
    4 https://www.grid.ac/institutes/grid.280664.e
    5 https://www.grid.ac/institutes/grid.415877.8
    6 https://www.grid.ac/institutes/grid.418853.3
    7 https://www.grid.ac/institutes/grid.418910.5
    8 https://www.grid.ac/institutes/grid.419817.2
    9 https://www.grid.ac/institutes/grid.464621.3
    10 https://www.grid.ac/institutes/grid.48336.3a
    11 https://www.grid.ac/institutes/grid.4886.2
    12 https://www.grid.ac/institutes/grid.77225.35
    13 schema:familyName Lavrik
    14 schema:givenName Olga I
    15 schema:sameAs https://app.dimensions.ai/discover/publication?and_facet_researcher=ur.014141015537.37
    16 schema:sdDatePublished 2019-03-07T13:34
    17 schema:sdLicense https://scigraph.springernature.com/explorer/license/
    18 schema:sdPublisher Nebb3989e568b44eb98d8bb0d14b5e77f
    19 sgo:license sg:explorer/license/
    20 sgo:sdDataset persons
    21 rdf:type schema:Person
    22 N48ecf3a71c2a44b2a5078b02988c6cca schema:affiliation https://www.grid.ac/institutes/grid.4605.7
    23 sgo:isCurrent true
    24 rdf:type schema:OrganizationRole
    25 Nebb3989e568b44eb98d8bb0d14b5e77f schema:name Springer Nature - SN SciGraph project
    26 rdf:type schema:Organization
    27 https://www.grid.ac/institutes/grid.14476.30 schema:Organization
    28 https://www.grid.ac/institutes/grid.214572.7 schema:Organization
    29 https://www.grid.ac/institutes/grid.280664.e schema:Organization
    30 https://www.grid.ac/institutes/grid.415877.8 schema:Organization
    31 https://www.grid.ac/institutes/grid.418853.3 schema:Organization
    32 https://www.grid.ac/institutes/grid.418910.5 schema:Organization
    33 https://www.grid.ac/institutes/grid.419817.2 schema:Organization
    34 https://www.grid.ac/institutes/grid.4605.7 schema:Organization
    35 https://www.grid.ac/institutes/grid.464621.3 schema:Organization
    36 https://www.grid.ac/institutes/grid.48336.3a schema:Organization
    37 https://www.grid.ac/institutes/grid.4886.2 schema:Organization
    38 https://www.grid.ac/institutes/grid.77225.35 schema:Organization

    Preview window. Press ESC to close (or click here)