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the extreme N-terminal part of Polkappa (show POLL ELISA Kits) is required for the processivity and fidelity of Polkappa (show POLL ELISA Kits) during translesion synthesis of 10S(+)-trans-anti-benzo[a]pyrene diol epoxide-N(2)-deoxyguanine adducts lesions.
Polk plays a predominant role in suppressing point mutations by carrying out error-free translesion DNA synthesis and contributes to the prevention of DNA strand breaks.
The structural gap physically accommodates the bulky aromatic adduct and the N-clasp (show CLASRP ELISA Kits) is essential for the structural integrity and flexibility of Polkappa (show POLL ELISA Kits) during translesion synthesis.
Polkappa (show POLL ELISA Kits) accumulates at laser-induced sites of DNA damage.
Structural basis of Rev1-mediated assembly of a quaternary vertebrate translesion polymerase complex consisting of Rev1, heterodimeric polymerase (Pol) zeta, and Pol kappa (show POLL ELISA Kits)
Data suggest that DNA polymerase kappa Polkapp (show POLL ELISA Kits)a functions in DNA interstrand crosslinks (ICLs) repair in (show APBB1 ELISA Kits) embryonic fibroblast cells (MEF), especially during the G0/G1 phases.
solution structure of the polymerase kappa-Rev1 complex
results are consistent with the notion that Pol kappa (show POLL ELISA Kits) is required for accurate translesion DNA synthesis past naturally occurring polycyclic guanine adducts, possibly generated by cholesterol and/or its metabolites.
Polkappa (show POLL ELISA Kits) plays an important role in suppressing mutations at DNA lesions generated by benzo[a]pyrene, but not UV or x-ray irradiation.
Rev7 competes directly with Pol kappa for binding to the Rev1 C-terminus.
The structure of polK captured at the lesion-extension stage is reported: the enzyme is extending the primer strand after the base pair containing the BP-dG adduct in the template strand at the -1 position. PolK accommodates the BP adduct in the nascent DNA's minor groove and keeps the adducted DNA helix in a B-form.
A report on the structure of human polkappa (show POLL ELISA Kits) in complex with a major benzo[a]pyrene adduct reveal a unique mechanism for accurate replication by translesion synthesis past the major bulky adduct.
These studies revealed that POLK is a crucial host factor required for covalently closed circular DNA formation during a de novo HBV infection
POLK protein polymorphisms may influence the risk of developing breast cancer among Chinese women.
Somatic Mutations in Catalytic Core of POLK Reported in Prostate Cancer Alter Translesion DNA Synthesis
POLK not only protects cells from genotoxic DNA lesions via DNA polymerase (show POLB ELISA Kits) activities, but also contributes to genome integrity by acting as a non-catalytic protein against oxidative damage caused by hydrogen peroxide and menadione.
The structural dynamics of DinB1 changes upon substrate binding, noncognate DNA damage prevents the formation of the active conformation of DINB1.
polymorphism of POLK, an important gene in TLS (show FUS ELISA Kits), participates in platinum-chemotherapy tolerance and side-effect
Mutations in PIP1 (show PAK1IP1 ELISA Kits) domain inhibits the stimulation of DNA synthesis by Polkappa (show POLL ELISA Kits) in the presence of proliferating cell nuclear antigen (show PCNA ELISA Kits), replication factor C, and replication protein A; and mutations in PIP2 have no effect on PCNA (show PCNA ELISA Kits)-dependent DNA synthesis.
The truncation R219X was devoid of polymerase activity, and the E419G and Y432S variants showed much lower polymerase activity than wild-type POLK.
DNA polymerase kappa-dependent DNA synthesis at stalled replication forks is important for CHK1 (show CHEK1 ELISA Kits) activation.
Data show that DNA polymerase kappa (Pol kappa (show POLL ELISA Kits)) is essential for replication-independent ICL repair (RIR (show APBB1 ELISA Kits)) of a site-specific DNA interstrand crosslinks (ICLs) lesion.
pol kappa (show POLL ELISA Kits) (translesion synthesis TLS4) may assist pol eta (TLS3 or Rad30 (show POLH ELISA Kits)) in error-free extension during cyclobutane pyrimidine dimer bypass during DNA replication in oocyte extracts.
External and internal DNA-damaging agents continually threaten the integrity of genetic material in cells. Although a variety of repair mechanisms exist to remove the resulting lesions, some lesions escape repair and block the replication machinery. Members of the Y family of DNA polymerases, such as POLK, permit the continuity of the replication fork by allowing replication through such DNA lesions. Each Y family polymerase has a unique DNA-damage bypass and fidelity profile. POLK is specialized for the extension step of lesion bypass (summary by Lone et al., 2007
DNA polymerase kappa
, DNA-directed DNA polymerase kappa
, polymerase (DNA directed) kappa
, DNA polymerase kappa-like
, DNA polymerase sigma
, PAP-associated domain-containing protein 7
, polymerase (DNA directed) sigma
, DINB protein
, DNA damage-inducible protein b
, DinB homolog 1