ReviewBiochemistry2014
Recent insight into the kinetic mechanisms and conformational dynamics of Y-Family DNA polymerases.
Review in Biochemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
24 citing papers in PubMed, 39 citations in OpenAlex.
- Conformational gating governs nucleotide incorporation by a DNA-crosslinked polymerase.Nucleic acids research · 2026Article
- Translesion synthesis of apurinic/apyrimidic site analogues by Y-family DNA polymerase Dbh fromActa biochimica et biophysica Sinica · 2022Article
- Mechanism Underlying the Bypass of Apurinic/Pyrimidinic Site Analogs byInternational journal of molecular sciences · 2022Article
- Cryo-EM structure of human Pol κ bound to DNA and mono-ubiquitylated PCNA.Nature communications · 2021Article
- Dynamic Processing of a Common Oxidative DNA Lesion by the First Two Enzymes of the Base Excision Repair Pathway.Journal of molecular biology · 2021Article
- Response of Sulfolobus solfataricus Dpo4 polymerase in vitro to a DNA G-quadruplex.Mutagenesis · 2019Article
- Kinetic Investigation of Translesion Synthesis across a 3-Nitrobenzanthrone-Derived DNA Lesion Catalyzed by Human DNA Polymerase Kappa.Chemical research in toxicology · 2019Article
- Bulky Lesion Bypass Requires Dpo4 Binding in Distinct Conformations.Scientific reports · 2017Article
- Translesion DNA polymerases in eukaryotes: what makes them tick?Critical reviews in biochemistry and molecular biology · 2017Review
- Advances in Structural and Single-Molecule Methods for Investigating DNA Lesion Bypass and Repair Polymerases.Chemical research in toxicology · 2017Article
- Review
- Significant impact of divalent metal ions on the fidelity, sugar selectivity, and drug incorporation efficiency of human PrimPol.DNA repair · 2017Article
- Investigation of Intradomain Motions of a Y-Family DNA Polymerase during Substrate Binding and Catalysis.Biochemistry · 2016Article
- Translesion synthesis past guanine(C8)-thymine(N3) intrastrand cross-links catalyzed by selected A- and Y-family polymerases.Molecular bioSystems · 2016Article
- Single-Molecule Investigation of Response to Oxidative DNA Damage by a Y-Family DNA Polymerase.Biochemistry · 2016Article
- Cooperative motion of a key positively charged residue and metal ions for DNA replication catalyzed by human DNA Polymerase-η.Nucleic acids research · 2016Article
- A new paradigm of DNA synthesis: three-metal-ion catalysis.Cell & bioscience · 2016Review
- Comparative Molecular Dynamics Studies of Human DNA Polymerase η.Journal of chemical information and modeling · 2015Article
- Molecular architecture of the Ub-PCNA/Pol η complex bound to DNA.Scientific reports · 2015Article
- Mechanistic Basis for the Bypass of a Bulky DNA Adduct Catalyzed by a Y-Family DNA Polymerase.Journal of the American Chemical Society · 2015Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The kinetic mechanisms by which DNA polymerases catalyze DNA replication and repair have long been areas of active research. Recently discovered Y-family DNA polymerases catalyze the bypass of damaged DNA bases that would otherwise block replicative DNA polymerases and stall replication forks. Unlike DNA polymerases from the five other families, the Y-family DNA polymerases have flexible, solvent-accessible active sites that are able to tolerate various types of damaged template bases and allow for efficient lesion bypass. Their promiscuous active sites, however, also lead to fidelities that are much lower than those observed for other DNA polymerases and give rise to interesting mechanistic properties. Additionally, the Y-family DNA polymerases have several other unique structural features and undergo a set of conformational changes during substrate binding and catalysis different from those observed for replicative DNA polymerases. In recent years, pre-steady-state kinetic methods have been extensively employed to reveal a wealth of information about the catalytic properties of these fascinating noncanonical DNA polymerases. Here, we review many of the recent findings on the kinetic mechanisms of DNA polymerization with undamaged and damaged DNA substrates by the Y-family DNA polymerases, and the conformational dynamics employed by these error-prone enzymes during catalysis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.