Human DNA polymerase θ grasps the primer terminus to mediate DNA repair
about
DNA polymerase θ (POLQ), double-strand break repair, and cancerDNA Polymerase θ: A Unique Multifunctional End-Joining MachineNoncanonical views of homology-directed DNA repairMicrohomology-Mediated End Joining: A Back-up Survival Mechanism or Dedicated Pathway?Drosophila DNA polymerase theta utilizes both helicase-like and polymerase domains during microhomology-mediated end joining and interstrand crosslink repairError-Prone Repair of DNA Double-Strand Breaks.Linking DNA polymerase theta structure and function in health and diseaseRepair Pathway Choices and Consequences at the Double-Strand BreakPolymerase θ is a robust terminal transferase that oscillates between three different mechanisms during end-joiningExcess Polθ functions in response to replicative stress in homologous recombination-proficient cancer cells.DNA polymerase θ specializes in incorporating synthetic expanded-size (xDNA) nucleotidesEssential Roles for Polymerase θ-Mediated End Joining in the Repair of Chromosome Breaks.Regulation of Single-Strand Annealing and its Role in Genome Maintenance.Structure of the Helicase Domain of DNA Polymerase Theta Reveals a Possible Role in the Microhomology-Mediated End-Joining Pathway.Mutagenic consequences of a single G-quadruplex demonstrate mitotic inheritance of DNA replication fork barriers.Expression and Structural Analyses of Human DNA Polymerase θ (POLQ).Polθ helicase: drive or reverse.Secondary structure forming sequences drive SD-MMEJ repair of DNA double-strand breaks.Off-Target Effects of Drugs that Disrupt Human Mitochondrial DNA Maintenance.Family A and B DNA Polymerases in Cancer: Opportunities for Therapeutic Interventions.Mutational signatures of non-homologous and polymerase theta-mediated end-joining in embryonic stem cells.DNA polymerase beta participates in DNA End-joining.The helicase domain of Polθ counteracts RPA to promote alt-NHEJ.Plant organellar DNA polymerases are replicative and translesion DNA synthesis polymerases.In Vitro Bypass of Thymidine Glycol by DNA Polymerase θ Forms Sequence-Dependent Frameshift Mutations.The A-Rule and Deletion Formation During Abasic and Oxidized Abasic Site Bypass by DNA Polymerase θ.Translesion and Repair DNA Polymerases: Diverse Structure and Mechanism.Genomic and Molecular Landscape of DNA Damage Repair Deficiency across The Cancer Genome Atlas.Structures of human DNA polymerases ν and θ expose their end game.
P2860
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P2860
Human DNA polymerase θ grasps the primer terminus to mediate DNA repair
description
2015 nî lūn-bûn
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2015 թուականի Մարտին հրատարակուած գիտական յօդուած
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2015 թվականի մարտին հրատարակված գիտական հոդված
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2015年の論文
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2015年論文
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2015年論文
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2015年論文
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2015年論文
@zh-mo
2015年論文
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2015年论文
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name
Human DNA polymerase θ grasps the primer terminus to mediate DNA repair
@ast
Human DNA polymerase θ grasps the primer terminus to mediate DNA repair
@en
type
label
Human DNA polymerase θ grasps the primer terminus to mediate DNA repair
@ast
Human DNA polymerase θ grasps the primer terminus to mediate DNA repair
@en
prefLabel
Human DNA polymerase θ grasps the primer terminus to mediate DNA repair
@ast
Human DNA polymerase θ grasps the primer terminus to mediate DNA repair
@en
P2860
P50
P356
P1476
Human DNA polymerase θ grasps the primer terminus to mediate DNA repair
@en
P2093
April M Averill
Karl E Zahn
P2860
P2888
P304
P356
10.1038/NSMB.2993
P577
2015-03-16T00:00:00Z