Structure of the Helicase Domain of DNA Polymerase Theta Reveals a Possible Role in the Microhomology-Mediated End-Joining Pathway-Reference-Cited by-同舟云学术

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Structure of the Helicase Domain of DNA Polymerase Theta Reveals a Possible Role in the Microhomology-Mediated End-Joining Pathway

Published:2015-12 Issue:12 Volume:23 Page:2319-2330
ISSN:0969-2126
Container-title:Structure
language:en
Short-container-title:Structure

Author:

Newman Joseph A.,Cooper Christopher D.O.,Aitkenhead Hazel,Gileadi Opher

Funder

E. P. Abraham Cephalosporin Fund

Linacre College

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference52 articles.

1. Low-fidelity DNA synthesis by human DNA polymerase theta;Arana;Nucleic Acids Res.,2008

2. High-resolution structure of the E.coli RecQ helicase catalytic core;Bernstein;EMBO J.,2003

3. Compilation, alignment, and phylogenetic relationships of DNA polymerases;Braithwaite;Nucleic Acids Res.,1993

4. Structural basis for DNA duplex separation by a superfamily-2 helicase;Buttner;Nat. Struct. Mol. Biol.,2007

5. Integrated genomic analyses of ovarian carcinoma;Cancer Genome Atlas Research Network;Nature,2011

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2. Structural basis for a Polθ helicase small-molecule inhibitor revealed by cryo-EM;Nature Communications;2024-08-14

3. PARG is essential for Polθ-mediated DNA end-joining by removing repressive poly-ADP-ribose marks;Nature Communications;2024-07-11

4. Structural Basis for Polθ-Helicase DNA Binding and Microhomology-Mediated End-Joining;2024-06-07

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