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Structure of the helicase domain of DNA polymerase theta reveals a possible role in the microhomology-mediated end-joining pathway

Abstract:

DNA polymerase theta (Polθ) has been identified as a crucial alternative non-homologous end-joining factor in mammalian cells. Polθ is upregulated in a range of cancer cell types defective in homologous recombination, and knockdown has been shown to inhibit cell survival in a subset of these, making it an attractive target for cancer treatment. We present crystal structures of the helicase domain of human Polθ in the presence and absence of bound nucleotides, and a characterization of its DNA...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1016/j.str.2015.10.014

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Institution:
University of Oxford
Department:
Oxford, MSD, NDM, Structural Genomics Consortium
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, NDM, Structural Genomics Consortium
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, NDM, Structural Genomics Consortium
Role:
Author
More by this author
Institution:
University of Oxford
Department:
Oxford, MSD, NDM, Structural Genomics Consortium
Role:
Author
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Funding agency for:
Cooper, CD
Bayer Pharma AG More from this funder
Boehringer Ingelheim More from this funder
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Publisher:
Elsevier (Cell Press) Publisher's website
Journal:
Structure Journal website
Volume:
23
Issue:
12
Pages:
2319-2330
Publication date:
2015-12-05
DOI:
EISSN:
1878-4186
ISSN:
0969-2126
URN:
uuid:57bbe073-022a-412e-8e78-29cb44d8dc01
Source identifiers:
580216
Local pid:
pubs:580216
Language:
English

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