Deinococcus radiodurans DR1088 is a novel RecF-interacting protein that stimulates single-stranded DNA annealing.

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Deinococcus radiodurans DR1088 is a novel RecF-interacting protein that stimulates single-stranded DNA annealing.

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2017 nî lūn-bûn

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2017年の論文

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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2017年学术文章

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Deinococcus radiodurans DR1088 ...... single-stranded DNA annealing.

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Deinococcus radiodurans DR1088 ...... single-stranded DNA annealing.

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Deinococcus radiodurans DR1088 ...... single-stranded DNA annealing.

@en

Deinococcus radiodurans DR1088 ...... single-stranded DNA annealing.

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Deinococcus radiodurans DR1088 ...... single-stranded DNA annealing.

@en

Deinococcus radiodurans DR1088 ...... single-stranded DNA annealing.

@nl

P1476

Deinococcus radiodurans DR1088 ...... single-stranded DNA annealing.

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P2093

Guangzhi Xu

http://www.w3.org/2001/XMLSchema#string

Hong Xu

http://www.w3.org/2001/XMLSchema#string

Kaiying Cheng

http://www.w3.org/2001/XMLSchema#string

Ye Zhao

http://www.w3.org/2001/XMLSchema#string

Yuejin Hua

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P2860

Genome Sequence of the Radioresistant Bacterium Deinococcus radiodurans R1

Structure of the single-strand annealing domain of human RAD52 protein

RecFOR and RecOR as distinct RecA loading pathways

The process of displacing the single-stranded DNA-binding protein from single-stranded DNA by RecO and RecR proteins

Preserving genome integrity: the DdrA protein of Deinococcus radiodurans R1

Classification and evolutionary history of the single-strand annealing proteins, RecT, Redbeta, ERF and RAD52

Mechanism of RecO recruitment to DNA by single-stranded DNA binding protein

Crystal structure of the DdrB/ssDNA complex from Deinococcus radiodurans reveals a DNA binding surface involving higher-order oligomeric states

Structural insight into substrate preference for TET-mediated oxidation

Rad52 forms ring structures and co-operates with RPA in single-strand DNA annealing.

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518-529

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scholarly article

P356

10.1111/MMI.13828

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English

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106

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P577

2017-09-01T00:00:00Z

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28862774

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