Improvement of duplex-specific nuclease salt tolerance by fusing DNA-binding domain of DNase from an extremely halotolerant bacterium Thioalkalivibrio sp. K90mix-Reference-Cited by-同舟云学术

Improvement of duplex-specific nuclease salt tolerance by fusing DNA-binding domain of DNase from an extremely halotolerant bacterium Thioalkalivibrio sp. K90mix

Published:2023-05-13 Issue:2 Volume:27 Page:
ISSN:1431-0651
Container-title:Extremophiles
language:en
Short-container-title:Extremophiles

Author:

Hu Wenhao,Wang Jin,Li Juan,Yang Mengxia,Li Zhixing,Zhang Xuning,Wu Fang,Zhang Yaqi,Luo Zhidan,Xu Henghao

Funder

Priority Academic Program Development of Jiangsu Higher Education Institutions

Publisher

Springer Science and Business Media LLC

Subject

Molecular Medicine,General Medicine,Microbiology

Link

https://link.springer.com/content/pdf/10.1007/s00792-023-01296-1.pdf

Reference28 articles.

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2. Alzbutas G, Kaniusaite M, Grybauskas A et al (2015) Domain organization of DNase from Thioalkalivibrio sp. provides insights into retention of activity in high salt environments. Front Microbiol. 6:661. https://doi.org/10.3389/fmicb.2015.00661. (PubMed PMID: 26191053; PubMed Central PMCID: PMCPMC4486849)

3. Alzbutas G, Kaniusaite M, Lagunavicius A (2016) Enhancement of DNaseI salt tolerance by mimicking the domain structure of dnase from an extremely halotolerant bacterium Thioalkalivibrio sp. K90mix. PLoS One. 11(3):e0150404. https://doi.org/10.1371/journal.pone.0150404. (PubMed PMID: 26939122; PubMed Central PMCID: PMCPMC4777378 conflicts of interest relevant to this article are reported. This does not alter the authors' adherence to PLOS ONE policies on sharing data and materials)

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5. Anisimova VE, Barsova EV, Bogdanova EA et al (2009) Thermolabile duplex-specific nuclease. Biotechnol Lett. 31(2):251–7. https://doi.org/10.1007/s10529-008-9850-y. (PubMed PMID: 18810329)