Architecture and characterization of a thermostable MoxR family AAA+ ATPase from Thermococcus kodakarensis KOD1-Reference-Cited by-同舟云学术

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Architecture and characterization of a thermostable MoxR family AAA+ ATPase from Thermococcus kodakarensis KOD1

Published:2014-03-18 Issue:3 Volume:18 Page:537-544
ISSN:1431-0651
Container-title:Extremophiles
language:en
Short-container-title:Extremophiles

Author:

Pham Bang Phuong,Lee Sangmin,Jia Baolei,Kwak Jae Myeong,Cheong Gang-Won

Publisher

Springer Science and Business Media LLC

Subject

Molecular Medicine,General Medicine,Microbiology

Link

http://link.springer.com/content/pdf/10.1007/s00792-014-0639-8.pdf

Reference22 articles.

1. Baumeister W, Dahlmann B et al (1988) Electron microscopy and image analysis of the multicatalytic proteinase. FEBS Lett 241(1–2):239–245

2. Chinnusamy V, Zhu J, Zhu J-K (2007) Cold stress regulation of gene expression in plants. Trends Plant Sci 12(10):444–451

3. Eggleston AK, Rahim NA et al (1996) A helicase assay based on the displacement of fluorescent, nucleic acid-binding ligands. Nucleic Acids Res 24(7):1179–1186

4. El Bakkouri M, Gutsche I et al (2010) Structure of RavA MoxR AAA+ protein reveals the design principles of a molecular cage modulating the inducible lysine decarboxylase activity. Proc Natl Acad Sci USA 107(52):22499–22504

5. Fukui T, Atomi H et al (2005) Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes. Genome Res 15(3):352–363

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