Relationship between thermal stability and 3-D structure in a homology model of 3-isopropylmalate dehydrogenase from Escherichia coli
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,Bioengineering,Biotechnology
Link
http://academic.oup.com/peds/article-pdf/9/8/663/4309753/9-8-663.pdf
Cited by 12 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Characterization of 3-isopropylmalate dehydrogenase from extremely halophilic archaeon Haloarcula japonica;Bioscience, Biotechnology, and Biochemistry;2021-07-02
2. Multifactorial level of extremostability of proteins: can they be exploited for protein engineering?;Extremophiles;2017-03-10
3. Rigidity versus flexibility: the dilemma of understanding protein thermal stability;FEBS Journal;2015-07-15
4. Highly thermostable and surfactant-activated chitinase from a subseafloor bacterium, Laceyella putida;Applied Microbiology and Biotechnology;2014-04-16
5. Atomic level description of the domain closure in a dimeric enzyme: Thermus thermophilus 3-isopropylmalate dehydrogenase;Molecular BioSystems;2011
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