Khalatova AG - Search Results

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The catalytic domain of Escherichia coli Lon protease has a unique fold and a Ser-Lys dyad in the active site.

Botos I, Melnikov EE, Cherry S, Tropea JE, Khalatova AG, Rasulova F, Dauter Z, Maurizi MR, Rotanova TV, Wlodawer A, Gustchina A. Botos I, et al. Among authors: khalatova ag. J Biol Chem. 2004 Feb 27;279(9):8140-8. doi: 10.1074/jbc.M312243200. Epub 2003 Dec 9. J Biol Chem. 2004. PMID: 14665623 Free article.

Crystal structure of the AAA+ alpha domain of E. coli Lon protease at 1.9A resolution.

Botos I, Melnikov EE, Cherry S, Khalatova AG, Rasulova FS, Tropea JE, Maurizi MR, Rotanova TV, Gustchina A, Wlodawer A. Botos I, et al. Among authors: khalatova ag. J Struct Biol. 2004 Apr-May;146(1-2):113-22. doi: 10.1016/j.jsb.2003.09.003. J Struct Biol. 2004. PMID: 15037242 Review.

Classification of ATP-dependent proteases Lon and comparison of the active sites of their proteolytic domains.

Rotanova TV, Melnikov EE, Khalatova AG, Makhovskaya OV, Botos I, Wlodawer A, Gustchina A. Rotanova TV, et al. Among authors: khalatova ag. Eur J Biochem. 2004 Dec;271(23-24):4865-71. doi: 10.1111/j.1432-1033.2004.04452.x. Eur J Biochem. 2004. PMID: 15606774 Free article.

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