The role of a topologically conserved isoleucine in glutathione transferase structure, stability and function-Reference-Cited by-同舟云学术

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The role of a topologically conserved isoleucine in glutathione transferase structure, stability and function

Published:2010-06-23 Issue:7 Volume:66 Page:776-780
ISSN:1744-3091
Container-title:Acta Crystallographica Section F Structural Biology and Crystallization Communications
language:
Short-container-title:Acta Cryst Sect F

Author:

Achilonu Ikechukwu,Gildenhuys Samantha,Fisher Loren,Burke Jonathan,Fanucchi Sylvia,Sewell B. Trevor,Fernandes Manuel,Dirr Heini W.

Publisher

International Union of Crystallography (IUCr)

Subject

Condensed Matter Physics,Genetics,Biochemistry,Structural Biology,Biophysics

Link

http://journals.iucr.org/f/issues/2010/07/00/en5420/en5420.pdf

Reference36 articles.

1. Structure, Catalytic Mechanism, and Evolution of the Glutathione Transferases

2. [2] Global analysis of biochemical and biophysical data

3. Folding Mechanism of the α-Subunit of Tryptophan Synthase, an α/β Barrel Protein: Global Analysis Highlights the Interconversion of Multiple Native, Intermediate, and Unfolded Forms through Parallel Channels

4. Zeta, a novel class of glutathione transferases in a range of species from plants to humans

5. An automated system for micro-batch protein crystallization and screening

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