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Your search keyword '"Emsley J"' showing total 32 results
Start Over Author "Emsley J" Publisher wiley-blackwell
32 results on '"Emsley J"'

31. "Bleeding in the jungle".

Author

Arbelaez A, Niemann J, Freney R, Othman M, Emsley J, Mohammed S, and Favaloro EJ

Subjects
Amino Acid Sequence, Epistaxis physiopathology, Hematuria physiopathology, Humans, Male, Middle Aged, Models, Molecular, Molecular Sequence Data, Platelet Glycoprotein GPIb-IX Complex chemistry, Platelet Glycoprotein GPIb-IX Complex metabolism, Protein Binding, Sequence Alignment, von Willebrand Diseases physiopathology, von Willebrand Factor chemistry, von Willebrand Factor metabolism, Mutation, Missense, von Willebrand Diseases diagnosis, von Willebrand Diseases genetics, von Willebrand Factor genetics
Published
2015
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32. Structure of Mycobacterium tuberculosis thioredoxin C.

Author

Hall G, Shah M, McEwan PA, Laughton C, Stevens M, Westwell A, and Emsley J

Subjects
Amino Acid Sequence, Crystallography, X-Ray, Humans, Models, Molecular, Molecular Sequence Data, Peptides chemistry, Protein Folding, Protein Structure, Secondary, Sequence Alignment, Thioredoxins metabolism, Mycobacterium tuberculosis chemistry, Thioredoxins chemistry
Abstract

Mycobacterium tuberculosis is a facultative intracellular parasite of alveolar macrophages. M. tuberculosis is able to propagate in harsh environments within cells such as phagocytes, despite being exposed to reactive oxygen and nitrogen intermediates. The thioredoxin redox system is conserved across the phyla and has a well characterized role in resisting oxidative stress and influencing gene expression within prokaryotic and eukaryotic cells. M. tuberculosis thioredoxin (MtbTrx) has similar functions in redox homeostasis and it has recently been shown that alkyl hydroperoxidase C is efficiently reduced to its active form by MtbTrxC, supporting this notion. To address whether the MtbTrx has similar features to other thioredoxin structures and to examine the opportunities for designing drugs against this target, MtbTrxC has been crystallized and its structure determined to 1.3 A resolution. Unexpectedly, the structure demonstrates an interesting crystal packing in which five C-terminal residues from the MtbTrxC fold insert into a groove adjacent to the active site. A very similar interaction is observed in structures of human thioredoxins bound to peptides from the target proteins NF-kappaB and Ref-1.

Published
2006
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