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Journal article

Structural and functional characterization of malate synthase G from opportunistic pathogen Pseudomonas aeruginosa

Abstract:: Pseudomonas aeruginosa is an opportunistic human pathogen recognized as a critical threat by the World Health Organization because of the dwindling number of effective therapies available to treat infections. Over the past decade, it has become apparent that the glyoxylate shunt plays a vital role in sustaining P. aeruginosa during infection scenarios. The glyoxylate shunt comprises two enzymes: isocitrate lyase and malate synthase isoform G. Inactivation of these enzymes has been reported to...
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Publication status:: Published

Peer review status:: Peer reviewed

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APA Style

McVey, A. C., Medarametla, P., Chee, X., Bartlett, S., Poso, A., Spring, D. R., Rahman, T., & Welch, M. (2017). Structural and functional characterization of malate synthase G from opportunistic pathogen Pseudomonas aeruginosa. Biochemistry, 56(41), 5539–5549.

MLA Style

McVey, A. C., et al. “Structural and Functional Characterization of Malate Synthase G from Opportunistic Pathogen Pseudomonas Aeruginosa.” Biochemistry, vol. 56, no. 41, American Chemical Society, 2017, pp. 5539–49.

Chicago Style

McVey, AC, P Medarametla, X Chee, S Bartlett, A Poso, DR Spring, T Rahman, and M Welch. 2017. “Structural and Functional Characterization of Malate Synthase G from Opportunistic Pathogen Pseudomonas Aeruginosa.” Biochemistry 56 (41): 5539–49.
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Publisher copy:: 10.1021/acs.biochem.7b00852

Authors

+ McVey, AC More by this author

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+ Medarametla, P More by this author

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+ Chee, X More by this author

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+ Bartlett, S More by this author

Institution:

University of Oxford

Division:

MSD

Department:

NDM

Sub department:

NDM Experimental Medicine

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+ Poso, A More by this author

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Bibliographic Details

Publisher:: American Chemical Society Publisher's website
Journal:: Biochemistry Journal website
Volume:: 56
Issue:: 41
Pages:: 5539–5549
Publication date:: 2017-10-06
DOI:: 10.1021/acs.biochem.7b00852
EISSN:: 1520-4995
ISSN:: 0006-2960
Pmid:: 28985053

Item Description

Language:: English
Pubs id:: pubs:736834
UUID:: uuid:6e1c346e-8bcd-4da6-987e-4befa33fee87
Local pid:: pubs:736834
Source identifiers:: 736834
Deposit date:: 2017-10-26

Terms of use

Copyright holder:: American Chemical Society
Copyright date:: 2017
Notes:: Copyright © 2017 American Chemical Society.

Licence:: Terms and Conditions of Use for Oxford University Research Archive

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