Title |
Structural and Functional Characterization of ScsC, a Periplasmic Thioredoxin-Like Protein from Salmonella enterica Serovar Typhimurium
|
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Published in |
Antioxidants & Redox Signaling, August 2013
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DOI | 10.1089/ars.2012.4939 |
Pubmed ID | |
Authors |
Mark Shepherd, Begoña Heras, Maud E. S. Achard, Gordon J. King, M. Pilar Argente, Fabian Kurth, Samantha L. Taylor, Mark J. Howard, Nathan P. King, Mark A. Schembri, Alastair G. McEwan |
Abstract |
The prototypical protein disulfide bond (Dsb) formation and protein refolding pathways in the bacterial periplasm involving Dsb proteins have been most comprehensively defined in Escherichia coli. However, genomic analysis has revealed several distinct Dsb-like systems in bacteria, including the pathogen Salmonella enterica serovar Typhimurium. This includes the scsABCD locus, which encodes a system that has been shown via genetic analysis to confer copper tolerance, but whose biochemical properties at the protein level are not defined. The aim of this study was to provide functional insights into the soluble ScsC protein through structural, biochemical, and genetic analyses. |
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United Kingdom | 1 | 100% |
Demographic breakdown
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Members of the public | 1 | 100% |
Mendeley readers
Geographical breakdown
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Unknown | 40 | 100% |
Demographic breakdown
Readers by professional status | Count | As % |
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Student > Ph. D. Student | 8 | 20% |
Researcher | 8 | 20% |
Student > Doctoral Student | 6 | 15% |
Student > Bachelor | 2 | 5% |
Lecturer > Senior Lecturer | 2 | 5% |
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Unknown | 9 | 23% |
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Medicine and Dentistry | 3 | 8% |
Other | 4 | 10% |
Unknown | 9 | 23% |