Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Emily J. Furlong"'
Autor:
Emily J. Furlong, Alvin W. Lo, Fabian Kurth, Lakshmanane Premkumar, Makrina Totsika, Maud E. S. Achard, Maria A. Halili, Begoña Heras, Andrew E. Whitten, Hassanul G. Choudhury, Mark A. Schembri, Jennifer L. Martin
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-10 (2017)
Bacterial disulfide isomerases shuffle incorrect disulfide bonds. Here, the authors structurally characterize the disulfide isomerase ScsC fromProteus mirabilisand identify a functionally important shape-shifting motif that allows ScsC to adopt a div
Externí odkaz:
https://doaj.org/article/8f04e6bca0c44df1aae8cb752f2ba122
Author Correction: A shape-shifting redox foldase contributes to Proteus mirabilis copper resistance
Autor:
Emily J. Furlong, Alvin W. Lo, Fabian Kurth, Lakshmanane Premkumar, Makrina Totsika, Maud E. S. Achard, Maria A. Halili, Begoña Heras, Andrew E. Whitten, Hassanul G. Choudhury, Mark A. Schembri, Jennifer L. Martin
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-2 (2019)
This Article contains errors in Fig. 1, Table 1 and the Methods section. In panel c, the labels for PmScsC and EcDsbC in the upper two curves are interchanged. In Table 1 and the Methods section entitled ‘Extended structure’, the space group of t
Externí odkaz:
https://doaj.org/article/c445ac5a13d6473e816f05d97dd6877f
Autor:
Russell J. Jarrott, Emily J. Furlong, Guillaume A. Petit, David Drew, Jennifer L. Martin, Maria A. Halili
Publikováno v:
Protein expression and purification. 193
Suppressor of copper sensitivity (Scs) proteins play a role in the bacterial response to copper stress in many Gram-negative bacteria, including in the human pathogen Proteus mirabilis. Recently, the ScsC protein from P. mirabilis (PmScsC) was charac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::633ac3f62492383917734f208d4ec9d4
https://pubmed.ncbi.nlm.nih.gov/35026386
https://pubmed.ncbi.nlm.nih.gov/35026386
Autor:
Emily J, Furlong, Hassanul G, Choudhury, Fabian, Kurth, Anthony P, Duff, Andrew E, Whitten, Jennifer L, Martin
Publikováno v:
The Journal of biological chemistry. 293(16)
Correct disulfide bond formation is essential for proper folding of many proteins, including bacterial virulence factors. The suppressor of copper sensitivity (Scs) proteins have roles in dithiol/disulfide interchange and the bacterial response to co
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::5a33ba7013e07a0ce2c65687c2010925
https://pubmed.ncbi.nlm.nih.gov/29491145
https://pubmed.ncbi.nlm.nih.gov/29491145