Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Heather R Williamson"'
Autor:
Kana Takematsu, Heather R Williamson, Pavle Nikolovski, Jens T. Kaiser, Yuling Sheng, Petr Pospíšil, Michael Towrie, Jan Heyda, Daniel Hollas, Stanislav Záliš, Harry B. Gray, Antonín Vlček, Jay R. Winkler
Publikováno v:
ACS Central Science, Vol 5, Iss 1, Pp 192-200 (2019)
Externí odkaz:
https://doaj.org/article/01ff81e0ca044a70a725b83fe1cc45a2
Autor:
Heather R Williamson, Lydia Mosi, Robert Donnell, Maha Aqqad, Richard W Merritt, Pamela L C Small
Publikováno v:
PLoS Neglected Tropical Diseases, Vol 8, Iss 4, p e2770 (2014)
Transmission of M. ulcerans, the etiological agent of Buruli ulcer, from the environment to humans remains an enigma despite decades of research. Major transmission hypotheses propose 1) that M. ulcerans is acquired through an insect bite or 2) that
Externí odkaz:
https://doaj.org/article/c4afd4c1d160494882f389a752a910b7
Detection of Mycobacterium ulcerans in the environment predicts prevalence of Buruli ulcer in Benin.
Autor:
Heather R Williamson, Mark E Benbow, Lindsay P Campbell, Christian R Johnson, Ghislain Sopoh, Yves Barogui, Richard W Merritt, Pamela L C Small
Publikováno v:
PLoS Neglected Tropical Diseases, Vol 6, Iss 1, p e1506 (2012)
BACKGROUND: Mycobacterium ulcerans is the causative agent of Buruli ulcer (BU). In West Africa there is an association between BU and residence in low-lying rural villages where aquatic sources are plentiful. Infection occurs through unknown environm
Externí odkaz:
https://doaj.org/article/de8bf3b5699c4cd9b682a6667fc0492b
Autor:
Heather R Williamson, Mark E Benbow, Khoa D Nguyen, Dia C Beachboard, Ryan K Kimbirauskas, Mollie D McIntosh, Charles Quaye, Edwin O Ampadu, Daniel Boakye, Richard W Merritt, Pamela L C Small
Publikováno v:
PLoS Neglected Tropical Diseases, Vol 2, Iss 3, p e205 (2008)
Mycobacterium ulcerans, the causative agent of Buruli ulcer, is an emerging environmental bacterium in Australia and West Africa. The primary risk factor associated with Buruli ulcer is proximity to slow moving water. Environmental constraints for di
Externí odkaz:
https://doaj.org/article/59ef0aeec673489da2a2562c8136f245
Publikováno v:
Biochemistry. 55:5738-5745
In the absence of its substrate, the auto-reduction of the high-valent bis-FeIV state of the hemes of MauG to the diferric state proceeds via a Compound I-like and then a Compound II-like intermediate. This process is coupled to oxidative damage to s
Publikováno v:
Biochemical Journal. 473:1769-1775
In the absence of its substrate, the auto-reduction of the high-valent bis-Fe(IV) state of the dihaem enzyme MauG is coupled to oxidative damage of a methionine residue. Transient kinetic and solvent isotope effect studies reveal that this process oc
Autor:
Antonio Sanchez-Amat, Victor L. Davidson, Jonatan C. Campillo-Brocal, Heather R. Williamson, Esha Sehanobish
Publikováno v:
Biochemistry. 55:2305-2308
GoxA is a glycine oxidase bearing a protein-derived cysteine tryptophylquinone (CTQ) cofactor that is formed by posttranslational modifications catalyzed by a flavoprotein, GoxB. Two forms of GoxA were isolated. An active form with mature CTQ and an
Autor:
Alan M. Shiller, Antonio Sanchez-Amat, Heather R. Williamson, Victor L. Davidson, Esha Sehanobish
Publikováno v:
Biochemistry. 56(7)
The first posttranslational modification step in the biosynthesis of the tryptophan-derived quinone cofactors is the auto-catalytic hydroxylation of a specific Trp residue at the C-7 position on the indole side-chain. Subsequent modifications are cat
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Bioenergetics. 1837:1595-1601
The 6 ×-Histidine tag which is commonly used for purification of recombinant proteins was converted to a catalytic redox-active center by incorporation of Co2 +. Two examples of the biological activity of this engineered protein-derived cofactor are
Autor:
Pavle Nikolovski, Lucie Sokolova, Ian P. Clark, Jens T. Kaiser, Ana María Blanco-Rodríguez, Kana Takematsu, Antonín Vlček, Jay R. Winkler, Michael Towrie, Harry B. Gray, Heather R. Williamson
Publikováno v:
Journal of the American Chemical Society. 135:15515-15525
We report a new metallolabeled blue copper protein, Re126W122Cu(I) Pseudomonas aeruginosa azurin, which has three redox sites at well-defined distances in the protein fold: Re(I)(CO)3(4,7-dimethyl-1,10-phenanthroline) covalently bound at H126, a Cu c