Zobrazeno 1 - 10
of 80
pro vyhledávání: '"Megan J Maher"'
Autor:
Aaron P McGrath, Elise L Laming, G Patricia Casas Garcia, Marc Kvansakul, J Mitchell Guss, Jill Trewhella, Benoit Calmes, Paul V Bernhardt, Graeme R Hanson, Ulrike Kappler, Megan J Maher
Publikováno v:
eLife, Vol 4 (2015)
Interprotein electron transfer underpins the essential processes of life and relies on the formation of specific, yet transient protein-protein interactions. In biological systems, the detoxification of sulfite is catalyzed by the sulfite-oxidizing e
Externí odkaz:
https://doaj.org/article/295666060edd460ba12dad15e6907a1a
Publikováno v:
PLoS ONE, Vol 6, Iss 8, p e23355 (2011)
The polytopic membrane protein FeoB is a ferrous iron transporter in prokaryotes. The protein contains a potassium-activated GTPase domain that is essential in regulating the import of iron and conferring virulence to many disease-causing bacteria. H
Externí odkaz:
https://doaj.org/article/d6a64bc01e444eca91094a40eefaf10a
Autor:
Sanjeedha S. M. Mubarak, Tess R. Malcolm, Hamish G. Brown, Eric Hanssen, Megan J. Maher, Gawain McColl, Guy N. L. Jameson
Publikováno v:
Biochemistry. 62:1484-1496
Publikováno v:
Acta Crystallographica Section D Structural Biology. 79:345-352
The arsenite oxidase (AioAB) from Pseudorhizobium banfieldiae sp. strain NT-26 catalyzes the oxidation of arsenite to arsenate and transfers electrons to its cognate electron acceptor cytochrome c 552 (cytc 552). This activity underpins the ability o
Autor:
Nilakhi Poddar, Shadi Maghool, Consuelo Badilla, Megan J. Maher, Thomas H. Osborne, Joanne M. Santini
Publikováno v:
Biochemistry. 60:465-476
The anaerobic bacterium Chrysiogenes arsenatis respires using the oxyanion arsenate (AsO43-) as the terminal electron acceptor, where it is reduced to arsenite (AsO33-) while concomitantly oxidizing various organic (e.g., acetate) electron donors. Th
Autor:
Oliver P. Ernst, Megan J. Maher
Publikováno v:
Current Opinion in Structural Biology. 69:vi-viii
Publikováno v:
Scientific Reports, Vol 10, Iss 1, Pp 1-10 (2020)
Intracellular copper (Cu) in eukaryotic organisms is regulated by homeostatic systems, which rely on the activities of soluble metallochaperones that participate in Cu exchange through highly tuned protein-protein interactions. Recently, the human en
Autor:
Erin B. Brazel, Aimee Tan, Stephanie L. Neville, Amy R. Iverson, Saumya R. Udagedara, Bliss A. Cunningham, Mwilye Sikanyika, David M.P. De Oliveira, Bernhard Keller, Lisa Bohlmann, Ibrahim M. El-Deeb, Katherine Ganio, Bart A. Eijkelkamp, Alastair G. McEwan, Mark von Itzstein, Megan J. Maher, Mark J. Walker, Jason W. Rosch, Christopher A. McDevitt
Streptococcus pneumoniae is the primary cause of community-acquired bacterial pneumonia with rates of penicillin and multidrug-resistance exceeding 80% and 40%, respectively. The innate immune response generates a variety of antimicrobial agents to c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62a4bec1a517e42f565efbfd3b08acdd
Autor:
Katherine Ganio, Andrew J. Hayes, Norimichi Nomura, Christopher A. McDevitt, Alex Carey Hulyer, Stephen J. Fairweather, Megan J. Maher, Tess R. Malcolm, Jacinta A. Watts, Aaron P. McGrath, Megan L. O'Mara, So Iwata, Jennie Sjöhamn, Stephanie L. Neville, Mark R. Davies, Hugo MacDermott-Opeskin
Publikováno v:
Science Advances
Bacterial manganese import is achieved by unique architectural features that are conserved across the kingdoms of life.
Metal ions are essential for all forms of life. In prokaryotes, ATP-binding cassette (ABC) permeases serve as the primary imp
Metal ions are essential for all forms of life. In prokaryotes, ATP-binding cassette (ABC) permeases serve as the primary imp
Autor:
Luke E. Formosa, Boris Reljic, Alice J. Sharpe, Megan J. Maher, Linden Muellner-Wong, David A. Stroud, Shadi Maghool, Michael T. Ryan
Cytochrome c oxidase assembly factor 7 (COA7) is a metazoan-specific assembly factor, critical for the biogenesis of mitochondrial complex IV (cytochrome c oxidase). Although mutations in COA7 have been linked in patients to complex IV assembly defec
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::b9daa438fa48726ff811a742103c6ad3
https://doi.org/10.1101/2021.06.10.447992
https://doi.org/10.1101/2021.06.10.447992