Zobrazeno 1 - 5
of 5
pro vyhledávání: '"Brooke K. Hayes"'
Autor:
Tess R. Malcolm, Brooke K Hayes, Chaille T. Webb, Nyssa Drinkwater, Karolina Weronika Swiderska, Marcin Drag, Sheena McGowan
Publikováno v:
Biochemical Journal
During malarial infection, Plasmodium parasites digest human hemoglobin to obtain free amino acids for protein production and maintenance of osmotic pressure. The Plasmodium M1 and M17 aminopeptidases are both postulated to have an essential role in
Autor:
James Fodor, Blake T. Riley, Kirill Tsyganov, Anne Geert Volbeda, Daniel C. Nelson, Kylie A Farrow, Brooke K. Hayes, Colin J. Jackson, Sheena McGowan, Sebastian S. Broendum, Ben E. Clifton, Ryan D. Heselpoth, Jeroen D. C. Codée, Felix Kraus, Daniel E. Williams, Nyssa Drinkwater, Ashley M. Buckle
Publikováno v:
Molecular Microbiology, 116(2), 397-415. WILEY
Endolysin enzymes from bacteriophage cause bacterial lysis by degrading the peptidoglycan cell wall. The streptococcal C1 phage endolysin PlyC, is the most potent endolysin described to date and can rapidly lyse group A, C, and E streptococci. PlyC i
Autor:
Chaille T. Webb, Wei Yang, Blake T. Riley, Brooke K. Hayes, Komagal Kannan Sivaraman, Tess R. Malcolm, Stephen Harrop, Sarah C. Atkinson, Itamar Kass, Ashley M. Buckle, Nyssa Drinkwater, Sheena McGowan
Publikováno v:
The Journal of biological chemistry. 298(7)
The metal-dependent M17 aminopeptidases are conserved throughout all kingdoms of life. This large enzyme family is characterized by a conserved binuclear metal center and a distinctive homohexameric arrangement. Recently, we showed that hexamer forma
Autor:
Tess R. Malcolm, Karolina Weronika Swiderska, Marcin Drag, Brooke K. Hayes, Nyssa Drinkwater, Sheena McGowan
During malarial infection, Plasmodium parasites digest human hemoglobin to obtain free amino acids for protein production and maintenance of osmotic pressure. The Plasmodium M1 and M17 aminopeptidases are both postulated to have an essential role in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::c3e500f8497530d3cf9be870c46fb870
https://doi.org/10.1101/2020.10.13.338178
https://doi.org/10.1101/2020.10.13.338178
Autor:
Nyssa Drinkwater, Tess R. Malcolm, Ashley M. Buckle, Blake T. Riley, Komagal Kannan Sivaraman, Itamar Kass, Brooke K. Hayes, Natalie A. Borg, Sarah C. Atkinson, Sheena McGowan, Wei Yang
The metal-dependent M17 aminopeptidases are conserved throughout all kingdoms of life. The large enzyme family is characterised by a conserved binuclear metal center and a distinctive homohexameric arrangement. To understand the mechanistic role of t
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::dae15017c9c103b1e44cc2c29f674331