Zobrazeno 1 - 8
of 8
pro vyhledávání: '"Susan M. Ekkel"'
Autor:
Charles Bayly-Jones, Bill H. T. Ho, Corinna Lau, Eleanor W. W. Leung, Laura D’Andrea, Christopher J. Lupton, Susan M. Ekkel, Hariprasad Venugopal, James C. Whisstock, Tom E. Mollnes, Bradley A. Spicer, Michelle A. Dunstone
Publikováno v:
Communications Biology, Vol 6, Iss 1, Pp 1-11 (2023)
The cryo-EM structure of monoclonal antibody aE11 bound to polyC9 reveals that the binding site within the Membrane Attack Complex is a quaternary discontinuous epitope formed by two separate surfaces of the oligomeric C9 periphery.
Externí odkaz:
https://doaj.org/article/96ef9aa75dd84880b13fa08f60261470
Autor:
Siew Siew Pang, Charles Bayly-Jones, Mazdak Radjainia, Bradley A. Spicer, Ruby H. P. Law, Adrian W. Hodel, Edward S. Parsons, Susan M. Ekkel, Paul J. Conroy, Georg Ramm, Hariprasad Venugopal, Phillip I. Bird, Bart W. Hoogenboom, Ilia Voskoboinik, Yann Gambin, Emma Sierecki, Michelle A. Dunstone, James C. Whisstock
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-9 (2019)
Macrophage-expressed gene 1 (MPEG1) functions within the phagolysosome to damage engulfed microbes, presumably via forming pores in target membranes. In order to provide insights into the mechanism of MPEG1 function and membrane binding, the authors
Externí odkaz:
https://doaj.org/article/2cd82268e003405ba51038290da8f4fe
Autor:
Natalya V. Dudkina, Bradley A. Spicer, Cyril F. Reboul, Paul J. Conroy, Natalya Lukoyanova, Hans Elmlund, Ruby H. P. Law, Susan M. Ekkel, Stephanie C. Kondos, Robert J. A. Goode, Georg Ramm, James C. Whisstock, Helen R. Saibil, Michelle A. Dunstone
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-6 (2016)
The membrane attack complex is a heteromeric assembly of complement proteins where multiple copies of C9 are recruited by the C5b678 complex to form lytic pores in pathogen membranes. Here the authors present the structure of a soluble pore-like form
Externí odkaz:
https://doaj.org/article/a2649e95879f4957bec6ff1711385015
Autor:
Charles Bayly-Jones, Bill Hy Tran Ho, Corinna Lau, Eleanor W.W. Leung, Laura D’Andrea, Christopher J. Lupton, Susan M. Ekkel, Hariprasad Venugopal, James C. Whisstock, Tom E. Mollnes, Bradley A. Spicer, Michelle A. Dunstone
The terminal C5b-9 complement complex (TCC) exists in two forms; the soluble sC5b-9 and the solid-phase inserted Membrane Attack Complex (MAC). The MAC is responsible for forming large β-barrel channels in the membranes of pathogens and can target c
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::15b8c84ec53c88673cb3100d7b2b0334
https://doi.org/10.1101/2022.07.06.498960
https://doi.org/10.1101/2022.07.06.498960
Autor:
Phillip I. Bird, Bart W. Hoogenboom, Adrian W. Hodel, Georg Ramm, Susan M. Ekkel, Hariprasad Venugopal, Charles Bayly-Jones, Mazdak Radjainia, Ilia Voskoboinik, Ruby H. P. Law, Paul J. Conroy, Yann Gambin, Siew Siew Pang, Michelle A. Dunstone, Emma Sierecki, Bradley A. Spicer, Edward S. Parsons, James C. Whisstock
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-9 (2019)
Nature Communications
Nature Communications
Macrophage-expressed gene 1 (MPEG1/Perforin-2) is a perforin-like protein that functions within the phagolysosome to damage engulfed microbes. MPEG1 is thought to form pores in target membranes, however, its mode of action remains unknown. We use cry
Autor:
Robert J. A. Goode, Bradley A. Spicer, Michelle A. Dunstone, S.C. Kondos, Georg Ramm, James C. Whisstock, Susan M. Ekkel, Cyril F. Reboul, Natalya Lukoyanova, Natalya V Dudkina, Helen R. Saibil, Paul J. Conroy, Hans Elmlund, Ruby H. P. Law
Publikováno v:
Nature Communications, Vol 7, Iss 1, Pp 1-6 (2016)
Nature Communications
Nature Communications
The membrane attack complex (MAC)/perforin-like protein complement component 9 (C9) is the major component of the MAC, a multi-protein complex that forms pores in the membrane of target pathogens. In contrast to homologous proteins such as perforin a
Autor:
James C. Whisstock, Rodney K. Tweten, Michelle A. Dunstone, Oded Kleifeld, Helen R. Saibil, Daouda A K Traore, S.C. Kondos, Bradley A. Spicer, Ruby H. P. Law, Cyril F. Reboul, Joseph A. Trapani, Katherine V. Oliver, Maya Topf, Ilia Voskoboinik, Tamas Zsolt Hatfaludi, Natalya Lukoyanova, Eileen M. Hotze, Irene Farabella, Susan M. Ekkel, Tom T. Caradoc-Davies
Publikováno v:
PLoS Biology
PLOS Biology
PLoS Biology, Vol 13, Iss 2, p e1002049 (2015)
PLOS Biology
PLoS Biology, Vol 13, Iss 2, p e1002049 (2015)
Membrane attack complex/perforin-like (MACPF) proteins comprise the largest superfamily of pore-forming proteins, playing crucial roles in immunity and pathogenesis. Soluble monomers assemble into large transmembrane pores via conformational transiti
Autor:
Natalya Lukoyanova, Stephanie C Kondos, Irene Farabella, Ruby H P Law, Cyril F Reboul, Tom T Caradoc-Davies, Bradley A Spicer, Oded Kleifeld, Daouda A K Traore, Susan M Ekkel, Ilia Voskoboinik, Joseph A Trapani, Tamas Hatfaludi, Katherine Oliver, Eileen M Hotze, Rodney K Tweten, James C Whisstock, Maya Topf, Helen R Saibil, Michelle A Dunstone
Publikováno v:
PLoS Biology, Vol 13, Iss 2, p e1002049 (2015)
Membrane attack complex/perforin-like (MACPF) proteins comprise the largest superfamily of pore-forming proteins, playing crucial roles in immunity and pathogenesis. Soluble monomers assemble into large transmembrane pores via conformational transiti
Externí odkaz:
https://doaj.org/article/61da81d52f214c008c291f4ba889cd9a