Zobrazeno 1 - 10
of 39
pro vyhledávání: '"Charles Bayly-Jones"'
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:
Charles Bayly-Jones, Christopher J. Lupton, Claudia Fritz, Hariprasad Venugopal, Daniel Ramsbeck, Michael Wermann, Christian Jäger, Alex de Marco, Stephan Schilling, Dagmar Schlenzig, James C. Whisstock
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-14 (2022)
Meprin α is a proteolytic regulator of the extracellular matrix that forms enormous oligomeric filaments of unknown purpose. Here, the authors determine by cryo-EM the structural basis of the meprin supercoiled filament and further characterise a sm
Externí odkaz:
https://doaj.org/article/38630ad799064ddaba5722e41c9934b6
Autor:
Conall McGuinness, James C Walsh, Charles Bayly-Jones, Michelle A Dunstone, Michelle P Christie, Craig J Morton, Michael W Parker, Till Böcking
Publikováno v:
eLife, Vol 11 (2022)
The cholesterol-dependent cytolysin perfringolysin O (PFO) is secreted by Clostridium perfringens as a bacterial virulence factor able to form giant ring-shaped pores that perforate and ultimately lyse mammalian cell membranes. To resolve the kinetic
Externí odkaz:
https://doaj.org/article/9c52c20469604be898a9fcf4065fd2d3
Autor:
Charles Bayly-Jones, James C Whisstock
Publikováno v:
PLoS Computational Biology, Vol 18, Iss 3, p e1009930 (2022)
Protein structure fundamentally underpins the function and processes of numerous biological systems. Fold recognition algorithms offer a sensitive and robust tool to detect structural, and thereby functional, similarities between distantly related ho
Externí odkaz:
https://doaj.org/article/768cbd929ad04d3091f17e1ac45822ec
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:
Charles Bayly-Jones, Siew Siew Pang, Bradley A. Spicer, James C. Whisstock, Michelle A. Dunstone
Publikováno v:
Frontiers in Immunology, Vol 11 (2020)
Macrophage-expressed gene 1 [MPEG1/Perforin-2 (PRF2)] is an ancient metazoan protein belonging to the Membrane Attack Complex/Perforin (MACPF) branch of the MACPF/Cholesterol Dependent Cytolysin (CDC) superfamily of pore-forming proteins (PFPs). MACP
Externí odkaz:
https://doaj.org/article/4a28db91836141f8abd5ad2c881d9efd
Autor:
Bradley A. Spicer, Ruby H. P. Law, Tom T. Caradoc-Davies, Sue M. Ekkel, Charles Bayly-Jones, Siew-Siew Pang, Paul J. Conroy, Georg Ramm, Mazdak Radjainia, Hariprasad Venugopal, James C. Whisstock, Michelle A. Dunstone
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-7 (2018)
The Complement component 9 (C9) is the pore-forming component of the Membrane Attack Complex which targets pathogens. Here authors use structural biology to compare monomeric C9 to C9 within the polymeric assembly and identify the element which inhib
Externí odkaz:
https://doaj.org/article/786ad92e96b04d58a33f04be085b9901
Autor:
Yong-Gang Chang, Christopher J. Lupton, Charles Bayly-Jones, Alastair C. Keen, Laura D’Andrea, Christina M. Lucato, Joel R. Steele, Hari Venugopal, Ralf B. Schittenhelm, James C. Whisstock, Michelle L. Halls, Andrew M. Ellisdon
Publikováno v:
Nature Structural & Molecular Biology. 29:767-773
P-Rex (PI(3,4,5)P3-dependent Rac exchanger) guanine nucleotide exchange factors potently activate Rho GTPases. P-Rex guanine nucleotide exchange factors are autoinhibited, synergistically activated by Gβγ and PI(3,4,5)P3 binding and dysregulated in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4933da63b86a93b7d7d691f3041d1107
https://doi.org/10.1038/s41594-022-00804-9
https://doi.org/10.1038/s41594-022-00804-9
Autor:
Christopher J. Lupton, Charles Bayly-Jones, Laura D’Andrea, Cheng Huang, Ralf B. Schittenhelm, Hari Venugopal, James C. Whisstock, Michelle L. Halls, Andrew M. Ellisdon
Publikováno v:
Nature Structural & Molecular Biology. 28:982-988
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::1230e71180614c37186a9c968d5591ab
https://doi.org/10.1038/s41594-021-00687-2
https://doi.org/10.1038/s41594-021-00687-2
Autor:
Joshua T Benton, Charles Bayly-Jones
Publikováno v:
Biochemical Society Transactions. 49:2749-2765
Pore-forming proteins (PFPs) are a broad class of molecules that comprise various families, structural folds, and assembly pathways. In nature, PFPs are most often deployed by their host organisms to defend against other organisms. In humans, this is
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::53c6e1512bf9d4ed131c3da7ecbf3289
https://doi.org/10.1042/bst20210706
https://doi.org/10.1042/bst20210706