Zobrazeno 1 - 10
of 64
pro vyhledávání: '"Paul J. Conroy"'
Autor:
Adam J. Quek, Nathan P. Cowieson, Tom T. Caradoc-Davies, Paul J. Conroy, James C. Whisstock, Ruby H. P. Law
Publikováno v:
International Journal of Molecular Sciences, Vol 24, Iss 18, p 14258 (2023)
Plasminogen (Plg) is the inactive form of plasmin (Plm) that exists in two major glycoforms, referred to as glycoforms I and II (GI and GII). In the circulation, Plg assumes an activation-resistant “closed” conformation via interdomain interactio
Externí odkaz:
https://doaj.org/article/0e25f129ee1a4bb79ced86f7bdf462b2
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:
Daouda A. K. Traore, Jessica A. Wisniewski, Sarena F. Flanigan, Paul J. Conroy, Santosh Panjikar, Yee-Foong Mok, Carmen Lao, Michael D. W. Griffin, Vicki Adams, Julian I. Rood, James C. Whisstock
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-11 (2018)
Conjugative transfer of antibiotic resistance plasmid pCW3 in Clostridium perfringens is mediated by the tcp locus. Here, the authors identify a wHTH-type protein, TcpK, that is essential for efficient plasmid transfer and interacts with the plasmid
Externí odkaz:
https://doaj.org/article/7cda5168800047dcbc57499355c58da2
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:
Ruby H.P. Law, Guojie Wu, Eleanor W.W. Leung, Koushi Hidaka, Adam J. Quek, Tom T. Caradoc-Davies, Devadharshini Jeevarajah, Paul J. Conroy, Nigel M. Kirby, Raymond S. Norton, Yuko Tsuda, James C. Whisstock
Publikováno v:
Blood Advances, Vol 1, Iss 12, Pp 766-771 (2017)
Abstract: The zymogen protease plasminogen and its active form plasmin perform key roles in blood clot dissolution, tissue remodeling, cell migration, and bacterial pathogenesis. Dysregulation of the plasminogen/plasmin system results in life-threate
Externí odkaz:
https://doaj.org/article/b3a0c868cfc44aa795c55be0ba7c2b58
Autor:
Sarah Gilgunn, Keefe Murphy, Henning Stöckmann, Paul J. Conroy, T. Brendan Murphy, R. William Watson, Richard J. O’Kennedy, Pauline M. Rudd, Radka Saldova
Publikováno v:
International Journal of Molecular Sciences, Vol 21, Iss 23, p 9233 (2020)
The diagnosis and treatment of prostate cancer (PCa) is a major health-care concern worldwide. This cancer can manifest itself in many distinct forms and the transition from clinically indolent PCa to the more invasive aggressive form remains poorly
Externí odkaz:
https://doaj.org/article/7155eeefe8874555b8a6201e91bab4c8
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:
Christoph Krisp, Carmen Sonntag, L. Hersey, A.J. Wood, Sara Gibertini, Alex J. Fulcher, Patricia R. Jusuf, A. Siegel, Marina Mora, Chi-Hung Lin, Peter D. Currie, Stefanie Dudczig, Sara Alaei, Nicolle H. Packer, M. Li, K. Nishtala, Lee B. Miles, Paul J. Conroy, Fernando J. Rossello
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-12 (2021)
Nature Communications
Nature Communications
The muscular dystrophies encompass a broad range of pathologies with varied clinical outcomes. In the case of patients carrying defects in fukutin-related protein (FKRP), these diverse pathologies arise from mutations within the same gene. This is su
Autor:
Sarah Gilgunn, Silvia Millán Martín, Mark R Wormald, Julia Zapatero-Rodríguez, Paul J Conroy, Richard J O'Kennedy, Pauline M Rudd, Radka Saldova
Publikováno v:
PLoS ONE, Vol 11, Iss 7, p e0159859 (2016)
Recent exploitation of the avian immune system has highlighted its suitability for the generation of high-quality, high-affinity antibodies to a wide range of antigens for a number of therapeutic and biotechnological applications. The glycosylation p
Externí odkaz:
https://doaj.org/article/bce45fb658ad4471830e7848741478d6
Autor:
Paul J. Conroy, Kamil A. Sokolowski, Simon Puttick, S. John Weroha, Thomas Kryza, James C. Whisstock, Brittney S. Harrington, Samantha J. Stehbens, Paul Haluska, T. Cuda, Rohan Lourie, Sarah Reed, Brian W.C. Tse, Buddhika J. Arachchige, Lewis Perrin, Yaowu He, Tashbib Khan, Katherine K. Robbins, Ruby H. P. Law, Carlos Salomon, Pamela M. Pollock, John D. Hooper
Publikováno v:
Theranostics
CUB-domain containing protein 1 (CDCP1) is a cancer associated cell surface protein that amplifies pro-tumorigenic signalling by other receptors including EGFR and HER2. Its potential as a cancer target is supported by studies showing that anti-CDCP1