Zobrazeno 1 - 10
of 173
pro vyhledávání: '"Jonathan M, Grimes"'
Autor:
Merlyn Latimer-Smith, Paula S. Salgado, Ismay Forsyth, Eugene Makeyev, Minna M. Poranen, Dave I. Stuart, Jonathan M. Grimes, Kamel El Omari
Publikováno v:
Scientific Reports, Vol 14, Iss 1, Pp 1-11 (2024)
Abstract The replication of RNA viruses relies on the activity of RNA-dependent RNA polymerases (RdRps). Despite large variations in their genomic sequences, viral RdRps share a common architecture generally known as a closed right hand. The P2 polym
Externí odkaz:
https://doaj.org/article/aa140bf7fc8449fe9a6711824b12a3ae
Autor:
Ecco Staller, Loïc Carrique, Olivia C. Swann, Haitian Fan, Jeremy R. Keown, Carol M. Sheppard, Wendy S. Barclay, Jonathan M. Grimes, Ervin Fodor
Publikováno v:
Nature Communications, Vol 15, Iss 1, Pp 1-10 (2024)
Abstract Avian influenza A viruses (IAVs) pose a public health threat, as they are capable of triggering pandemics by crossing species barriers. Replication of avian IAVs in mammalian cells is hindered by species-specific variation in acidic nuclear
Externí odkaz:
https://doaj.org/article/00ffc1857d274ff1aec0d37f48d9400f
Autor:
Kamel El Omari, Ramona Duman, Vitaliy Mykhaylyk, Christian M. Orr, Merlyn Latimer-Smith, Graeme Winter, Vinay Grama, Feng Qu, Kiran Bountra, Hok Sau Kwong, Maria Romano, Rosana I. Reis, Lutz Vogeley, Luca Vecchia, C. David Owen, Sina Wittmann, Max Renner, Miki Senda, Naohiro Matsugaki, Yoshiaki Kawano, Thomas A. Bowden, Isabel Moraes, Jonathan M. Grimes, Erika J. Mancini, Martin A. Walsh, Cristiane R. Guzzo, Raymond J. Owens, E. Yvonne Jones, David G. Brown, Dave I. Stuart, Konstantinos Beis, Armin Wagner
Publikováno v:
Communications Chemistry, Vol 6, Iss 1, Pp 1-11 (2023)
Abstract Despite recent advances in cryo-electron microscopy and artificial intelligence-based model predictions, a significant fraction of structure determinations by macromolecular crystallography still requires experimental phasing, usually by mea
Externí odkaz:
https://doaj.org/article/8684a241320c432f8b25757e0cf6d695
Autor:
Jeremy R. Keown, Adam D. Crawshaw, Jose Trincao, Loïc Carrique, Richard J. Gildea, Sam Horrell, Anna J. Warren, Danny Axford, Robin Owen, Gwyndaf Evans, Annie Bézier, Peter Metcalf, Jonathan M. Grimes
Publikováno v:
Nature Communications, Vol 14, Iss 1, Pp 1-10 (2023)
Abstract Infectious protein crystals are an essential part of the viral lifecycle for double-stranded DNA Baculoviridae and double-stranded RNA cypoviruses. These viral protein crystals, termed occlusion bodies or polyhedra, are dense protein assembl
Externí odkaz:
https://doaj.org/article/52663ececd974c08bbcf8a519f0e1636
Mapping inhibitory sites on the RNA polymerase of the 1918 pandemic influenza virus using nanobodies
Autor:
Jeremy R. Keown, Zihan Zhu, Loïc Carrique, Haitian Fan, Alexander P. Walker, Itziar Serna Martin, Els Pardon, Jan Steyaert, Ervin Fodor, Jonathan M. Grimes
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-11 (2022)
Influenza viruses carry their own RNAdependent RNA-polymerase that is highly conserved and a promising anti-viral target. Combining functional and structural data, Keown et al. characterise the inhibitory effect of nanobodies on 1918 pandemic H1N1 in
Externí odkaz:
https://doaj.org/article/7162090586c140f3b1741bc087eb5d6f
Autor:
Max Renner, Wanwisa Dejnirattisai, Loïc Carrique, Itziar Serna Martin, Dimple Karia, Serban L. Ilca, Shu F. Ho, Abhay Kotecha, Jeremy R. Keown, Juthathip Mongkolsapaya, Gavin R. Screaton, Jonathan M. Grimes
Publikováno v:
Nature Communications, Vol 12, Iss 1, Pp 1-9 (2021)
Here, the authors provide cryo-EM structures of mature and immature Spondweni virus, defining the furin recognition site at high resolution, and identifying a lipid that binds E upon capsid maturation and is also present in Zika and Dengue virions.
Externí odkaz:
https://doaj.org/article/c1e60ed8086c474ea0ccecd7e38b5686
Autor:
Kamel El Omari, Sai Li, Abhay Kotecha, Thomas S. Walter, Eduardo A. Bignon, Karl Harlos, Pentti Somerharju, Felix De Haas, Daniel K. Clare, Mika Molin, Felipe Hurtado, Mengqiu Li, Jonathan M. Grimes, Dennis H. Bamford, Nicole D. Tischler, Juha T. Huiskonen, David I. Stuart, Elina Roine
Publikováno v:
Nature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
Lipid membrane fusion is an essential function in many biological processes but little is known about membrane fusion in prokaryotes. The authors here study how haloarchaeal pleomorphic viruses (HRPVs) infect archaeal hosts. The structure-function an
Externí odkaz:
https://doaj.org/article/31855e58b674426b946b1b8cc027fb2e
Autor:
Gundeep Kaur, Soni Kaundal, Srajan Kapoor, Jonathan M. Grimes, Juha T. Huiskonen, Krishan Gopal Thakur
Publikováno v:
Scientific Reports, Vol 8, Iss 1, Pp 1-13 (2018)
Abstract CarD is an essential global transcription regulator from Mycobacterium tuberculosis (Mtb) that binds RNA polymerase and activates transcription by stabilizing the transcription initiation complex. Available crystal structures have captured t
Externí odkaz:
https://doaj.org/article/a9492ed5026b4972a6e8434e695cc730
Autor:
Sina Wittmann, Max Renner, Beth R. Watts, Oliver Adams, Miles Huseyin, Carlo Baejen, Kamel El Omari, Cornelia Kilchert, Dong-Hyuk Heo, Tea Kecman, Patrick Cramer, Jonathan M. Grimes, Lidia Vasiljeva
Publikováno v:
Nature Communications, Vol 8, Iss 1, Pp 1-15 (2017)
Termination of RNA polymerase II is a critical step in transcription. Here, the authors provide evidence that the fission yeast CID-RRM protein Seb1 is required for termination of coding and non-coding genes through interaction with both the polymera
Externí odkaz:
https://doaj.org/article/ef394db5756b48a9bb4c2015dc21a112
Autor:
Haitian Fan, David L.V. Bauer, J.R. Keown, Jonathan M. Grimes, Michael L. Knight, Ervin Fodor
Publikováno v:
Acta Crystallographica. Section F, Structural Biology Communications
The influenza virus nucleoprotein binds to the viral RNA genome and is essential for virus replication. Here, the structure of the nucleoprotein from an H3N2 virus is presented at 2.2 Å resolution.
Influenza A viruses of the H1N1 and H3N2 subty
Influenza A viruses of the H1N1 and H3N2 subty