Zobrazeno 1 - 9
of 9
pro vyhledávání: '"Benjamin G, Butt"'
Autor:
Benjamin G Butt, Daniela Fischer, Alison R Rep, Martin Schauflinger, Clarissa Read, Thomas Böck, Manuel Hirner, Frederik Wienen, Stephen C Graham, Jens von Einem
Publikováno v:
PLoS Pathogens, Vol 20, Iss 6, p e1012300 (2024)
The AAA-type ATPase VPS4 is recruited by proteins of the endosomal sorting complex required for transport III (ESCRT-III) to catalyse membrane constriction and membrane fission. VPS4A accumulates at the cytoplasmic viral assembly complex (cVAC) of ce
Externí odkaz:
https://doaj.org/article/1fe94aebbe7442fcac4469b72cc32685
Publikováno v:
Wellcome Open Research, Vol 5 (2020)
Background: The multi-subunit homotypic fusion and vacuole protein sorting (HOPS) membrane-tethering complex is involved in regulating the fusion of late endosomes and autophagosomes with lysosomes in eukaryotes. The C-terminal regions of several HOP
Externí odkaz:
https://doaj.org/article/2d06ad609b92425bb8e6809e6a2081c0
Publikováno v:
Wellcome Open Research, Vol 5 (2020)
Background: The multi-subunit homotypic fusion and vacuole protein sorting (HOPS) membrane-tethering complex is involved in regulating the fusion of late endosomes and autophagosomes with lysosomes in eukaryotes. The C-terminal regions of several HOP
Externí odkaz:
https://doaj.org/article/8bfee8db83f64b98bc63ac5a9554a0af
Autor:
Benjamin G Butt, Danielle J Owen, Cy M Jeffries, Lyudmila Ivanova, Chris H Hill, Jack W Houghton, Md Firoz Ahmed, Robin Antrobus, Dmitri I Svergun, John J Welch, Colin M Crump, Stephen C Graham
Publikováno v:
eLife, Vol 9 (2020)
Herpesviruses acquire their membrane envelopes in the cytoplasm of infected cells via a molecular mechanism that remains unclear. Herpes simplex virus (HSV)−1 proteins pUL7 and pUL51 form a complex required for efficient virus envelopment. We show
Externí odkaz:
https://doaj.org/article/cfd82648c6a14487a1d5e6ed851657bb
Autor:
Shannon J. McKie, Alex S. Nicholson, Emily Smith, Stuart Fawke, Eve Caroe, James C. Williamson, Benjamin G. Butt, Denisa Kolářová, Ondřej Peterka, Michal Holčapek, Paul J. Lehner, Stephen C. Graham, Janet E. Deane
Myelin is a multilayered membrane that tightly wraps neuronal axons, enabling efficient, high-speed signal propagation. The axon and myelin sheath form tight contacts, mediated by specific plasma membrane proteins and lipids, and disruption of these
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::40889ef2ce23d4837ae6d4f59083cfed
https://doi.org/10.1101/2022.09.15.508082
https://doi.org/10.1101/2022.09.15.508082
Publikováno v:
Wellcome Open Research
Background: The multi-subunit homotypic fusion and vacuole protein sorting (HOPS) membrane-tethering complex is involved in regulating the fusion of late endosomes and autophagosomes with lysosomes in eukaryotes. The C-terminal regions of several HOP
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::77605671018d1d342bdd8ca8fa241404
https://www.repository.cam.ac.uk/handle/1810/308304
https://www.repository.cam.ac.uk/handle/1810/308304
Autor:
John J. Welch, Chris H. Hill, Dmitri I. Svergun, Cy M. Jeffries, Firoz Ahmed, Robin Antrobus, Lyudmila Ivanova, Jack W. Houghton, Danielle J Owen, Colin M. Crump, Stephen C. Graham, Benjamin G Butt
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::06a46ca31ae8ddc8d38e2182a25c7a11
https://doi.org/10.7554/elife.53789.sa2
https://doi.org/10.7554/elife.53789.sa2
Publikováno v:
Journal of General Virology
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=r3c4b2081b22::7c3d6697ede32b4e53b54ec85fc4bd74
Publikováno v:
The Journal of general virology
The substitution rates of viral polymerases have been studied extensively. However less is known about the tendency of these enzymes to ‘slip’ during RNA synthesis to produce progeny RNAs with nucleotide insertions or deletions. We recently descr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=pmid________::8813dd8eb4e54c645ee7dfdd58ec0d9a
https://pubmed.ncbi.nlm.nih.gov/30507373
https://pubmed.ncbi.nlm.nih.gov/30507373