Zobrazeno 1 - 10
of 106
pro vyhledávání: '"Alfred A Antson"'
Publikováno v:
PLoS Pathogens, Vol 17, Iss 7, p e1009740 (2021)
Nipah and its close relative Hendra are highly pathogenic zoonotic viruses, storing their ssRNA genome in a helical nucleocapsid assembly formed by the N protein, a major viral immunogen. Here, we report the first cryoEM structure for a Henipavirus R
Externí odkaz:
https://doaj.org/article/c60530bf710e4d7babc9fea8351a1771
Publikováno v:
eLife, Vol 9 (2020)
The portal protein is a key component of many double-stranded DNA viruses, governing capsid assembly and genome packaging. Twelve subunits of the portal protein define a tunnel, through which DNA is translocated into the capsid. It is unknown how the
Externí odkaz:
https://doaj.org/article/6a8dc92bf5d44e89be37a2f03d2a0db0
Autor:
Oliver W Bayfield, Chao-Sheng Chen, Andrea R Patterson, Weisha Luan, Callum Smits, Paul Gollnick, Alfred A Antson
Publikováno v:
PLoS ONE, Vol 7, Iss 9, p e44309 (2012)
Subunit number is amongst the most important structural parameters that determine size, symmetry and geometry of a circular protein oligomer. The L-tryptophan biosynthesis regulator, TRAP, present in several Bacilli, is a good model system for invest
Externí odkaz:
https://doaj.org/article/a858ee0d002a4c28b915b213ccab8aa6
Autor:
Chao-Sheng Chen, Callum Smits, Guy G Dodson, Mikhail B Shevtsov, Natalie Merlino, Paul Gollnick, Alfred A Antson
Publikováno v:
PLoS ONE, Vol 6, Iss 10, p e25296 (2011)
Many critical cellular functions are performed by multisubunit circular protein oligomers whose internal geometry has evolved to meet functional requirements. The subunit number is arguably the most critical parameter of a circular protein assembly,
Externí odkaz:
https://doaj.org/article/f7801003277d4445899bdce6414be90e
Publikováno v:
iScience, Vol 26, Iss 11, Pp 108104- (2023)
Summary: Although membrane-containing dsDNA bacterial viruses are some of the most prevalent predators in aquatic environments, we know little about how they function due to their intractability in the laboratory. Here, we have identified and thoroug
Externí odkaz:
https://doaj.org/article/0f99befcc1a54626a1670b2fb1f78963
Autor:
Oliver W. Bayfield, Andrey N. Shkoporov, Natalya Yutin, Ekaterina V. Khokhlova, Jake L. R. Smith, Dorothy E. D. P. Hawkins, Eugene V. Koonin, Colin Hill, Alfred A. Antson
Publikováno v:
Nature. 617:409-416
CrAssphage and related viruses of the order Crassvirales (hereafter referred to as crassviruses) were originally discovered by cross-assembly of metagenomic sequences. They are the most abundant viruses in the human gut, are found in the majority of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::a6cff0e082cc8d364097123fd72c46e2
https://doi.org/10.1038/s41586-023-06019-2
https://doi.org/10.1038/s41586-023-06019-2
Publikováno v:
Nature Communications, Vol 9, Iss 1, Pp 1-7 (2018)
Solid state nanopores are robust but the sizing can be variable, whereas protein nanopores are precisely sized but lack robustness. Here the authors cork a solid state nanopore with the DNA-translocating portal protein from the virus G20c to obtain a
Externí odkaz:
https://doaj.org/article/216d0e35b27d41b39d8e6b39fdbece4c
Autor:
Herman K H Fung, Shelley Grimes, Alexis Huet, Robert L Duda, Maria Chechik, Joseph Gault, Carol V Robinson, Roger W Hendrix, Paul J Jardine, James F Conway, Christoph G Baumann, Alfred A Antson
Publikováno v:
Nucleic Acids Research. 50:8719-8732
Many essential cellular processes rely on substrate rotation or translocation by a multi-subunit, ring-type NTPase. A large number of double-stranded DNA viruses, including tailed bacteriophages and herpes viruses, use a homomeric ring ATPase to proc
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::17267723c01e98aacbd033f16eeecc1a
https://doi.org/10.1093/nar/gkac647
https://doi.org/10.1093/nar/gkac647
Autor:
Dorothy E.D.P. Hawkins, Oliver Bayfield, Herman K.H. Fung, Daniel N Grba, Alexis Huet, James F. Conway, Alfred A. Antson
Double-stranded DNA viruses utilise machinery, made of terminase proteins, to package viral DNA into the capsid. Forcosbacteriophage, a defined signal, recognised by small terminase, flanks each genome unit. Here we present the first structural data
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::f642988aff33ecac693e522539cc58cf
https://doi.org/10.1101/2023.02.24.529869
https://doi.org/10.1101/2023.02.24.529869
The application of nanopores as label-free, single-molecule biosensors for electrical or optical probing of structural features in biomolecules has been widely explored. While biological nanopores (membrane proteins and bacteriophage portal proteins)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8ca33030a4623684d9a803cf5bae4337
https://doi.org/10.1101/2022.08.07.503088
https://doi.org/10.1101/2022.08.07.503088