Zobrazeno 1 - 10
of 97
pro vyhledávání: '"Jonathan D F, Wadsworth"'
Autor:
Graham S. Jackson, Jacqueline Linehan, Sebastian Brandner, Emmanuel A. Asante, Jonathan D. F. Wadsworth, John Collinge
Publikováno v:
Scientific Reports, Vol 12, Iss 1, Pp 1-9 (2022)
Abstract Transgenic mice over-expressing human PRNP or murine Prnp transgenes on a mouse prion protein knockout background have made key contributions to the understanding of human prion diseases and have provided the basis for many of the fundamenta
Externí odkaz:
https://doaj.org/article/436ec582413448b5a496b4820ef97f59
Autor:
Szymon W. Manka, Wenjuan Zhang, Adam Wenborn, Jemma Betts, Susan Joiner, Helen R. Saibil, John Collinge, Jonathan D. F. Wadsworth
Publikováno v:
Nature Communications, Vol 13, Iss 1, Pp 1-11 (2022)
High-resolution structures of mammalian prions have remained elusive. Here, Manka et al. report the cryo-EM structure of infectious RML prion fibrils from mice. Structural similarity with recently reported infectious 263K prion fibrils from hamsters
Externí odkaz:
https://doaj.org/article/9b6eb942195b4bc19be04c9aa47b9d02
Autor:
Emmanuel A Asante, Jacqueline M Linehan, Andrew Tomlinson, Tatiana Jakubcova, Shyma Hamdan, Andrew Grimshaw, Michelle Smidak, Asif Jeelani, Akin Nihat, Simon Mead, Sebastian Brandner, Jonathan D F Wadsworth, John Collinge
Publikováno v:
PLoS Biology, Vol 18, Iss 6, p e3000725 (2020)
Inherited prion diseases are caused by autosomal dominant coding mutations in the human prion protein (PrP) gene (PRNP) and account for about 15% of human prion disease cases worldwide. The proposed mechanism is that the mutation predisposes to confo
Externí odkaz:
https://doaj.org/article/23162b9d52f24df19f6d1cd295aceaa2
Publikováno v:
Cell and Tissue Research. 392:167-178
Mammalian prions are lethal transmissible pathogens that cause fatal neurodegenerative diseases in humans and animals. They consist of fibrils of misfolded, host-encoded prion protein (PrP) which propagate through templated protein polymerisation. Pr
Publikováno v:
Frontiers in Molecular Neuroscience, Vol 12 (2019)
Prions are lethal pathogens, which cause fatal neurodegenerative diseases in mammals. They are unique infectious agents and are composed of self-propagating multi-chain assemblies of misfolded host-encoded prion protein (PrP). Understanding prion str
Externí odkaz:
https://doaj.org/article/9239cd6e87034867bea517f2eeafecf4
Autor:
Claire J. Sarell, Emma Quarterman, Daniel C.-M. Yip, Cassandra Terry, Andrew J. Nicoll, Jonathan D. F. Wadsworth, Mark A. Farrow, Dominic M. Walsh, John Collinge
Publikováno v:
Open Biology, Vol 7, Iss 11 (2017)
Mammalian prions cause lethal neurodegenerative diseases such as Creutzfeldt–Jakob disease (CJD) and consist of multi-chain assemblies of misfolded cellular prion protein (PrPC). Ligands that bind to PrPC can inhibit prion propagation and neurotoxi
Externí odkaz:
https://doaj.org/article/229b8c2701a0414b8a25fe465d116345
Autor:
Cassandra Terry, Adam Wenborn, Nathalie Gros, Jessica Sells, Susan Joiner, Laszlo L. P. Hosszu, M. Howard Tattum, Silvia Panico, Daniel K. Clare, John Collinge, Helen R. Saibil, Jonathan D. F. Wadsworth
Publikováno v:
Open Biology, Vol 6, Iss 5 (2016)
Mammalian prions are hypothesized to be fibrillar or amyloid forms of prion protein (PrP), but structures observed to date have not been definitively correlated with infectivity and the three-dimensional structure of infectious prions has remained ob
Externí odkaz:
https://doaj.org/article/66baab80ced54423ba33dae7af2b24e3
Autor:
Emmanuel A Asante, Andrew Grimshaw, Michelle Smidak, Tatiana Jakubcova, Andrew Tomlinson, Asif Jeelani, Shyma Hamdan, Caroline Powell, Susan Joiner, Jacqueline M Linehan, Sebastian Brandner, Jonathan D F Wadsworth, John Collinge
Publikováno v:
PLoS Pathogens, Vol 11, Iss 7, p e1004953 (2015)
Inherited prion disease (IPD) is caused by autosomal-dominant pathogenic mutations in the human prion protein (PrP) gene (PRNP). A proline to leucine substitution at PrP residue 102 (P102L) is classically associated with Gerstmann-Sträussler-Scheink
Externí odkaz:
https://doaj.org/article/cbedaacc47634d168258a9c11682a9a1
Autor:
Christian Schmidt, Jeremie Fizet, Francesca Properzi, Mark Batchelor, Malin K. Sandberg, Julie A. Edgeworth, Louise Afran, Sammy Ho, Anjna Badhan, Steffi Klier, Jacqueline M. Linehan, Sebastian Brandner, Laszlo L. P. Hosszu, M. Howard Tattum, Parmjit Jat, Anthony R. Clarke, Peter C. Klöhn, Jonathan D. F. Wadsworth, Graham S. Jackson, John Collinge
Publikováno v:
Open Biology, Vol 5, Iss 12 (2015)
According to the protein-only hypothesis, infectious mammalian prions, which exist as distinct strains with discrete biological properties, consist of multichain assemblies of misfolded cellular prion protein (PrP). A critical test would be to produc
Externí odkaz:
https://doaj.org/article/d9df89cc5c84457ea1d505bc18d78e06
Autor:
Emmanuel A. Asante, Kezia Jack, Maged Taema, Fuquan Zhang, Jørn Våge, Thea Ingold, Malin K. Sandberg, Bjørnar Ytrehus, Helena Costa, Linh T. Tran, Knut Madslien, Sebastian Brandner, Sylvie L. Benestad, Susan Joiner, Jacqueline M. Linehan, Jonathan D. F. Wadsworth, Turid Vikøren, Huda Al-Doujaily, John Collinge
Publikováno v:
The Journal of infectious diseases. 226(5)
Chronic wasting disease (CWD) is the transmissible spongiform encephalopathy or prion disease affecting cervids. In 2016, the first cases of CWD were reported in Europe in Norwegian wild reindeer and moose. The origin and zoonotic potential of these