Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Alexandre G. O. Rhie"'
Autor:
Ashraf A Choglay, Michael E. Cheetham, J. Paul Chapple, Simon Wilkins, Christopher R. Birkett, Alexandre G. O. Rhie, Jacqueline van der Spuy
Publikováno v:
The International Journal of Biochemistry & Cell Biology. 42:1226-1232
Conformational transitions in the prion protein (PrP) are thought to be central to the pathogenesis of the transmissible spongiform encephalopathies (TSE), such as Creutzfeldt-Jacob disease and bovine spongiform encephalopathy. Studies of prion pheno
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::b83a1de5ce4390f0115588591a489743
https://doi.org/10.1016/j.biocel.2010.04.013
https://doi.org/10.1016/j.biocel.2010.04.013
Autor:
Andrew C. Gill, James Hope, Lutz Hecht, Alexandre G. O. Rhie, Ewan W. Blanch, Kurt Nielsen, Laurence D. Barron
Publikováno v:
Blanch, E W, Gill, A C, Rhie, A G O, Hope, J, Hecht, L, Nielsen, K & Barron, L D 2004, ' Raman optical activity demonstrates poly(L-proline) II helix in the N-terminal region of the ovine prion protein: Implications for function and misfunction ', Journal of Molecular Biology, vol. 343, no. 2, pp. 467-476 . https://doi.org/10.1016/j.jmb.2004.08.058
The aqueous solution structure of the full-length recombinant ovine prion protein PrP25-233, together with that of the N-terminal truncated version PrP94-233, have been studied using vibrational Raman optical activity (ROA) and ultraviolet circular d
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::67202da3c048f063ef9c6aa630554a2b
https://doi.org/10.1016/j.jmb.2004.08.058
https://doi.org/10.1016/j.jmb.2004.08.058
Autor:
Andrew C. Gill, Petra Disterer, I. Sylvester, Abdessamad Tahiri-Alaoui, James Hope, Natalie M. Sayer, Alexandre G. O. Rhie, William James, Louise Kirby, Rosanna Wellesley
Publikováno v:
Journal of Biological Chemistry. 278:39697-39705
We have isolated artificial ligands or aptamers for infectious prions in order to investigate conformational aspects of prion pathogenesis. The aptamers are 2'-fluoro-modified RNA produced by in vitro selection from a large, randomized library. One o
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::749eb2aef3f7a4f3e13880e25d3f35b2
https://doi.org/10.1074/jbc.m305297200
https://doi.org/10.1074/jbc.m305297200
Autor:
Alexandre G. O. Rhie, Andrew C. Gill, Mark A Ritchie, Ewan W Blanch, Iain H. McColl, Kurt Nielsen, Lutz Hecht, Laurence D. Barron
Publikováno v:
Journal of the American Chemical Society. 125:10019-10026
The vibrational Raman optical activity (ROA) spectrum of a polypeptide in a model beta-sheet conformation, that of poly(l-lysine), was measured for the first time, and the alpha-helix --> beta-sheet transition monitored as a function of temperature i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::74103e00c6e97c36c3f1a9ef284d5f1a
https://doi.org/10.1021/ja021464v
https://doi.org/10.1021/ja021464v
Autor:
Alexandre G. O. Rhie, Abdessamad Tahiri-Alaoui, Marc Bullock, Matthew Cubin, William James, Natalie M. Sayer
Publikováno v:
The Journal of biological chemistry. 279(13)
We have recently described the isolation of 2'-fluoropyrimidine-substituted RNA aptamers that bind selectively to disease-associated beta-sheet-rich forms of the prion protein, PrP, from a number of mammalian species. These aptamers inhibit the accum
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f59e5d27872df7b28c2e4a84fc61a232
http://ora.ox.ac.uk/objects/uuid:d0183eb0-cd50-4263-923c-67d6d02d933c
http://ora.ox.ac.uk/objects/uuid:d0183eb0-cd50-4263-923c-67d6d02d933c
Autor:
Alexandre G. O. Rhie, James Hope, Lawrence G. Hunt, Alan D. Bennett, Andrew C. Gill, Sharon P. Bocking, Mark Ritchie, Sarah E. Steane, Kenneth G. Davies
Publikováno v:
Gill, A, Ritchie, M A, Hunt, L G, Steane, S E, Davis, K G, Bocking, S P, Rhie, A G O, Bennett, A D & Hope, J 2000, ' Post-translational hydroxylation at the N-terminus of the prion protein reveals presence of PPII structure in vivo ', EMBO Journal, vol. 19, no. 20, pp. 5324-5331 .
The transmissible spongiform encephalopathies are characterized by conversion of a host protein, PrPC (cellular prion protein), to a protease-resistant isoform, PrPSc (prion protein scrapie isoform). The importance of the highly-flexible, N-terminal
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d5af6ac321e949a10d396c3e1a981877
https://europepmc.org/articles/PMC314005/
https://europepmc.org/articles/PMC314005/
