Ex vivo mammalian prions are formed of paired double helical prion protein fibrils

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

Detection and characterization of proteinase K-sensitive disease-related prion protein with thermolysin

Autor: Sabrina Cronier, Anthony R. Clarke, John Collinge, Graham S. Jackson, Jonathan D. F. Wadsworth, M. Howard Tattum, Nathalie Gros

Publikováno v: UK Funders’ TSE Workshop
UK Funders’ TSE Workshop, Labo/service de l'auteur, Ville service., Oct 1999, Warwick, United Kingdom. pp.Inconnu
Biochemical Journal

Disease-related PrP(Sc) [pathogenic PrP (prion protein)] is classically distinguished from its normal cellular precursor, PrP(C)(cellular PrP) by its detergent insolubility and partial resistance to proteolysis. Although molecular diagnosis of prion

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4111cf3755a12dc833b8d1db20cb7ed5
https://hal.inrae.fr/hal-02812714

Discrimination between prion-infected and normal blood samples by protein misfolding cyclic amplification

Autor: Samantha Jones, Suvankar Pal, Graham S. Jackson, M. Howard Tattum, John Collinge

Publikováno v: Transfusion. 50:996-1002

BACKGROUND:Diagnosis of prion disease from blood samples requires the detection of minute quantities of misfolded protein (PrPSc) against a high background of correctly folded material (PrPC). Protein misfolding cyclic amplification (PMCA) is a techn

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::216354fe43388a28315166a3414971e8
https://doi.org/10.1111/j.1537-2995.2010.02595.x

Pharmacological chaperone for the structured domain of human prion protein

Autor: Jonathan P. Waltho, John Collinge, Emmanuel Risse, M. Howard Tattum, Connor Wright, M Farrow, Anthony R. Clarke, Andrew J. Nicoll, Graham S. Jackson, Clare R. Trevitt, Richard B. Sessions, Emma Quarterman, Amaurys Avila Ibarra

Publikováno v: Proceedings of the National Academy of Sciences of the United States of America. 107(41)

In prion diseases, the misfolded protein aggregates are derived from cellular prion protein (PrP C ). Numerous ligands have been reported to bind to human PrP C (huPrP), but none to the structured region with the affinity required for a pharmacologic

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::4e9c5b1873c7cd8afc35be1869d897c9
https://pubmed.ncbi.nlm.nih.gov/20876144

A highly sensitive immunoassay for the detection of prion-infected material in whole human blood without the use of proteinase K

Autor: M Howard, Tattum, Samantha, Jones, Suvankar, Pal, Azedeh, Khalili-Shirazi, John, Collinge, Graham S, Jackson

Publikováno v: Transfusion. 50(12)

The causal association of variant Creutzfeldt-Jakob disease (vCJD) with bovine spongiform encephalopathy has raised significant concerns for public health. Assays for vCJD infection are vital for the application of therapeutics, for the screening of

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::d1adc49f961616c83ea7621476b6b4d1
https://pubmed.ncbi.nlm.nih.gov/20561299