Zobrazeno 1 - 10
of 66
pro vyhledávání: '"Jan Bieschke"'
Autor:
Daljit Sangar, Elizabeth Hill, Kezia Jack, Mark Batchelor, Beenaben Mistry, Juan M Ribes, Graham S Jackson, Simon Mead, Jan Bieschke
Publikováno v:
eLife, Vol 13 (2024)
Prions replicate via the autocatalytic conversion of cellular prion protein (PrPC) into fibrillar assemblies of misfolded PrP. While this process has been extensively studied in vivo and in vitro, non-physiological reaction conditions of fibril forma
Externí odkaz:
https://doaj.org/article/2c2634c1479647b1a828b41cf5d5cf73
Autor:
Jiang Zhu, Sara Pittman, Dhruva Dhavale, Rachel French, Jessica N. Patterson, Mohamed Salman Kaleelurrrahuman, Yuanzi Sun, Jaime Vaquer-Alicea, Gianna Maggiore, Christoph S. Clemen, William J. Buscher, Jan Bieschke, Paul Kotzbauer, Yuna Ayala, Marc I. Diamond, Albert A. Davis, Conrad Weihl
Publikováno v:
Molecular Neurodegeneration, Vol 17, Iss 1, Pp 1-25 (2022)
Abstract Background Neuronal uptake and subsequent spread of proteopathic seeds, such as αS (alpha-synuclein), Tau, and TDP-43, contribute to neurodegeneration. The cellular machinery participating in this process is poorly understood. One proteinop
Externí odkaz:
https://doaj.org/article/47c9b932aac447af8c16f13a657d0a0e
Publikováno v:
Biomolecules, Vol 12, Iss 11, p 1694 (2022)
Prion diseases are a class of neurodegenerative diseases that are uniquely infectious. Whilst their general replication mechanism is well understood, the components required for the formation and propagation of highly infectious prions are poorly cha
Externí odkaz:
https://doaj.org/article/23cc9bac1e484d3e828dad98d7a3583c
Publikováno v:
BioTechniques, Vol 55, Iss 1, Pp 28-33 (2013)
We present a very simple procedure yielding high-contrast images of adherent, confluent cells such as human neuroblastoma (SH-EP) cells by ordinary bright-field microscopy. Cells are illuminated through a color filter and a pinhole aperture placed be
Externí odkaz:
https://doaj.org/article/23d21e9d0cc04d7596e32323460a288b
Seed amplification and neurodegeneration marker trajectories in individuals at risk of prion disease
Autor:
Tze How Mok, Akin Nihat, Nour Majbour, Danielle Sequeira, Leah Holm-Mercer, Thomas Coysh, Lee Darwent, Mark Batchelor, Bradley R Groveman, Christina D Orr, Andrew G Hughson, Amanda Heslegrave, Rhiannon Laban, Elena Veleva, Ross W Paterson, Ashvini Keshavan, Jonathan M Schott, Imogen J Swift, Carolin Heller, Jonathan D Rohrer, Alexander Gerhard, Christopher Butler, James B Rowe, Mario Masellis, Miles Chapman, Michael P Lunn, Jan Bieschke, Graham S Jackson, Henrik Zetterberg, Byron Caughey, Peter Rudge, John Collinge, Simon Mead
Human prion diseases are remarkable for long incubation times followed typically by rapid clinical decline. Seed amplification assays and neurodegeneration biofluid biomarkers are remarkably useful in the clinical phase, but their potential to predic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::01793c1b3a290902fc8ea00f8ec41a6a
https://www.repository.cam.ac.uk/handle/1810/350803
https://www.repository.cam.ac.uk/handle/1810/350803
Autor:
Savroop K. Bhamra, Parineeta Arora, Laszlo L. P. Hosszu, Jan Bieschke, Anthony R. Clarke, John Collinge, Parmjit S. Jat
Mutational analysis of the cellular prion protein (PrPC) has revealed various regions of the protein that modulate prion propagation. However, most approaches involve deletions, insertions, or replacements in the presence of the wild-type cellular pr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::49405a2f604d3a2ab0b884ab8a548b11
https://doi.org/10.1101/2023.01.19.524767
https://doi.org/10.1101/2023.01.19.524767
Autor:
Tze How Mok, Akin Nihat, Nour Majbour, Danielle Sequeira, Leah Holm-Mercer, Thomas Coysh, Lee Darwent, Mark Batchelor, Bradley R Groveman, Christina D Orrù, Andrew G Hughson, Amanda Heslegrave, Rhiannon Laban, Elena Veleva, Ross W Paterson, Ashvini Keshavan, Jonathan Schott, Imogen J Swift, Carolin Heller, Jonathan D Rohrer, Alexander Gerhard, Christopher Butler, James B Rowe, Mario Masellis, Miles Chapman, Michael P Lunn, Jan Bieschke, Graham Jackson, Henrik Zetterberg, Byron Caughey, Peter Rudge, John Collinge, Simon Mead
Human prion diseases are remarkable for long incubation times followed by typically rapid clinical decline. Seed amplification assays and neurodegeneration biofluid biomarkers are remarkably useful in the clinical phase, but their potential to predic
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::da3aac789cb837499652c75f72d24073
https://doi.org/10.1101/2022.10.30.22281644
https://doi.org/10.1101/2022.10.30.22281644
Autor:
Laszlo Luis Pereira Hosszu, Daljit Sangar, Mark Batchelor, Emmanuel Risse, Andrea M. Hounslow, Jonathan P. Waltho, John Collinge, Jan Bieschke
Prion diseases, a group of incurable, lethal neurodegenerative disorders of mammals including humans, are caused by prions, assemblies of misfolded host prion protein (PrP). The pathway of PrP misfolding is still unclear, though previous data indicat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7943559c2079282e34a026b2035ff433
https://doi.org/10.1101/2022.09.20.508729
https://doi.org/10.1101/2022.09.20.508729
Autor:
Yuanzi Sun, Kezia Jack, Tiziana Ercolani, Daljit Sangar, Laszlo Hosszu, John Collinge, Jan Bieschke
SummaryIn prion diseases, fibrillar assemblies of misfolded prion protein (PrP) self-propagate by incorporating PrP monomers. Using total internal reflection and transient amyloid binding super-resolution microscopy, our study analyses elongation of
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::98fd7ed3412c55c34ceedd4cb88ef95d
https://doi.org/10.1101/2022.08.10.503301
https://doi.org/10.1101/2022.08.10.503301
Autor:
Laszlo L. P. Hosszu, Daljit Sangar, Mark Batchelor, Emmanuel Risse, Andrea M. Hounslow, John Collinge, Jonathan P. Waltho, Jan Bieschke
Publikováno v:
Journal of Molecular Biology. :168158