Zobrazeno 1 - 10
of 96
pro vyhledávání: '"Joel C Watts"'
Autor:
Daniel J Walsh, Judy R Rees, Surabhi Mehra, Matthew E C Bourkas, Lech Kaczmarczyk, Erica Stuart, Walker S Jackson, Joel C Watts, Surachai Supattapone
Publikováno v:
PLoS Pathogens, Vol 20, Iss 4, p e1012087 (2024)
Prion diseases uniquely manifest in three distinct forms: inherited, sporadic, and infectious. Wild-type prions are responsible for the sporadic and infectious versions, while mutant prions cause inherited variants like fatal familial insomnia (FFI)
Externí odkaz:
https://doaj.org/article/bc72e3d470f04611b70c93e0829e5d34
Autor:
Declan Williams, Mohadeseh Mehrabian, Hamza Arshad, Shehab Eid, Christopher Sackmann, Wenda Zhao, Xinzhu Wang, Farinaz Ghodrati, Claire E Verkuyl, Joel C Watts, Gerold Schmitt-Ulms
Publikováno v:
PLoS ONE, Vol 16, Iss 11, p e0258682 (2021)
The prion protein (PrP) is best known for its ability to cause fatal neurodegenerative diseases in humans and animals. Here, we revisited its molecular environment in the brain using a well-developed affinity-capture mass spectrometry workflow that o
Externí odkaz:
https://doaj.org/article/2a6e7645933d479ea87063ce25ab1eef
Autor:
Cassandra M Burke, Kenneth M K Mark, Daniel J Walsh, Geoffrey P Noble, Alexander D Steele, Abigail B Diack, Jean C Manson, Joel C Watts, Surachai Supattapone
Publikováno v:
PLoS Pathogens, Vol 16, Iss 9, p e1008875 (2020)
Prions are unorthodox pathogens that cause fatal neurodegenerative diseases in humans and other mammals. Prion propagation occurs through the self-templating of the pathogenic conformer PrPSc, onto the cell-expressed conformer, PrPC. Here we study th
Externí odkaz:
https://doaj.org/article/56f2eed8818d434daa5cbc4eb00e3299
Autor:
Cassandra M Burke, Daniel J Walsh, Alexander D Steele, Umberto Agrimi, Michele Angelo Di Bari, Joel C Watts, Surachai Supattapone
Publikováno v:
PLoS Pathogens, Vol 15, Iss 3, p e1007662 (2019)
The protein-only hypothesis predicts that infectious mammalian prions are composed solely of PrPSc, a misfolded conformer of the normal prion protein, PrPC. However, protein-only PrPSc preparations lack significant levels of prion infectivity, leadin
Externí odkaz:
https://doaj.org/article/faa03f4b1582437aac6477a3c8949854
Autor:
Hansen Wang, Lisa D Muiznieks, Punam Ghosh, Declan Williams, Michael Solarski, Andrew Fang, Alejandro Ruiz-Riquelme, Régis Pomès, Joel C Watts, Avi Chakrabartty, Holger Wille, Simon Sharpe, Gerold Schmitt-Ulms
Publikováno v:
eLife, Vol 6 (2017)
The amyloid β peptide (Aβ) is a key player in the etiology of Alzheimer disease (AD), yet a systematic investigation of its molecular interactions has not been reported. Here we identified by quantitative mass spectrometry proteins in human brain e
Externí odkaz:
https://doaj.org/article/335a92b94e58463380f20574bebf20a3
'Prion-like' seeding and propagation of oligomeric protein assemblies in neurodegenerative disorders
Publikováno v:
Frontiers in Neuroscience, Vol 18 (2024)
Intra- or extracellular aggregates of proteins are central pathogenic features in most neurodegenerative disorders. The accumulation of such proteins in diseased brains is believed to be the end-stage of a stepwise aggregation of misfolded monomers t
Externí odkaz:
https://doaj.org/article/c1e48e850d5b47848ab565dc12d52b9e
Publikováno v:
PLoS Pathogens, Vol 10, Iss 4, p e1003990 (2014)
Bank voles are uniquely susceptible to a wide range of prion strains isolated from many different species. To determine if this enhanced susceptibility to interspecies prion transmission is encoded within the sequence of the bank vole prion protein (
Externí odkaz:
https://doaj.org/article/156873200a4b4cd5a91bbf5c44f8dddd
Autor:
Joel C Watts, Jan Stöhr, Sumita Bhardwaj, Holger Wille, Abby Oehler, Stephen J Dearmond, Kurt Giles, Stanley B Prusiner
Publikováno v:
PLoS Pathogens, Vol 7, Iss 11, p e1002382 (2011)
The central event in prion diseases is the conformational conversion of the cellular prion protein (PrP(C)) into PrP(Sc), a partially protease-resistant and infectious conformer. However, the mechanism by which PrP(Sc) causes neuronal dysfunction rem
Externí odkaz:
https://doaj.org/article/231bd22d391c4443a3bd25e5e8b0c570
Autor:
Joel C Watts, Hairu Huo, Yu Bai, Sepehr Ehsani, Amy Hye Won Jeon, Tujin Shi, Nathalie Daude, Agnes Lau, Rebecca Young, Lei Xu, George A Carlson, David Williams, David Westaway, Gerold Schmitt-Ulms
Publikováno v:
PLoS Pathogens, Vol 5, Iss 10, p e1000608 (2009)
The physiological environment which hosts the conformational conversion of the cellular prion protein (PrP(C)) to disease-associated isoforms has remained enigmatic. A quantitative investigation of the PrP(C) interactome was conducted in a cell cultu
Externí odkaz:
https://doaj.org/article/67628af0e08d41bbbc288033fce3128f
Publikováno v:
PLoS ONE, Vol 4, Iss 9, p e7208 (2009)
In the more than twenty years since its discovery, both the phylogenetic origin and cellular function of the prion protein (PrP) have remained enigmatic. Insights into a possible function of PrP may be obtained through the characterization of its mol
Externí odkaz:
https://doaj.org/article/742c5ba06463426ab2c0451aee8f2e35