Results 31 to 40 of about 3,400,014 (272)

Insight into the conserved structural dynamics of the C-terminus of mammal PrPC identifies structural core and possible structural role of pharmacological chaperones

Prion, 2023
Misfolding of the prion protein is central to prion disease aetiology. Although understanding the dynamics of the native fold helps to decipher the conformational conversion mechanism, a complete depiction of distal but coupled prion protein sites common
Patricia Soto, Garrett M. Gloeb, Kaitlin A. Tsuchida, Austin A. Charles, Noah M. Greenwood, Heidi Hendrickson   +5 more
doaj   +1 more source

Proteinase K-Resistant Material in ARR/VRQ Sheep Brain Affected with Classical Scrapie Is Composed Mainly of VRQ Prion Protein [PDF]

, 2011
Classical scrapie is a prion disease in sheep and goats. In sheep, susceptibility to disease is genetically influenced by single amino acid substitutions.
Bossers, A., A. Bossers, T. Sklaviadis, I. Lantier, F. Lantier, L. J. M. van Keulen, Van Keulen, L., S. McCutcheon, Berthon, P., Lantier, Isabelle, van Keulen, L.J.M., van Zijderveld, F.G., P. Berthon, Lantier, Frédéric, F., Zijderveld, F.G., van, Jacobs, J.G., Keulen, L., Van, Langeveld, J.P.M., Lantier, I., H. Rezaei, J. P. M. Langeveld, Rezaei, Human, Sklaviadis, T., Berthon, Patricia, J. G. Jacobs, F. G. van Zijderveld, Lantier, F., McCutcheon, S., Rezaei, H.   +28 more
core   +1 more source

The cellular prion protein beyond prion diseases

Swiss Medical Weekly, 2020
The cellular prion protein (PrPC), a cell surface glycoprotein originally identified for its central role in prion diseases (also called transmissible spongiform encephalopathies), has recently been implicated in the pathogenesis of other neurodegenerative disorders, such as Alzheimer’s and Parkinson’s diseases, by acting as a toxicity-transducing ...
Manni, Giorgia, Lewis, Victoria, Senesi, Matteo, Spagnolli, Giovanni, Fallarino, Francesca, Collins, Steven, Mouillet-Richard, Sophie, Biasini, Emiliano   +7 more
openaire   +6 more sources

Potential Therapeutic Use of Stem Cells for Prion Diseases

Cells, 2023
Prion diseases are neurodegenerative disorders that are progressive, incurable, and deadly. The prion consists of PrPSc, the misfolded pathogenic isoform of the cellular prion protein (PrPC).
Mohammed Zayed, Sung-Ho Kook, Byung-Hoon Jeong   +2 more
doaj   +1 more source

Prion protein in the cerebrospinal fluid of healthy and naturally scrapie-affected sheep [PDF]

, 2006
The aim of this study was to characterize the cerebrospinal fluid (CSF) prion protein (PrP) of healthy and naturally scrapie-affected sheep. The soluble form of CSF PrPC immunoblotted with an anti-octarepeat and an anti-C terminus mAb showed two isoforms
Vé Ronique Gayrard, Moudjou, Mohammed, Gayrard-Troy, Véronique, V., Pierre-Louis Toutain, Mohammed Moudjou, Chantal Imbs, Viguié, Catherine, Toutain, Pierre-Louis, Imbs, Chantal, Moudjou, Mohammed, M., Catherine Viguié, Nicole Picard-Hagen, Picard-Hagen, Nicole, Gayrard, Véronique   +13 more
core   +1 more source

Molecular Barriers to Zoonotic Transmission of Prions

Emerging Infectious Diseases, 2014
The risks posed to human health by individual animal prion diseases cannot be determined a priori and are difficult to address empirically. The fundamental event in prion disease pathogenesis is thought to be the seeded conversion of normal prion protein
Marcelo A. Barria, Aru Balachandran, Masanori Morita, Tetsuyuki Kitamoto, Rona Barron, Jean Manson, Richard Knight, James W. Ironside, Mark W. Head   +8 more
doaj   +1 more source

The crystal structure of the globular domain of sheep prion protein [PDF]

, 2004
The prion protein PrP is a naturally occurring polypeptide that becomes transformed from a normal conformation to that of an aggregated form, characteristic of pathological states in fatal transmissible spongiform conditions such as Creutzfeld–Jacob ...
Vasisht N, Whyte, SM, Dodson EJ, Vasisht, N, Gill, A.C., Whyte, S.M., Dodson, G.G., Whyte, S M, Vasisht, N., Bayley, P M, Verma, C., Verma C, Gill, A C, Bayley, PM, Bayley, P.M., Whyte SM, Haire LF, Gill AC, Gill, AC, Bayley PM, Dodson, EJ, Haire, L.F., Dodson, GG, Dodson, E.J., Haire, L F, Verma, C, Haire, LF, Dodson, E J, Dodson, G G   +28 more
core   +1 more source

Sequence features governing aggregation or degradation of prion-like proteins. [PDF]

PLoS Genetics, 2018
Enhanced protein aggregation and/or impaired clearance of aggregates can lead to neurodegenerative disorders such as Alzheimer's Disease, Huntington's Disease, and prion diseases.
Sean M Cascarina, Kacy R Paul, Satoshi Machihara, Eric D Ross   +3 more
doaj   +1 more source

Intra- and interspecies interactions between prion proteins and effects of mutations and polymorphisms [PDF]

, 2003
Recently, crystallization of the prion protein in a dimeric form was reported. Here we show that native soluble homogenous FLAG-tagged prion proteins from hamster, man and cattle expressed in the baculovirus system are predominantly dimeric.
Hundt, C., Weiss, S., Riley, M. L., Gauczynski, S., Leucht, C.   +4 more
core   +1 more source

Prion protein and cancers [PDF]

Acta Biochimica et Biophysica Sinica, 2014
The normal cellular prion protein, PrP(C) is a highly conserved and widely expressed cell surface glycoprotein in all mammals. The expression of PrP is pivotal in the pathogenesis of prion diseases; however, the normal physiological functions of PrP(C) remain incompletely understood.
Xiaowen, Yang, Yan, Zhang, Lihua, Zhang, Tianlin, He, Jie, Zhang, Chaoyang, Li   +5 more
openaire   +2 more sources