Results 31 to 40 of about 56,657 (298)

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

A Sequence-Dependent DNA Condensation Induced by Prion Protein

Journal of Nucleic Acids, 2018
Different studies indicated that the prion protein induces hybridization of complementary DNA strands. Cell culture studies showed that the scrapie isoform of prion protein remained bound with the chromosome. In present work, we used an oxazole dye, YOYO,
Alakesh Bera, Sajal Biring
doaj   +1 more source

A quantitative characterization of interaction between prion protein with nucleic acids

Biochemistry and Biophysics Reports, 2018
Binding of recombinant prion protein with small highly structured RNAs, prokaryotic and eukaryotic prion protein mRNA pseudoknots, tRNA and polyA has been studied by the change in fluorescence anisotropy of the intrinsic tryptophan groups of the protein.
Alakesh Bera, Sajal Biring
doaj   +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

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

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

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

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 L108I polymorphism in mouse prion protein drives spontaneous disease and enhances transmission of atypical and classical prion strains. [PDF]

Brain Pathol
A single amino acid change (L108I) combined with PrP overexpression drives spontaneous atypical prion formation in mice, enabling also efficient propagation of diverse prion strains. This model allows studying how spontaneous prion diseases arise and provides powerful tools for investigating strain emergence, transmission barriers, and mechanisms ...
Eraña H, Vidal E, Fernández-Borges N, Charco JM, Díaz-Domínguez CM, Sampedro-Torres-Quevedo C, Galarza-Ahumada J, Fernández-Muñoz E, San-Juan-Ansoleaga M, Pérez-Castro MÁ, Gonçalves-Anjo N, Piñeiro P, Giler S, González-Martín N, Lorenzo NL, Manero-Azua A, Perez de Nanclares G, Geijo M, Sánchez-Martín MA, Requena JR, Castilla J.   +20 more
europepmc   +2 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