Results 21 to 30 of about 4,254,953 (206)

Volume and energy folding landscape of prion protein revealed by pressure

Brazilian Journal of Medical and Biological Research, 2005
The main hypothesis for prion diseases proposes that the cellular protein (PrP C) can be altered into a misfolded, ß-sheet-rich isoform, the PrP Sc (from scrapie).
Y. Cordeiro, J. Kraineva, R. Winter, J.L. Silva   +3 more
doaj   +1 more source

Different isoforms of the non-integrin laminin receptor are present in mouse brain and bind PrP [PDF]

, 2003
The prion protein (PrP) plays a central role in prion diseases, and identifying its cellular receptor appears to be of crucial interest. We previously showed in the yeast twohybrid system that PrP interacts with the 37 kDa precursor (LRP) of the high ...
S. Weiss, J.-P. Deslys, Weiss, S., D. Dormont, Simoneau, S., S. Simoneau, Deslys, J.-P., Lasmézas, C., S. Haïk, C. Leucht, Haik, S., Leucht, C., Dormont, D., C. Lasmézas   +13 more
core   +3 more sources

Therapeutic implications of prion diseases

Biosafety and Health, 2021
Prions are unconventional infectious agents that cause lethal transmissible neurodegenerative diseases in human and animals. Prions can be distinguished from other known pathogens by their lack of nucleic acids.
Cao Chen, Xiaoping Dong
doaj   +1 more source

Effects of post-translational modifications on prion protein aggregation and the propagation of scrapie-like characteristics in vitro [PDF]

, 2007
Prion diseases, or transmissible spongiform encephalopathies (TSEs) are typically characterised by CNS accumulation of PrPSc, an aberrant conformer of a normal cellular protein PrPC.
Oxley, David, Meersman, Filip, Webster, Judith, Kazlauskaite, Jurate, Pinheiro, Teresa J. T., Young, Duncan S., Dear, Denise V., Lowe, Christopher R., Gill, Andrew C., Bronstein, Igor   +9 more
core   +1 more source

Characterization of the prion protein in relation to normal cellular function and in disease [PDF]

, 2012
Transmissible spongiform encephalopathies (TSEs), also known as prion diseases, are a group of rare and fatal neurodegenerative disorders that can affect both human and animals.
Wik, Lotta
core   +1 more source

Differential Accumulation of Misfolded Prion Strains in Natural Hosts of Prion Diseases

Viruses, 2021
Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of neurodegenerative protein misfolding diseases that invariably cause death.
Zoe J. Lambert, Justin J. Greenlee, Eric D. Cassmann, M. Heather West Greenlee   +3 more
doaj   +1 more source

Synthesis and structural characterization of a mimetic membrane-anchored prion protein [PDF]

, 2006
During pathogenesis of transmissible spongiform encephalopathies (TSEs) an abnormal form (PrPSc) of the host encoded prion protein (PrPC) accumulates in insoluble fibrils and plaques. The two forms of PrP appear to have identical covalent structures, but
Hicks, M R, David H. Crout, Crout, D H, Teresa J. T. Pinheiro, Ian D. Sylvester, Andrew C. Gill, Imanpreet K. Bath, Atvinder K. Rullay, Gill, A C, Bath, I K, Pinheiro, T J T, Matthew R. Hicks, Sylvester, I D, Rullay, A K   +13 more
core   +1 more source

Inhibition of group-I metabotropic glutamate receptors protects against prion toxicity.

PLoS Pathogens, 2017
Prion infections cause inexorable, progressive neurological dysfunction and neurodegeneration. Expression of the cellular prion protein PrPC is required for toxicity, suggesting the existence of deleterious PrPC-dependent signaling cascades.
Despoina Goniotaki, Asvin K K Lakkaraju, Amulya N Shrivastava, Pamela Bakirci, Silvia Sorce, Assunta Senatore, Rajlakshmi Marpakwar, Simone Hornemann, Fabrizio Gasparini, Antoine Triller, Adriano Aguzzi   +10 more
doaj   +1 more source

Neural Stem Cell Differentiation and Prion Infection

Bio-Protocol, 2014
Prion diseases are transmissible, fatal, neurodegenerative diseases in human and animals. The molecular basis of neurodegeneration in prion diseases is largely unclear. Developing a cellular model capable of monitoring prion-induced cytotoxicity would be
Yoshi Iwamaru, Takato Takenouchi, Hiroshi Kitani   +2 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