Results 21 to 30 of about 1,549,882 (213)

TDP-43 Aggregation: The Healthy-Toxic Balance of the Prion-Like Domain. [PDF]

Adv Sci (Weinh)
TDP‐43 function relies on a delicate balance between reversible phase‐separated states and irreversible aggregation. Under physiological conditions, TDP‐43 forms dynamic droplets and oligomers that support normal cellular functions. In pathological contexts, this balance shifts toward aberrant aggregation, leading to toxic species.
Zangrando L, Buratti E, Paron F.
europepmc   +2 more sources

Characteristic distribution and molecular properties of normal cellular prion protein in human endocrine and exocrine tissues

Scientific Reports, 2022
Prion disease is an infectious and fatal neurodegenerative disease. Human prion disease autopsy studies have revealed abnormal prion protein (PrPSc) deposits in the central nervous system and systemic organs.
Sachiko Koyama, Hideko Noguchi, Kaoru Yagita, Hideomi Hamasaki, Masahiro Shijo, Motoi Yoshimura, Kohei Inoshita, Naokazu Sasagasako, Hiroyuki Honda   +8 more
doaj   +1 more source

Preclinical deposition of pathological prion protein PrPSc in muscles of hamsters orally exposed to scrapie [PDF]

Journal of Clinical Investigation, 2004
Recently, pathological prion protein PrP(Sc), the putative key constituent of infectious agents causing transmissible spongiform encephalopathies (TSEs), was found in muscles of rodents experimentally infected with scrapie and in patients with Creutzfeldt-Jakob disease (CJD).
Thomzig, A., Schulz-Schaeffer, Walter J., Kratzel, C., Mai, J., Beekes, M.   +4 more
openaire   +3 more sources

Beyond PrP res type 1/type 2 dichotomy in Creutzfeldt-Jakob disease [PDF]

, 2008
Sporadic Creutzfeldt-Jakob disease (sCJD) cases are currently subclassified according to the methionine/valine polymorphism at codon 129 of the PRNP gene and the proteinase K (PK) digested abnormal prion protein (PrPres)identified on Western blotting ...
Ironside, James W, Uro-Coste, Emmanuelle, Grassi, J., Head, Mark, Jean-Marc Bilheude, Lacroux, Caroline, Cassard Hervé, Armand Perret-Liaudet, Marie Bernadette Delisle, Grassi, Jacques, Head, M.W., Hauw, J.J., Head Mark W., Andréoletti Olivier, Bilheude, Jean-Marc, Peoch, Katell, Delisle, Marie-Bernadette, Streichenberger, Nathalie, Ironside, J.E., Simon Stéphanie, Lacroux Caroline, Simon, S., Haik, S., Peoch' Katell, Hervé Cassard, Jean-Jacques Hauw, Haik Stéphane, Basset-Leobon Christelle, Bilheude, J.M., Andreoletti, O., Jan Langeveld, Bilheude Jean-Marc, Stéphanie Simon, Uro-Coste Emmanuelle, Schelcher, F., Ironside, James, W., Langeveld, Jan, Christelle Basset-Leobon, Jacques Grassi, Olivier Andréoletti, Lugan, Séverine, Andréoletti, Olivier, Emmanuelle Uro-Coste, Lugan, S., Caroline Lacroux, Ironside, James, Hauw, Jean-Jacques, Perret-Liaudet, Armand, Basset-Leobon, Christelle, Basset-Leobon, C., Cassard, Hervé, Stéphane Haik, Head, Mark, W., Hauw Jean-Jacques, Langeveld Jan, James W Ironside, Simon, Stéphanie, Peoch, K., Séverine Lugan, Streichenberger Nathalie, Langeveld, J.P.M., Perret-Liaudet, A., Streichenberger, N., Cassard, H., Delisle, M.B., Uro-Coste, E., Haik, Stéphane, Schelcher, Francois, Grassi Jacques, Peoc’h, Katell, Mark W Head, Delisle, Marie Bernadette, Lacroux, C., Lugan Séverine, Schelcher Francois, Delisle Marie Bernadette, Head, Mark W, Ironside James W., Nathalie Streichenberger, Francois Schelcher, Katell Peoch', Perret-Liaudet Armand, Peoch', Katell, Head, Mark,, Ironside, James,   +84 more
core   +1 more source

Glycosylphosphatidylinositols: More than just an anchor?

Communicative & Integrative Biology, 2016
There is increasing interest in the role of glycosylphosphatidylinositol (GPI) anchors that attach some proteins to cell membranes. Far from being biologically inert, GPIs influence the targeting, intracellular trafficking and function of the attached ...
Clive Bate, William Nolan, Alun Williams
doaj   +1 more source

BSE infectivity in jejunum, ileum and ileocaecal junction of incubating cattle [PDF]

, 2011
To establish bovine spongiform encephalopathy (BSE) public health protection measures it is important to precisely define the cattle tissues considered as specified risk materials (SRM).
Rogers Ron, Ziegler Ute, Ziegler, U., Groschup, Martin H., Keller, M., van Keulen Lucien, Eiden, M., Hoffmann Christine, Eiden, Martin, Keller Markus, Eiden Martin, Bob Hills, Hills Bob, Christine Hoffmann, Jorg G Jacobs, Balkema-Buschmann, A., Van Keulen, L., Martin Kaatz, Ziegler, Ute, Ute Ziegler, Keulen, L., Van, Jacobs, J.G., Balkema-Buschmann Anne, Rogers, R., Keller, Markus, Groschup Martin H, Hoffmann, C., Hills, B., Lucien van Keulen, Balkema-Buschmann, Anne, Markus Keller, Martin Eiden, Kaatz, Martin, Fast, Christine, Anne Balkema-Buschmann, Kaatz Martin, Groschup, M.H., Martin H Groschup, Jacobs Jorg G, Kaatz, M., Ron Rogers   +40 more
core   +1 more source

Prion Protein Misfolding, Strains, and Neurotoxicity: An Update from Studies on Mammalian Prions

International Journal of Cell Biology, 2013
Prion diseases, also known as transmissible spongiform encephalopathies (TSEs), are a group of fatal neurodegenerative disorders affecting humans and other mammalian species.
Ilaria Poggiolini, Daniela Saverioni, Piero Parchi   +2 more
doaj   +1 more source

PrPSc-like prion protein peptide inhibits the function of cellular prion protein [PDF]

Biochemical Journal, 2000
Mice lacking expression of the prion protein are protected against infection with prion disease. Neurodegeneration in prion disease requires the formation of the abnormal isoform of the prion protein (PrPSc) from host prion protein. Therefore expression of normal host prion protein is necessary for prion disease.
openaire   +2 more sources

Heterogeneity of the Abnormal Prion Protein (PrPSc) of the Chandler Scrapie Strain [PDF]

Pathogens, 2013
The pathological prion protein, PrPSc, displays various sizes of aggregates. In this study, we investigated the conformation, aggregation stability and proteinase K (PK)-sensitivity of small and large PrPSc aggregates of mouse-adapted prion strains.
Kasai, Kazuo, Iwamaru, Yoshifumi, Masujin, Kentaro, Imamura, Morikazu, Mohri, Shirou, Yokoyama, Takashi   +5 more
openaire   +3 more sources

Prion protein self-peptides modulate prion interactions and conversion [PDF]

, 2009
Background: Molecular mechanisms underlying prion agent replication, converting host-encoded cellular prion protein (PrPC) into the scrapie associated isoform (PrPSc), are poorly understood.
Bossers, A., Fred G van Zijderveld, Priem, J., Drophatie Timmers-Parohi, Rigter, A., Alex Bossers, Alan Rigter, Timmers-Parohi, D., Jan PM Langeveld, van Zijderveld, F.G., Zijderveld, F.G., van, Jan Priem, Langeveld, J.P.M.   +12 more
core   +1 more source