Results 91 to 100 of about 56,657 (298)

Discrimination of Prion Strain Targeting in the Central Nervous System via Reactive Astrocyte Heterogeneity in CD44 Expression

Frontiers in Cellular Neuroscience, 2019
Prion diseases or transmissible spongiform encephalopathies are fatal, progressive, neurodegenerative, protein-misfolding disorders. Prion diseases may arise spontaneously, be inherited genetically or be acquired by infection and affect a variety of ...
Barry M. Bradford, Christianus A. W. Wijaya, Neil A. Mabbott   +2 more
doaj   +1 more source

TDP‐43 Aggregation: The Healthy‐Toxic Balance of the Prion‐Like Domain

Advanced Science, EarlyView.
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.
Luca Zangrando, Emanuele Buratti, Francesca Paron   +2 more
wiley   +1 more source

Glycosylation and prion protein

Current Opinion in Structural Biology, 2002
Recent advances have elucidated the detailed glycosylation of the prion protein and highlighted the size of the sugars, which shield large areas of the protein and confer some conformational stability on the normal cellular form. The reliability of SDS-PAGE banding patterns of different "glycoforms" as a diagnostics tool has been discussed.
Rudd, P, Merry, A, Wormald, M, Dwek, R
openaire   +2 more sources

Prion Protein in Glioblastoma Multiforme [PDF]

International Journal of Molecular Sciences, 2019
The cellular prion protein (PrPc) is an evolutionarily conserved cell surface protein encoded by the PRNP gene. PrPc is ubiquitously expressed within nearly all mammalian cells, though most abundantly within the CNS. Besides being implicated in the pathogenesis and transmission of prion diseases, recent studies have demonstrated that PrPc contributes ...
Larisa Ryskalin, Carla L. Busceti, Francesca Biagioni, Fiona Limanaqi, Pietro Familiari, Alessandro Frati, Francesco Fornai   +6 more
openaire   +2 more sources

Equine models in translational medicine: A comparative approach to human health

Animal Models and Experimental Medicine, EarlyView.
This diagram summarizes and contrasts rodent and equine models, outlining their strengths, limitations, and applications. Horses offer naturally occurring diseases, genetic and physiological similarities to humans, and suitability for longitudinal and clinical‐scale studies.
Shayan Boozarjomehri Amnieh, Katarzyna Ropka‐Molik   +1 more
wiley   +1 more source

Raman optical activity demonstrates poly(L-proline) II helix in the N-terminal region of the ovine prion protein: Implications for function and misfunction

, 2004
The aqueous solution structure of the full-length recombinant ovine prion protein PrP25-233, together with that of the N-terminal truncated version PrP94-233, have been studied using vibrational Raman optical activity (ROA) and ultraviolet circular ...
Rhie, A G O, Nielsen, Kurt, Blanch, EW, Rhie, AGO, Gill, AC, Hope, James, Hecht, L, Gill, Andrew C., Gill, A C, Blanch, E W, Barron, Laurence D., Barron, L D, Nielsen, K, Hope, J, Hecht, Lutz, Barron, LD, Blanch, Ewan W., Rhie, Alexandre G. O., Rhie, Alexandre G O   +18 more
core   +1 more source

The Prion-like domain in the exomer-dependent cargo Pin2 serves as a trans-Golgi retention motif [PDF]

, 2014
Prion and prion-like domains (PLDs) are found in many proteins throughout the animal kingdom. We found that the PLD in the S. cerevisiae exomer-depen- dent cargo protein Pin2 is involved in the regulation of protein transport and localization. The domain
Ritz, Alicja M., Mark Trautwein, Trautwein, Mark, Anne Spang, Spang, Anne, Grassinger, Franziska, Alicja M. Ritz, Franziska Grassinger, Ritz, A. M., Grassinger, F., Spang, A., Trautwein, M.   +11 more
core   +1 more source

Prion Protein Amyloidosis

Brain Pathology, 1996
The prion protein (PrP) plays an essential role in the pathogenesis of a group of sporadic, genetically determined and infectious fatal degenerative diseases, referred to as “prion diseases”, affecting the central nervous system of humans and other mammals. The cellular PrP is encoded by a single copy gene, highly conserved across mammalian species. In
B, Ghetti, P, Piccardo, B, Frangione, O, Bugiani, G, Giaccone, K, Young, F, Prelli, M R, Farlow, S R, Dlouhy, F, Tagliavini   +9 more
openaire   +2 more sources

Effect of enzymatic deimination on the conformation of recombinant prion protein

, 2009
Deimination is the post-translational conversion of arginine residues to citrulline. It has been implicated as a causative factor in autoimmune diseases such as multiple sclerosis and rheumatoid arthritis and more recently, as a marker of ...
Oxley, David, Meersman, Filip, Webster, Judith, Young, Duncan S., Dear, Denise V., Bronstein, Igor, Gill, Andy   +6 more
core  

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

, 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