Results 61 to 70 of about 1,598,142 (264)

Evolutionary descent of prion genes from the ZIP family of metal ion transporters. [PDF]

PLoS ONE, 2009
In the more than twenty years since its discovery, both the phylogenetic origin and cellular function of the prion protein (PrP) have remained enigmatic.
Gerold Schmitt-Ulms, Sepehr Ehsani, Joel C Watts, David Westaway, Holger Wille   +4 more
doaj   +1 more source

Prion protein interconversions† [PDF]

Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences, 2001
The transmissible spongiform encephalopathies (TSEs), or prion diseases, remain mysterious neurodegenerative diseases that involve perturbations in prion protein (PrP) structure. This article summarizes our use of in vitro models to describe how PrP is converted to the disease–associated ...
openaire   +2 more sources

Prion Protein Biology [PDF]

Cell, 1998
We thank G. Carlson, N. Nathanson, and J. Safar for carefully reviewing sections of this manuscript. This research was supported by grants from the National Institute of Aging and the National Institute of Neurologic Diseases and Stroke of the National Institutes of Health, International Human Frontiers of Science Program, and American Health ...
Prusiner, Stanley B, Scott, Michael R, DeArmond, Stephen J, Cohen, Fred E   +3 more
openaire   +2 more sources

MARK4 enhances stress granule formation under oxidative stress and increases tau accumulation

FEBS Open Bio, EarlyView.
MARK4 (red dots) localizes to stress granules (orange dots) and promotes their formation under oxidative stress by modulating TIA1 (blue dots). MARK4 and TIA1 synergistically increase tau (purple) accumulation, and the reduction of the TIA1 ortholog suppresses neurodegeneration in a fly model.
Sho Nakajima, Kotone Watanabe, Grigorii Sultanakhmetov, Aoi Fukuchi, Keiya Ito, Sawako Shimizu, Taro Saito, Akiko Asada, Kanae Ando   +8 more
wiley   +1 more source

Exploring the mechanisms involved in prion degradation and spreading from cell-to-cell in neuronal cell models [PDF]

, 2011
Transmissible spongiform encephalopathies (TSE), also known as prion diseases, are fatal neurodegenerative disorders present both in human and animals with different aetiology as they can occur genetically, spontaneously or by infection (Prusiner 1998 ...
Marzo, Ludovica
core   +1 more source

SPG4 and Dementia: Expanding the Clinical Spectrum

Annals of Clinical and Translational Neurology, EarlyView.
ABSTRACT Objective Hereditary spastic paraplegia (HSP) is a group of disorders characterized by progressive spasticity and lower limb weakness, with mutations in SPG4/SPAST being the most common cause. Detailed studies and clinical and molecular comparisons across different populations are missing.
Emanuele Panza, Arun Meyyazhagan, Eliseo Picchi, Gustavo Ribas, Ingrid Faber, Ryosuke Miyamoto, Preethi Basavaraju, Paolo Eusebi, Haripriya Kuchi Bhotla, Mario Stasi, Fabrizio Gaudiello, Francesco Patti, Filippo Maria Santorelli, Marcondes Cavalcante França Jr, José Luiz Pedroso, Orlando Graziani Povoas Barsottini, Hélio Afonso Ghizoni Teive, Peter Henry St George‐Hyslop, Toshitaka Kawarai, Antonio Orlacchio   +19 more
wiley   +1 more source

Analysis of the hippocampal proteome in ME7 prion disease reveals a predominant astrocytic signature and highlights the brain-restricted production of clusterin in chronic neurodegeneration

, 2014
Prion diseases are characterized by accumulation of misfolded protein, gliosis, synaptic dysfunction, and ultimately neuronal loss. This sequence, mirroring key features of Alzheimer disease, is modeled well in ME7 prion disease.
Asuni, Ayodeji A, Skipp, Paul, Gray, Bryony, Bailey, Joanne, O'Connor, Vincent, Perry, V Hugh   +5 more
core   +1 more source

Exogenous prion-like proteins and their potential to trigger cognitive dysfunction

Molecular Systems Biology
The gut is exposed to a wide range of proteins, including ingested proteins and those produced by the resident microbiota. While ingested prion-like proteins can propagate across species, their implications for disease development remain largely unknown.
Jofre Seira Curto, Adan Dominguez Martinez, Genis Perez Collell, Estrella Barniol Simon, Marina Romero Ruiz, Berta Franco Bordés, Paula Sotillo Sotillo, Sandra Villegas Hernandez, Maria Rosario Fernandez, Natalia Sanchez de Groot   +9 more
doaj   +1 more source

Chronic Wasting Disease Prion Strain Emergence and Host Range Expansion

Emerging Infectious Diseases, 2017
Human and mouse prion proteins share a structural motif that regulates resistance to common chronic wasting disease (CWD) prion strains. Successful transmission of an emergent strain of CWD prion, H95+, into mice resulted in infection. Thus, emergent CWD
Allen Herbst, Camilo Duque Velásquez, Elizabeth Triscott, Judd M. Aiken, Debbie McKenzie   +4 more
doaj   +1 more source

Cytosolic Prion Protein Toxicity Is Independent of Cellular Prion Protein Expression and Prion Propagation [PDF]

Journal of Virology, 2007
ABSTRACT Prion diseases are transmissible neurodegenerative diseases caused by a conformational isoform of the prion protein (PrP), a host-encoded cell surface sialoglycoprotein. Recent evidence suggests a cytosolic fraction of PrP (cyPrP) functions either as an initiating factor or toxic element of prion disease.
Eric M, Norstrom, Mark F, Ciaccio, Benjamin, Rassbach, Robert, Wollmann, James A, Mastrianni   +4 more
openaire   +2 more sources