Results 81 to 90 of about 97,377 (307)

Metabolism of minor isoforms of prion proteins: Cytosolic prion protein and transmembrane prion protein.

open access: yesNeural regeneration research, 2013
Transmissible spongiform encephalopathy or prion disease is triggered by the conversion from cellular prion protein to pathogenic prion protein. Growing evidence has concentrated on prion protein configuration changes and their correlation with prion disease transmissibility and pathogenicity.
Song, Zhiqi, Zhao, Deming, Yang, Lifeng
openaire   +2 more sources

Conformational conversion of prion protein in prion diseases [PDF]

open access: yesActa Biochimica et Biophysica Sinica, 2013
Prion diseases are a group of infectious fatal neurodegenerative diseases. The conformational conversion of a cellular prion protein (PrP(C)) into an abnormal misfolded isoform (PrP(Sc)) is the key event in prion diseases pathology. Under normal conditions, the high-energy barrier separates PrP(C) from PrP(Sc) isoform.
Zheng, Zhou, Gengfu, Xiao
openaire   +2 more sources

"Alternative" endocytic mechanisms exploited by pathogens: new avenues for therapeutic delivery? [PDF]

open access: yes, 2007
Some pathogens utilize unique routes to enter cells that may evade the intracellular barriers encountered by the typical clathrin-mediated endocytic pathway.
Medina-Kauwe, LK
core   +1 more source

Alzheimer's Disease Risk Factor APOE4 Exerts Dimorphic Effects on Female Bone

open access: yesAdvanced Science, EarlyView.
In aging bone, osteocytes accumulate neurodegenerative risk factor Apolipoprotein E (APOE). A humanized version of the Alzheimer's disease risk allele APOE4 altered the mouse bone transcriptome and proteome, with effects in female bone surpassing the brain, including bone fragility due to suppressed osteocytic maintenance of bone quality, identifying ...
Charles A. Schurman   +15 more
wiley   +1 more source

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

open access: yesFrontiers 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   +2 more
doaj   +1 more source

Nanoplastics and Neurodegeneration: A Roadmap From Mechanism to Causation

open access: yesAdvanced Science, EarlyView.
Nanoplastics are pervasive environmental contaminants with potentially profound implications for human health. Emerging evidence suggests a possible link between nanoplastic exposure and neurodegeneration, a key driver of ageing and dementia, yet causality remains unresolved.
Yuhuan Li   +5 more
wiley   +1 more source

Prion protein and cancers [PDF]

open access: yesActa 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   +5 more
openaire   +2 more sources

Cystatin F is a biomarker of prion pathogenesis in mice.

open access: yesPLoS ONE, 2017
Misfolding of the cellular prion protein (PrPC) into the scrapie prion protein (PrPSc) results in progressive, fatal, transmissible neurodegenerative conditions termed prion diseases.
Mario Nuvolone   +17 more
doaj   +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

open access: yes, 2013
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   +5 more
core   +1 more source

The prion protein constitutively controls neuronal store-operated ca2+ entry through Fyn Kinase [PDF]

open access: yes, 2015
The prion protein (PrPC) is a cell surface glycoprotein mainly expressed in neurons, whose misfolded isoforms generate the prion responsible for incurable neurodegenerative disorders.
Agnese eDe Mario   +8 more
core   +4 more sources

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