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Jungers Center for Neurosciences Research Department of Neurology Oregon Health & Science University Portland, Oregon 97239, USA
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Marine Chemistry and Geochemistry, Woods Hole Oceanographic Institution, Unites States
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Oregon Health & Science University 2720 S Moody Ave Portland, Oregon 97201, USA
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Universidade Federal de Goiás - Instituto de Ciências Biológicas - Brasil.
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Optimized platelet rich plasma releasate (O-rPRP) repairs galactosemia-induced ovarian follicular loss in rats by activating mTOR signaling and inhibiting apoptosis.
Not available
S-EPMC7509792
|
biostudies-literature
Cite
Self-propagating, protease-resistant, recombinant prion protein conformers with or without in vivo pathogenicity.
Not available
S-EPMC5524416
|
biostudies-literature
Cite
Preserving prion strain identity upon replication of prions in vitro using recombinant prion protein.
Not available
S-EPMC6134792
|
biostudies-literature
Cite
Role of the central lysine cluster and scrapie templating in the transmissibility of synthetic prion protein aggregates.
Not available
S-EPMC5614645
|
biostudies-literature
Cite
The amino-terminal PrP domain is crucial to modulate prion misfolding and aggregation.
Not available
S-EPMC1366767
|
biostudies-literature
Cite
Liquid-liquid phase separation of full-length prion protein initiates conformational conversion in vitro.
Not available
S-EPMC8289115
|
biostudies-literature
Cite
RNA-seq analyses reveal the relevance of RNAs involved in ribosomal complex to induce mammalian prion protein aggregation and phase separation <i>in vitro</i>.
Not available
S-EPMC12123958
|
biostudies-literature
Cite
Bank vole prion protein extends the use of RT-QuIC assays to detect prions in a range of inherited prion diseases.
Not available
S-EPMC7933407
|
biostudies-literature
Cite
Recombinant ovine prion protein can be mutated at position 136 to improve its efficacy as an inhibitor of prion propagation.
Not available
S-EPMC9978027
|
biostudies-literature
Cite
Isolation of novel synthetic prion strains by amplification in transgenic mice coexpressing wild-type and anchorless prion proteins.
Not available
S-EPMC3486332
|
biostudies-literature
Cite
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