Results 161 to 170 of about 1,553,593 (211)

AI-designed prion-capping proteins provide evidence that prion fibril ends are replication-competent surfaces that contribute to prion seeding activity and infectivity. [PDF]

open access: yesmBio
Slota JA   +10 more
europepmc   +1 more source

PrPC Directly Interacts with Proteins Involved in Signaling Pathways* [PDF]

open access: yesJournal of Biological Chemistry, 2001
The cellular prion protein (PrP(C)) is a conserved glycoprotein predominantly expressed in neuronal cells. Its purpose in living cells is still enigmatic. To elucidate on its cellular function, we performed a yeast two-hybrid screen for interactors.
Hermann M. Schätzl
exaly   +3 more sources
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Mitochondrial localization of cellular prion protein (PrPC) invokes neuronal apoptosis in aged transgenic mice overexpressing PrPC

Neuroscience Letters, 2005
Recent studies suggest that the disease isoform of prion protein (PrPSc) is non-neurotoxic in the absence of cellular isoform of prion protein (PrPC), indicating that PrPC may participate directly in the neurodegenerative damage by itself. Meanwhile, transgenic mice harboring a high-copy-number of wild-type mouse (Mo) PrPC develop a spontaneous ...
Naomi S, Hachiya   +9 more
openaire   +2 more sources

Bovine PrPC directly interacts with αB-crystalline [PDF]

open access: yesFEBS Letters, 2005
We used a bovine brain cDNA library to perform a yeast two-hybrid assay with bovine mature PrPC as bait. The screening result showed that αB-crystalline interacted with PrPC.
Po Tien, Mingxiong Guo, Rui Gong
exaly   +2 more sources

Isolation and characterization of full-length recombinant cattle PrPC protein

Bulletin of Experimental Biology and Medicine, 2006
Full-length Bos taurus PrPC protein was obtained in the eu- and prokaryotic expression systems. Immunoblotting and indirect enzyme immunoassay demonstrated high specificity and antigenic activity of full-length proteins in the reactions with monoclonal antibodies (anti-SAF-32 and VRQ-84).
S L, Kal'nov   +8 more
openaire   +2 more sources

Prion protein (PrPc) promotes β-amyloid plaque formation

Neurobiology of Aging, 2005
Prion protein (PrP) has been localized to amyloid-beta (Abeta) senile plaques in aging and Alzheimer disease, but it is unknown whether PrP is directly involved in plaque formation or represents a reaction to amyloid deposition. To evaluate possible functional effects of PrP in Abeta plaque formation, we analyzed bigenic mice (TgCRND8/Tg7), carrying ...
Katja, Schwarze-Eicker   +5 more
openaire   +2 more sources

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