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Literature summary for 3.4.21.64 extracted from

  • Imamura, M.; Kato, N.; Okada, H.; Yoshioka, M.; Iwamaru, Y.; Shimizu, Y.; Mohri, S.; Yokoyama, T.; Murayama, Y.
    Insect cell-derived cofactors become fully functional after proteinase K and heat treatment for high-fidelity amplification of glycosylphosphatidylinositol-anchored recombinant scrapie and BSE prion proteins (2013), PLoS ONE, 8, e82538.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
recombinant expression of tagged cellular Bac-prion protein fusion in Spodoptera frugiperda SF21 insect cells via baculovirus transfection system Parengyodontium album

Organism

Organism UniProt Comment Textmining
Parengyodontium album P06873
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Purification (Commentary)

Purification (Comment) Organism
tagged cellular Bac-prion protein fusion partially 37fold from SF21 insect cells using immobilized metal ion affinity chromatography Parengyodontium album

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
normal cellular prion protein + H2O in mouse brain Parengyodontium album pathogenic cellular prion protein + ?
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?

Synonyms

Synonyms Comment Organism
Proteinase K
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Parengyodontium album

General Information

General Information Comment Organism
metabolism the central event in prion infection is the conformational conversion of host-encoded cellular prion protein into the pathogenic isoform. For the in vitro replication of pathogenic prion protein by protein-misfolding cyclic amplification, cofactors are required that are not produced by lower organism, e.g. insects, but by mammalia, e.g. C57BL/6J mice. Brain-derived factors are also necessary for the in vitro replication of glycosylphosphatidylinositol-anchored baculovirus-derived recombinant prion protein. Cofactor activity of insect cell lysates becomes functional after proteinase K digestion and heat treatment, following protease digestion and heat treatment, insect cell lysates had the functional cofactor activity required for Bac-prion protein replication by protein-misfolding cyclic amplification. Not only RNA, but also DNA, are the key components of protein-misfolding cyclic amplification, although other cellular factors were necessary for the expression of the cofactor activity of nucleic acids in insect cells Parengyodontium album
additional information proteinase K-resistant Bac-prion protein is generated by protein-misfolding cyclic amplification using insect cells expressing the protein and prionprotein null mouse brain homogenate Parengyodontium album