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Literature summary for 3.4.21.64 extracted from

  • Cronier, S.; Gros, N.; Tattum, M.H.; Jackson, G.S.; Clarke, A.R.; Collinge, J.; Wadsworth, J.D.
    Detection and characterization of proteinase K-sensitive disease-related prion protein with thermolysin (2008), Biochem. J., 416, 297-305.
    View publication on PubMedView publication on EuropePMC
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Application

Application Comment Organism
pharmacology In human variant Creutzfeldt–Jakob disease, up to 90% of total prion protein present in the brain resists degradation with thermolysin, whereas only ?15% of this material resists digestion by proteinase K. Detection of proteinase K-sensitive isoforms of disease-related prion protein using thermolysin should be useful for improving diagnostic sensitivity in human prion diseases Parengyodontium album

Organism

Organism UniProt Comment Textmining
Parengyodontium album
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Source Tissue

Source Tissue Comment Organism Textmining
commercial preparation
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 Parengyodontium album
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
prion protein + H2O for mouse RML prions, the majority of proteinase K-sensitive disease-related prion protein isoforms do not appear to contribute significantly to infectivity. In human variant Creutzfeldt-Jakob disease, up to 90% of total prion protein present in the brain resists degradation with thermolysin, whereas only 15% of this material resists digestion by proteinase K Parengyodontium album ?
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