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"Any protein that interacts with PrP is likely to be interesting," says cell biologist David Harris of Washington University in St . Louis because it may be involved in both the protein's normal function as well as the disease-causing conversion.
The conversion of the host encoded prion protein (PrPC) into the disease causing isoform PrPSc is the key molecular event in prion disease.
Treat the disease causing the jaundice.
Channel catfish exhibits superior growth, feed conversion efficiency, resistance to the bacterial disease caused by Flavobacterium columnare, and tolerance to low oxygen.
Protozoal disease, disease caused by protozoans.
Strokes and other diseases cause the remainder.
The disease can cause great harm.
When I asked what had caused his conversion, Pastor Sidney looked away.
Formation of the PrP−nucleic acid complex seems to accelerate the conversion of the cellular form of the protein into the disease-causing isoform.
Thus, they are responsible for creating genetic variation but also might be the reason for creation disease-causing mutations within the human genome (i.e., insertional mutagenesis, recombination, retrotransposition-mediated and gene conversion-mediated deletion, and 3′ transduction).
Now it is well known that prion diseases are caused in part (or at least accompanied by) the conversion of the prion protein PrP from its normal form PrPC to a conformationally distinct version PrPSc and that the latter can autocatalyse this conversion (Aguzzi and Heikenwälder 2006; Aguzzi et al. 2008b; Prusiner 1998, 2001; Tamgüney et al. 2008; Watts and Westaway 2007).
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com