PrionDB: Extraction of mutation data from the literature

2005, PrionDB.

This data was extracted from Medline abstracts and full texts (when available) in an automated manner.

The table below describes the selected point mutation and provides links to other documents. The sentence(s) where the point mutation T198N was found are listed after the table.

The mutated residues are also indicated in the family sequence alignments and hyperlinked to the corresponding mutation pages.

Point mutation T198N in PRIO_MOUSE

Point mutation:	T198N
Domain:	Not determined
General numbering (PrionDB):	-
Protein:	PRIO_MOUSE (Prnp,Prn-p)	Swiss-Prot Cross-reference table Family page
Other point mutations / same protein / same position	Point mutations at position 198 in PRIO_MOUSE
Other point mutations / same protein	List of mutations in PRIO_MOUSE
Family alignments	Mammalian prion proteins Prion proteins (PRP, PRNP)
Other point mutations / same position	Position 199 in Mammalian prion proteins family Position 199 in Prion proteins (PRP, PRNP) family
Reference:	Glycosylation deficiency at either one of the two glycan attachment sites of cellular prion protein preserves susceptibility to bovine spongiform encephalopathy and scrapie infections. Neuendorf E, Weber A, Saalmueller A, Schatzl H, Reifenberg K, Pfaff E, Groschup MH J Biol Chem 2004 Dec 17;279(51):53306-16. Epub 2004 Sep 23.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	True positive

Relevant sentences:

T198N

When looking at the total PrP res levels in the transduced ScN2a cells , with the exception of T182N / T198N , none of the glycosylation mutants lead to a stronger reduction of PrP res than the wild type 3F4PrP that was used as a control (Fig. 6b )
Note that mutants T182N and T198A PrP C lack the diglycosylated band , whereas mutant T182N / T198N PrP only displays unglycosylated PrP C

F.Horn (priondbcmbi.ru.nl), 22-Aug-2005