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 A117V 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 A117V in PRIO_MOUSE

Point mutation:	A117V
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 117 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 118 in Mammalian prion proteins family Position 118 in Prion proteins (PRP, PRNP) family
Reference:	A pathogenic PrP mutation and doppel interfere with polarized sorting of the prion protein. Uelhoff A, Tatzelt J, Aguzzi A, Winklhofer KF, Haass C J Biol Chem 2005 Feb 18;280(7):5137-40. Epub 2004 Dec 21.	Medline
Other point mutations / same article	List
Text source	HTML full text
Validation status	Not yet checked

Relevant sentences:

A117V

For instance , mutations in the hydrophobic domain (HD) 1 of PrP , like A117V and AV3 (alanines at positions 112 , 114 , and 117 replaced by valines) lead to an aberrant folding of PrP during import into the endoplasmic reticulum (ER) and induce neurodegeneration in transgenic animals (5 )
Two mutations , A117V and AV3 (alanine residues at positions 112 , 114 , and 117 replaced by valines) (Fig. 3A ) , are linked to prion diseases in humans and transgenic mice , respectively (5 )

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