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 D202N 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.
|General numbering (PrionDB):||-|
|Other point mutations / same protein / same position||Point mutations at position 202 in PRIO_HUMAN|
|Other point mutations / same protein||List of mutations in PRIO_HUMAN|
Mammalian prion proteins|
Prion proteins (PRP, PRNP)
|Other point mutations / same position||
Position 202 in Mammalian prion proteins family |
Position 202 in Prion proteins (PRP, PRNP) family
|Reference:||Identification of a conserved N-capping box important for the structural autonomy of the prion alpha 3-helix: the disease associated D202N mutation destabilizes the helical conformation.|
Gallo M, Paludi D, Cicero DO, Chiovitti K, Millo E, Salis A, Damonte G, Corsaro A, Thellung S, Schettini G, Melino S, Florio T, Paci M, Aceto A
Int J Immunopathol Pharmacol 2005 Jan-Mar;18(1):95-112.
|Other point mutations / same article||List|
|Validation status||Not yet checked|