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Title: Effect of enzymatic deimination on the conformation of recombinant prion protein
Authors: Young, Duncan S
Meersman, Filip
Oxley, David
Webster, Judith
Gill, Andrew C
Bronstein, Igor
Lowe, Christopher R
Dear, Denise V # ×
Issue Date: Aug-2009
Publisher: Elsevier science bv
Series Title: Biochimica et biophysica acta-proteins and proteomics vol:1794 issue:8 pages:1123-1133
Abstract: Deimination is the post-translational conversion of arginine residues to citrulline. It has been implicated as a causative factor in autoimmune diseases such as multiple sclerosis and rheumatoid arthritis and more recently, as a marker of neurodegeneration. We have investigated the effect of the post-translational modification of arginine residues on the structure of recombinant ovine prion protein. Deiminated prion protein exhibited biophysical properties characteristic of the scrapie-associated conformer of prion protein viz. an increased P-sheet secondary structure, congophilic structures indicative of amyloid and proteinase K resistance which could be templated onto normal unmodified prion protein. in the light of these findings, a potential role of post-translational modifications to prion protein in disease initiation or propagation is discussed. (C) 2009 Elsevier B.V. All rights reserved.
URI: 
ISSN: 1570-9639
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Molecular Imaging and Photonics
× corresponding author
# (joint) last author

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