Zobrazeno 1 - 4
of 4
pro vyhledávání: '"Johannes Stöckel"'
Publikováno v:
Biochemistry. 37:7185-7193
The infectious isoform of the prion protein (PrPSc) is derived from cellular PrP (PrPC) in a conversion reaction involving a dramatic reorganization of secondary and tertiary structure. While our understanding of the pathogenic role of PrPSc has grow
Publikováno v:
European Journal of Biochemistry. 248:684-691
We investigated the mechanism of refolding and reassembly of recombinant alpha and beta chains of the class II major histocompatibility molecules (MHC-II) HLA-DRB5*0101. Both chains were expressed in the cytosol of Escherichia coli, purified in urea
Autor:
Fred E. Cohen, Ingrid Mehlhorn, Darlene Groth, Michael A. Baldwin, Hong Zhang, Johannes Stöckel, Thomas L. James, Stanley B. Prusiner
Publikováno v:
Biochemistry. 36:3543-3553
PrP(Sc) is known to be the major, if not the only, component of the infectious prion. Limited proteolysis of PrP(Sc) produces an N-terminally truncated polypeptide of about 142 residues, designated PrP 27-30. Recently, a recombinant protein (rPrP) of
Autor:
D Reilly, Michael A. Baldwin, D Yansura, Darlene Groth, Fred E. Cohen, Robert J. Fletterick, W S Willett, R Vandlen, Ingrid Mehlhorn, D Henner, B Moffat, Johannes Stöckel, Stanley B. Prusiner
Publikováno v:
Biochemistry. 35(17)
The major, and possible only, component of the infectious prion is the scrapie prion protein (PrPSc); the protease resistant core of PrPSc is PrP 27-30, a protein of approximately 142 amino acids. PrPSc is derived from the cellular PrP isoform (PrPC)