Rudi Glockshuber

TL;DR: The nuclear magnetic resonance (NMR) structure of the autonomously folding PrP domain contains most of the point-mutation sites that have been linked, in human PrP, to the occurrence of familial prion diseases, and shows that these mutations occur within, or directly adjacent to, regular secondary structures.

TL;DR: The recombinant murine prion protein, mPrP(23-231), was expressed in E. coli with uniform 15N-labeling and NMR experiments showed that the previously determined globular three-dimensional structure of the C-terminal domain mPrp(121-231) is preserved in the intact protein, and that the Nterminal polypeptide segment 23-120 is flexibly disordered as mentioned in this paper, based on nearly complete sequence-specific assignments for the backbone amide nitrogens, amide protons and alpha-protols of

TL;DR: A monoclonal antibody is described, 15B3, that can discriminate between the normal and disease-specific forms of PrP, suggesting that it recognizes an epitope common to prions from different species.

TL;DR: Three different strategies on the Fv-fragment of the well-characterized phosphocholine binding antibody McPC603 expressed and secreted in Escherichia coli are tested: chemical cross-linking of the variable domains, introduction of an intermolecular disulfide bond, and construction of a peptide linker to produce a "single-chain" Fv

TL;DR: The results indicate that the structurally related uroplakins Ia and Ib are glycosylated differently, that Uroplakin Ia serves as the urothelial receptor for the type 1-fimbriated E. coli, and that the binding of uropathogenic bacteria to uroPlakin IA may play a key role in mediating the u rothelial responses to bacterial attachment.