Nix, "Crystal structure at 2.8 A˚ of the DLLRKN-containing coiled-coil domain of Huntingtin-interacting protein 1 (HIP1) reveals a surface suitable for clathrin light chain binding," Journal of Molecular Biology, vol. 367, no. 1, pp. 8-15, 2007....
The processes underlying formation and growth of unfolded protein inclusions are relevant to neurodegenerative diseases but poorly characterized in living cells. In S. cerevisiae, inclusions formed by mutant huntingtin (mHtt) have some characteristics of
ENSMUSG00000027102 Hoxd8 95.0 1.30E − 07 protein_coding ENSMUSG00000027833 Shox2 58.8 6.18E − 08 protein_coding ENSMUSG00000054667 Irs4 37.1 1.39E − 05 protein_coding ENSMUSG00000078302 Foxd1 35.8 2.30E − 06 protein_coding ENSMUSG00000028825 Rhd 33.3 2.80E − 04 protein_coding ENSMUSG...
The crystal structures of the PP2A PR65/A subunit and β-importin show these proteins to be composed almost entirely of 15 and 19 HEAT repeats, respectively, which form a flexible solenoid-like structure as they cooperate to mediate a number of different protein-protein interactions central to ...
The latter required using the fewest possible amino acid changes, relative to the host organism protein scaffold (in this case, the mouse zinc finger domain, Zif268). The design changes we introduced were sufficient to reduce neuronal cell loss, making the gene therapy construct less toxic than...
We present the crystal structure and biophysical characterization of a human VL [variable domain immunoglobulin (Ig) light chain] single-domain intrabody that binds to the huntingtin (Htt) protein and has been engineered for antigen recognition in the absence of its intradomain disulfide bond, ...
Crystal structure of the human, FIC-domain containing protein HYPE and implications for its functions. Structure 2014, 22, 1831–1843. [Google Scholar] [CrossRef] [Green Version] Goehler, H.; Lalowski, M.; Stelzl, U.; Waelter, S.; Stroedicke, M.; Worm, U.; Droege, A.; ...