“p48ZnF is a C3H1 zinc finger domain-containing protein th

“p48ZnF is a C3H1 zinc finger domain-containing protein that is involved in the control of gene transcription and translation. In the present study a novel transgenic p48ZnF mouse model is described that is useful for in vivo brain imaging using luciferase as bioluminescence-mediating reporter gene. Yeast two-hybrid screening and western blot analyses revealed Drg1 (developmentally regulated GTP binding protein 1) and Pcbp1 (poly (rC)-binding protein 1) as p48ZnF-associated

proteins. Interestingly, p48ZnF’ cellular location of action depends on the cell’s differentiation status: nuclear in proliferating cells and cytoplasmic in differentiated neurons. (C) 2013 Elsevier Ireland Ltd. All rights reserved.”
“Calcium binding in proteins exhibits a wide range of polygonal geometries that relate directly to an equally

diverse set of biological functions. The binding process stabilizes protein structures and typically Everolimus research buy results in local conformational change and/or global restructuring of the backbone. Previously, we established the MUG program, which utilized multiple geometries in the Ca(2+)-binding pockets of holoproteins to identify such pockets, ignoring possible Ca(2+)-induced conformational change. In this article, we first report our progress in the analysis LY3039478 research buy of Ca(2+)-induced conformational changes followed by improved prediction of Ca(2+)-binding sites in the large group of Ca(2+)-binding proteins that exhibit only localized conformational changes. The MUG(SR) algorithm was devised to incorporate side chain torsional rotation as a predictor. The output from MUG(SR) presents groups of residues where each group, typically containing two to five residues, is a potential binding pocket. MUG(SR) was applied to both X-ray apo structures and NMR holo structures, which did not use calcium distance constraints in structure calculations. Predicted pockets were validated by comparison with homologous holo structures. Defining a “”correct hit”" as a group of residues containing Dehydratase at least two true ligand residues, the sensitivity was at least 90%; whereas for a “”correct hit”" defined as a group of residues containing at least three true

ligand residues, the sensitivity was at least 78%. These data suggest that Ca(2+)-binding pockets are at least partially prepositioned to chelate the ion in the apo form of the protein.”
“Excessive stretch of the cervical facet capsular ligament induces persistent pain and spinal plasticity at later time points. Yet, it is not known when such spinal modifications are initiated following this painful injury. This study investigates the development of hyperalgesia and neuronal hyperexcitability in the spinal cord after a facet joint injury. Behavioral sensitivity was measured in a model of painful C6/C7 facet joint injury in the rat, and neuronal hyperexcitability in the spinal cord was evaluated at 6 h and 1 day after injury or a sham procedure, in separate groups.

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