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Force Plate Gait Analysis and Clinical Results after Tibial Plateau Levelling Osteotomy for Cranial Cruciate Ligament Rupture in Small Breed Dogs.

 The aim of this study was to evaluate objective limb function using force plate gait analysis after tibial plateau levelling osteotomy (TPLO) in small breed dogs with cranial cruciate ligament rupture (CCLR).

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Comparison of the ViOptix Intra.Ox Near Infrared Tissue Spectrometer and Indocyanine Green Angiography in a Porcine Bowel Model.

 This study aims to directly compare measurements of tissue oxygenation obtained using the Intra.Ox (Vioptix Inc., Fremont, CA) near infrared spectrometer with the perfusion assessment of the indocyanine green (ICG)-based SPY Elite imaging system (Stryker Co., Kalamazoo, MI) in a porcine bowel model.

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Near-Infrared In Vivo Whole-Body Fluorescence Imaging of PNA.

Using near-infrared fluorophore Alexa Fluor 680 labeled peptide nucleic acids (PNAs) the biodistribution of such antisense agents can be analyzed in real time in live mice using in vivo imaging. Using the fluorescence intensity emitted from the mouse at different time points following administration, the systemic distribution and organ accumulation of PNA can be tracked. In addition, an estimation of the body half-life of the compound can be obtained by the change in fluorescence intensity over time. With this technique, the distribution of compounds can be monitored real time, while reducing the number of animals and amount of compounds required.

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A mutation near the active site of S-RNase causes self-compatibility in S-RNase-based self-incompatible plants.

The structurally simplest amino acid glycine could make contribution to nuclease activity of S-RNase and self-incompatibility in S-RNase-based plants. S-RNase is regarded as inhibitor of self-pollen tube in S-RNase-based self-incompatibility plants. Certain residues like histidine are necessary for RNase activity and self-incompatibility; however, it is unknown whether any other residues contribute to this. Previously, we identified an association between the self-compatible Chinese pear (Pyrus × bretschneideri) cultivar 'Yanzhuang' (YZ) and a mutation causing a residue shift (glycine-to-valine) in the 2nd conserved region (C2) of S-RNase; however, it was unclear how this nonpolar aliphatic amino acid substitution caused self-compatibility. In this study, we observed that 'YZ' offspring were self-compatible when S-RNases were all mutated. In vitro pollen tube (SS) growth was not completely arrested by the mutated S-RNase. Residue frequency analysis showed that the glycine residue is highly conserved in diverse S-RNases across many plant species. We therefore generated a mutated petunia S'-RNase (glycine to valine) and transformed it into SS petunia. The transformed pistil could not inhibit S pollen tubes. Three-dimensional protein prediction suggested that the glycine-to-valine mutation alters the spatial structure near the active site, and RNase activity of mutated S-RNase was reducing. Thus, the glycine residue in the C2 is essential for RNase activity, substitution of this residue leads to a failure of self-incompatibility.

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