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The changing forest disturbance regimes emphasize the need for improved damage risk information. Here, our aim was to (1) improve the current understanding of snow damage risks by assessing the importance of abiotic factors, particularly the modelled snow load on trees, versus forest properties in predicting the probability of snow damage, (2) produce a snow damage probability map for Finland. We also compared the results for winters with typical snow load conditions and a winter with exceptionally heavy snow loads. To do this, we used damage observations from the Finnish national forest inventory (NFI) to create a statistical snow damage occurrence model, spatial data layers from different sources to use the model to predict the damage probability for the whole country in 16 x 16 m resolution. Snow damage reports from forest owners were used for testing the final map. Our results showed that best results were obtained when both abiotic and forest variables were included in the model. However, in the case of the high snow load winter, the model with only abiotic predictors performed nearly as well as the full model and the ability of the models to identify the snow damaged stands was higher than in other years. The results showed patterns of forest adaptation to high snow loads, as spruce stands in the north were less susceptible to damage than in southern areas and long-term snow load reduced the damage probability. The model and the derived wall-to-wall map were able to discriminate damage from no-damage cases on a good level (AUC > 0.7). The damage probability mapping approach identifies the drivers of snow disturbances across forest landscapes and can be used to spatially estimate the current and future disturbance probabilities in forests, informing practical forestry and decision-making and supporting the adaptation to the changing disturbance regimes., Competing Interests: The authors have declared that no competing interests exist.

Background: Spinal fusion surgery causes severe pain. Strong opioids, commonly used as postoperative analgesics, may have unwanted side effects. S-ketamine may be an effective analgesic adjuvant in opioid patient-controlled analgesia (PCA). However, the optimal adjunct S-ketamine dose to reduce postoperative opioid consumption is still unknown., Methods: We randomized 107 patients at two tertiary hospitals in a double-blinded, placebo-controlled clinical trial of adults undergoing major lumbar spinal fusion surgery. Patients were randomly allocated to four groups in order to compare the effects of three different doses of adjunct S-ketamine (0.25, 0.5, and 0.75 mg ml-1) or placebo on postoperative analgesia in oxycodone PCA. Study drugs were administered for 24 hours postoperative after which oxycodone-PCA was continued for further 48 hours. Our primary outcome was cumulative oxycodone consumption at 24 hours after surgery., Results: Of the 100 patients analyzed, patients receiving 0.75 mg ml-1 S-ketamine in oxycodone PCA needed 25% less oxycodone at 24 h postoperatively (61.2 mg) compared with patients receiving 0.5 mg ml-1 (74.7 mg) or 0.25 mg ml-1 (74.1 mg) S-ketamine in oxycodone or oxycodone alone (81.9 mg) (mean difference: -20.6 mg; 95% confidence interval [CI]: -41 to -0.20; P = 0.048). A beneficial effect in mean change of pain intensity at rest was seen in the group receiving 0.75 mg ml-1 S-ketamine in oxycodone PCA compared with patients receiving lower ketamine doses or oxycodone alone (standardized effect size: 0.17, 95% CI: 0.013-0.32, P = 0.033). The occurrence of adverse events was similar among the groups., Conclusions: Oxycodone PCA containing S-ketamine as an adjunct at a ratio of 1: 0.75 decreased cumulative oxycodone consumption at 24 h after major lumbar spinal fusion surgery without additional adverse effects., Competing Interests: The authors have declared that no competing interests exist.

Most glycosyltransferases, including B4GalT1 (EC 2.4.1.38), are known to assemble into enzyme homomers and functionally relevant heteromers in vivo. However, it remains unclear why and how these enzymes interact at the molecular/atomic level. Here, we solved the crystal structure of the wild-type human B4GalT1 homodimer. We also show that B4GalT1 exists in a dynamic equilibrium between monomer and dimer, since a purified monomer reappears as a mixture of both and as we obtained crystal forms of the monomer and dimer assemblies in the same crystallization conditions. These two crystal forms revealed the unliganded B4GalT1 in both the open and the closed conformation of the Trp loop and the lid regions, responsible for donor and acceptor substrate binding, respectively. The present structures also show the lid region in full in an open conformation, as well as a new conformation for the GlcNAc acceptor loop (residues 272-288). The physiological relevance of the homodimer in the crystal was validated by targeted mutagenesis studies coupled with FRET assays. These showed that changing key catalytic amino acids impaired homomer formation in vivo. The wild-type human B4GalT1 structure also explains why the variant proteins used for crystallization in earlier studies failed to reveal the homodimers described in this study., Competing Interests: The authors have declared that no competing interests exist.