Smart Change in Strategy: IBM‘s Response to Challenging Times

International Business Machines, or IBM, has been an indisputable force in the communications industry, leading the world into the modern, global technological age. Currently, IBM has revamped its business paradigm, allocating the majority of its resources to consulting work and data analyses rather than manufacturing as it had done so in the past — for the primary objectives of optimizing existing assets, resolving problems of burgeoning cities and beleaguered governments, and enhancing peoples‘ lives in a sustainable way

Co-regularized Alignment for Unsupervised Domain Adaptation

Deep neural networks, trained with large amount of labeled data, can fail to generalize well when tested with examples from a \emph{target domain} whose distribution differs from the training data distribution, referred as the \emph{source domain}. It can be expensive or even infeasible to obtain required amount of labeled data in all possible domains. Unsupervised domain adaptation sets out to address this problem, aiming to learn a good predictive model for the target domain using labeled examples from the source domain but only unlabeled examples from the target domain. Domain alignment approaches this problem by matching the source and target feature distributions, and has been used as a key component in many state-of-the-art domain adaptation methods. However, matching the marginal feature distributions does not guarantee that the corresponding class conditional distributions will be aligned across the two domains. We propose co-regularized domain alignment for unsupervised domain adaptation, which constructs multiple diverse feature spaces and aligns source and target distributions in each of them individually, while encouraging that alignments agree with each other with regard to the class predictions on the unlabeled target examples. The proposed method is generic and can be used to improve any domain adaptation method which uses domain alignment. We instantiate it in the context of a recent state-of-the-art method and observe that it provides significant performance improvements on several domain adaptation benchmarks.Comment: NIPS 2018 accepted versio

Physiological responses of reared sea bream (Sparus aurata Linnaeus, 1758) to an Amyloodinium ocellatum outbreak

Amyloodiniosis represents a major bottleneck for semi-intensive aquaculture production in Southern Europe, causing extremely high mortalities. Amyloodinium ocellatum is a parasitic dinoflagellate that can infest almost all fish, crustacean and bivalves that live within its ecological range. Fish mortalities are usually attributed to anoxia, associated with serious gill hyperplasia, inflammation, haemorrhage and necrosis in heavy infestations; or with osmoregulatory impairment and secondary microbial infections due to severe epithelial damage in mild infestation. However, physiological information about the host responses to A.ocellatum infestation is scarce. In this work, we analysed the proteome of gilthead sea bream (Sparus aurata) plasma and relate it with haematological and immunological indicators, in order to enlighten the different physiological responses when exposed to an A.ocellatum outbreak. Using 2D-DIGE, immunological and haematological analysis and in response to the A.ocellatum contamination we have identified several proteins associated with acute-phase response, inflammation, lipid transport, homoeostasis, and osmoregulation, wound healing, neoplasia and iron transport. Overall, this preliminary study revealed that amyloodiniosis affects some fish functional pathways as revealed by the changes in the plasma proteome of S. aurata, and that the innate immunological system is not activated in the presence of the parasite.DIVERSIAQUA, Portugal [MAR2020]Fundacao para a Ciencia e Tecnologia [SFRH/BD/118601/2016]info:eu-repo/semantics/publishedVersio

The Drosophila Inhibitor of Apoptosis (IAP) DIAP2 Is Dispensable for Cell Survival, Required for the Innate Immune Response to Gram-negative Bacterial Infection, and Can Be Negatively Regulated by the Reaper/Hid/Grim Family of IAP-binding Apoptosis Inducers

Many inhibitor of apoptosis (IAP) family proteins inhibit apoptosis. IAPs contain N-terminal baculovirus IAP repeat domains and a C-terminal RING ubiquitin ligase domain. Drosophila IAP DIAP1 is essential for the survival of many cells, protecting them from apoptosis by inhibiting active caspases. Apoptosis initiates when proteins such as Reaper, Hid, and Grim bind a surface groove in DIAP1 baculovirus IAP repeat domains via an N-terminal IAP-binding motif. This evolutionarily conserved interaction disrupts DIAP1-caspase interactions, unleashing apoptosis-inducing caspase activity. A second Drosophila IAP, DIAP2, also binds Rpr and Hid and inhibits apoptosis in multiple contexts when overexpressed. However, due to a lack of mutants, little is known about the normal functions of DIAP2. We report the generation of diap2 null mutants. These flies are viable and show no defects in developmental or stress-induced apoptosis. Instead, DIAP2 is required for the innate immune response to Gram-negative bacterial infection. DIAP2 promotes cytoplasmic cleavage and nuclear translocation of the NF-{kappa}B homolog Relish, and this requires the DIAP2 RING domain. Increasing the genetic dose of diap2 results in an increased immune response, whereas expression of Rpr or Hid results in down-regulation of DIAP2 protein levels. Together these observations suggest that DIAP2 can regulate immune signaling in a dose-dependent manner, and this can be regulated by IBM-containing proteins. Therefore, diap2 may identify a point of convergence between apoptosis and immune signaling pathways