1,402 research outputs found

    GIS i de gymnasiale uddannelser

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    Kinect Depth Sensor Evaluation for Computer Vision Applications

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    This technical report describes our evaluation of the Kinect depth sensor by Microsoft for Computer Vision applications. The depth sensor is able to return images like an ordinary camera, but instead of color, each pixel value represents the distance to the point. As such, the sensor can be seen as a range- or 3D-camera. We have used the sensor in several different computer vision projects and this document collects our experiences with the sensor. We are only focusing on the depth sensing capabilities of the sensor since this is the real novelty of the product in relation to computer vision. The basic technique of the depth sensor is to emit an infrared light pattern (with an IR laser diode) and calculate depth from the reflection of the light at different positions (using a traditional IR sensitive camera). In this report, we perform an extensive evaluation of the depth sensor and investigate issues such as 3D resolution and precision, structural noise, multi-cam setups and transient response of the sensor. The purpose is to give the reader a well-founded background to choose whether or not the Kinect sensor is applicable to a specific problem

    Affinity proteomic dissection of the human nuclear cap-binding complex interactome

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    A 5',7-methylguanosine cap is a quintessential feature of RNA polymerase II-transcribed RNAs, and a textbook aspect of co-transcriptional RNA processing. The cap is bound by the cap-binding complex (CBC), canonically consisting of nuclear cap-binding proteins 1 and 2 (NCBP1/2). Interest in the CBC has recently renewed due to its participation in RNA-fate decisions via interactions with RNA productive factors as well as with adapters of the degradative RNA exosome. A novel cap-binding protein, NCBP3, was recently proposed to form an alternative CBC together with NCBP1, and to interact with the canonical CBC along with the protein SRRT. The theme of post-transcriptional RNA fate, and how it relates to co-transcriptional ribonucleoprotein assembly, is abundant with complicated, ambiguous, and likely incomplete models. In an effort to clarify the compositions of NCBP1-, 2- and 3-related macromolecular assemblies, we have applied an affinity capture-based interactome screen where the experimental design and data processing have been modified to quantitatively identify interactome differences between targets under a range of experimental conditions. This study generated a comprehensive view of NCBP-protein interactions in the ribonucleoprotein context and demonstrates the potential of our approach to benefit the interpretation of complex biological pathways
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