LATTE: Latent Type Modeling for Biomedical Entity Linking

Entity linking is the task of linking mentions of named entities in natural language text, to entities in a curated knowledge-base. This is of significant importance in the biomedical domain, where it could be used to semantically annotate a large volume of clinical records and biomedical literature, to standardized concepts described in an ontology such as Unified Medical Language System (UMLS). We observe that with precise type information, entity disambiguation becomes a straightforward task. However, fine-grained type information is usually not available in biomedical domain. Thus, we propose LATTE, a LATent Type Entity Linking model, that improves entity linking by modeling the latent fine-grained type information about mentions and entities. Unlike previous methods that perform entity linking directly between the mentions and the entities, LATTE jointly does entity disambiguation, and latent fine-grained type learning, without direct supervision. We evaluate our model on two biomedical datasets: MedMentions, a large scale public dataset annotated with UMLS concepts, and a de-identified corpus of dictated doctor's notes that has been annotated with ICD concepts. Extensive experimental evaluation shows our model achieves significant performance improvements over several state-of-the-art techniques.

Design of Injection Mould for the Mouse Shell with Two-Step Parting Mechanism

Theinjection mould was designed through process analysis of the mouse shell.According to its size and structural features, the mould adopted double-cavitymould with two-step mechanism, latent type point gate feeding, lateralcore-pulling mechanism with inclined guide pillar, internal core-pullingmechanism with diagonal handspike. The practice use proved that everymechanism of mould worked flexibly with safety and reliable operation, qualityof plastic partmeted the requirements.

Possible Actions of Metalloproteinases Found in Porcine Enamel in an Early Secretory Stage

In an outermost layer of porcine secretory enamel, metalloproteinases were detected by enzymography with gelatin used as a substrate. When the sample extracted from the outermost layer of the secretory enamel was incubated with calcium ions at 37°C prior to electrophoresis, an increase of the 34-kDa proteinase activity and a decrease of the 76- and/or 78-kDa proteinase activities were observed. The results suggest that the metalloproteinases mediate the conversion from 76- and/or 78-kDa proteinases to the 34-kDa proteinase or the activation of a latent type of the 34-kDa proteinase, and that their activities are regulated by free Ca ions.