74 resultados para Language - Functional usage
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Sign language is the form of communication used by Deaf people, which, in most cases have been learned since childhood. The problem arises when a non-Deaf tries to contact with a Deaf. For example, when non-Deaf parents try to communicate with their Deaf child. In most cases, this situation tends to happen when the parents did not have time to properly learn sign language. This dissertation proposes the teaching of sign language through the usage of serious games. Currently, similar solutions to this proposal do exist, however, those solutions are scarce and limited. For this reason, the proposed solution is composed of a natural user interface that is intended to create a new concept on this field. The validation of this work, consisted on the implementation of a serious game prototype, which can be used as a source for learning (Portuguese) sign language. On this validation, it was first implemented a module responsible for recognizing sign language. This first stage, allowed the increase of interaction and the construction of an algorithm capable of accurately recognizing sign language. On a second stage of the validation, the proposal was studied so that the pros and cons can be determined and considered on future works.
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Dissertação apresentada na Faculdade de Ciências e Tecnologia da Universidade Nova de Lisboa para a obtenção do Grau de Mestre em Engenharia Informática.
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Dissertação apresentada na Faculdade de Ciências e Tecnologia da Universidade Nova de Lisboa para a obtenção do grau de Mestre em Engenharia Informática.
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Thesis submitted to the Universidade Nova de Lisboa,Faculdade de Ciências e Tecnologia for the degree of Doctor of Philosophy in Environmental Engineering
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Trabalho apresentado no âmbito do Mestrado em Engenharia Informática, como requisito parcial para obtenção do grau de Mestre em Engenharia Informática
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Dissertation submitted in partial fulfilment of the requirements for the Degree of Master of Science in Geospatial Technologies
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Dissertação apresentada na Faculdade de Ciências e Tecnologia da Universidade Nova de Lisboa para obtenção do grau de Mestre em Engenharia Informática
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Journal of Bacteriology (Apr 2006) 3024-3036
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Dissertação apresentada para obtenção do Grau de Doutor em Engenharia Química Pela Universidade Nova de Lisboa,Faculdade de Ciências e Tecn
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MSc. Dissertation presented at Faculdade de Ciências e Tecnologia of Universidade Nova de Lisboa to obtain the Master degree in Electrical and Computer Engineering
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Dissertation submitted in Faculdade de Ciências e Tecnologia of Universidade Nova de Lisboa for the degree of Master in Biomedical Engineering
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Trabalho apresentado no âmbito do Mestrado em Engenharia Informática, como requisito parcial para obtenção do grau de Mestre em Engenharia Informática
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Dissertation presented to obtain a PhD degree in Biochemistry at Instituto de Tecnologia Química e Biológica, Universidade Nova de Lisboa
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Dissertação apresentada na Faculdade de Ciências e Tecnologia da Universidade Nova de Lisboa para a obtenção do Grau de Mestre em Engenharia Informática
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The S100 proteins are 10-12 kDa EF-hand proteins that act as central regulators in a multitude of cellular processes including cell survival, proliferation, differentiation and motility. Consequently, many S100 proteins are implicated and display marked changes in their expression levels in many types of cancer, neurodegenerative disorders, inflammatory and autoimmune diseases. The structure and function of S100 proteins are modulated by metal ions via Ca2+ binding through EF-hand motifs and binding of Zn2+ and Cu2+ at additional sites, usually at the homodimer interfaces. Ca2+ binding modulates S100 conformational opening and thus promotes and affects the interaction with p53, the receptor for advanced glycation endproducts and Toll-like receptor 4, among many others. Structural plasticity also occurs at the quaternary level, where several S100 proteins self-assemble into multiple oligomeric states, many being functionally relevant. Recently, we have found that the S100A8/A9 proteins are involved in amyloidogenic processes in corpora amylacea of prostate cancer patients, and undergo metal-mediated amyloid oligomerization and fibrillation in vitro. Here we review the unique chemical and structural properties of S100 proteins that underlie the conformational changes resulting in their oligomerization upon metal ion binding and ultimately in functional control. The possibility that S100 proteins have intrinsic amyloid-forming capacity is also addressed, as well as the hypothesis that amyloid self-assemblies may, under particular physiological conditions, affect the S100 functions within the cellular milieu.