43 research outputs found

    Sauraja Pattojo: Private House of Queen of Ke-Datu-an Pattojo XII

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    Pattojo is a small kingdom in the past, and at this time, Pattojo was called village of Pattojo. The Kingdom of Pattojo is also called ke-datu-an Pattojo whose the king or queen was called datu. To be a king or queen, one must of the highest Nobel or Datu title. Bugis house is identical to the stilt on the house and the rectangular facet is elongated. The house's mention in the bugis tribe has a difference between the noble house and the ordinary people's house. The noble house is called saoraja (Sao=house, raja=big so that saoraja is a big house), and the people's house is called the bola. Generally, noble houses in ancient times were larger than ordinary people's houses. This research is a study on the form of Bugis noble house or king's private house (saoraja datu pattojo: local language) built before Indonesia's independence. The form of façade the arrangement of space in the house has nothing in common with the original Bugis house. It may indicate that the king's house did not follow the original form of Bugis house but has combined between the Bugis and European architecture. Some things that are very clearly undergoing a change from the original of Bugis house is the roof, position of the stairs, there is an arc shape on the underside of the house, and the arrangement of the room has also undergone changes. Beside that, the thing that is very clear also is the tamping position that has shifted from its function as a connection between the inner space of the house and then switching positions in front of the main house. This research is qualitative research using method literature studies and field surveys. Keywords: Sauraja Pattojo, room plan, façad

    UniHI 4: new tools for query, analysis and visualization of the human protein–protein interactome

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    Human protein interaction maps have become important tools of biomedical research for the elucidation of molecular mechanisms and the identification of new modulators of disease processes. The Unified Human Interactome database (UniHI, http://www.unihi.org) provides researchers with a comprehensive platform to query and access human protein–protein interaction (PPI) data. Since its first release, UniHI has considerably increased in size. The latest update of UniHI includes over 250 000 interactions between ∼22 300 unique proteins collected from 14 major PPI sources. However, this wealth of data also poses new challenges for researchers due to the complexity of interaction networks retrieved from the database. We therefore developed several new tools to query, analyze and visualize human PPI networks. Most importantly, UniHI allows now the construction of tissue-specific interaction networks and focused querying of canonical pathways. This will enable researchers to target their analysis and to prioritize candidate proteins for follow-up studies

    UniHI: an entry gate to the human protein interactome

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    Systematic mapping of protein–protein interactions has become a central task of functional genomics. To map the human interactome, several strategies have recently been pursued. The generated interaction datasets are valuable resources for scientists in biology and medicine. However, comparison reveals limited overlap between different interaction networks. This divergence obstructs usability, as researchers have to interrogate numerous heterogeneous datasets to identify potential interaction partners for proteins of interest. To facilitate direct access through a single entry gate, we have started to integrate currently available human protein interaction data in an easily accessible online database. It is called UniHI (Unified Human Interactome) and is available at . At present, it is based on 10 major interaction maps derived by computational and experimental methods. It includes more than 150 000 distinct interactions between more than 17 000 unique human proteins. UniHI provides researchers with a flexible integrated tool for finding and using comprehensive information about the human interactome

    HIPPIE: Integrating Protein Interaction Networks with Experiment Based Quality Scores

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    Protein function is often modulated by protein-protein interactions (PPIs) and therefore defining the partners of a protein helps to understand its activity. PPIs can be detected through different experimental approaches and are collected in several expert curated databases. These databases are used by researchers interested in examining detailed information on particular proteins. In many analyses the reliability of the characterization of the interactions becomes important and it might be necessary to select sets of PPIs of different confidence levels. To this goal, we generated HIPPIE (Human Integrated Protein-Protein Interaction rEference), a human PPI dataset with a normalized scoring scheme that integrates multiple experimental PPI datasets. HIPPIE's scoring scheme has been optimized by human experts and a computer algorithm to reflect the amount and quality of evidence for a given PPI and we show that these scores correlate to the quality of the experimental characterization. The HIPPIE web tool (available at http://cbdm.mdc-berlin.de/tools/hippie) allows researchers to do network analyses focused on likely true PPI sets by generating subnetworks around proteins of interest at a specified confidence level

    Functional Implications of Novel Human Acid Sphingomyelinase Splice Variants

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    BACKGROUND: Acid sphingomyelinase (ASM) hydrolyses sphingomyelin and generates the lipid messenger ceramide, which mediates a variety of stress-related cellular processes. The pathological effects of dysregulated ASM activity are evident in several human diseases and indicate an important functional role for ASM regulation. We investigated alternative splicing as a possible mechanism for regulating cellular ASM activity. METHODOLOGY/PRINCIPAL FINDINGS: We identified three novel ASM splice variants in human cells, termed ASM-5, -6 and -7, which lack portions of the catalytic- and/or carboxy-terminal domains in comparison to full-length ASM-1. Differential expression patterns in primary blood cells indicated that ASM splicing might be subject to regulatory processes. The newly identified ASM splice variants were catalytically inactive in biochemical in vitro assays, but they decreased the relative cellular ceramide content in overexpression studies and exerted a dominant-negative effect on ASM activity in physiological cell models. CONCLUSIONS/SIGNIFICANCE: These findings indicate that alternative splicing of ASM is of functional significance for the cellular stress response, possibly representing a mechanism for maintaining constant levels of cellular ASM enzyme activity
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