• Title/Summary/Keyword: System Scaffolding

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Development of the Approximate Cost Estimating Model for PSC Box Girder Bridge based on the Breakdown of Standard Work (대표공종 기반의 PSC Box 교량 상부공사 개략공사비 산정모델에 관한 연구)

  • Kim, Sang-Bum;Cho, Ji-Hoon
    • KSCE Journal of Civil and Environmental Engineering Research
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    • v.33 no.2
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    • pp.791-800
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    • 2013
  • Needs for developing a better way of cost estimating process for public construction projects have been widely recognized. Those needs are mainly from the early phases of the project through the construction life cycle due to the its importance to the control process. In contrast to the traditional estimating method based on unit-price references, this research utilized this following process. The first step is analyzing the real cost data from actual cost activities (2000~2010) about the statement of P.S.C(Prestressed Concrete) Box Girder Bridge. The collected data was broken into four categories based on technical construction methods such as I.L.M(Incremental Launching Method), M.S.S(Movable Scaffolding System), F.S.M(Full Staging Method), and F.C.M(Free Cantilever Method). The second, actual design documents including the actual cost estimating documents, drawings and specifications were carefully reviewed to cluster the cost itemized statement from four categories. It was also attempted to seek the proper breakdown of standard works that are responsible for more than 95 percentage in each categories in terms of its cost. The third, this research comes up the index for standard unit materials and unit price of standard work and develops the approximate estimating model applying for the specification(length and breadth of bridges) per square area that the user takes as well as suggests the practical application plan within the original time alloted.

Construction Methodology for Chum-Sung-Dae Validation through the Present Configuration (첨성대 건립에 대한 시공방법론 첨성대의 얼개를 통한 논증)

  • Kim, Jang Hoon;Park, Sang Hun
    • Korean Journal of Heritage: History & Science
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    • v.42 no.2
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    • pp.40-61
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    • 2009
  • A new construction methodology has been proposed on a scientific basis to reason a rational explanation for the structure and the present configuration of Chum-Sung-Dae. This is because there is no way to otherwise explain the gap between our expectation that the people in Shilla are assumed to be and the problems, such as the use of a temporary supporting structure including falsework, the use of a conveying device for stonework and the practice of soil fill, raised when the construction method in nowadays is applied to the structure. Furthermore, it is because the questions, such as the difference of an azimuth angle between the southward opening and the square podium, the skewed circular plan in layers of the body, misalignment between neighboring layers of the body, disagreement between the inclination due to slight sidesway and the eccentricity in each layer of the circular body, perfectly aligned vertical and horizontal joints and the existence of soil fill, raised from the present configuration of Chum-Sung-Dae, also require a reasonable explanation based on scientific evidences, if any. Therefore, the proposed new construction methodology, in which the soil hill outside as well as the soil fill inside the Chum-Sung-Dae may have been utilized as a temporary scaffolding system for construction, is the highly probable one that the builders of Chum-Sung-Dae might have inevitably employed. The existence of great tombs, scattered in Hwang-Nam-Dong close to Chum-Sung-Dae, implies that the people of Shilla might have accepted the proposed new construction methodology as a natural one.

Developement and Application of Patent Technology for the Improvement of Scaffolding Safety Facilities in Small-scale Muliti-Family Housing System for the Prevention of Severe Disasters (중대재해 예방을 위한 소규모 공동주택 시스템비계 안전시설물 개선 특허기술 개발 및 활용)

  • Kim, Sung Soo
    • Journal of Korean Society of Disaster and Security
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    • v.15 no.3
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    • pp.57-66
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    • 2022
  • According to the official letter of the Ministry of Employment and Labor (recent guidance on the status of deaths in the construction industry and thorough safety management, April 4, 2022), 17 deaths occurred in construction works worth more than 5 billion won until March 31, 2022. In terms of the size of the construction, 7 cases of 5 billion won to 12 billion won, 5 cases of 12 billion won to 80 billion won, and 5 cases of more than 80 billion won occurred. The causes of death accidents were found to be nine cases (50%), five cases (28%), two cases of collapse (11%), one case of entrapment (5%), and one case of drowning (5%). Safety facilities need to be strengthened to reduce deaths caused by falling, which accounts for most of the deaths, and if fall prevention nets, openings, and safety rails are completely installed, most falling accidents can be prevented. Therefore, this paper intends to present cases of development and use of patent technology through improvement of safety facilities in order to prevent accidents corresponding to the fall of new urban living housing sites, which are small apartment houses.

Cadms/SynCAMs/Necls/TSLCs Interact with Multi-PDZ Domain Protein MUPP1 (Cadms/SynCAMs/Necls/TSLCs와 multi-PDZ domain protein MUPP1 단백질의 결합)

  • Jang, Won Hee;Jeong, Young Joo;Choi, Sun Hee;Kim, Sang-Jin;Urm, Sang-Hwa;Moon, Il Soo;Seog, Dae-Hyun
    • Journal of Life Science
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    • v.24 no.12
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    • pp.1276-1283
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    • 2014
  • Cell adhesion molecules determine the cell-cell binding and the interactions between cells and extracellular signals. Cell-cell junctional complexes, which maintain the structural integrity of tissues, consist of more than 50 proteins including multi-PDZ domain protein 1 (MUPP1). MUPP1 contains 13 postsynaptic density-95/disks large/zonula occludens-1 (PDZ) domains and serves a scaffolding function for transmembrane proteins and cytoskeletal proteins or signaling proteins, but the mechanism how MUPP1 links and stabilizes the juxtamembrane proteins has not yet been elucidated. We used the yeast two-hybrid system to identify proteins that interact with PDZ domains of MUPP1. We found an interaction between MUPP1 and cell adhesion molecule 1 (Cadm1, also known as SynCAM1, Necl-2, or TSLC1). Cadm1 bound to the second PDZ domain of MUPP1. The carboxyl (C)-terminal end of Cadm1 has a type II PDZ-association motif (-Y-F-I) which was essential for the interaction with MUPP1 in the yeast two-hybrid assay. MUPP1 also bound to the C-terminal cytoplasmic tail region of other Cadm family members (Cadm2, Cadm3, and Cadm4). In addition, these protein-protein interactions were observed in the glutathione S-transferase (GST) pull-down assay and by co-immunoprecipitation. Anti-MUPP1 antibody co-immunoprecipitated Cadm1 and Cadm4 with MUPP1 from mouse brain extracts. These results suggest that MUPP1 could mediate interaction between Cadms and cytoskeletal proteins.

Muskelin Interacts with Multi-PDZ Domain Protein 1 (MUPP1) through the PDZ Domain (Muskelin과 multi-PDZ domain protein 1 (MUPP1) 단백질의 PDZ 도메인을 통한 결합)

  • Jang, Won Hee;Jeong, Young Joo;Choi, Sun Hee;Lee, Won Hee;Kim, Mooseong;Kim, Sang-Jin;Urm, Sang-Hwa;Moon, Il Soo;Seog, Dae-Hyun
    • Journal of Life Science
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    • v.25 no.5
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    • pp.594-600
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    • 2015
  • Protein-protein interactions have a critical role in the regulation of many cellular functions. Postsynaptic density-95/disks large/zonula occludens-1 (PDZ) domain is one of domains that mediate protein-protein interactions. PDZ domains typically bind to the specific motif at the carboxyl (C)-terminal end of partner proteins. Multi-PDZ domain protein 1 (MUPP1), which has 13 PDZ domains, serves a scaffolding function for structure proteins and signaling proteins, but the cellular function of MUPP1 has not been fully elucidated. We used the yeast two-hybrid system to identify proteins that interact with PDZ domains of MUPP1. We found an interaction between MUPP1 and muskelin. Muskelin was recently identified as a GABAA receptor (GABAAR) α1 subunit binding protein and known to have a role in receptor endocytosis and degradation. Muskelin bound to the 3rd PDZ domain, but not to other PDZ domains of MUPP1. The C-terminal end of muskelin was essential for the interaction with MUPP1 in the yeast two-hybrid assay. When co-expressed in HEK-293T cells, muskelin but not the C-terminal deleted muskelin was co-immunoprecipitated with MUPP1. In addition, MUPP1 co-localized with muskelin at the same subcellular region in cells. These findings collectively suggest that MUPP1 or its interacting proteins could modulate GABAAR trafficking and turnover through the interaction with muskelin.

Parkin Interacts with the PDZ Domain of Multi-PDZ Domain Protein MUPP1 (Parkin과 Multi-PDZ Domain Protein (MUPP1) 단백질 간의 PDZ 결합)

  • Jang, Won Hee;Jeong, Young Joo;Choi, Sun Hee;Lee, Won Hee;Kim, Mooseong;Kim, Sang-Jin;Urm, Sang-Hwa;Moon, Il Soo;Seog, Dae-Hyun
    • Journal of Life Science
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    • v.24 no.8
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    • pp.820-826
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    • 2014
  • The localization to specific subcellular sites and the regulation of cell surface receptors and channels are crucial for proper functioning. Postsynaptic density-95/Disks large/Zonula occludens-1 (PDZ)-domain is involved in recognition of and interaction between various proteins, by which the localization and the regulation are mediated. Multi-PDZ domain protein 1 (MUPP1) contains 13 PDZ domains. MUPP1 serves a scaffolding function for structure proteins and signaling proteins, but the mechanism how MUPP1 is stabilized and signalized has not yet been elucidated. We used the yeast two-hybrid system to identify proteins that interact with PDZ domains of MUPP1. We found an interaction between MUPP1 and Parkin. Parkin is an E3 ubiquitin ligase. Loss-of-function mutations of Parkin gene are known to cause an autosomal recessive juvenile parkinsonism. Parkin bound to the $12^{th}$ PDZ domain, but not to other PDZ domains of MUPP1. The C-terminal end of Parkin has a type II PDZ-association motif, which was essential for the interaction with MUPP1 in the yeast two-hybrid assay. When co-expressed in HEK-293T cells, Parkin co-localized with MUPP1. When co-expressed with ubiquitin in HEK-293T cells, MUPP1 has been strongly ubiquitinated by Parkin. These findings collectively suggest that MUPP1 is a novel substrate of Parkin and its function or stability could be modulated by Parkin-mediated ubiquitination.