6,563 research outputs found
Investigation of Visual Management Cases in Construction by an Analytical Framework from Manufacturing
Along with the progress of globalization, speed and efficiency have become more critical for any industry than ever before. In this sense, the concept and methods of lean management, promoting these performances, have been deployed from manufacturing, its origin industry, to other industries. This paper deals with this management style in the construction industry, called lean construction. In particular, visual management (VM) as one effective tool in this scheme is focused on. A number of VM cases, 306 in total, was collected from both construction and manufacturing sites and investigated by the so-called 5W1H analytical framework developed in the manufacturing industry. Obtained results suggest that the VM cases in construction have common attributes such as purpose and location, target to attain, users’ attributes, timing to use and elemental technologies for case development. A comparison analysis of the VM cases from construction and those from manufacturing was also carried out, for a mutual transfer of this technology between these industries
Inhibition of cellular protein secretion by norwalk virus nonstructural protein p22 requires a mimic of an endoplasmic reticulum export signal.
Protein trafficking between the endoplasmic reticulum (ER) and Golgi apparatus is central to cellular homeostasis. ER export signals are utilized by a subset of proteins to rapidly exit the ER by direct uptake into COPII vesicles for transport to the Golgi. Norwalk virus nonstructural protein p22 contains a YXΦESDG motif that mimics a di-acidic ER export signal in both sequence and function. However, unlike normal ER export signals, the ER export signal mimic of p22 is necessary for apparent inhibition of normal COPII vesicle trafficking, which leads to Golgi disassembly and antagonism of Golgi-dependent cellular protein secretion. This is the first reported function for p22. Disassembly of the Golgi apparatus was also observed in cells replicating Norwalk virus, which may contribute to pathogenesis by interfering with cellular processes that are dependent on an intact secretory pathway. These results indicate that the ER export signal mimic is critical to the antagonistic function of p22, shown herein to be a novel antagonist of ER/Golgi trafficking. This unique and well-conserved human norovirus motif is therefore an appealing target for antiviral drug development
Activity measurement of solid Cu-In alloys by EMF method with solid electrolyte
The thermodynamic activity of indium in the solid Cu-In alloys was obtained from the EMF measurement of cell: In,In2O3, ZrO2(+11mol%CaO), Cu-In,In2O3 for 16 alloys in the temperature range 773 to 900K. Activity changes with composition at 823K are very large in the and - phase regions. Activity and free energies of formation are derived and compared with the published data
Pressure-induced changes in the magnetic and valence state of EuFe2As2
We present the results of electrical resistivity, ac specific heat, magnetic
susceptibility, X-ray absorption spectroscopy (XAS) and X-ray magnetic circular
dichroism (XMCD) of the ternary iron arsenide EuFe2As2 single crystal under
pressure. Applying pressure leads to a continuous suppression of the
antiferromagnetism associated with Fe moments and the antiferromagnetic
transition temperature becomes zero in the vicinity of a critical pressure Pc
~2.5-2.7 GPa. Pressure-induced re-entrant superconductivity, which is highly
sensitive to the homogeneity of the pressure, only appears in the narrow
pressure region in the vicinity of Pc due to the competition between
superconductivity and the antiferromagnetic ordering of Eu2+ moments. The
antiferromagnetic state of Eu2+ moments changes to the ferromagnetic state
above 6 GPa. We also found that the ferromagnetic order is suppressed with
further increasing pressure, which is connected with a valence change of Eu
ions.Comment: 7 pages, 7 figures, accepted for publication in Phys. Rev.
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