Who Is Caring for the Caregiver? The Role of Cybercoping for Dementia Caregivers

The purpose of this study is to investigate the relationship between dementia caregivers’ communication behaviors (information seeking and forwarding) and their outcomes (coping outcomes: e.g., dealing better with negative feelings or improved medical outcomes). A survey data set of dementia patients’ caregivers substantiates the effects of communication behaviors about dementia illness on coping outcomes, as well as the mediating role of emotion-focused and problem-focused coping processes. Using structural equation modeling (SEM), this study found positive effects of communication behaviors on outcomes through coping processes. Further, the results indicate that communication behaviors in cyberspace are crucial for caregivers to cope with dementia, both affectively (improvement of caregivers’ emotional control) and physically (health improvement of patients). The implications for the improvement of public health through online health communication behaviors are discussed

Scale-free trees: the skeletons of complex networks

We investigate the properties of the spanning trees of various real-world and model networks. The spanning tree representing the communication kernel of the original network is determined by maximizing total weight of edges, whose weights are given by the edge betweenness centralities. We find that a scale-free tree and shortcuts organize a complex network. The spanning tree shows robust betweenness centrality distribution that was observed in scale-free tree models. It turns out that the shortcut distribution characterizes the properties of original network, such as the clustering coefficient and the classification of networks by the betweenness centrality distribution

Technical Efficiency in the Iron and Steel Industry: A Stochastic Frontier Approach

In this paper we examine the technical efficiency of firms in the iron and steel industry and try to identify the factors contributing to the industry's efficiency growth, using a time-varying stochastic frontier model. Based on our findings, which pertain to 52 iron and steel firms over the period of 1978-1997, POSCO and Nippon Steel were the most efficient firms, with their production, on average, exceeding 95 percent of their potential output. Our findings also shed light on possible sources of efficiency growth in the industry. If a firm is government-owned, its privatization is likely to improve its technical efficiency to a great extent. A firm's technical efficiency also tends to be positively related to its production level as measured by a share of the total world production of crude steel. Another important source of efficiency growth identified by our empirical findings is adoption of new technologies and equipment. Our findings clearly indicate that continued efforts to update technologies and equipment are critical in pursuit of efficiency in the iron and steel industry.

Low-voltage-driven soft actuators

Soft actuators based on electroactive polymers (EAPs) are the core constituents of future soft robots owing to their fascinating properties such as Lightweight, compactness, easy fabrication into various forms, and Low cost. Ionic EAP actuators are particularly attractive owing to the Low driving voltages (<3 V) as compared to those of electronic EAP actuators (usually kilovolts). This paper presents a brief overview of the recent progress in a range of EAP actuators by focusing on Low voltage operation, in addition to the challenges and future strategies for their wide applicability in artificial muscles and various innovative soft robot technologies.11Ysciescopu

Phosphorylation of α-syntrophin is responsible for its subcellular localization and interaction with dystrophin in muscle cells

79-85Syntrophin is a well-known adaptor protein that links intracellular proteins with the dystrophin-glycoprotein complex (DGC) at the sarcolemma. However, little is known about the underlying mechanism that regulates the intracellular localization of α-syntrophin and its interaction with dystrophin. In this study, we demonstrate that α-syntrophin phosphorylation determines its intracellular localization and interaction with dystrophin in muscle cells. α-Syntrophin, a predominant isoform in skeletal muscles, directly interacts with ion channels, enzymes, receptors, and DGC proteins. Despite α-syntrophin being a potential signaling molecule, most studies focus on its function as a dystrophin-associated protein. However, we previously reported that α-syntrophin has a variety of DGC-independent functions to modulate cell migration, differentiation, survival, and protein stability. According to the results of the in vitro phosphorylation assays using subcellular fractions, the phosphorylated α-syntrophin accumulated only at the plasma membrane, and this event occurred regardless of dystrophin expression. However, the α-syntrophin interacting with dystrophin at the membrane was not in a phosphorylated state. We also identified that protein kinase C (PKC) was involved in the phosphorylation of α-syntrophin, which restricted α-syntrophin to interact with dystrophin. In conclusion, we demonstrate that the phosphorylation of α-syntrophin by PKC regulates its intracellular localization and interaction with dystrophin

Phosphorylation of α-syntrophin is responsible for its subcellular localization and interaction with dystrophin in muscle cells

Syntrophin is a well-known adaptor protein that links intracellular proteins with the dystrophin-glycoprotein complex (DGC) at the sarcolemma. However, little is known about the underlying mechanism that regulates the intracellular localization of α-syntrophin and its interaction with dystrophin. In this study, we demonstrate that α-syntrophin phosphorylation determines its intracellular localization and interaction with dystrophin in muscle cells. α-Syntrophin, a predominant isoform in skeletal muscles, directly interacts with ion channels, enzymes, receptors, and DGC proteins. Despite α-syntrophin being a potential signaling molecule, most studies focus on its function as a dystrophin-associated protein. However, we previously reported that α-syntrophin has a variety of DGC-independent functions to modulate cell migration, differentiation, survival, and protein stability. According to the results of the in vitro phosphorylation assays using subcellular fractions, the phosphorylated α-syntrophin accumulated only at the plasma membrane, and this event occurred regardless of dystrophin expression. However, the α-syntrophin interacting with dystrophin at the membrane was not in a phosphorylated state. We also identified that protein kinase C (PKC) was involved in the phosphorylation of α-syntrophin, which restricted α-syntrophin to interact with dystrophin. In conclusion, we demonstrate that the phosphorylation of α-syntrophin by PKC regulates its intracellular localization and interaction with dystrophin