A new dynamic property of human consciousness

As pointed out by William James, "the consciousness is a dynamic process, not a thing" , during which short term integration is succeeded by another differentiated neural state through the continual interplay between the environment, the body, and the brain itself. Thus, the dynamic structure underlying successive states of the brain is important for understanding human consciousness as a process. In order to investigate the dynamic property of human consciousness, we developed a new method to reconstruct a state space from electroencephalogram(EEG), in which a trajectory, reflecting states of consciousness, is constructed based on the global information integration of the brain. EEGs were obtained from 14 subjects received an intravenous bolus of propopol. Here we show that the degree of human consciousness is directly associated with the information integration capacity of gamma wave, which is significantly higher in the conscious state than in the unconscious state. And we found a new time evolutional property of human consciousness. The conscious state showed a lower dimensional dynamic process which changed to a random-like process after loss of consciousness. This characteristic dynamic property, appeared only in the gamma band, might be used as an indicator to distinguish the conscious and unconscious states and also considered as an important fact for the human consciousness model

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

Feature-domain Adaptive Contrastive Distillation for Efficient Single Image Super-Resolution

Recently, CNN-based SISR has numerous parameters and high computational cost to achieve better performance, limiting its applicability to resource-constrained devices such as mobile. As one of the methods to make the network efficient, Knowledge Distillation (KD), which transfers teacher's useful knowledge to student, is currently being studied. More recently, KD for SISR utilizes Feature Distillation (FD) to minimize the Euclidean distance loss of feature maps between teacher and student networks, but it does not sufficiently consider how to effectively and meaningfully deliver knowledge from teacher to improve the student performance at given network capacity constraints. In this paper, we propose a feature-domain adaptive contrastive distillation (FACD) method for efficiently training lightweight student SISR networks. We show the limitations of the existing FD methods using Euclidean distance loss, and propose a feature-domain contrastive loss that makes a student network learn richer information from the teacher's representation in the feature domain. In addition, we propose an adaptive distillation that selectively applies distillation depending on the conditions of the training patches. The experimental results show that the student EDSR and RCAN networks with the proposed FACD scheme improves not only the PSNR performance of the entire benchmark datasets and scales, but also the subjective image quality compared to the conventional FD approaches.Comment: Under revie

Propofol Induction Reduces the Capacity for Neural Information Integration: Implications for the Mechanism of Consciousness and General Anesthesia

The cognitive unbinding paradigm suggests that the synthesis of cognitive information is attenuated by general anesthesia. Here, we investigated the functional organization of brain activities in the conscious and anesthetized states, based on characteristic functional segregation and integration of electroencephalography (EEG). EEG recordings were obtained from 14 subjects undergoing induction of general anesthesia with propofol. We quantified changes in mean information integration capacity in each band of the EEG. After induction with propofol, mean information integration capacity was reduced most prominently in the gamma band of the EEG (p=0.0001). Furthermore, we demonstrate that loss of consciousness is reflected by the breakdown of the spatiotemporal organization of gamma waves. Induction of general anesthesia with propofol reduces the capacity for information integration in the brain. These data directly support the information integration theory of consciousness and the cognitive unbinding paradigm of general anesthesia

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