8,174 research outputs found
ANALYSIS OF IDIOMATIC EMOTION EXPRESSIONS DETECTED FROM ONLINE MOVIE REVIEWS
A large number of idiomatic emotion expressions in Korean are composed of certain nouns
of human body parts accompanied by selected predicates, which represent a âphysiological
metonymyâ of sentiment (Lakoff 1987, Ungerer & Schmid 1996)or instance, kasum-i ttwita
literally means a physiological reaction (i.e. oneâs heart beat) but also can represent the emotion
like being thrilled to bits. We compared idiomatic emotion expressions used in English online movie
reviews and those observed in Korean, and noticed that the nouns of body parts such as kasum
âheartâ, maum âmindâ or nwun âeyesâ emerge frequently in both languages, whereas ekkay
âshoulderâ, kancang âintestinesâ or ppye âbonesâ seem to be rather reserved for Korean emotion
expressions.
In this study, we extract idiomatic emotion expressions based on the 13 nouns of body parts
listed by Lim (2001) from Korean online movie reviews. For instance, nouns such as meli âheadâ, ip
âmouthâ or simcang âcardiaâ are frequently used for constituting the emotion expressions of
POSITIVE values as shown in ip-ul tamwul-swu epsta âbe with open mouth (with delight) these
nouns hardly occur in NEGATIVE emotion expressions, which is not predictable from their semantic
features, but reveals their lexical idiosyncrasy. The frequent emotion expressions observed in online
movie reviews will be analyzed and classified according to their semantic properties. We will show
what salient traits of Korean emotion expressions can be remarked in current online subjective
documents such as usersâ reviews, blogs or opinion texts
Formulation of biologically-inspired silk-based drug carriers for pulmonary drug delivery targeted for lung cancer
A novel controlled release delivery system has been formulated using natural silk proteins extracted from cocoons of silkworms. The benefits of using silk fibroin, the major protein in silk, has been widely established in many applications, however this is the first time to report silk fibroin as being formulated and tested for pulmonary drug delivery. Silk fibroin particles were formulated and engineered for efficient delivery to the airways via dry powder inhalers and demonstrated high aerosolisation performance through the measurement of in vitro lung deposition. Various drugs were incorporated into the silk particles, and ultimately silk particles were loaded with cisplatin to develop controlled-release drug delivery systems that target lung cancer. Human lung epithelial cell line was used to test cytocompatibility of silk particles and the cytotoxicity of silk-cisplatin particles with normal or cross-linked silk formulations. Positive results were obtained and contributed for the optimisation of silk-based controlled-release delivery systems for pulmonary drug delivery
The BishopâPhelpsâBollobĂĄs property and lush spaces
AbstractWe prove that for every lush space X, the couple (â1,X) has the BishopâPhelpsâBollobĂĄs property for operators, that is, every lush space has the AHSP (standing for the approximate hyperplane series property). While every lush space has the alternative Daugavet property, there exists a space with the alternative Daugavet property that does not have the AHSP. We also show that there is a Banach space with both the AHSP and the alternative Daugavet property which is not lush
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
Synthesis of VO_2 Nanowire and Observation of the Metal-Insulator Transition
We have fabricated crystalline nanowires of VO_2 using a new synthetic
method. A nanowire synthesized at 650^oC shows the semiconducting behavior and
a nanowire at 670^oC exhibits the first-order metal-insulator transition which
is not the one-dimensional property. The temperature coefficient of resistance
in the semiconducting nanowire is 7.06 %/K at 300 K, which is higher than that
of commercial bolometer.Comment: 3 pages, 4 figures, This was presented in NANOMAT 2006 "International
workshop on nanostructed materials" on June 21-23th of 2006 in Antalya/TURKE
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