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천이신호는 지속시간이 짧으면서 길이의 변화가 크고, 시변성 및 비정재성 특성을 갖는다. 이러한 천이신호의 식별에는 분석 프레임 단위로 참조신호에 대한 기준패턴을 만들어 입력신호와의 유사도를 비교하는 방법이 효과적일 수 있다. 본 연구에서는 참조신호의 기준패턴으로 프레임 기반의 특징벡터들에 대해 확률통계 모형인 정규혼합모델을 적용하는 방법을 제안하고, 다양한 수중 천이신호에 대한 식별 실험을 통해 제안한 방법의 타당성을 검증하였다. Transient signals generally have short duration and variable length with time-varying and non-stationary characteristics. Thus frame-based pattern matching method is useful for classification of transient signals. In this paper, we propose a new method for classification of underwater transient signals using a Gaussian mixture model(GMM). We carried out classification experiments for various underwater transient signals depending upon the types of noise, signal-to-noise ratio, and number of mixtures in the GMM. Experimental results have verified that the proposed method works quite well for classification of underwater transient signals.
최근 들어 전국의 곳곳에서 화재가 발생하여 귀중한 인명과 재산을 잃는 대형 참사(慘事)로 이어지고 있다. 화재가 발생했을 때에 초기진화(初期鎭火) 및 인명(人命)의 대피시간(待避時間)인 소위 골든타임은 대략 5분정도이다. 또한 화재사고를 직접체험하게 되면 패닉(panic)현상을 초래하여 우왕좌왕, 혼란의 블랙홀(Black hole)에 함몰(陷沒)되게 마련이다. 의정부 아파트 화재에서처럼 대부분의 골목길은 많은 차량들이 주차되어 소방차 긴급출동에 장애가 되고 있는 실정이다. 보편적으로 화재발생 시 소방대는 5분 내에 출동을 목표로 훈련을 한다. 하지만 화재현장에서 소방대에 화재신고가 신속히 이루지지 못하는 지체시간(遲滯時間)을 감안하면 소방대가 현장에 도착하여 진압작업을 개시하는 시점에는 이미 골든타임을 벗어나 화재가 확산되어 있는 상황인 것이다. 그러므로 골든타임을 감안(勘案)하여 소방대의 출동이전에 자체적으로 초기진압을 할 수 있는 방재시스템을 구축(構築)하여야 하는 것이다. 이에 소방대의 도착이전의 골든타임 이내에 자체적으로 조기진압 및 피난을 할 수 있어야 할 것이며, 다만 출동한 소방대는 인접한 건물이나, 주유소 등으로의 연소 확산(延燒 擴散)을 방지하는 역할로 개념(槪念)을 정리할 필요가 있는 것이다. 소방관련 법령 및 화재안전기준 등은 수시로 개정 발전 되어 오늘날에 이르렀다, 하지만 아직까지도 불합리하고 모순된 규정 등이 곳곳에 산재해 있다. 이에 틀에 박힌 고정관념에서 벗어나 보다 논리적이고 합리적이며 현장여건에 부합하는 선진화된 소방제도를 구축하여 화재참사로부터 국민의 생명과 재산보호는 물론 그 손실을 최소화하기 위한 선진화된 소방관련 제도로 정착시켜야 할 것이다.
Human serum albumin, bovine serum albumin, ovalbumin, IgG, lysozyme and ribonuclease A were reacted with 3-deoxyglucosone under physiological conditions of 37℃ and pH 6.4, and polymerization of proteins and the impairments of amino acid residues were investigated. Proteins tested, especially lysozyme, IgG and ribonuclease A, were polymerized significantly, and lysine residue and arginine residue, especially arginine residue of proteins, were impaired remarkable. Experimental results strongly suggested that 3-deoxyglucosone, formed from proteins-glucose reaction system, was the corss-linker responsible for the polymerization of proteins.
Background: Leptin gene is known to be related to obesity in human and animals and complete genetic defect of the gene in ob/ob mouse has been identified. Therefore, ob/ob mouse is widely used as an animal model for the study of etiology and therapy of obesity. The main biological function of leptin was thought to involve in the regulation of food intake and weight gain, however, the regulatory mechanisms by which leptin functions in the weight reduction and lowering the blood glucose level are uncertain. In the present study, retroviral-mediated leptin gene transduction into ob/ob mouse was attempted for the correction of biochemical parameters of obesity. Methods: Leptin cDNA was inserted into pLXSN retroviral vector (pLXSN-lep) and recombinant leptin expressing retrovirus particles (3 X10 CFU/mL) were produced in ?2 ecotropic packaging cells and subsequent transfection into PA317 amphotropic packaging cells. The leptin expressing recombinant viruses (LER) were transduced into NIH3T3 mouse fibroblasts and nsertion of leptin cDNA into chromosomal DNA of PA317 and MH3T3 mouse fibroblasts was confirmed by Southern blot hybridizations. Leptin mRNA and its protein expressed in the cells were identified by Northern blot hybridization and Western blot immunodetection method, respectively. LER were injected I. P. into ob/ob mice, and body weight, food intake, serum leptin level and blood glucose level were measured. Results: Expression of leptin was identified in PA317 and NIH3T3 mouse fibroblasts transduced with LER. Leptin content in sera of mice transfused with LER was drastically increased after 1 week and decreased to the almost basal level at 3 weeks after the transfusion. The body weight as well as food intake of ob/ob mouse transduced by LER decreased for the first 3 weeks and slightly increased thereafter. The reduction of both body weight and food intake in ob/ob mice transduced with LER was observed with the concomitant increase of serum leptin level, indicating that retroviral-mediated transduction of leptin gene in ob/ob mouse in vivo produced a biologically active leptin protein and released it into blood circulation. Conclusion: A transient expression of leptin cDNA in ob/ob mice by a retroviral-mediated transduction was performed and further studies are required for long term expression of the gene in vivo (J Kor Soc Endocrinol 15:502-512, 2000).
The purpose of this study was to evaluate the physical properties of hydrophilic polyvinyl siloxane impression materials as change of material's storage temperatures. Working time, strain-in-compression, elastic recovery and consistency were tested according to ISO Standard NO. 1563. The results are as followed. 1. Working time decreased in cold storage. 2. Strain-in-compression was different in storage temperatures. Material's strain-in compression in cold temperatures were higher than in room temperature and in incubator. 3. A coefficient of elastic recovery varied by storage temperatures. The rate in cold temperature was the lowest and in incubator was the highest. 4. Consistency of impression substance different in storage temperatures. The extent in cold temperature is the highest and in incubator was the lowest. Statistical analysis(SPSS 14.0k, p>0.05) showed that storage temperature affect to material's physical properties. We recognized that the physical properties of polyvinyl siloxane impression materials were changed according to storage temperature.
Background: Purified major allergens of house dust mite are essential for evaluation of the allergic mechanism in molecular basis and development of new modalities of immunemodulation. Objective: In this study, we aimed to purif group 1 and group 2 allergens from Dermatophagoides pteronyssinus (Dp). In addition, cDNAs corresponding to Der pI and II in Korean Dp were isolated and recombinant Der p1 and Der pII were synthesized. Materials and method: Der pI allergen was purified by ammonium sulfate precipitation, anionexchange column chromatography, and gel filtrat,ion chromatography. Der pII allergen was purified by anion exchange chromatography, gel filtration chromatography, and a preparative isoelectric focusing method. Results: Eight hundred ug of Der pI and 50㎍ of Der pII were obtained from 100 g of culture medium and 1 g of mite bodies, respectively. The purities of these allergens were confirmed by SDS PAGE and the strong reactivity to the patient sera was identified. In order to produce a recombinant allergens, poly(A) RNA from house dust mites were isolated and used for cDNA synthesis by RT PCR. The cDNA was inserted into prokaryotic expression vector and the vectors were transformed into E. coli. A little amount of recombinant Der pI protein was produced due to the low solubility, and 1.2 mg of recombinant Der pII was produced from 1 L of E. coli culture medium. The antigenicity of Der pI was relatively weak, however, Der pII showed a strong antigenicity. Amino acid sequence of the amplified cDNA deduced from DNA sequences of Der pII showed 6 different variants. The variation of amino acid sequences suggests the possibility of high incidence of mutation of Der pII protein. Conclusion: A simplified method for the purification of Der pI and Der pII was developed. Recombinant allergens will be useful for the diagnosis and treatment of allergy with lower costs.
In order to get further informations on the loss of biologic function by the nonenzymatic reaction of glucose with proteins, reducing sugars (glucose, fructose, galactose, mannose, ribose and xylose) were reacted with proteins (bovine serum albumin, lysozyme, ovalbumin, RNase A) in 0.2 M phosphate buffer (pH 7.4) at 37℃, and polymerization of proteins and changes in amino acid composition were compared. Proteins tested were polymerized and some amino acid residues were impaired significantly by Maillard reaction. The degree of polymerization and impairment of amino acid residues, however, were different, depending on the kinds of proteins and reducing sugars.