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      • KCI등재

        종설논문 : 의사-제약회사 상호관계가 연구에 미치는 영향

        김승후 ( Seong Who Kim ),홍정화 ( Jeong Hwa Hong ),김옥주 ( Ock Joo Kim ) 한국의료윤리학회 2011 한국의료윤리학회지 Vol.14 No.3

        This article examines the influence of physician-pharmaceutical industry interaction upon medical research. We analyze some of the problems arising from pharmaceutical companies` sponsorship of clinical trials, such as biased results caused by multiple trials with predictable outcomes and publication biases. Furthermore, we propose specific measures to address and overcome these problems.

      • KCI등재

        노후 저층주거지 도시재생활성화계획에서 스마트기술의 특성 및 적용방안에 관한 연구

        김승후(Kim, Seung Hoo),나인수(Na, In-Su) 도시정책학회 2020 도시부동산연구 Vol.11 No.1

        The 4th industrial revolution introduced various smart city technologies but it is rarely adopted in urban regeneration field. In the Urban Regeneration New Deal project, the characteristics of smart technology will be derived by analyzing the projects and programs of the residential support type urban regeneration plan for deteriorated low-rise and residential areas. The Urban Regeneration Plan of Shinheung District in 2019 categorized by 14 unit projects by setting each goal and core strategies under the Urban Regeneration New Deal policy such as job creation, urban competitiveness improvement, housing welfare realization, and social integration. This study proposed 13 smart technologies of ICTs for Junggu Gomgammaul in Incheon. Residential environment, street environment, community facilities are drawn for the physical hardware programs and urban management platform and life and welfare are derived for non-physical software programs.

      • SCOPUSKCI등재

        체외순환후 혈중 Thromboxane $B_2$와 Endothelin-1 농도 변화에 미치는 Aprotinin의 효과

        임청,윤태진,김연승,김승후,이재담,노준량,송명근,Lim, Cheong,Yun, Tae-jin,Kim, Yeon-seung,Kim, Seung-hoo,Lee, Jae-dam,Rho, Joon-Ryang,Song, Meong-Gun 대한흉부심장혈관외과학회 2000 Journal of Chest Surgery (J Chest Surg) Vol.33 No.3

        Background: Thromboxane A2 and endothelin-1 are the potent vasoconstrictors affecting pulmonary pathophysiology in response to whole body inflammatin following CPB. Aprotinin, as an antiiflammatory agent, may decrease the release of such vasoactive substance from pulmonary tissues, preventing pulmonary hypertension after cardiopulmonary bypass. Material and Method: Ten mongrel dogs(Bwt. ac. 20kg) were subjected to cardioupulmonary bypass for 2 hours and postbypass pulmonary vascular resistance(0, 1, 2, 3 hours) were compared with prebypass level. The dogs were divided into 2 groups; control group(n-5) and aprotinin group(n=5). In the aprotinin group, aprotinin was administered as follows; 50,000 KIU/kg mixed in pump priming solution, 50,000 KIU/kg prebypass intravenous infusion over 30 minutes, 10,000 KIU/kg/hour postbypass continuous infusion. Prebypass and postbypass 0, 1, 2, 3 hour pulmonary vascular resistance were measured. At prebypass and postbypass 0, 90, 180 minutes, blood samples were obtained from pulmonary arterial and left atrial catherers for the assay of plasma thromboxane B2 a stable metabolite of thromboxane A2, and endothelin-1 concentrations. Result: The ratios of pustbypass over prebypass pulmonary vascular at postbypass 0, 1, 2, 3 hours were 1.28$\pm$0.20, 1.82$\pm$0.23, 1.90$\pm$0.19, 2.14$\pm$0.18 in control group, 1.58$\pm$0.18, 1.73$\pm$0.01, 1.66$\pm$0.10, 1.50$\pm$0.08 in aprotinin group ; the ratios gradually increased in control group while decreased or fluctuated after postbypass 1 hour in aprotinin group. There was statistically significant difference between control group and aprotinin group at postbypass 3 hours(P=0.014). Pulmonary arterial plasma concentration of thromboxane B2(pg/ml) at prebypass, postbypass 0, 90, 180 minutes were 346.4$\pm$61.9, 529.3$\pm$197.6, 578.3$\pm$255.8, 493.3$\pm$171.3 in control group, 323.8$\pm$118.0, 422.6$\pm$75.6, 412.3$\pm$59.9, 394.5$\pm$154.0 in aprotinin group. Left atrial concentrations were 339.3$\pm$89.2, 667.0$\pm$65.7, 731.2$\pm$192.7, 607.5$\pm$165.9 in control group, 330.0$\pm$111.2, 468.4$\pm$190.3, 425.4$\pm$193.6, 4.7.3$\pm$142.8 in aprotinin group. These results showed decrement of pulmonary thromboxane A2 generation in aprotinin group. Pulmonary arterial concentrations of endothelin-1(fmol/ml) at the same time sequence were 7.84$\pm$0.31, 13.2$\pm$0.51, 15.0$\pm$1.22, 16.3$\pm$1.73 in control group, 7.76$\pm$0.12, 15.3$\pm$0.71, 22.6$\pm$6.62, 14.9$\pm$1.11 in aprotinin group. Left atrial concentrations were 7.61$\pm$17.2, 57.1$\pm$28.4, 18.9$\pm$18.2, 31.5$\pm$20.5 in control group, 5.61$\pm$7.61, 37.0$\pm$26.2, 28.6$\pm$21.7, 37.8$\pm$30.6 in aprotinin group. These results showed that aprotinin had no effect on plasma endothelin-1 concentration after cardiopulmonary bypass. Conclusion: Administration of aprotinin during cardiopulmonary bypass could attenuate the increase in pulmonary vascular resistance after bypass. Inhibition of pulmonary thromboxane A2 generation was thought to be one of the mechanism of this effect. Aprotinin had no effect on postbypass endothelin-1 concentration.

      • 사람 내피세포에서 염증 전구사이토카인이 VCAM - 1의 발현에 미치는 영향

        장윤혜(Yun Hae Chang),박수길(Su Kil Park),문희범(Hee Bom Moon),이재담(Jae Dam Lee),김승후(Seong Who Kim),황온유(On You Hwang),홍혜남(Hae Nam Hong),조영주(Young Joo Cho) 대한천식알레르기학회 1999 천식 및 알레르기 Vol.19 No.2

        Background: The expression of adhesion molecules contribute to development of systemic diseases. Vascular cell adhesion molecule-l(VCAM-1) is an endothelial cell membrane gly- coprotein that has been implicated in leukocyte/endothelial cell interactions in inflammation. Ojective: The aim of this study was to characterize the surface expression and regulation of VCAM-1 on two different endothelial cells. Methods: We examined the effects of the expression of VCAM-1 in two different endothelial cells, isolated from human umbilical cords and human glomerulus. Expression of VCAM-1 was measured by enzyme-linked immunosorbent assay(ELISA) and flow cytometry. Results: In human umbilical cord endothelial cells(HUVECs), both interleukin-l B(IL-lB) and tumor necrosis factor-a (TNF-a) increased VCAM-1 expression. VCAM-1 expression increased by TNF-a was higher than that increased by IL-lB. In human glomerular endothelial cells(HGECs), IL-lB and TNF-a markedly increased VCAM-1 expression. Conclusion. The regulation of VCAM-1 appears to be somewhat different in HGECs compared with HUVECs. These differences between the responsiveness of the two cells may possibly indicate inherent differences in endothelial cell derived from different vascular beds.

      • KCI등재
      • 사람 혈청 Vitronectin의 정제 및 항 Vitronectin 다클론 항체의 생산

        장윤혜,김백남,이성순,문경,김승후,이재담 大韓免疫學會 1996 大韓免疫學會誌 Vol.18 No.2

        Background: Vitronectin is one of major cell- adhesive glycoprotein in mammalian serum and plasma ; the other is fibronectin. It is a mixture of 65 and 75kDa protein in plasma which promotes spreading of a variety of cultured cells ,inhibits the cytotoxicity of membrane attacks complex C5b-7 and modulates thrombin-antithrombin III activity. Human plasma and serum contain 10-40mg of vitronectin per 100ml,but only a few mg or less of vitronectin can be isolated with a 0.5-20% recovery efficiency through very long processes or with expensive,commercially available monoclonal antibody. In this study, we purified the vitronectin from human plasma and produced anti-vitronectin polyclonal antibody using purified vitronectin. Methods: Vitronectin was purified from the human plasma by heparin-sepharose column and its efficacy was measured by cell spreading assay. Anti-vitronectin polyclonal antibody produced and confirmed by ELISA and immunoblotting. Results: This procedures produced about 0.8mg vitronectin from 100ml human plasma within 2 days. 1) Purified vitronectin promoted spreading of HepG2 hepatoma cells on substrates with a half maximal activity at 0.lug/ml. 2) In SDS-PAGE analysis of purified protein, 2 bands were found and their molecular weights were 75kDa and 65kDa,respectively. 3) The immunoblotting assay showed that the bands of molecular were same site as SDSPAGE analysis. Conclusion: Simple,rapid purified vitronectin by heparin-sepharose column and anti-vitronectin antibody may facilitate the elucidation of vitronectin function and action mechanism in human body.

      • SCOPUSKCI등재

        IGF-I이 배양된 연골세포의 콜라젠 합성에 미치는 영향

        한상훈,조종한,이종환,홍혜남,김승후,이재담 大韓成形外科學會誌 2000 Archives of Plastic Surgery Vol.27 No.1

        Cartilage is one of the most commonly manipulated tissue in esthetic and reconstructive surgery. Cartilage has an important role in longitudinal bone growth. Anabolic hormones and locally produced peptide growth factors are known to influence this process Matrix composition changes through proliferation, maturation, and differentiation of chondrocytes, and endochondral ossification thereafter. Defined cartilage matrix is synthesized during the maturation of chondrocytes where the major change is the increment of type Ⅱ collagen. Variable sulfated mucololysaccharides and hyaluronic acid are also synthesized during this maturation. IGF-I(insulin like growth factor-I), so called somatomedin C, is a prominent growth factor in serum. IGF-I is known to be involved in long growth. IGF-I is affected by pituitary growth hormone. There are few studies done on IGF-I effect in cartilage matrix formation and possible changes of collagen subtypes. This experiment was designed to see the IGF-I effect on the colagen synthesis of cultured chondrocytes. Optimal concentration of IGF-I for the experiment was determined using H3-thymidine incorporation into DNA. The IGF-I effect on collagen synthesis was studied using H3-proline. The IGF-I effect on the synthesis of subtypes of collagen was studied using SDS-PAGE and immunocytochemical staining. Chondrocytes were isolated from the ears of New Zealand white rabbit and cultured in 2 X 10??cells/300㎍ density. IGF-I increased DNA synthesis, and optimal concentration of IGF-I was determined by dose-relationship curve as 10ng/ml. Collagen synthesis was increased by IGF-I. Type Ⅱ collagen was increased on SDS-PAGE with IGF-I and this gel electrophoresis showed thpe X collagen, also. The increase in type Ⅱ collagen was confirmed with immunocytochemical staining, the reaction becoming stronger with the addition of IGF-I. Type Ⅰ collagen was not changed with IGF-I on immunocytochemistry. We conclude that IGE-I is an important modulator influencing not only proliferation and maturation but also terminal different-iation of chondrocytes.

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