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      • KCI등재

        데페록사민 전처치가 토끼 심근경색 크기의 감소에 미치는 효과

        양관모,오동렬,박승현,박규남,이원재,김형국,황두영,최승필,채장성 대한응급의학회 1998 대한응급의학회지 Vol.9 No.4

        Background: Reperfusion of ischemic myocardium has been postulated to result in a specific oxygen radical mediated tissue injury. Iron may liberate during ischemia and we hypothesized that administration of the iron chelator, deferoxamine during ischemia would result in improved recovery after postischemic reperfusion. Purpose: To test whether iron-catalyzed processes contribute to myocardial necrosis during ischemia and reperfusion, deferoxamine was administered to block iron catalyzed hydroxyl radical formation in rabbits. Methods: Eleven rabbits were divided into two groups : control group (n=5) and deferoxamine pretreatment group (n=6). The left circumflex coronay artery was ligated for 30 minutes and reperfused for 180 minutes. Area at risk (AR) was measured by non-stained area with methylene blue injection into left atrium after left circumflex coronary artery ligation. Infarct size was measured by weighing after triphenyltetrazolium chloride staining. Heart rate was measured using electrocardiographic recording and systemic blood pressure was monitored by pressure transducer connected to the catheter in the left ventricle. Results: 1. There was no significant difference of heart rate and blood pressure in deferoxamine pretreatment group compared with control group. 2. There was significant decrease of serum iron concentration after continuous infusion of deferoxamine compared with serum iron concentration before ligation of coronary artery(P<0.05). 3. There was no significant difference of area at risk between control and deferoxamine pretreatment group. 4. Area at necrosis to area at risk was significantly reduced in deferoxamine pretreatment group compared with control group(P<0.05). The results suggest that deferoxamine infusion prior to coronary artery occlusion has a significant benefit in reducing infarct size in this model.

      • SCOPUSKCI등재
      • KCI등재

        Mapping of the equine herpesvirus type 1 immediate-early protein interaction domain within the general transcription factor human TFIIB

        ( Hyung Kwan Jang ),( Jeong Gon Cho ),( Hee Jong Song ) 한국가축위생학회 2002 韓國家畜衛生學會誌 Vol.25 No.4

        We previously reported that the equine herpesvirus type 1(EHV-1) immediate-early protein (IE protein) physically interacts with the general transcription factor human TFIIB(Jang et al, J Virol 75:10219-10230, 2001). The interaction between the IE protein and TFIIB is necessary for the IE protein to efficiently transactivate the early TK and late IR5 EFV-1 promoters. A panel of deletion and truncation mutants of the TFIIB gene was constructed and employed in protein-binding assays to map the IE protein-binding domain within TFIIB. Evidence is presented that the first direct repeat of TFIIB interacts specifically with the EIIV-1 IE protein.

      • KCI등재후보

        Characterization and localization of the unique Marek's disease virus type 2 ORF873 gene product

        Hyung-Kwan Jang 대한수의학회 2004 Journal of Veterinary Science Vol.5 No.3

        Studies on Marek’s disease virus (MDV)-unique genes are important for understanding the biological nature of the virus. Based on complete DNA sequence analyses of the MDV genomes, the MDV genomes contain presumably at least five MDV-unique genes, which are commonly conserved among the three MDV serotypes. A recombinant baculovirus that contains the MDV serotype 2 (MDV2)-unique gene, ORF873, under the polyhedrin promoter was constructed and designated rAcORF873. Polyclonal and monoclonal antibodies, which recognize the recombinant MDV2 ORF873 protein in Spodoptera frugiperda clone 9 (Sf9) cells infected with rAcORF873, were prepared by immunizing mice with a recombinant fusion protein expressed in Escherichia coli. Immunoblot analyses with the antibodies revealed a major protein band with a molecular mass of 108-kDa in both MDV2-infected chick embryo fibroblasts (CEF) and rAcORF873- infected Sf9 cells. By indirect immunofluorescence analyses using monoclonal antibody, the authentic ORF873 protein was localized in the cytoplasm of MDV2- infected CEF cells. The monoclonal and polyclonal sera, which were generated in the present study and reacted effectively to MDV2 ORF873 protein, are considered to be useful reagents for further studying the role(s) of the ORF873 protein in MDV2 infection.

      • KCI등재

        Mapping of the equine herpesvirus type 1 immediate-early protein interaction domain within the general transcription factor human TFIIB

        Jang, Hyung-Kwan,Cho, Jeong-Gon,Song, Hee-Jong The Korean Society of Veterinary Service 2002 韓國家畜衛生學會誌 Vol.25 No.4

        We previously reported that the equine herpesvirus type 1(EHV-1) immediate-early protein(IE protein) physically interacts with the general transcription factor human TFIIB(Jang et al, J Virol 75:10219-10230, 2001). The interaction between the IE protein and TFIIB is necessary for the IE protein to efficiently transactivate the early TK and late IR5 EHV-1 promoters. A panel of deletion and truncation mutants of the TFIIB gene was constructed and employed in protein-binding assays to map the IE protein-binding domain within TFIIB. Evidence is presented that the first direct repeat of TFIIB interacts specifically with the EHV-1 IE protein.

      • KCI등재

        Characterization of the molecular and biological properties between the equine herpesvirus type 1 immediate-early protein and the general transcription factor human TFIIB

        Jang Hyung-Kwan The Korean Society of Veterinary Service 2004 韓國家畜衛生學會誌 Vol.27 No.4

        The equine herpesvirus type 1 (EHV-1) immediate-early (IE) protein is a potent transactivator responsible for the activation of both early and late genes during the course of infection and is comprised of discrete functional domains that mediate its many functions. Interaction between trans activators such as the IE protein and various components of the RNA polymerase II transcription initiation machinery has been demonstrated to be critical for transactivation. In the present report, it is addressed the hypothesis that the IE protein interacts with various components of transcription machinery to mediate transactivation of target viral genes. In these studies, it is demonstrated that in vitro transcribed and translated IE protein interacts with TFIIB-agarose conjugate but not with TFIID-agarose conjugate. Additional immunoprecipitation studies using nuclear extracts derived from EHV-1 infected RK-13 cells confirmed that the IE protein interacts strongly with TFIIB, but fails to interact with TFIID. IR2, a truncated form of the IE protein lacking the potent transactivation domain and involved in the down-regulation of the IE gene, also interacted with TFIIB but not with TFIID. Studies were also performed to ascertain if particular TBP-associated factors (TAFs) could mediate IE or IR2 binding to TFIID. In vitro transcribed and translated TAF250 added to nuclear extracts generated from EHV-1 infected cells also failed to mediate an interaction between the IE protein or the IR2 protein and TFIID. This study demonstrated that the IE protein mediates transactivation of target viral genes by a mechanism that involves TFIIB. This is in contrast to mechanisms that have been proposed for both the herpes simplex virus ICP4 and VP16 protein which have been proposed to transactivate viral genes through interactions involving both TFIIB and TFIID. This study also intimates that IR2 mediate its repressive effects during the course of EHV-1 infection by a mechanism that involves sequestration of various transcription factors.

      • KCI등재

        Characterization of the molecular and biological properties between the equine herpesvirus type 1 immediate-early protein and the general transcription factor human TFIIB

        ( Hyung Kwan Jang ) 한국가축위생학회 2004 韓國家畜衛生學會誌 Vol.27 No.4

        The equine herpesvirus type 1(EHV-1) immediate-early(IE) protein is a potent transactivator responsible for the activation of both early and late genes during the course of infection and is comprised of discrete functional domains that mediate its many functions. Interaction between transactivators such as the IE protein and various components of the RNA polymerase II transcription initiation machinery has been demonstrated to be critical for transactivation. In the present report, it is addressed the hypothesis that the IE protein interacts with various components of transcription machinery to mediate transactivation of target viral genes. In these studies, it is demonstrated that in vitro transcribed and translated IE protein interacts with TFIIB-agarose conjugate but not with TFIID-agarose conjugate. Additional immunoprecipitation studies using nuclear extracts derived from EHV-1 infected RK-13 cells confirmed that the IE protein interacts strongly with TFIIB, but fails to interact with TFIID. IR2, a truncated form of the IE protein lacking the potent transactivation domain and involved in the down-regulation of the IE gene, also interacted with TFIIB but not with TFIID. Studies were also performed to ascertain if particular TBP-associated factors(TAFs) could mediate IE or IR2 binding to TFIID. In vitro transcribed and translated TAF250 added to nuclear extracts generated from EHV-1 infected cells also failed to mediate an interaction between the IE protein or the IR2 protein and TFIID. This study demonstrated that the IE protein mediates transactivation of target viral genes by a mechanism that involves TFIIB. This is in contrast to mechani는 that have been proposed for both the herpes simplex virus ICP4 and VP16 protein which have been proposed to transactivate viral genes through interactions involving both TFIIB and TFIID. This study also intimates that IR2 mediate its repressive effects during the course of EHV-1 infection by a mechanism that involves sequestration of various transcription factors.

      • KCI등재

        동물바이러스의 새로운 분류

        장형관 ( Hyung Kwan Jang ),송희종 ( Hee Jong Song ) 한국가축위생학회 2005 韓國家畜衛生學會誌 Vol.28 No.1

        More than 30 years have elapsed since the first report of the International Committee on Taxonomy of Viruses(ICTV) was published in 1971. Since that publication, the ICTV recognizes about 1,550 virus species, but some 30,000 virus strains and isolates are being tracked by virologists in different fields of biology. The ICTV is the "international court" of experts that rules on names and relationships of all virus, but only to the level of species. Virus taxonomy is changing rapidly, with changes ranging from the trivial(use of italics for species names) to profound reorganization driven by the explosion of sequence information. The universal system of viral taxonomy now accepts Linnean-like classification at the levels of order, family, subfamily, genus, and species. The suffix "-virales" identifies an order. Families are identified by the suffix "-viridae", subfamilies are identified by the suffix "-virinae", and genera are identified by the suffix "-virus". The importance of distinguishing subspecies, strains, and isolates in vaccine development, diagnostics, etc. is recognized, but these lower levels are not formally classified by ICTV. This paper mainly introduces taxonomy and classification of animal viruses on the basis of the seventh report of the ICTV edited by Van Regenmortal et al. in 2000.

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