• Title/Summary/Keyword: Family Structures

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Molecular differentiation of Korean Newcastle disease virus (NDV) by restriction enzyme analysis and pathotype-specific RT-PCR

  • Kwon, Hyuk-Joon;Cho, Sun-Hee;Kim, Sun-Joong
    • 대한수의학회지
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    • 제46권4호
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    • pp.371-379
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    • 2006
  • Newcastle disease virus (NDV) is a single-stranded negative sense RNA virus, which has been classified as a member of the Avulavirus genus of the Paramyxoviridae family. It is also one of the most important pathogens in the poultry industry. The glycoproteins, fusion (F) and hemagglutinin-neuraminidase (HN), determine the virulence of NDV, and the relevant molecular structures have already been determined. NDV isolates differ in terms of virulence, and at least 2 of 9 genotypes (I-IX) have been shown to co-circulate. Therefore, it is clearly important to differentiate between vaccine strains and field isolates. In vivo pathogenicity tests have been the standard protocol for some time, but molecular methods appear preferable in terms of the rapidity of diagnosis, as well as animal welfare concerns. In this study, we have designed primer sets from HN gene for phylogenetic analysis and restriction enzyme analysis, and from F gene for pathotype-specific RT-PCR. Via the combination of 2 methods, 106 Korean NDV isolates obtained from 1980 to 2005 were differentiated into vaccine strains, and virulent genotypes VI and VII. The genotype VI viruses were only rarely isolated after 1999, and genotype VII, after it was initially isolated from poultry in 1995, recurred in 2000, and then became the main NDV constituting a threat to the Korean poultry industry.

섬진강 중.상류 수계의 어류상과 군집구조 (Fish Fauna and Community Structure in the Mid-Upper Region of the Seomjin River)

  • 장성현;류희성;이정호
    • 생태와환경
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    • 제42권3호
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    • pp.394-403
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    • 2009
  • 본 연구는 섬진강 중 상류 수계의 어류상과 어류군집을 밝히기 위하여 2008년 8월부터 2009년 4월까지 총 15개 정점에서 조사를 실시하였다. 총 11과 42종의 어류가 채집되었으며, 이 중 잉어과(Cyprinidae) 어류가 28종이 채집되어 66.7%의 상대풍부도로 우점하였다. 총 42종의 어종 중 일차담수어는 40종, 주연성 담수어는 2종으로 일차담수어의 구성비가 매우 높게 나타났다. 우점종은 피라미 (Zacco platypus: 22.3%), 아우점종은 꺽지 (Coreoperca herzi: 10.8%)이었으며, 모래무지 (Pseudogobio esocinus: 9.0%)와 붕어 (Carassius auratus: 5.8%) 등도 높은 서식을 보였다. 한국고유종은 각시붕어(Rhodeus ocellatus)와 칼납자루(Acheilgnathus koreensis) 등 17종(40.5%)으로 고유종의 빈도가 매우 높았으며, 이 중 환경부지정 멸종위기 야생동물 II급 종인 임실납자루(Acheilgnathus somjinensis)의 서식이 확인되었다. 따라서 섬진강 중 상류 수계는 어류가 서식하기에 매우 적합한 수 환경을 유지하고 있는 것으로 나타났다.

배추(Brassica campestris ssp pekinensis) 지상부의 화학성분 (Chemical Constituents of Brassica campestris ssp pekinensis)

  • 최연희;김정숙;서지희;이정원;김영섭;유시용;이강노;김영균;김성훈
    • 생약학회지
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    • 제35권3호통권138호
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    • pp.255-258
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    • 2004
  • Chinese cabbage (Brassica campestris ssp pekinensis) is one of the most popular green vegetables in Cruciferae family, which consisted in many Korean food. All kinds of Chinese cabbage are used both fresh and cooked with certain varieties being more suitable than others for some uses. A unique dish, Kimchi, has been developed in Korea and elsewhere by fermenting Chinese cabbage and pickling it in salt solution. Though lots of beneficial effect of Kimchi on human health has been published before, it is still debatable and in vague on the active origin of the Kimchi or of the Chinese cabbage responsible for the corresponding biological activities. We have recently conducted photochemical investigation of the Chinese cabbage, which is the main ingredient of the Korean traditional food, Kimchi. The MeOH extract of Chinese cabbage was partitioned with ethylacetate and BuOH, successively. The ethyl acetate soluble part was subjected to column chromatography with silica gel and RP-18, which gave finally five minor components, i.e., ${\beta}-sitosterol$ (1), indole-3-acetonitrile (2), 4-methoxyindole-3-acetonitrile (3), methyl ferulate (4), glycerol 1-(9,12,15-octadecatrienoate) (5). The structures of them were established on the basis of spectral $(^1H-NMR,\;^{13}C-NMR)$ evidences.

Chemical Constituents from Leaves of Pileostegia viburnoides Hook.f.et Thoms

  • Li, Xiao Jun;Liu, Zu Zhen;Kim, Kwan-Woo;Wang, Xiang;Li, Zhi;Kim, Youn-Chul;Yook, Chang Soo;Liu, Xiang Qian
    • Natural Product Sciences
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    • 제22권3호
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    • pp.154-161
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    • 2016
  • Phytochemical investigation on the leaves of Pileostegia viburnoides Hook.f.et Thoms led to the isolation of twenty-five compounds, and their structures were identified as n-dotriacontane (1), taraxeryl acetate (2), friedelin (3), epifriedelinol (4), canophyllal (5), stigmast-4-en-3-one (6), stigmasterol (7), (24R)-5A-stigmastane-3,6-dione (8), ursolic acid (9), pomolic acid (10), umbelliferone (11), 4-epifriedelin (12), n-octatriacontanol (13), ${\beta}$-amyrin (14), ${\alpha}$-amyrin (15), taraxerol (16), nonadecanol (17), friedelane (18), arachic acid (19), protocatechuic acid (20), n-pentatriacontanol (21), hexadecanoic acid (22), vincosamide (23), daucosterol (24), and skimming (25), respectively. To our best knowledge, compounds 1, 2, 12, 13, 17 - 19 and 21-23 were new within Saxifragaceae family. Compounds 15, 16, and 20 were produced from this genus for the first time. Compounds 4, 14 and 25 were first obtained from species P. viburnoides and compounds 3, 5 - 11, and 24 were achieved from the leaves of P. viburnoides for the first time. Furthermore, the anti-neuroinflammatory activity of these isolates was evaluated.

Gelastatins, New Inhibitors of Matrix Metalloproteinases from Westerdykella multispora F50733

  • Lee, Ho-Jae;Chung, Myung-Chul;Lee, Choong-Hwan;Chun, Hyo-Kon;Rhee, Joon-Shick;Kho, Yung-Hee
    • 한국응용약물학회:학술대회논문집
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    • 한국응용약물학회 1998년도 Proceedings of UNESCO-internetwork Cooperative Regional Seminar and Workshop on Bioassay Guided Isolation of Bioactive Substances from Natural Products and Microbial Products
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    • pp.128-128
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    • 1998
  • Matrix metalloproteinases (MMPs) are a family of zinc-dependent proteases that degrade extracellular matrix and basement membrane. These enzymes are play important roles in tumor cell invasion and metastasis, as well as angiogenesis and other connective tissue diseases. In our screening program for inhibitors of MMP-2 from fungal metabolites, we have isolated novel non-peptidic inhibitors of MMPs, designated gelastatin A and B from the culture broth of Westerdykella multispora F50733. The structures of gelastatin A and B were determined to be 3-(5E-hexa-2E,4E-dienylidene-2-oxo-5,6-dihydro-2H-pyran-3yl)-propanoic acid and 3-(5Z-hexa-2E,4E-dienylidene-2-oxo-5,6-dihydro-2H-pyran-3yl)-propanoic acid, respectively. Gelastatin A and B exist as a mixture of two stereoisomers in a ratio of 2: 1. The 2: 1 mixture of gelastatin A and B inhibited activated MMP-2 and MMP-9 with an IC$\sub$50/ value of 0.63, 5.29 ${\mu}$M, respectively. They inhibited the invasion of B16F10 melanoma cells through basement membrane Matrigel with dose dependent.

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Isolation, Molecular Phylogeny, and Tissue Distribution of Four cDNAs Encoding the Apolipoprotein Multigene Family in Barred Knifejaw, Oplegnathus fasciatus (Teleostei, Perciformes)

  • Kim, Keun-Yong;Cho, Young-Sun;Kim, Sung-Koo;Nam, Yoon-Kwon
    • Fisheries and Aquatic Sciences
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    • 제11권2호
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    • pp.88-97
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    • 2008
  • Lipoproteins are complexes of lipids and specific apolipoproteins that are involved in lipid transport and redistribution among various tissues. In this study, we isolated full-length apolipoprotein cDNA sequences encoding apolipoprotein A-I (apoA-I), apoE, apoC-II, and apo-14 kDa in barred knifejaw, Oplegnathus fasciatus. In addition, we reconstructed phylogenetic trees and investigated mRNA tissue distributions. Alignment analyses of amino acid sequences revealed that secondary structures of the polypeptides apoA-I, apoE, and apoC-II in barred knifejaw are well conserved with their teleostean and mammalian counterparts in terms of characteristic tandem repetitive units forming amphipathic ${\alpha}$-helices. Both the sequence alignment data and cleavage sites of apo-14 kDa indicated a clear differentiation between Percomorpha and Cypriniformes. Meanwhile, the phylogenetic trees of apolipoprotein sub-families suggested that the common ancestor prior to the split of the Actinopterygii (ray-finned fishes) and Sarcopterygii (tetrapods) would have possessed the primordial protein-encoding genes. Tissue distribution of each apolipoprotein transcript determined by semi-quantitative RTPCR showed that barred knifejaw apoA-I transcripts were more or less ubiquitously expressed in the liver, intestines, brain, muscle, spleen, and kidney. The most striking difference from previous observations on barred knifejaw was the ubiquitous expression of apoE across all somatic tissues. Barred knifejaw apoC-II showed tissue-specific expression in the liver and intestines, while the liver and brain were the major sites of apo-14kDa mRNA synthesis.

BIM 기반의 준설매립전용 Library Browser 개발 (Developing Object Library Browser for Reclamation Based BIM)

  • 이동윤;이준호;이상웅;최차석;구본효
    • 한국지반환경공학회 논문집
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    • 제15권3호
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    • pp.57-63
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    • 2014
  • 본 연구에서는 준설매립분야의 설계자동화를 위하여 준설토 투기장 설계 시 고려되는 상부 및 하부 구조물을 대상으로 Library를 구축하고, 이를 통합 관리할 수 있는 브라우저를 개발하였다. 개발 Library는 주요 단면제원을 변수화하여 형상의 가변성 확보가 가능한 파라메트릭 모델링 방법을 이용하여 작성하였으며, 작업환경에 맞게 표준횡단 및 패밀리 Library로 구분하여 작성하였다. 작성된 Library를 특성별로 구분하여 객체를 관리하고 BIM 기반 모델링 작업 시 객체의 적용이 간편하도록 C# 언어를 이용하여 브라우저를 개발하였다. 개발된 브라우저를 BIM 기반의 3차원 캐드 프로그램에 연동함으로써 간편하게 3차원 모델링, 도면작성 및 물량산출이 가능하고 신규 Library의 작성 및 관리 또한 가능하다.

Crystal Structure of GRIP1 PDZ6-peptide complex reveals the structural basis for class II PDZ target recognition and PDZ domain-mediated multimerization

  • Im, Young-Jun;Park, Seong-Ho;Park, Seong-Hwan;Lee, Jun-Hyuck;Kang, Gil-Bu;Morgan Sheng;Kim, Eunjoon;Eom, Soo-Hyun
    • 한국결정학회:학술대회논문집
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    • 한국결정학회 2002년도 정기총회 및 추계학술연구발표회
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    • pp.4-4
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    • 2002
  • PDZ domains bind to short segments within target proteins in a sequence-specific fashion. GRIP/ABP family proteins contain six to seven PDZ domains and interact via its sixth PDZ domain (class Ⅱ) with the C-termini of various proteins, including liprin-α. In addition the PDZ456 domain mediates the formation of homo- and heteromultimers of GRIP proteins. To better understand the structural basis of peptide recognition by a class Ⅱ PDZ domain and DZ-mediated multimerization, we determined the crystal structures of the GRIPI PDZ6 domain, alone and in complex with a synthetic C-terminal octapeptide of human liprin-α, at resolutions of 1.5 Å and 1.8 Å, respectively. Remarkably, unlike other class Ⅱ PDZ domains, Ile736 at αB5 rather than conserved Leu732 at αB1 makes a direct hydrophobic contact with the side chain of the Tyr at the -2 position of the ligand. Moreover, the peptide-bound structure of PDZ6 shows a slight reorientation of helix αB, indicating that the second hydrophobic pocket undergoes a conformational adaptation to accommodate the bulkiness of the Tyr's side chain, and forms an antiparallel dimer through an interface located at a site distal to the peptide-binding groove. This configuration may enable formation of GRIP multimers and efficient clustering of GRIP-binding proteins.

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RPK118, a PX Domain-containing Protein, Interacts with Peroxiredoxin-3 through Pseudo-Kinase Domains

  • Liu, Lungling;Yang, Chenyi;Yuan, Jian;Chen, Xiujuan;Xu, Jianing;Wei, Youheng;Yang, Jingchun;Lin, Gang;Yu, Long
    • Molecules and Cells
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    • 제19권1호
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    • pp.39-45
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    • 2005
  • RPK118 is a sphingosine kinase-1-binding protein that has been implicated in sphingosine 1 phosphate-mediated signaling. It contains a PX (phox homology) domain and two pseudo-kinase domains, and co-localizes with sphingosine kinase-1 on early endosomes. In this study we identified a novel RPK118-binding protein, PRDX3 (peroxiredoxin-3), by yeast two-hybrid screening. The interaction between these proteins was confirmed by pull-down assays and co-immunoprecipitation experiments. Deletion studies showed that RPK118 interacted with PRDX3 through its pseudokinase domains, and with early endosomes through its PX domain. Double immunofluorescence experiments demonstrated that PRDX3 co-localized with RPK118 on early endosomes in COS7 cells. PRDX3 is a member of the antioxidant family of proteins synthesized in the cytoplasm and functioning in mitochondria. Our findings indicate that RPK118 is a PRDX3-binding protein that may be involved in transporting PRDX3 from the cytoplasm to its mitochondrial site of function or to other membrane structures via endosome trafficking.

GTP Binding Is Required for SEPT12 to Form Filaments and to Interact with SEPT11

  • Ding, Xiangming;Yu, Wenbo;Liu, Ming;Shen, ShuQing;Chen, Fang;Cao, Lihuan;Wan, Bo;Yu, Long
    • Molecules and Cells
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    • 제25권3호
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    • pp.385-389
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    • 2008
  • Septins are a family of filament-forming GTP-binding proteins involved in a variety of cellular process such as cytokinesis, exocytosis, and membrane dynamics. Here we report the biochemical and immunocytochemical characterization of a recently identified mammalian septin, SEPT12. SEPT12 binds GTP in vitro, and a mutation (Gly56 to Asn) in the GTP-binding motif abolished binding. Immunocytochemical analysis revealed that wild-type SEPT12 formed filamentous structures when transiently expressed in Hela cells whereas $SEPT12^{G56A}$ generated large aggregates. In addition, wild-type SEPT12 failed to form filaments when coexpressed with $SEPT12^{G56A}$. We also observed that GTP-binding by SEPT12 is required for interaction with SEPT11 but not with itself.