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  1. AU=Kodoyianni Voula
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  1. Article ; Online: Label-free analysis of biomolecular interactions using SPR imaging.

    Kodoyianni, Voula

    BioTechniques

    2011  Volume 50, Issue 1, Page(s) 32–40

    Abstract: Surface plasmon resonance (SPR) is a label-free detection method by which molecular interactions may be analyzed on a surface. Binding data are collected in real time, allowing the determination of interaction kinetics. SPR imaging (SPRi), the focus of ... ...

    Abstract Surface plasmon resonance (SPR) is a label-free detection method by which molecular interactions may be analyzed on a surface. Binding data are collected in real time, allowing the determination of interaction kinetics. SPR imaging (SPRi), the focus of this review, improves upon the efficiency of SPR by facilitating analysis of multiple interactions simultaneously. Here we summarize the principles of SPRi, provide examples of how SPRi arrays can be fabricated, and illustrate the utility of SPRi through example applications from the fields of proteomics, genomics and bioengineering.
    MeSH term(s) Binding Sites ; Bioengineering ; Biomarkers/chemistry ; Genomics ; Gold/chemistry ; Kinetics ; Proteomics ; Surface Plasmon Resonance/instrumentation ; Surface Plasmon Resonance/methods
    Chemical Substances Biomarkers ; Gold (7440-57-5)
    Language English
    Publishing date 2011-01
    Publishing country England
    Document type Journal Article ; Research Support, U.S. Gov't, Non-P.H.S. ; Review
    ZDB-ID 48453-2
    ISSN 1940-9818 ; 0736-6205
    ISSN (online) 1940-9818
    ISSN 0736-6205
    DOI 10.2144/000113569
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    In stock of ZB MED Cologne/Königswinter

    Zs.A 2435: Show issues Location:
    Je nach Verfügbarkeit (siehe Angabe bei Bestand)
    bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular
    Jg. 1995 - 2021: Lesesall (2.OG)
    ab Jg. 2022: Lesesaal (EG)

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  2. Article: Specific capture of mammalian cells by cell surface receptor binding to ligand immobilized on gold thin films.

    Peelen, Dora / Kodoyianni, Voula / Lee, Jieun / Zheng, Ting / Shortreed, Michael R / Smith, Lloyd M

    Journal of proteome research

    2006  Volume 5, Issue 7, Page(s) 1580–1585

    Abstract: Aldehyde-terminated self-assembled monolayers (SAMs) on gold surfaces were modified with proteins and employed to capture intact living cells through specific ligand-cell surface receptor interactions. In our model system, the basic fibroblast growth ... ...

    Abstract Aldehyde-terminated self-assembled monolayers (SAMs) on gold surfaces were modified with proteins and employed to capture intact living cells through specific ligand-cell surface receptor interactions. In our model system, the basic fibroblast growth factor (bFGF) binding receptor was targeted on baby hamster kidney (BHK-21) cells. Negative control and target proteins were immobilized on a gold surface by coupling protein primary amines to surface aldehyde groups. Cell-binding was monitored by phase contrast microscopy or surface plasmon resonance (SPR) imaging. The specificity of the receptor-ligand interaction was confirmed by the lack of cell binding to the negative control proteins, cytochrome c and insulin, and by the disruption of cell binding by treatment with heparitinase to destroy heparan sulfate which plays an essential role in the binding of bFGF to FGF receptors. This approach can simultaneously probe a large number of receptor-ligand interactions in cell populations and has potential for targeting and isolating cells from mixtures according to the receptors expressed on their surface.
    MeSH term(s) Animals ; Cell Adhesion/drug effects ; Cell Culture Techniques ; Cell Line ; Cricetinae ; Culture Media/chemistry ; Cytochromes c/metabolism ; Dose-Response Relationship, Drug ; Fibroblast Growth Factor 2/genetics ; Fibroblast Growth Factor 2/metabolism ; Gene Expression Profiling ; Gold/chemistry ; Heparitin Sulfate/metabolism ; Insulin/metabolism ; Kidney/cytology ; Ligands ; Polysaccharide-Lyases/pharmacology ; Protein Array Analysis ; Protein Binding/drug effects ; Receptors, Cell Surface/drug effects ; Receptors, Cell Surface/genetics ; Receptors, Cell Surface/metabolism ; Substrate Specificity
    Chemical Substances Culture Media ; Insulin ; Ligands ; Receptors, Cell Surface ; Fibroblast Growth Factor 2 (103107-01-3) ; Gold (7440-57-5) ; Cytochromes c (9007-43-6) ; Heparitin Sulfate (9050-30-0) ; Polysaccharide-Lyases (EC 4.2.2.-) ; heparitinsulfate lyase (EC 4.2.2.8)
    Language English
    Publishing date 2006-07-02
    Publishing country United States
    Document type Journal Article ; Research Support, N.I.H., Extramural ; Research Support, U.S. Gov't, Non-P.H.S.
    ZDB-ID 2078618-9
    ISSN 1535-3893
    ISSN 1535-3893
    DOI 10.1021/pr050467e
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Comparative genomics of Salmonella enterica serovar Typhi strains Ty2 and CT18.

    Deng, Wen / Liou, Shian-Ren / Plunkett, Guy / Mayhew, George F / Rose, Debra J / Burland, Valerie / Kodoyianni, Voula / Schwartz, David C / Blattner, Frederick R

    Journal of bacteriology

    2003  Volume 185, Issue 7, Page(s) 2330–2337

    Abstract: We present the 4.8-Mb complete genome sequence of Salmonella enterica serovar Typhi strain Ty2, a human-specific pathogen causing typhoid fever. A comparison with the genome sequence of recently isolated S. enterica serovar Typhi strain CT18 showed that ... ...

    Abstract We present the 4.8-Mb complete genome sequence of Salmonella enterica serovar Typhi strain Ty2, a human-specific pathogen causing typhoid fever. A comparison with the genome sequence of recently isolated S. enterica serovar Typhi strain CT18 showed that 29 of the 4,646 predicted genes in Ty2 are unique to this strain, while 84 genes are unique to CT18. Both genomes contain more than 200 pseudogenes; 9 of these genes in CT18 are intact in Ty2, while 11 intact CT18 genes are pseudogenes in Ty2. A half-genome interreplichore inversion in Ty2 relative to CT18 was confirmed. The two strains exhibit differences in prophages, insertion sequences, and island structures. While CT18 carries two plasmids, one conferring multiple drug resistance, Ty2 has no plasmids and is sensitive to antibiotics.
    MeSH term(s) Adenosine Triphosphatases/genetics ; Bacterial Proteins/genetics ; Chromosomes, Bacterial ; DNA Transposable Elements ; DNA-Binding Proteins ; Drug Resistance, Multiple, Bacterial/genetics ; Escherichia coli Proteins/genetics ; Genes, Bacterial ; Genome, Bacterial ; Genomics ; Molecular Sequence Data ; MutS DNA Mismatch-Binding Protein ; Nitrate Reductase ; Nitrate Reductases/genetics ; Plasmids/genetics ; Prophages/genetics ; Pseudogenes ; Salmonella typhi/genetics ; Sequence Analysis, DNA ; Sigma Factor/genetics
    Chemical Substances Bacterial Proteins ; DNA Transposable Elements ; DNA-Binding Proteins ; Escherichia coli Proteins ; Sigma Factor ; sigma factor KatF protein, Bacteria ; Nitrate Reductases (EC 1.7.-) ; Nitrate Reductase (EC 1.7.99.4) ; Adenosine Triphosphatases (EC 3.6.1.-) ; MutS DNA Mismatch-Binding Protein (EC 3.6.1.3) ; MutS protein, E coli (EC 3.6.1.3)
    Language English
    Publishing date 2003-04
    Publishing country United States
    Document type Comparative Study ; Journal Article ; Research Support, U.S. Gov't, P.H.S.
    ZDB-ID 2968-3
    ISSN 1098-5530 ; 0021-9193
    ISSN (online) 1098-5530
    ISSN 0021-9193
    DOI 10.1128/JB.185.7.2330-2337.2003
    Database MEDical Literature Analysis and Retrieval System OnLINE

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    Ud II Zs.50: Show issues Location:
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