A protein chip based inhibitor screening for influenza neuraminidases: the importance of glycan-specific recognition
Abstract A protein chip assay system based on a specific carbohydrate-protein interaction has been constructed for the identification of chemical inhibitors of influenza neuraminidase. The devised chip is composed of three layered proteins, that is, a matrix, a probe, and a neuraminidase protein. Tr...
Ausführliche Beschreibung
Autor*in: |
Lee, Jung-kyu [verfasserIn] |
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Format: |
E-Artikel |
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Sprache: |
Englisch |
Erschienen: |
2014 |
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Schlagwörter: |
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Anmerkung: |
© The Korean BioChip Society and Springer-Verlag Berlin Heidelberg 2014 |
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Übergeordnetes Werk: |
Enthalten in: BioChip journal - Seoul : Soc., 2007, 8(2014), 3 vom: Sept., Seite 209-217 |
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Übergeordnetes Werk: |
volume:8 ; year:2014 ; number:3 ; month:09 ; pages:209-217 |
Links: |
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DOI / URN: |
10.1007/s13206-014-8307-8 |
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Katalog-ID: |
SPR030869269 |
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245 | 1 | 2 | |a A protein chip based inhibitor screening for influenza neuraminidases: the importance of glycan-specific recognition |
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520 | |a Abstract A protein chip assay system based on a specific carbohydrate-protein interaction has been constructed for the identification of chemical inhibitors of influenza neuraminidase. The devised chip is composed of three layered proteins, that is, a matrix, a probe, and a neuraminidase protein. Transferrin, the matrix protein, was immobilized onto a chip panel to provide biological glycan chains. Fluorescence-labeled lectin or hemagglutinin was added as a glycan-interacting protein probe. Finally specific sialic acid moiety on the transferrin was then cleaved by an avian or human influenza neuraminidase. Each lectin or hemagglutinin showed different glycan specificity as a result of catalytic action of different influenza neuraminidase. Using this principle, we finally tested the neuraminidase of strain H1N1 as a model system to verify the screening capability of this protein chip approach. | ||
650 | 4 | |a Carbohydrate-protein interaction |7 (dpeaa)DE-He213 | |
650 | 4 | |a Drug screening |7 (dpeaa)DE-He213 | |
650 | 4 | |a Neuraminidase |7 (dpeaa)DE-He213 | |
650 | 4 | |a Protein chip |7 (dpeaa)DE-He213 | |
650 | 4 | |a Anti-viral |7 (dpeaa)DE-He213 | |
700 | 1 | |a Park, Chan-Won |4 aut | |
700 | 1 | |a Kwon, Hyuk-Ku |4 aut | |
700 | 1 | |a Jung, Seunho |4 aut | |
700 | 1 | |a Jeong, Hyun-Ja |4 aut | |
700 | 1 | |a Kang, In-Cheol |4 aut | |
700 | 1 | |a Choi, Youngjin |4 aut | |
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10.1007/s13206-014-8307-8 doi (DE-627)SPR030869269 (SPR)s13206-014-8307-8-e DE-627 ger DE-627 rakwb eng Lee, Jung-kyu verfasserin aut A protein chip based inhibitor screening for influenza neuraminidases: the importance of glycan-specific recognition 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Korean BioChip Society and Springer-Verlag Berlin Heidelberg 2014 Abstract A protein chip assay system based on a specific carbohydrate-protein interaction has been constructed for the identification of chemical inhibitors of influenza neuraminidase. The devised chip is composed of three layered proteins, that is, a matrix, a probe, and a neuraminidase protein. Transferrin, the matrix protein, was immobilized onto a chip panel to provide biological glycan chains. Fluorescence-labeled lectin or hemagglutinin was added as a glycan-interacting protein probe. Finally specific sialic acid moiety on the transferrin was then cleaved by an avian or human influenza neuraminidase. Each lectin or hemagglutinin showed different glycan specificity as a result of catalytic action of different influenza neuraminidase. Using this principle, we finally tested the neuraminidase of strain H1N1 as a model system to verify the screening capability of this protein chip approach. Carbohydrate-protein interaction (dpeaa)DE-He213 Drug screening (dpeaa)DE-He213 Neuraminidase (dpeaa)DE-He213 Protein chip (dpeaa)DE-He213 Anti-viral (dpeaa)DE-He213 Park, Chan-Won aut Kwon, Hyuk-Ku aut Jung, Seunho aut Jeong, Hyun-Ja aut Kang, In-Cheol aut Choi, Youngjin aut Enthalten in BioChip journal Seoul : Soc., 2007 8(2014), 3 vom: Sept., Seite 209-217 (DE-627)608497258 (DE-600)2513796-7 2092-7843 nnns volume:8 year:2014 number:3 month:09 pages:209-217 https://dx.doi.org/10.1007/s13206-014-8307-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 8 2014 3 09 209-217 |
spelling |
10.1007/s13206-014-8307-8 doi (DE-627)SPR030869269 (SPR)s13206-014-8307-8-e DE-627 ger DE-627 rakwb eng Lee, Jung-kyu verfasserin aut A protein chip based inhibitor screening for influenza neuraminidases: the importance of glycan-specific recognition 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Korean BioChip Society and Springer-Verlag Berlin Heidelberg 2014 Abstract A protein chip assay system based on a specific carbohydrate-protein interaction has been constructed for the identification of chemical inhibitors of influenza neuraminidase. The devised chip is composed of three layered proteins, that is, a matrix, a probe, and a neuraminidase protein. Transferrin, the matrix protein, was immobilized onto a chip panel to provide biological glycan chains. Fluorescence-labeled lectin or hemagglutinin was added as a glycan-interacting protein probe. Finally specific sialic acid moiety on the transferrin was then cleaved by an avian or human influenza neuraminidase. Each lectin or hemagglutinin showed different glycan specificity as a result of catalytic action of different influenza neuraminidase. Using this principle, we finally tested the neuraminidase of strain H1N1 as a model system to verify the screening capability of this protein chip approach. Carbohydrate-protein interaction (dpeaa)DE-He213 Drug screening (dpeaa)DE-He213 Neuraminidase (dpeaa)DE-He213 Protein chip (dpeaa)DE-He213 Anti-viral (dpeaa)DE-He213 Park, Chan-Won aut Kwon, Hyuk-Ku aut Jung, Seunho aut Jeong, Hyun-Ja aut Kang, In-Cheol aut Choi, Youngjin aut Enthalten in BioChip journal Seoul : Soc., 2007 8(2014), 3 vom: Sept., Seite 209-217 (DE-627)608497258 (DE-600)2513796-7 2092-7843 nnns volume:8 year:2014 number:3 month:09 pages:209-217 https://dx.doi.org/10.1007/s13206-014-8307-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 8 2014 3 09 209-217 |
allfields_unstemmed |
10.1007/s13206-014-8307-8 doi (DE-627)SPR030869269 (SPR)s13206-014-8307-8-e DE-627 ger DE-627 rakwb eng Lee, Jung-kyu verfasserin aut A protein chip based inhibitor screening for influenza neuraminidases: the importance of glycan-specific recognition 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Korean BioChip Society and Springer-Verlag Berlin Heidelberg 2014 Abstract A protein chip assay system based on a specific carbohydrate-protein interaction has been constructed for the identification of chemical inhibitors of influenza neuraminidase. The devised chip is composed of three layered proteins, that is, a matrix, a probe, and a neuraminidase protein. Transferrin, the matrix protein, was immobilized onto a chip panel to provide biological glycan chains. Fluorescence-labeled lectin or hemagglutinin was added as a glycan-interacting protein probe. Finally specific sialic acid moiety on the transferrin was then cleaved by an avian or human influenza neuraminidase. Each lectin or hemagglutinin showed different glycan specificity as a result of catalytic action of different influenza neuraminidase. Using this principle, we finally tested the neuraminidase of strain H1N1 as a model system to verify the screening capability of this protein chip approach. Carbohydrate-protein interaction (dpeaa)DE-He213 Drug screening (dpeaa)DE-He213 Neuraminidase (dpeaa)DE-He213 Protein chip (dpeaa)DE-He213 Anti-viral (dpeaa)DE-He213 Park, Chan-Won aut Kwon, Hyuk-Ku aut Jung, Seunho aut Jeong, Hyun-Ja aut Kang, In-Cheol aut Choi, Youngjin aut Enthalten in BioChip journal Seoul : Soc., 2007 8(2014), 3 vom: Sept., Seite 209-217 (DE-627)608497258 (DE-600)2513796-7 2092-7843 nnns volume:8 year:2014 number:3 month:09 pages:209-217 https://dx.doi.org/10.1007/s13206-014-8307-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 8 2014 3 09 209-217 |
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10.1007/s13206-014-8307-8 doi (DE-627)SPR030869269 (SPR)s13206-014-8307-8-e DE-627 ger DE-627 rakwb eng Lee, Jung-kyu verfasserin aut A protein chip based inhibitor screening for influenza neuraminidases: the importance of glycan-specific recognition 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Korean BioChip Society and Springer-Verlag Berlin Heidelberg 2014 Abstract A protein chip assay system based on a specific carbohydrate-protein interaction has been constructed for the identification of chemical inhibitors of influenza neuraminidase. The devised chip is composed of three layered proteins, that is, a matrix, a probe, and a neuraminidase protein. Transferrin, the matrix protein, was immobilized onto a chip panel to provide biological glycan chains. Fluorescence-labeled lectin or hemagglutinin was added as a glycan-interacting protein probe. Finally specific sialic acid moiety on the transferrin was then cleaved by an avian or human influenza neuraminidase. Each lectin or hemagglutinin showed different glycan specificity as a result of catalytic action of different influenza neuraminidase. Using this principle, we finally tested the neuraminidase of strain H1N1 as a model system to verify the screening capability of this protein chip approach. Carbohydrate-protein interaction (dpeaa)DE-He213 Drug screening (dpeaa)DE-He213 Neuraminidase (dpeaa)DE-He213 Protein chip (dpeaa)DE-He213 Anti-viral (dpeaa)DE-He213 Park, Chan-Won aut Kwon, Hyuk-Ku aut Jung, Seunho aut Jeong, Hyun-Ja aut Kang, In-Cheol aut Choi, Youngjin aut Enthalten in BioChip journal Seoul : Soc., 2007 8(2014), 3 vom: Sept., Seite 209-217 (DE-627)608497258 (DE-600)2513796-7 2092-7843 nnns volume:8 year:2014 number:3 month:09 pages:209-217 https://dx.doi.org/10.1007/s13206-014-8307-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 8 2014 3 09 209-217 |
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10.1007/s13206-014-8307-8 doi (DE-627)SPR030869269 (SPR)s13206-014-8307-8-e DE-627 ger DE-627 rakwb eng Lee, Jung-kyu verfasserin aut A protein chip based inhibitor screening for influenza neuraminidases: the importance of glycan-specific recognition 2014 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier © The Korean BioChip Society and Springer-Verlag Berlin Heidelberg 2014 Abstract A protein chip assay system based on a specific carbohydrate-protein interaction has been constructed for the identification of chemical inhibitors of influenza neuraminidase. The devised chip is composed of three layered proteins, that is, a matrix, a probe, and a neuraminidase protein. Transferrin, the matrix protein, was immobilized onto a chip panel to provide biological glycan chains. Fluorescence-labeled lectin or hemagglutinin was added as a glycan-interacting protein probe. Finally specific sialic acid moiety on the transferrin was then cleaved by an avian or human influenza neuraminidase. Each lectin or hemagglutinin showed different glycan specificity as a result of catalytic action of different influenza neuraminidase. Using this principle, we finally tested the neuraminidase of strain H1N1 as a model system to verify the screening capability of this protein chip approach. Carbohydrate-protein interaction (dpeaa)DE-He213 Drug screening (dpeaa)DE-He213 Neuraminidase (dpeaa)DE-He213 Protein chip (dpeaa)DE-He213 Anti-viral (dpeaa)DE-He213 Park, Chan-Won aut Kwon, Hyuk-Ku aut Jung, Seunho aut Jeong, Hyun-Ja aut Kang, In-Cheol aut Choi, Youngjin aut Enthalten in BioChip journal Seoul : Soc., 2007 8(2014), 3 vom: Sept., Seite 209-217 (DE-627)608497258 (DE-600)2513796-7 2092-7843 nnns volume:8 year:2014 number:3 month:09 pages:209-217 https://dx.doi.org/10.1007/s13206-014-8307-8 lizenzpflichtig Volltext GBV_USEFLAG_A SYSFLAG_A GBV_SPRINGER SSG-OLC-PHA GBV_ILN_11 GBV_ILN_20 GBV_ILN_22 GBV_ILN_23 GBV_ILN_24 GBV_ILN_31 GBV_ILN_32 GBV_ILN_39 GBV_ILN_40 GBV_ILN_60 GBV_ILN_62 GBV_ILN_63 GBV_ILN_65 GBV_ILN_69 GBV_ILN_70 GBV_ILN_73 GBV_ILN_74 GBV_ILN_90 GBV_ILN_95 GBV_ILN_100 GBV_ILN_101 GBV_ILN_105 GBV_ILN_110 GBV_ILN_120 GBV_ILN_138 GBV_ILN_150 GBV_ILN_151 GBV_ILN_161 GBV_ILN_170 GBV_ILN_171 GBV_ILN_187 GBV_ILN_213 GBV_ILN_224 GBV_ILN_230 GBV_ILN_250 GBV_ILN_281 GBV_ILN_285 GBV_ILN_293 GBV_ILN_370 GBV_ILN_602 GBV_ILN_636 GBV_ILN_702 GBV_ILN_2001 GBV_ILN_2003 GBV_ILN_2004 GBV_ILN_2005 GBV_ILN_2006 GBV_ILN_2007 GBV_ILN_2008 GBV_ILN_2009 GBV_ILN_2010 GBV_ILN_2011 GBV_ILN_2014 GBV_ILN_2015 GBV_ILN_2020 GBV_ILN_2021 GBV_ILN_2025 GBV_ILN_2026 GBV_ILN_2027 GBV_ILN_2031 GBV_ILN_2034 GBV_ILN_2037 GBV_ILN_2038 GBV_ILN_2039 GBV_ILN_2044 GBV_ILN_2048 GBV_ILN_2049 GBV_ILN_2050 GBV_ILN_2055 GBV_ILN_2057 GBV_ILN_2059 GBV_ILN_2061 GBV_ILN_2064 GBV_ILN_2065 GBV_ILN_2068 GBV_ILN_2070 GBV_ILN_2086 GBV_ILN_2088 GBV_ILN_2093 GBV_ILN_2106 GBV_ILN_2107 GBV_ILN_2108 GBV_ILN_2110 GBV_ILN_2111 GBV_ILN_2112 GBV_ILN_2113 GBV_ILN_2116 GBV_ILN_2118 GBV_ILN_2119 GBV_ILN_2122 GBV_ILN_2129 GBV_ILN_2143 GBV_ILN_2144 GBV_ILN_2147 GBV_ILN_2148 GBV_ILN_2152 GBV_ILN_2153 GBV_ILN_2188 GBV_ILN_2232 GBV_ILN_2336 GBV_ILN_2446 GBV_ILN_2470 GBV_ILN_2472 GBV_ILN_2507 GBV_ILN_2522 GBV_ILN_2548 GBV_ILN_4035 GBV_ILN_4037 GBV_ILN_4046 GBV_ILN_4112 GBV_ILN_4125 GBV_ILN_4242 GBV_ILN_4246 GBV_ILN_4249 GBV_ILN_4251 GBV_ILN_4305 GBV_ILN_4306 GBV_ILN_4307 GBV_ILN_4313 GBV_ILN_4322 GBV_ILN_4323 GBV_ILN_4324 GBV_ILN_4325 GBV_ILN_4326 GBV_ILN_4333 GBV_ILN_4334 GBV_ILN_4335 GBV_ILN_4336 GBV_ILN_4338 GBV_ILN_4393 GBV_ILN_4700 AR 8 2014 3 09 209-217 |
language |
English |
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Enthalten in BioChip journal 8(2014), 3 vom: Sept., Seite 209-217 volume:8 year:2014 number:3 month:09 pages:209-217 |
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Enthalten in BioChip journal 8(2014), 3 vom: Sept., Seite 209-217 volume:8 year:2014 number:3 month:09 pages:209-217 |
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topic_facet |
Carbohydrate-protein interaction Drug screening Neuraminidase Protein chip Anti-viral |
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Lee, Jung-kyu @@aut@@ Park, Chan-Won @@aut@@ Kwon, Hyuk-Ku @@aut@@ Jung, Seunho @@aut@@ Jeong, Hyun-Ja @@aut@@ Kang, In-Cheol @@aut@@ Choi, Youngjin @@aut@@ |
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2014-09-01T00:00:00Z |
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Lee, Jung-kyu |
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Lee, Jung-kyu misc Carbohydrate-protein interaction misc Drug screening misc Neuraminidase misc Protein chip misc Anti-viral A protein chip based inhibitor screening for influenza neuraminidases: the importance of glycan-specific recognition |
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A protein chip based inhibitor screening for influenza neuraminidases: the importance of glycan-specific recognition Carbohydrate-protein interaction (dpeaa)DE-He213 Drug screening (dpeaa)DE-He213 Neuraminidase (dpeaa)DE-He213 Protein chip (dpeaa)DE-He213 Anti-viral (dpeaa)DE-He213 |
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A protein chip based inhibitor screening for influenza neuraminidases: the importance of glycan-specific recognition |
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Lee, Jung-kyu Park, Chan-Won Kwon, Hyuk-Ku Jung, Seunho Jeong, Hyun-Ja Kang, In-Cheol Choi, Youngjin |
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protein chip based inhibitor screening for influenza neuraminidases: the importance of glycan-specific recognition |
title_auth |
A protein chip based inhibitor screening for influenza neuraminidases: the importance of glycan-specific recognition |
abstract |
Abstract A protein chip assay system based on a specific carbohydrate-protein interaction has been constructed for the identification of chemical inhibitors of influenza neuraminidase. The devised chip is composed of three layered proteins, that is, a matrix, a probe, and a neuraminidase protein. Transferrin, the matrix protein, was immobilized onto a chip panel to provide biological glycan chains. Fluorescence-labeled lectin or hemagglutinin was added as a glycan-interacting protein probe. Finally specific sialic acid moiety on the transferrin was then cleaved by an avian or human influenza neuraminidase. Each lectin or hemagglutinin showed different glycan specificity as a result of catalytic action of different influenza neuraminidase. Using this principle, we finally tested the neuraminidase of strain H1N1 as a model system to verify the screening capability of this protein chip approach. © The Korean BioChip Society and Springer-Verlag Berlin Heidelberg 2014 |
abstractGer |
Abstract A protein chip assay system based on a specific carbohydrate-protein interaction has been constructed for the identification of chemical inhibitors of influenza neuraminidase. The devised chip is composed of three layered proteins, that is, a matrix, a probe, and a neuraminidase protein. Transferrin, the matrix protein, was immobilized onto a chip panel to provide biological glycan chains. Fluorescence-labeled lectin or hemagglutinin was added as a glycan-interacting protein probe. Finally specific sialic acid moiety on the transferrin was then cleaved by an avian or human influenza neuraminidase. Each lectin or hemagglutinin showed different glycan specificity as a result of catalytic action of different influenza neuraminidase. Using this principle, we finally tested the neuraminidase of strain H1N1 as a model system to verify the screening capability of this protein chip approach. © The Korean BioChip Society and Springer-Verlag Berlin Heidelberg 2014 |
abstract_unstemmed |
Abstract A protein chip assay system based on a specific carbohydrate-protein interaction has been constructed for the identification of chemical inhibitors of influenza neuraminidase. The devised chip is composed of three layered proteins, that is, a matrix, a probe, and a neuraminidase protein. Transferrin, the matrix protein, was immobilized onto a chip panel to provide biological glycan chains. Fluorescence-labeled lectin or hemagglutinin was added as a glycan-interacting protein probe. Finally specific sialic acid moiety on the transferrin was then cleaved by an avian or human influenza neuraminidase. Each lectin or hemagglutinin showed different glycan specificity as a result of catalytic action of different influenza neuraminidase. Using this principle, we finally tested the neuraminidase of strain H1N1 as a model system to verify the screening capability of this protein chip approach. © The Korean BioChip Society and Springer-Verlag Berlin Heidelberg 2014 |
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title_short |
A protein chip based inhibitor screening for influenza neuraminidases: the importance of glycan-specific recognition |
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Park, Chan-Won Kwon, Hyuk-Ku Jung, Seunho Jeong, Hyun-Ja Kang, In-Cheol Choi, Youngjin |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">SPR030869269</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20230519121855.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">201007s2014 xx |||||o 00| ||eng c</controlfield><datafield tag="024" ind1="7" ind2=" "><subfield code="a">10.1007/s13206-014-8307-8</subfield><subfield code="2">doi</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)SPR030869269</subfield></datafield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(SPR)s13206-014-8307-8-e</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="100" ind1="1" ind2=" "><subfield code="a">Lee, Jung-kyu</subfield><subfield code="e">verfasserin</subfield><subfield code="4">aut</subfield></datafield><datafield tag="245" ind1="1" ind2="2"><subfield code="a">A protein chip based inhibitor screening for influenza neuraminidases: the importance of glycan-specific recognition</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">2014</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">Text</subfield><subfield code="b">txt</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">Computermedien</subfield><subfield code="b">c</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">Online-Ressource</subfield><subfield code="b">cr</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="500" ind1=" " ind2=" "><subfield code="a">© The Korean BioChip Society and Springer-Verlag Berlin Heidelberg 2014</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract A protein chip assay system based on a specific carbohydrate-protein interaction has been constructed for the identification of chemical inhibitors of influenza neuraminidase. The devised chip is composed of three layered proteins, that is, a matrix, a probe, and a neuraminidase protein. Transferrin, the matrix protein, was immobilized onto a chip panel to provide biological glycan chains. Fluorescence-labeled lectin or hemagglutinin was added as a glycan-interacting protein probe. Finally specific sialic acid moiety on the transferrin was then cleaved by an avian or human influenza neuraminidase. Each lectin or hemagglutinin showed different glycan specificity as a result of catalytic action of different influenza neuraminidase. Using this principle, we finally tested the neuraminidase of strain H1N1 as a model system to verify the screening capability of this protein chip approach.</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Carbohydrate-protein interaction</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Drug screening</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Neuraminidase</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Protein chip</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="650" ind1=" " ind2="4"><subfield code="a">Anti-viral</subfield><subfield code="7">(dpeaa)DE-He213</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Park, Chan-Won</subfield><subfield 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