Prediction of avian influenza A binding preference to human receptor using conformational analysis of receptor bound to hemagglutinin
- Location
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Deutsche Nationalbibliothek Frankfurt am Main
- ISSN
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1471-2164
- Extent
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Online-Ressource
- Language
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Englisch
- Notes
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online resource.
- Bibliographic citation
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Prediction of avian influenza A binding preference to human receptor using conformational analysis of receptor bound to hemagglutinin ; volume:10 ; number:3 ; day:3 ; month:12 ; year:2009 ; pages:1-9 ; date:12.2009
BMC genomics ; 10, Heft 3 (3.12.2009), 1-9, 12.2009
- Creator
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Jongkon, Nipa
- Contributor
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Mokmak, Wanwimon
Chuakheaw, Daungmanee
Shaw, Philip J.
Tongsima, Sissades
Sangma, Chak
SpringerLink (Online service)
- DOI
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10.1186/1471-2164-10-S3-S24
- URN
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urn:nbn:de:1111-2016072811586
- Rights
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Der Zugriff auf das Objekt ist unbeschränkt möglich.
- Last update
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14.08.2025, 10:57 AM CEST
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Associated
- Jongkon, Nipa
- Mokmak, Wanwimon
- Chuakheaw, Daungmanee
- Shaw, Philip J.
- Tongsima, Sissades
- Sangma, Chak
- SpringerLink (Online service)
Other Objects (12)
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Effects of Receptor Specificity and Conformational Stability of Influenza A Virus Hemagglutinin on Infection and Activation of Different Cell Types in Human PBMCs
Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis
The T160A hemagglutinin substitution affects not only receptor binding property but also transmissibility of H5N1 clade 2.3.4 avian influenza virus in guinea pigs
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Studies on conformational stability of the ectodomain of influenza virus hemagglutinin
Host shifts and molecular evolution of H7 avian influenza virus hemagglutinin
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Conformational transitions and allosteric modulation in a heteromeric glycine receptor
Epistasis mediates the evolution of the receptor binding mode in recent human H3N2 hemagglutinin
Publisher Correction: Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis
Increased Conformational Flexibility of a Macrocycle–Receptor Complex Contributes to Reduced Dissociation Rates
Analysis of hemagglutinin-mediated entry tropism of H5N1 avian influenza
Effects of Receptor Specificity and Conformational Stability of Influenza A Virus Hemagglutinin on Infection and Activation of Different Cell Types in Human PBMCs
Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis
The T160A hemagglutinin substitution affects not only receptor binding property but also transmissibility of H5N1 clade 2.3.4 avian influenza virus in guinea pigs
Studies on conformational stability of the ectodomain of influenza virus hemagglutinin
Studies on conformational stability of the ectodomain of influenza virus hemagglutinin
Host shifts and molecular evolution of H7 avian influenza virus hemagglutinin
Ligand efficacy modulates conformational dynamics of the µ-opioid receptor
Conformational transitions and allosteric modulation in a heteromeric glycine receptor
Epistasis mediates the evolution of the receptor binding mode in recent human H3N2 hemagglutinin
Publisher Correction: Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis
Increased Conformational Flexibility of a Macrocycle–Receptor Complex Contributes to Reduced Dissociation Rates
Analysis of hemagglutinin-mediated entry tropism of H5N1 avian influenza
Effects of Receptor Specificity and Conformational Stability of Influenza A Virus Hemagglutinin on Infection and Activation of Different Cell Types in Human PBMCs
Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysis
The T160A hemagglutinin substitution affects not only receptor binding property but also transmissibility of H5N1 clade 2.3.4 avian influenza virus in guinea pigs
Studies on conformational stability of the ectodomain of influenza virus hemagglutinin
Studies on conformational stability of the ectodomain of influenza virus hemagglutinin
Host shifts and molecular evolution of H7 avian influenza virus hemagglutinin
Ligand efficacy modulates conformational dynamics of the µ-opioid receptor
Conformational transitions and allosteric modulation in a heteromeric glycine receptor
Epistasis mediates the evolution of the receptor binding mode in recent human H3N2 hemagglutinin