Twelve receptor molecules attach per viral particle of human rhinovirus serotype 2 via multiple modules.
about
Viral entry pathways: the example of common cold virusesMinor group human rhinovirus-receptor interactions: geometry of multimodular attachment and basis of recognitionThe minor receptor group of human rhinovirus (HRV) includes HRV23 and HRV25, but the presence of a lysine in the VP1 HI loop is not sufficient for receptor bindingMultiple receptors involved in human rhinovirus attachment to live cells.A mutation in the first ligand-binding repeat of the human very-low-density lipoprotein receptor results in high-affinity binding of the single V1 module to human rhinovirus 2.Picornaviruses.Affinity capillary electrophoresis to evaluate the complex formation between poliovirus and nanobodies.Rhinovirus-stabilizing activity of artificial VLDL-receptor variants defines a new mechanism for virus neutralization by soluble receptors.Characterization of rhinovirus subviral A particles via capillary electrophoresis, electron microscopy and gas-phase electrophoretic mobility molecular analysis: Part I.
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P2860
Twelve receptor molecules attach per viral particle of human rhinovirus serotype 2 via multiple modules.
description
2004 nî lūn-bûn
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2004年の論文
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name
Twelve receptor molecules atta ...... rotype 2 via multiple modules.
@en
Twelve receptor molecules atta ...... rotype 2 via multiple modules.
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type
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Twelve receptor molecules atta ...... rotype 2 via multiple modules.
@en
Twelve receptor molecules atta ...... rotype 2 via multiple modules.
@nl
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Twelve receptor molecules atta ...... rotype 2 via multiple modules.
@en
Twelve receptor molecules atta ...... rotype 2 via multiple modules.
@nl
P2093
P2860
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Twelve receptor molecules atta ...... rotype 2 via multiple modules.
@en
P2093
Christian Rankl
Dieter Blaas
Ernst Kenndler
Leopold Kremser
Luc Snyers
Tünde Konecsni
P2860
P304
P356
10.1016/J.FEBSLET.2004.05.015
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P50
P577
2004-06-01T00:00:00Z