Glycan shield and fusion activation of a deltacoronavirus spike glycoprotein fine-tuned for enteric infections.
about
Cryo-EM structure of infectious bronchitis coronavirus spike protein reveals structural and functional evolution of coronavirus spike proteins.Contribution of porcine aminopeptidase N to porcine deltacoronavirus infection.Broad receptor engagement of an emerging global coronavirus may potentiate its diverse cross-species transmissibility.Porcine deltacoronavirus engages the transmissible gastroenteritis virus functional receptor porcine aminopeptidase N for infectious cellular entry.Stabilized coronavirus spikes are resistant to conformational changes induced by receptor recognition or proteolysisCryo-EM structure of the SARS coronavirus spike glycoprotein in complex with its host cell receptor ACE2
P2860
Glycan shield and fusion activation of a deltacoronavirus spike glycoprotein fine-tuned for enteric infections.
description
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Glycan shield and fusion activ ...... -tuned for enteric infections.
@en
Glycan shield and fusion activ ...... -tuned for enteric infections.
@nl
type
label
Glycan shield and fusion activ ...... -tuned for enteric infections.
@en
Glycan shield and fusion activ ...... -tuned for enteric infections.
@nl
prefLabel
Glycan shield and fusion activ ...... -tuned for enteric infections.
@en
Glycan shield and fusion activ ...... -tuned for enteric infections.
@nl
P2093
P2860
P50
P356
P1433
P1476
Glycan Shield and Fusion Activ ...... e-Tuned for Enteric Infections
@en
P2093
Berend-Jan Bosch
Craig Yoshioka
David Veesler
Félix A Rey
Joost Snijder
Xiaoli Xiong
P2860
P356
10.1128/JVI.01628-17
P407
P577
2018-01-30T00:00:00Z