trypsin cleavage
Trypsin Cleavage Stabilizes the Rotavirus VP4 Spike
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Antibodies to the trypsin cleavage peptide VP8 neutralize rotavirus by inhibiting binding of virions to target cells in culture.
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Location of intrachain disulfide bonds in the VP5* and VP8* trypsin cleavage fragments of the rhesus rotavirus spike protein VP4.
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A comparison of the folding characteristics of free and ribosome-tethered polypeptide chains using limited proteolysis and mass spectrometry.
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Trypsin activation pathway of rotavirus infectivity.
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Presence of a Surface-Exposed Loop Facilitates Trypsinization of Particles of Sinsiro Virus, a Genogroup II.3 Norovirus
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Identification of an Epitope Common to Genogroup 1 “Norwalk Like Viruses”
5
A Metastable Form of the Large Envelope Protein of Duck Hepatitis B Virus: Low-pH Release Results in a Transition to a Hydrophobic, Potentially Fusogenic Conformation
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Specific proteolytic cleavage of recombinant Norwalk virus capsid protein.
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Proteolytic Activation of the Porcine Epidemic Diarrhea Coronavirus Spike Fusion Protein by Trypsin in Cell Culture
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A Single Point Mutation Creating a Furin Cleavage Site in the Spike Protein Renders Porcine Epidemic Diarrhea Coronavirus Trypsin Independent for Cell Entry and Fusion
5
Embryo signals for successful implantation
225
Cleavage and Activation of the Severe Acute Respiratory Syndrome Coronavirus Spike Protein by Human Airway Trypsin-Like Protease
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Comparative analysis of trypsin inhibitor activity in common pulses and its partial purification
5
Trypsin Inhibitors of Human Serum I Standardization Mechanism of Reaction, and Normal Values
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Effects of antibodies, trypsin, and trypsin inhibitors on susceptibility of neonates to rotavirus infection
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Genomic analysis of the tryptome reveals molecular mechanisms of gland cell evolution
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VP2 Cleavage and the Leucine Ring at the Base of the Fivefold Cylinder Control pH-Dependent Externalization of both the VP1 N Terminus and the Genome of Minute Virus of Mice
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Modification of the Trypsin-Dependent Cleavage Activation Site of the Human Metapneumovirus Fusion Protein To Be Trypsin Independent Does Not Increase Replication or Spread in Rodents or Nonhuman Primates
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A vitellogenin polyserine cleavage site: highly disordered conformation protected from proteolysis by phosphorylation
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