The S2 subunit of the murine coronavirus spike protein is not involved in receptor binding.
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Current advancements and potential strategies in the development of MERS-CoV vaccinesThe Coronavirus Spike Protein Is a Class I Virus Fusion Protein: Structural and Functional Characterization of the Fusion Core ComplexIdentification of the membrane-active regions of the severe acute respiratory syndrome coronavirus spike membrane glycoprotein using a 16/18-mer peptide scan: implications for the viral fusion mechanismIdentification and characterization of the putative fusion peptide of the severe acute respiratory syndrome-associated coronavirus spike proteinCoronavirus pathogenesis and the emerging pathogen severe acute respiratory syndrome coronavirus.Severe acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides.Identification of an antigenic determinant on the S2 domain of the severe acute respiratory syndrome coronavirus spike glycoprotein capable of inducing neutralizing antibodies.Structural characterization of the fusion-active complex of severe acute respiratory syndrome (SARS) coronavirus.Receptor-independent infection of murine coronavirus: analysis by spinoculationBinding of avian coronavirus spike proteins to host factors reflects virus tropism and pathogenicity.Analysis of the receptor-binding site of murine coronavirus spike proteinMurine coronavirus membrane fusion is blocked by modification of thiols buried within the spike proteinAmino acid substitutions in the S2 subunit of mouse hepatitis virus variant V51 encode determinants of host range expansionIdentification of spike protein residues of murine coronavirus responsible for receptor-binding activity by use of soluble receptor-resistant mutants.Human respiratory coronavirus OC43: genetic stability and neuroinvasion.Inhibition of severe acute respiratory syndrome-associated coronavirus (SARS-CoV) infectivity by peptides analogous to the viral spike protein.Amino acid substitutions within the leucine zipper domain of the murine coronavirus spike protein cause defects in oligomerization and the ability to induce cell-to-cell fusion.A role for naturally occurring variation of the murine coronavirus spike protein in stabilizing association with the cellular receptor.The murine coronavirus mouse hepatitis virus strain A59 from persistently infected murine cells exhibits an extended host range.Coronavirus spike glycoprotein, extended at the carboxy terminus with green fluorescent protein, is assembly competent.
P2860
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P2860
The S2 subunit of the murine coronavirus spike protein is not involved in receptor binding.
description
1995 nî lūn-bûn
@nan
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
1995年论文
@zh
1995年论文
@zh-cn
name
The S2 subunit of the murine c ...... involved in receptor binding.
@ast
The S2 subunit of the murine c ...... involved in receptor binding.
@en
type
label
The S2 subunit of the murine c ...... involved in receptor binding.
@ast
The S2 subunit of the murine c ...... involved in receptor binding.
@en
prefLabel
The S2 subunit of the murine c ...... involved in receptor binding.
@ast
The S2 subunit of the murine c ...... involved in receptor binding.
@en
P2860
P1433
P1476
The S2 subunit of the murine c ...... t involved in receptor binding
@en
P2093
P2860
P304
P407
P577
1995-11-01T00:00:00Z