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.
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Mechanisms of coronavirus cell entry mediated by the viral spike proteinThe 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 mechanismThe amino terminus of Epstein-Barr virus glycoprotein gH is important for fusion with epithelial and B cells.Activity of the Mason-Pfizer monkey virus fusion protein is modulated by single amino acids in the cytoplasmic tail.Coronavirus pathogenesis and the emerging pathogen severe acute respiratory syndrome coronavirus.Variable sensitivity to substitutions in the N-terminal heptad repeat of Mason-Pfizer monkey virus transmembrane protein.Amino acid substitutions in the S2 subunit of mouse hepatitis virus variant V51 encode determinants of host range expansionSARS coronavirus spike protein-induced innate immune response occurs via activation of the NF-kappaB pathway in human monocyte macrophages in vitro.The N-terminal domain of the murine coronavirus spike glycoprotein determines the CEACAM1 receptor specificity of the virus strain.Functional importance of the coiled-coil of the Ebola virus glycoprotein.Conformational changes in the spike glycoprotein of murine coronavirus are induced at 37 degrees C either by soluble murine CEACAM1 receptors or by pH 8.Recombinant avian infectious bronchitis virus expressing a heterologous spike gene demonstrates that the spike protein is a determinant of cell tropismSynthesis and characterization of a native, oligomeric form of recombinant severe acute respiratory syndrome coronavirus spike glycoprotein.Important role for the transmembrane domain of severe acute respiratory syndrome coronavirus spike protein during entry.Conserved leucines in N-terminal heptad repeat HR1 of envelope fusion protein F of group II nucleopolyhedroviruses are important for correct processing and essential for fusogenicity.GxxxG motif of severe acute respiratory syndrome coronavirus spike glycoprotein transmembrane domain is not involved in trimerization and is not important for entry.Poplar metal tolerance protein 1 confers zinc tolerance and is an oligomeric vacuolar zinc transporter with an essential leucine zipper motif.Rotation-Activated and Cooperative Zipping Characterize Class I Viral Fusion Protein Dynamics.
P2860
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P2860
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.
description
1999 nî lūn-bûn
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1999年の論文
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1999年論文
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1999年論文
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1999年論文
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1999年論文
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Amino acid substitutions withi ...... to induce cell-to-cell fusion.
@en
Amino acid substitutions withi ...... to induce cell-to-cell fusion.
@nl
type
label
Amino acid substitutions withi ...... to induce cell-to-cell fusion.
@en
Amino acid substitutions withi ...... to induce cell-to-cell fusion.
@nl
prefLabel
Amino acid substitutions withi ...... to induce cell-to-cell fusion.
@en
Amino acid substitutions withi ...... to induce cell-to-cell fusion.
@nl
P2093
P2860
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P1476
Amino acid substitutions withi ...... to induce cell-to-cell fusion.
@en
P2093
P2860
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1999-10-01T00:00:00Z