Author: Qiao, Hui; Pelletier, Sandra L.; Hoffman, Lucas; Hacker, Jill; Armstrong, R. Todd; White, Judith M.
Title: Specific Single or Double Proline Substitutions in the “Spring-loaded” Coiled-Coil Region of the Influenza Hemagglutinin Impair or Abolish Membrane Fusion Activity Document date: 1998_6_15
ID: 78fjem8s_39
Snippet: Collectively, the results presented in Figs. 2 and 3 indicate that: ( a ) The introduction of specific mutations into HA2 54-81 can affect the glycosylation pattern of HA, likely by affecting the packing of the globular head domains ( Fig. 1) . ( b ) In some cases, notably V55P, the mutations appear to affect susceptibility to trypsin activation. Nonetheless, ( c ) all of the mutant HAs can be expressed at the cell surface and can be cleaved to H.....
Document: Collectively, the results presented in Figs. 2 and 3 indicate that: ( a ) The introduction of specific mutations into HA2 54-81 can affect the glycosylation pattern of HA, likely by affecting the packing of the globular head domains ( Fig. 1) . ( b ) In some cases, notably V55P, the mutations appear to affect susceptibility to trypsin activation. Nonetheless, ( c ) all of the mutant HAs can be expressed at the cell surface and can be cleaved to HA1 and HA2. Furthermore, ( d ) mutants substituted with either coiled-coil facilitators (Ala) or coiled-coil inhibitors (Pro) form stable trimers.
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