Nature, Količina 427Sir Norman Lockyer Macmillan Journals Limited, 2004 |
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Zadetki 1–3 od 67
Stran 312
... fusion loops ' at one end , to insert into the host - cell membrane . Their structure allows us to model directly how these fusion loops interact with a lipid bilayer . The protein folds back on itself , directing its carboxy terminus ...
... fusion loops ' at one end , to insert into the host - cell membrane . Their structure allows us to model directly how these fusion loops interact with a lipid bilayer . The protein folds back on itself , directing its carboxy terminus ...
Stran 317
... fusion . ( 1 ) E associates with a cell - surface receptor , probably through domain III22-28 ( Fig . 5a ) ; there is evidence for glycan - mediated interactions as well29-31 . Receptor binding leads to endosomal uptake . ( 2 ) Reduced ...
... fusion . ( 1 ) E associates with a cell - surface receptor , probably through domain III22-28 ( Fig . 5a ) ; there is evidence for glycan - mediated interactions as well29-31 . Receptor binding leads to endosomal uptake . ( 2 ) Reduced ...
Stran 320
... fusion pore . Here we report the crystal structure of the ectodomain of the Semliki Forest virus fusion glycoprotein E1 in its low - pH - induced trimeric form . E1 adopts a folded - back conformation that , in the final post - fusion ...
... fusion pore . Here we report the crystal structure of the ectodomain of the Semliki Forest virus fusion glycoprotein E1 in its low - pH - induced trimeric form . E1 adopts a folded - back conformation that , in the final post - fusion ...
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