Taipei Medical University

A B C D E F G H I J K L M N O P Q R S T U V W X Y Z
S.Chen, C.N. Lee, W.R. Lee, K. McIntosh, and T.H. Lee
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------>journal_name=J. Virol
------>paper_name=Mutational analysis of the leucine zipper-like motif of the human immunodeficiency virus type 1 envelope transmembrane glycoprotein
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------>fullAbstract=The N-terminal region of the envelope (env) transmembrane protein of human immunodeficiency virus type 1 (HIV-1) has a leucine zipper-like motif. This highly conserved zipper motif, which consists of a heptad repeat of leucine or isoleucine residues, has been suggested to play a role in HIV-1 env glycoprotein oligomerization. This hypothesis was tested by replacing the highly conserved leucine or isoleucine residues in the zipper motif with a strong alpha-helix breaker, proline. We report here that such substitutions did not abolish the ability of env protein to form oligomers, indicating that this highly conserved zipper motif does not have a crucial role in env protein oligomerization. However, the mutant viruses all showed impaired infectivity, suggesting that this conserved zipper motif can have an important role in the virus life cycle.
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------>authors=S.Chen, C.N. Lee, W.R. Lee, K. McIntosh, and T.H. Lee
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------>updateTitle=Mutational analysis of the leucine zipper-like motif of the human immunodeficiency virus type 1 envelope transmembrane glycoprotein.
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------>publish_year=1993
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A B C D E F G H I J K L M N O P Q R S T U V W X Y Z