Characterization of the betaherpesviral pUL69 protein family reveals binding of the cellular mRNA export factor UAP56 as a prerequisite for stimulation of nuclear mRNA export and for efficient viral replication.
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A Sub-Element in PRE enhances nuclear export of intronless mRNAs by recruiting the TREX complex via ZC3H18The many roles of the highly interactive HSV protein ICP27, a key regulator of infection.pUL69 of Human Cytomegalovirus Recruits the Cellular Protein Arginine Methyltransferase 6 via a Domain That Is Crucial for mRNA Export and Efficient Viral ReplicationTransfer of the UAP56 interaction motif of human cytomegalovirus pUL69 to its murine cytomegalovirus homolog converts the protein into a functional mRNA export factor that can substitute for pUL69 during viral infectionThe ICP27 Homology Domain of the Human Cytomegalovirus Protein UL69 Adopts a Dimer-of-Dimers Structure.
P2860
Characterization of the betaherpesviral pUL69 protein family reveals binding of the cellular mRNA export factor UAP56 as a prerequisite for stimulation of nuclear mRNA export and for efficient viral replication.
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2010 nî lūn-bûn
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2010年の論文
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2010年学术文章
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Characterization of the betahe ...... r efficient viral replication.
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Characterization of the betahe ...... r efficient viral replication.
@en
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Characterization of the betahe ...... r efficient viral replication.
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P2093
P2860
P356
P1433
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Characterization of the betahe ...... r efficient viral replication.
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P2093
Antje Giede-Jeppe
Barbara Zielke
Marco Thomas
Regina Müller
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P304
P356
10.1128/JVI.01347-10
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P577
2010-12-08T00:00:00Z