The structure of the folded domain from the signature multifunctional protein ICP27 from herpes simplex virus-1 reveals an intertwined dimer.
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The KSHV RNA regulator ORF57: target specificity and its role in the viral life cycleHerpes simplex virus ICP27 regulates alternative pre-mRNA polyadenylation and splicing in a sequence-dependent manner.The ICP27 Homology Domain of the Human Cytomegalovirus Protein UL69 Adopts a Dimer-of-Dimers Structure.Overlapping motifs on the herpes viral proteins ICP27 and ORF57 mediate interactions with the mRNA export adaptors ALYREF and UIFThe crystal structure of KSHV ORF57 reveals dimeric active sites important for protein stability and function
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The structure of the folded domain from the signature multifunctional protein ICP27 from herpes simplex virus-1 reveals an intertwined dimer.
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The structure of the folded do ...... reveals an intertwined dimer.
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The structure of the folded do ...... reveals an intertwined dimer.
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The structure of the folded do ...... reveals an intertwined dimer.
@ast
The structure of the folded do ...... reveals an intertwined dimer.
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The structure of the folded do ...... reveals an intertwined dimer.
@ast
The structure of the folded do ...... reveals an intertwined dimer.
@en
P2093
P2860
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The structure of the folded do ...... 1 reveals an intertwined dimer
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P2093
Mitchell Schacht
Richard B Tunnicliffe
Rozanne M Sandri-Goldin
Thomas A Jowitt
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P2888
P356
10.1038/SREP11234
P407
P577
2015-06-11T00:00:00Z