The Epstein-Barr virus polymerase accessory factor BMRF1 adopts a ring-shaped structure as visualized by electron microscopy.
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The Crystal Structure of PF-8, the DNA Polymerase Accessory Subunit from Kaposi's Sarcoma-Associated HerpesvirusCrystal Structure of Epstein-Barr Virus DNA Polymerase Processivity Factor BMRF1Regulated transport into the nucleus of herpesviridae DNA replication core proteins.Epstein-Barr viral productive amplification reprograms nuclear architecture, DNA replication, and histone deposition.Spatiotemporally different DNA repair systems participate in Epstein-Barr virus genome maturation.Tetrameric ring formation of Epstein-Barr virus polymerase processivity factor is crucial for viral replication.
P2860
The Epstein-Barr virus polymerase accessory factor BMRF1 adopts a ring-shaped structure as visualized by electron microscopy.
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The Epstein-Barr virus polymer ...... alized by electron microscopy.
@en
type
label
The Epstein-Barr virus polymer ...... alized by electron microscopy.
@en
prefLabel
The Epstein-Barr virus polymer ...... alized by electron microscopy.
@en
P2093
P2860
P356
P1476
The Epstein-Barr virus polymer ...... alized by electron microscopy.
@en
P2093
Alexander M Makhov
Deepa Subramanian
Elizabeth Holley-Guthrie
Jack D Griffith
Shannon C Kenney
P2860
P304
40358-40361
P356
10.1074/JBC.M408733200
P407
P577
2004-07-30T00:00:00Z