Dimerization of the papillomavirus E2 protein is required for efficient mitotic chromosome association and Brd4 binding.
about
Analysis of the papillomavirus E2 and bromodomain protein Brd4 interaction using bimolecular fluorescence complementationPapillomavirus genomes associate with BRD4 to replicate at fragile sites in the host genome.Papillomavirus interaction with cellular chromatin.A point mutation in the DNA-binding domain of HPV-2 E2 protein increases its DNA-binding capacity and reverses its transcriptional regulatory activity on the viral early promoter.Recruitment of Brd4 to the human papillomavirus type 16 DNA replication complex is essential for replication of viral DNA.Replication and partitioning of papillomavirus genomes.Failure to interact with Brd4 alters the ability of HPV16 E2 to regulate host genome expression and cellular movementCurrent understanding of the role of the Brd4 protein in the papillomavirus lifecycle.DNA Damage Reduces the Quality, but Not the Quantity of Human Papillomavirus 16 E1 and E2 DNA ReplicationHitchhiking on host chromatin: how papillomaviruses persist.Tumor suppressor or oncogene? A critical role of the human papillomavirus (HPV) E2 protein in cervical cancer progression.Evidence supporting a role for TopBP1 and Brd4 in the initiation but not continuation of human papillomavirus 16 E1/E2-mediated DNA replication.The human papillomavirus type 8 E2 tethering protein targets the ribosomal DNA loci of host mitotic chromosomes.Interaction of the betapapillomavirus E2 tethering protein with mitotic chromosomes.
P2860
Q28534628-7B2E95F6-1380-46FA-81AC-C47D65183B46Q31161320-9A5FA1A6-3252-4A48-8FA7-F843F94D765FQ33729502-CC223540-763E-495B-B171-A42533991254Q34158732-744EBFDC-0886-4E57-BD0D-AF3856E85FCAQ34568110-3CB966AC-818F-4168-B670-9FAC9571F45FQ35150925-C77A87C7-6335-467C-9E82-ED209FBF332FQ36943823-F32B161D-6555-4AEE-AE71-4F10787405AEQ37030691-9A54140A-8242-48D5-B909-959471806E0EQ37049984-DA0EFA3A-8CC7-41D9-B063-AC03A6EEC338Q37981512-178F4912-1396-44CC-9AA2-C735CA16A244Q38561398-6ACB9528-51A7-424A-BBF8-BA16F1F6C608Q39037424-7BA147E0-9534-4D89-A6BF-896FAA9B16C0Q39917723-48BF1461-1EF7-4E4A-B18D-5A251C3185A3Q42947239-5CF7D270-A855-43A9-BFAA-9F65D42DA197
P2860
Dimerization of the papillomavirus E2 protein is required for efficient mitotic chromosome association and Brd4 binding.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年論文
@yue
2008年論文
@zh-hant
2008年論文
@zh-hk
2008年論文
@zh-mo
2008年論文
@zh-tw
2008年论文
@wuu
2008年论文
@zh
2008年论文
@zh-cn
name
Dimerization of the papillomav ...... association and Brd4 binding.
@ast
Dimerization of the papillomav ...... association and Brd4 binding.
@en
type
label
Dimerization of the papillomav ...... association and Brd4 binding.
@ast
Dimerization of the papillomav ...... association and Brd4 binding.
@en
prefLabel
Dimerization of the papillomav ...... association and Brd4 binding.
@ast
Dimerization of the papillomav ...... association and Brd4 binding.
@en
P2093
P2860
P356
P1433
P1476
Dimerization of the papillomav ...... association and Brd4 binding.
@en
P2093
Alison A McBride
Jonathan E Spindler
Juan Cardenas-Mora
Moon Kyoo Jang
P2860
P304
P356
10.1128/JVI.00772-08
P407
P577
2008-05-21T00:00:00Z