The bovine papillomavirus E2 protein modulates the assembly of but is not stably maintained in a replication-competent multimeric E1-replication origin complex.
about
Two classes of human papillomavirus type 16 E1 mutants suggest pleiotropic conformational constraints affecting E1 multimerization, E2 interaction, and interaction with cellular proteinsEffect of bovine papillomavirus E2 protein-specific monoclonal antibodies on papillomavirus DNA replication.Crystal structures of two intermediates in the assembly of the papillomavirus replication initiation complex.The DNA-binding domain of human papillomavirus type 18 E1. Crystal structure, dimerization, and DNA bindingNuclear accumulation of the papillomavirus E1 helicase blocks S-phase progression and triggers an ATM-dependent DNA damage responseCellular topoisomerase I modulates origin binding by bovine papillomavirus type 1 E1.Identification, purification, and molecular cloning of autonomously replicating sequence-binding protein 1 from fission yeast Schizosaccharomyces pombe.Transient viral DNA replication and repression of viral transcription are supported by the C-terminal domain of the bovine papillomavirus type 1 E1 protein.Characterization of the DNA-binding domain of the bovine papillomavirus replication initiator E1.A C-terminal helicase domain of the human papillomavirus E1 protein binds E2 and the DNA polymerase alpha-primase p68 subunit.Identification of domains of the human papillomavirus type 11 E1 helicase involved in oligomerization and binding to the viral origin.Role of the ATP-binding domain of the human papillomavirus type 11 E1 helicase in E2-dependent binding to the originThe E1 initiator recognizes multiple overlapping sites in the papillomavirus origin of DNA replication.Nuclear export of human papillomavirus type 31 E1 is regulated by Cdk2 phosphorylation and required for viral genome maintenance.Sequential and ordered assembly of E1 initiator complexes on the papillomavirus origin of DNA replication generates progressive structural changes related to melting.E1 initiator DNA binding specificity is unmasked by selective inhibition of non-specific DNA binding.Development of quantitative and high-throughput assays of polyomavirus and papillomavirus DNA replicationMutational analysis of the 18-base-pair inverted repeat element at the bovine papillomavirus origin of replication: identification of critical sequences for E1 binding and in vivo replicationCellular factors required for papillomavirus DNA replication.Functional interactions between papillomavirus E1 and E2 proteins.Bovine papillomavirus type 1 E1 and simian virus 40 large T antigen share regions of sequence similarity required for multiple functions.The initiator protein E1 binds to the bovine papillomavirus origin of replication as a trimeric ring-like structureRecent advances in the search for antiviral agents against human papillomaviruses.CK2 phosphorylation inactivates DNA binding by the papillomavirus E1 and E2 proteins.The E1 proteins.The X-ray structure of the papillomavirus helicase in complex with its molecular matchmaker E2.Characterization of recombinant HPV6 and 11 E1 helicases: effect of ATP on the interaction of E1 with E2 and mapping of a minimal helicase domain.Biochemical and electron microscopic image analysis of the hexameric E1 helicase.Transcription factor YY1 represses cell-free replication from human papillomavirus origins.Transcriptional and replicational activation functions in the bovine papillomavirus type 1 E2 protein are encoded by different structural determinants.A fifteen-amino-acid peptide inhibits human papillomavirus E1-E2 interaction and human papillomavirus DNA replication in vitro.Distinct roles of two binding sites for the bovine papillomavirus (BPV) E2 transactivator on BPV DNA replication.The hinge of the human papillomavirus type 11 E2 protein contains major determinants for nuclear localization and nuclear matrix associationChaperone proteins abrogate inhibition of the human papillomavirus (HPV) E1 replicative helicase by the HPV E2 protein.Characterization of the minimal DNA binding domain of the human papillomavirus e1 helicase: fluorescence anisotropy studies and characterization of a dimerization-defective mutant proteinTopography of bovine papillomavirus E2 protein on the viral genome during the cell cycle.E1 recognition sequences in the bovine papillomavirus type 1 origin of DNA replication: interaction between half sites of the inverted repeats.Amino-terminal domains of the bovine papillomavirus type 1 E1 and E2 proteins participate in complex formation.AP1 enhances polyomavirus DNA replication by promoting T-antigen-mediated unwinding of DNATranscriptional activation function is not required for stimulation of DNA replication by bovine papillomavirus type 1 E2.
P2860
Q24317609-27FB9E9A-00DA-4542-9FD7-94FBF63FB055Q24527237-1C9AD0E4-47EE-4CF6-9C3D-A45F499B8BA8Q27638318-508E8752-B6F3-4ADA-8AA8-238094A6B9B3Q27642462-08F49682-8880-4983-B4E7-2899D076F39BQ28740849-30FC19EF-0BE8-45AF-B009-FA3DC7266A42Q33239795-F8BA1AE1-CF73-43A3-90D1-A6F7841A5644Q33633493-D28A0FCE-0A40-4030-A2F1-553DDAFE623CQ33782171-1D761197-F67E-4CF5-A793-FCE1460B192EQ33782934-2C088892-A245-4C81-96C9-EC8EF08A5D23Q33783875-B8E9CED8-3439-45A4-9B9A-63F4F5046916Q33809498-2E08B759-DBB8-41A7-AE4C-CDE554DFD724Q33814813-BE9915FE-70EB-4030-971F-ED1A010B53E8Q33834839-A05F9A0C-B599-4FCE-90AA-1095AA51FB9FQ34295899-857DA190-7A32-408A-99E5-B0DEBF723DD5Q34325784-9A574B23-14DF-4CB7-95DF-F1F3E85693D5Q34583176-08EB6DAD-C0AB-45DC-8208-591C706808D1Q35158114-295D5E98-BB73-4E58-9619-93458516673AQ35849102-5E634F1C-843B-4598-9E6B-6523FA2B9431Q35852375-0E17FB93-2407-4F2F-96DC-4D210041E723Q35883567-F6BC4C7E-86F4-4F4D-ADF5-B702D897EE65Q35895667-8C0A2B21-32F3-4E3E-AB79-F4458C8E5036Q35909239-18F80FCC-8C8D-46C3-A0AD-D668CED1924CQ36284493-395C0C2C-EF91-47C8-9D59-623175ACC4C8Q36978987-8D97E7DE-B7F7-4877-BB59-10DB0CA5E3FFQ37262962-A28EF9A2-D7BE-4031-B4B3-482277575EB4Q37480430-5695D28C-BADD-4D34-B897-EEABDA0E18DCQ38301958-B82CFD93-124F-4E7B-BD5D-5A6BE79A6498Q38328578-E9E4D638-4278-4E4E-AC28-2ACC6DF9FF98Q38337180-543A8627-1648-41D0-9915-435B2E95A7B2Q38353685-3549A426-25A3-44DF-8FE9-587E36BC904AQ39581284-C3915F60-5F3F-4E14-A5CD-2F0FB74DD4B1Q39581735-52826831-F5B1-4B32-965F-A2170D858DBDQ39590559-CA7E3068-3D6B-484D-A15B-A954094E9D8CQ39681443-E4403536-28F6-456D-8408-F90ACD8B3312Q39748610-BEE3EDAB-8CD3-4A16-8A1B-40B8B9FAF209Q39806563-53CE4856-FC4B-47AB-889A-E685CE9D9A54Q39870415-FDCD355D-83C1-4FFA-BE47-60D1CC3A8D96Q39870724-27DC62CB-0B91-486C-A899-8EE3F4E4DE5AQ39875386-93131A2A-B505-4396-830F-F54CFD540957Q39876630-B408CB2E-77B7-45EF-A880-185DBC9ECFFF
P2860
The bovine papillomavirus E2 protein modulates the assembly of but is not stably maintained in a replication-competent multimeric E1-replication origin complex.
description
1994 nî lūn-bûn
@nan
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
1994年论文
@zh
1994年论文
@zh-cn
name
The bovine papillomavirus E2 p ...... E1-replication origin complex.
@ast
The bovine papillomavirus E2 p ...... E1-replication origin complex.
@en
type
label
The bovine papillomavirus E2 p ...... E1-replication origin complex.
@ast
The bovine papillomavirus E2 p ...... E1-replication origin complex.
@en
prefLabel
The bovine papillomavirus E2 p ...... E1-replication origin complex.
@ast
The bovine papillomavirus E2 p ...... E1-replication origin complex.
@en
P2093
P2860
P356
P1476
The bovine papillomavirus E2 p ...... E1-replication origin complex.
@en
P2093
P2860
P304
P356
10.1073/PNAS.91.19.8895
P407
P577
1994-09-01T00:00:00Z