Characterization of the DNA-binding domain of the bovine papillomavirus replication initiator E1.
about
Crystal structures of two intermediates in the assembly of the papillomavirus replication initiation complex.The Crystal Structure of the SV40 T-Antigen Origin Binding Domain in Complex with DNATranscription activator structure reveals redox control of a replication initiation reactionStructure of the NS1 Protein N-Terminal Origin Recognition/Nickase Domain from the Emerging Human BocavirusTwo heads are better than one: regulation of DNA replication by hexameric helicasesCellular topoisomerase I modulates origin binding by bovine papillomavirus type 1 E1.Mismatch Repair proteins are recruited to replicating DNA through interaction with Proliferating Cell Nuclear Antigen (PCNA)A C-terminal helicase domain of the human papillomavirus E1 protein binds E2 and the DNA polymerase alpha-primase p68 subunit.Two patches of amino acids on the E2 DNA binding domain define the surface for interaction with E1.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.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.Replication and partitioning of papillomavirus genomes.Assessing parallel gene histories in viral genomesRecent advances in the search for antiviral agents against human papillomaviruses.CK2 phosphorylation inactivates DNA binding by the papillomavirus E1 and E2 proteins.The papillomavirus E2 proteinsThe E1 proteins.The X-ray structure of the papillomavirus helicase in complex with its molecular matchmaker E2.Dynamic look at DNA unwinding by a replicative helicase.Identification of a short, hydrophilic amino acid sequence critical for origin recognition by the bovine papillomavirus E1 protein.Functional mapping of the DNA binding domain of bovine papillomavirus E1 proteinPhosphorylation of simian virus 40 T antigen on Thr 124 selectively promotes double-hexamer formation on subfragments of the viral core origin.Bacteriophage T5 gene D10 encodes a branch-migration proteinCharacterization of the minimal DNA binding domain of the human papillomavirus e1 helicase: fluorescence anisotropy studies and characterization of a dimerization-defective mutant proteinCharacterization of the DNA-binding properties of the origin-binding domain of simian virus 40 large T antigen by fluorescence anisotropySeparate domains in E1 and E2 proteins serve architectural and productive roles for cooperative DNA binding.Structure-based mutational analysis of the bovine papillomavirus E1 helicase domain identifies residues involved in the nonspecific DNA binding activity required for double trimer formation.Cyclin/CDK regulates the nucleocytoplasmic localization of the human papillomavirus E1 DNA helicase.Papillomavirus E1 protein binds to and stimulates human topoisomerase IA conserved regulatory module at the C terminus of the papillomavirus E1 helicase domain controls E1 helicase assembly.Architecture of bacterial replication initiation complexes: orisomes from four unrelated bacteriaATP-dependent minor groove recognition of TA base pairs is required for template melting by the E1 initiator protein.Role of papillomavirus E1 initiator dimerization in DNA replicationRecruitment and loading of the E1 initiator protein: an ATP-dependent process catalysed by a transcription factor.Surface mutagenesis of the bovine papillomavirus E1 DNA binding domain reveals residues required for multiple functions related to DNA replication.A DNA-binding activity in BPV initiator protein E1 required for melting duplex ori DNA but not processive helicase activity initiated on partially single-stranded DNA.
P2860
Q27638318-137CB154-E3E0-4D4B-9C5A-4B9D98109102Q27643659-B6165559-595D-460C-9D5B-9C0A09BF9F97Q27644700-E0F99B75-8751-45FD-AA9D-17E42B1A67C2Q27679779-95A37F7A-B0F8-49AF-B8E9-4268884999ACQ28755124-486EF81A-FF01-4CF5-AA3A-898BC3FD9ECAQ33239795-08DD4E03-3EE5-4B21-9677-0CC303C15A7EQ33305049-C2B591F4-4FCA-48CD-9702-6D7A56585A52Q33783875-739DEAF3-67B4-47F0-A5BD-EB42A423EA32Q33793757-C492DDE4-0B45-4F09-BE2B-ABEBACF63D27Q33809498-4B5048BD-2243-44CA-A0A0-0007BCF75E43Q33814813-000A5EEC-3215-4661-B8AC-101015DE3688Q33834839-D89C75FC-16FB-4BCE-99A2-1E81F9EA1767Q34325784-47271C36-1A32-4138-91C4-4B1D6D83E250Q34583176-E15DD166-2BB8-49FB-AEA0-F2A3932AA0A1Q35150925-B5C0C5DD-1C1F-4E7C-92C6-B27CE2797A91Q35915034-D51616B6-3A3C-4117-8374-1696AF52782EQ36284493-00541583-8F0A-41FA-A4BB-3CFF1F4DE6A9Q36978987-7129D301-04BA-4772-A936-E4D8395597E0Q37198619-8F425713-A68E-4557-BB22-C8A4E5948592Q37262962-FC3B29D6-BF69-41D4-B426-49472B94C159Q37480430-3C511B2E-C3E5-46AD-9C31-C9CCCC6A83A0Q37628012-39A9F09F-A029-41C7-9CDD-6411E6CC1F93Q38317796-3303EA7E-4996-43A1-BEFD-3377CF4810A8Q39611068-F035B5EE-AFC9-49A1-A22A-755980DE783DQ39612347-ECEAF6E5-EC01-4305-A437-336FF4527525Q39738711-681195E1-B3A5-4AD3-A71E-AB1C20F9A040Q39748610-CB34D0D9-D056-4669-AD83-3547E8A9E4ADQ39748616-5A3611C7-7B21-4E6F-8D68-5861B841CD2CQ39922743-E992CD7A-F892-4248-A129-3358EB352C3AQ40339706-A21FB11B-91F2-4CF1-8FAE-867C4667067AQ40487864-A1720DD7-5DF5-4A89-9A8A-997492B1BCEAQ41819618-5DBDBA8E-E17A-458A-A02F-36A5E4B4C329Q41840185-B18B3D0A-B09C-45BB-9255-51AC9413B298Q41981022-DA79EAF0-48DB-4EA0-B541-5DFFC3B4FC86Q42119457-FCBB0AA6-97DD-425E-A94E-BD3590695F98Q42223004-8DCA5A26-62F5-414C-8969-6F3DD82AC628Q42662203-A5C844E4-E2D5-42D2-A89A-BE2875F30D99Q43155596-CF7B0FB3-97A3-4779-A023-19144A1A2DC3Q43161101-7BBCB95D-AFAE-4526-8B0F-4C550213D492
P2860
Characterization of the DNA-binding domain of the bovine papillomavirus replication initiator E1.
description
1998 nî lūn-bûn
@nan
1998 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
Characterization of the DNA-bi ...... irus replication initiator E1.
@ast
Characterization of the DNA-bi ...... irus replication initiator E1.
@en
type
label
Characterization of the DNA-bi ...... irus replication initiator E1.
@ast
Characterization of the DNA-bi ...... irus replication initiator E1.
@en
prefLabel
Characterization of the DNA-bi ...... irus replication initiator E1.
@ast
Characterization of the DNA-bi ...... irus replication initiator E1.
@en
P2860
P1433
P1476
Characterization of the DNA-bi ...... irus replication initiator E1.
@en
P2093
P2860
P304
P577
1998-04-01T00:00:00Z