Capsid assembly and DNA packaging in herpes simplex virus.
about
Novel class of thiourea compounds that inhibit herpes simplex virus type 1 DNA cleavage and encapsidation: resistance maps to the UL6 gene.Molecular biology of pseudorabies virus: impact on neurovirology and veterinary medicine.Determination of interactions between tegument proteins of herpes simplex virus type 1Involvement of the portal at an early step in herpes simplex virus capsid assembly.Identification of a region in the herpes simplex virus scaffolding protein required for interaction with the portalHerpesvirus capsid assembly: insights from structural analysis.Assembly of the herpes simplex virus capsid: identification of soluble scaffold-portal complexes and their role in formation of portal-containing capsids.Complete sequence and comparative analysis of the genome of herpes B virus (Cercopithecine herpesvirus 1) from a rhesus monkeyA putative leucine zipper within the herpes simplex virus type 1 UL6 protein is required for portal ring formationUncoating the herpes simplex virus genome.Crystal structure of the DNA-recognition component of the bacterial virus Sf6 genome-packaging machineThe host outer membrane proteins OmpA and OmpC are associated with the Shigella phage Sf6 virionStructural and Functional Studies of the Phage Sf6 Terminase Small Subunit Reveal a DNA-Spooling Device Facilitated by Structural PlasticityThe Structure of the Herpes Simplex Virus DNA-Packaging Terminase pUL15 Nuclease Domain Suggests an Evolutionary Lineage among Eukaryotic and Prokaryotic VirusesThe delta domain of the HK97 major capsid protein is essential for assemblyImproper tagging of the non-essential small capsid protein VP26 impairs nuclear capsid egress of herpes simplex virus.RNA is a structural element in retrovirus particlesAssembly of the herpes simplex virus procapsid from purified components and identification of small complexes containing the major capsid and scaffolding proteins.Isolation of herpes simplex virus procapsids from cells infected with a protease-deficient mutant virus.Lytic replication of Kaposi's sarcoma-associated herpesvirus results in the formation of multiple capsid species: isolation and molecular characterization of A, B, and C capsids from a gammaherpesvirus.The UL6 gene product forms the portal for entry of DNA into the herpes simplex virus capsid.Inhibition of herpes simplex virus replication by WAY-150138: assembly of capsids depleted of the portal and terminase proteins involved in DNA encapsidationDe novo infection with rhesus monkey rhadinovirus leads to the accumulation of multiple intranuclear capsid species during lytic replication but favors the release of genome-containing virions.Transient contacts on the exterior of the HK97 procapsid that are essential for capsid assembly.The putative herpes simplex virus 1 chaperone protein UL32 modulates disulfide bond formation during infectionMaturation and vesicle-mediated egress of primate gammaherpesvirus rhesus monkey rhadinovirus require inner tegument protein ORF52.Disulfide bond formation contributes to herpes simplex virus capsid stability and retention of pentons.Uncoupling uncoating of herpes simplex virus genomes from their nuclear import and gene expression.Labeling and localization of the herpes simplex virus capsid protein UL25 and its interaction with the two triplexes closest to the penton.Time-dependent transformation of the herpesvirus tegument.Role of the UL25 protein in herpes simplex virus DNA encapsidationLocalization of herpes simplex virus type 1 UL37 in the Golgi complex requires UL36 but not capsid structures.Herpes simplex virus capsid structure: DNA packaging protein UL25 is located on the external surface of the capsid near the verticesAmino acids 143 to 150 of the herpes simplex virus type 1 scaffold protein are required for the formation of portal-containing capsids.Handedness of the herpes simplex virus capsid and procapsidThe product of the herpes simplex virus type 1 UL25 gene is required for encapsidation but not for cleavage of replicated viral DNA.Capsid structure of Kaposi's sarcoma-associated herpesvirus, a gammaherpesvirus, compared to those of an alphaherpesvirus, herpes simplex virus type 1, and a betaherpesvirus, cytomegalovirusHerpes simplex virus DNA cleavage and packaging proteins associate with the procapsid prior to its maturation.Evidence for controlled incorporation of herpes simplex virus type 1 UL26 protease into capsidsThe herpes simplex virus type 1 DNA packaging protein UL17 is a virion protein that is present in both the capsid and the tegument compartments
P2860
Q24515073-E457AFAB-B4BA-477B-BEA7-5CAAD1C37266Q24531303-9274611B-4781-433D-91F4-A43A75A47A50Q24533075-98EDD1CD-BBC6-4465-AE23-7A4EC66E00B6Q24534403-646D8846-86E0-443F-B8A7-EC2E9BA92C92Q24558694-2DC28002-6B73-4785-8DC0-3E71FFECCFA2Q24596737-E11954DC-B4B9-456E-A1AB-1BF831771B90Q24646283-E94C0AAE-1E21-4B5E-8DB3-951E12480EA0Q24675195-2E094FB3-A0B9-46F8-B812-4CEA20EE71CCQ24676065-39FD8F99-7C8A-4537-B827-B18CF9E31DACQ24684501-64213BBE-D98B-431D-8D77-09ACA42A80C4Q27659594-F22E30E5-17D8-4079-8102-73361B4F302AQ27665846-82ADD754-6931-4CB5-A2E3-70172CE3EFD5Q27671091-C7DE1D46-9704-498A-8AB3-2F1924F66070Q27677441-FC7B655A-222C-4B66-9A51-A515FB2BDC7FQ28241163-F9C98E23-454E-45E9-9F16-73FD27D199A0Q28483224-3EC9FF80-2B5A-44C2-90AF-AE93938A8278Q30054778-894984A3-3B54-4BCB-9168-F4F755602D1AQ30303887-6AC42A16-B35D-4DCB-9440-E5129B706A09Q30304621-C42254E6-771D-4BE8-8702-9238AE9093F4Q30306907-40756623-B48E-469F-91AB-C4C1E76CD8CDQ30308062-59AF4072-B5CD-4AF3-AA67-6B3D08E9586AQ30309880-836D3F3B-B6EF-4448-8812-20A4315086ADQ30311978-47BD2E55-9335-4056-8445-1F51DD2E51DBQ30360528-B2085368-1FF0-4D32-9701-5FC6C0813503Q30384479-AC0CA1C4-8D1C-4248-9964-653091730E8BQ30408375-43B33DAE-ACD7-4E5A-B743-4E03D79569EEQ30428144-E9EAE6C9-34E9-4A21-8F63-C171E8D41A59Q30430017-100A5909-19CB-43BB-97A9-9BDD6B859A4EQ30432892-BBB1AA89-828F-44F7-A1B7-B7A64347682AQ30437209-C9F8B807-B517-4F8E-AE79-ADA28B93D2C2Q30439328-4359276D-6F9F-47A2-BB4D-53D8013F52F6Q30439761-9495CAFA-C68E-41D6-A3C1-1720F9889408Q30440721-2CAF4C9A-9B79-4D17-B870-F6A63CDC0707Q30440972-4ED46FCA-7B17-4FB4-A300-67C90E4B88FDQ30453268-A53F5285-9262-4428-BCFC-8BE422BB0296Q30453387-AA99E9DB-0E33-4A71-BA8A-507170E44BEEQ30453457-DAB3F1E7-86D3-4172-8F24-708C706B9742Q30453463-2883DF07-3EED-4321-B7AA-324E60F899FEQ30453469-A3A95B14-0DD7-4C6D-8018-9D915CDB1C04Q33551408-E081564E-38F0-40CE-871F-64DB2A1EC99C
P2860
Capsid assembly and DNA packaging in herpes simplex virus.
description
1997 nî lūn-bûn
@nan
1997 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
1997 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
1997年の論文
@ja
1997年学术文章
@wuu
1997年学术文章
@zh-cn
1997年学术文章
@zh-hans
1997年学术文章
@zh-my
1997年学术文章
@zh-sg
1997年學術文章
@yue
name
Capsid assembly and DNA packaging in herpes simplex virus.
@en
type
label
Capsid assembly and DNA packaging in herpes simplex virus.
@en
prefLabel
Capsid assembly and DNA packaging in herpes simplex virus.
@en
P2860
P1476
Capsid assembly and DNA packaging in herpes simplex virus.
@en
P2093
P2860
P304
P356
10.1002/(SICI)1099-1654(199707)7:2<107::AID-RMV191>3.0.CO;2-M
P577
1997-07-01T00:00:00Z