Assembly of herpes simplex virus (HSV) intermediate capsids in insect cells infected with recombinant baculoviruses expressing HSV capsid proteins.
about
Involvement of the portal at an early step in herpes simplex virus capsid assembly.Herpesvirus 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.Determination and analysis of the complete nucleotide sequence of human herpesvirusSelf-assembling protein nanoparticles in the design of vaccinesThe delta domain of the HK97 major capsid protein is essential for assemblyDimerization-Induced Allosteric Changes of the Oxyanion-Hole Loop Activate the Pseudorabies Virus Assemblin pUL26N, a Herpesvirus Serine ProteaseAssembly 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.De 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.Cryo-electron tomography of Kaposi's sarcoma-associated herpesvirus capsids reveals dynamic scaffolding structures essential to capsid assembly and maturationHerpes simplex virus capsid structure: DNA packaging protein UL25 is located on the external surface of the capsid near the verticesThree-dimensional structures of the A, B, and C capsids of rhesus monkey rhadinovirus: insights into gammaherpesvirus capsid assembly, maturation, and DNA packaging.Cell-free assembly of the herpes simplex virus capsid.Assembly of herpes simplex virus capsids using the human cytomegalovirus scaffold protein: critical role of the C terminusSeparate functional domains of the herpes simplex virus type 1 protease: evidence for cleavage inside capsids.Identification of a minimal hydrophobic domain in the herpes simplex virus type 1 scaffolding protein which is required for interaction with the major capsid protein.Herpes simplex virus capsids assembled in insect cells infected with recombinant baculoviruses: structural authenticity and localization of VP26.Release of the catalytic domain N(o) from the herpes simplex virus type 1 protease is required for viral growthThe C-terminal 25 amino acids of the protease and its substrate ICP35 of herpes simplex virus type 1 are involved in the formation of sealed capsidsAssembly of the herpes simplex virus capsid: requirement for the carboxyl-terminal twenty-five amino acids of the proteins encoded by the UL26 and UL26.5 genesThe 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, cytomegalovirusEvidence for controlled incorporation of herpes simplex virus type 1 UL26 protease into capsidsAssembly of the herpes simplex virus capsid: preformed triplexes bind to the nascent capsid.The herpes simplex virus type 1 cleavage/packaging protein, UL32, is involved in efficient localization of capsids to replication compartmentsFinding a needle in a haystack: detection of a small protein (the 12-kDa VP26) in a large complex (the 200-MDa capsid of herpes simplex virus).Visualizing Herpesvirus Procapsids in Living CellsComprehensive mutational analysis of a herpesvirus gene in the viral genome context reveals a region essential for virus replicationAb initio modeling of the herpesvirus VP26 core domain assessed by CryoEM density.Silencing herpes simplex virus type 1 capsid protein encoding genes by siRNA: a promising antiviral therapeutic approach.The major determinant for addition of tegument protein pUL48 (VP16) to capsids in herpes simplex virus type 1 is the presence of the major tegument protein pUL36 (VP1/2)ATP depletion blocks herpes simplex virus DNA packaging and capsid maturationThe herpes simplex virus type 1 U(L)17 gene encodes virion tegument proteins that are required for cleavage and packaging of viral DNA.Incorporation of the green fluorescent protein into the herpes simplex virus type 1 capsid.ATP-Dependent localization of the herpes simplex virus capsid protein VP26 to sites of procapsid maturation.Three-dimensional structure of the human herpesvirus 8 capsid.A hydrophobic domain within the small capsid protein of Kaposi's sarcoma-associated herpesvirus is required for assembly.
P2860
Q24534403-95C8F303-E353-4495-988C-8A4C4E0F96A4Q24596737-227E9007-420C-4A32-8789-BBFFBC34CB19Q24646283-034B58BE-5B5B-4E08-BDB3-5566453E5150Q24681462-A94AC8E8-7F97-4797-855F-861EE238630CQ26767097-1A8FE2C5-9CD7-42FC-A0CA-223552419EF2Q28241163-A0B1014E-DC2E-4005-A484-342BC5EBBB39Q28546429-8F552DEB-557E-4678-9F11-462EA460EE66Q30303887-D245F8B4-35D2-42B8-8115-AA64880CD897Q30304621-A799EFC1-70F4-4B2B-A93F-4385B39E94D2Q30306907-A1FD9FB4-6FD3-4FB4-8E3F-CB4DDF3ECCF9Q30308062-821B1EBE-47EE-43EC-8260-CE2EFE52E929Q30311978-016F6ABA-3EC7-46BC-A6E0-FFD7800501D2Q30439469-5C425048-D4B5-477D-AE13-BAF3282DB7D8Q30440721-13F4C06A-E6CF-41DA-B009-61572A33D4FFQ30450951-1639B642-2A3B-4E57-9A71-8C497536B16CQ30452106-77B68859-B3FE-4455-8356-84FB8AC50260Q30452580-0F428F77-C6E0-4993-AE6D-7D6E0D908E52Q30452589-DCD8CA8F-FE11-449A-970E-286CFBB4875FQ30452599-0F187BC7-F219-4048-85B9-39AFE5F67089Q30452609-B2ECDCFE-28C4-4F32-9AB1-248922A17FC1Q30452610-B1F1B7C5-C47F-44E8-9ECB-323007EBFFBBQ30452629-CD2B9D64-46F0-4441-9BD4-B77DF883C325Q30452635-F58C5F4F-93CD-4978-82CC-1E86D7F4EA98Q30453387-7F4E0762-F0C8-4C7E-8242-3EA0A44FEB60Q30453457-B4702678-F393-4903-A9F7-04CE44097C22Q30453469-310D5506-3F67-4EB6-BF43-AB2D228E3807Q30453526-F8ED745A-3CB6-46C2-B5B6-BB33E0F21871Q30453534-172D7E0F-28C9-4403-A7F7-3AF2489BE569Q30454016-F380E856-DD53-4166-A8D1-47C4CF6A0CDCQ30828374-E61326DC-46C9-49BA-ADC4-310989842730Q31094095-AE8CBD00-E79C-491C-A669-B5535FF9715BQ33261808-073F9A01-AC6A-4F72-BA48-3BE76451BCA3Q33560548-B3A333FF-8E78-493D-B977-3EFAE678E0B6Q33614481-28800AE7-587E-4655-B8C0-DDF3D5CF0E9AQ33653063-9DDA5CC8-64F3-450A-B2C9-5FA14427FC7BQ33782652-F790117B-6758-4D49-A7CA-03D42B1CCB5BQ33784001-8F6A141E-D20F-493C-9913-8A7DF0A0DE45Q33793651-69ACB3E1-7988-4A0D-8E6B-92A76AF8E3CEQ33811735-CD478B62-B785-4F01-9D14-058BEDFF3495Q33918642-5EB84492-2D67-4AE2-ADFD-217EF1D89450
P2860
Assembly of herpes simplex virus (HSV) intermediate capsids in insect cells infected with recombinant baculoviruses expressing HSV capsid proteins.
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
Assembly of herpes simplex vir ...... xpressing HSV capsid proteins.
@ast
Assembly of herpes simplex vir ...... xpressing HSV capsid proteins.
@en
type
label
Assembly of herpes simplex vir ...... xpressing HSV capsid proteins.
@ast
Assembly of herpes simplex vir ...... xpressing HSV capsid proteins.
@en
prefLabel
Assembly of herpes simplex vir ...... xpressing HSV capsid proteins.
@ast
Assembly of herpes simplex vir ...... xpressing HSV capsid proteins.
@en
P2093
P2860
P1433
P1476
Assembly of herpes simplex vir ...... xpressing HSV capsid proteins.
@en
P2093
P2860
P304
P407
P577
1994-04-01T00:00:00Z