Multiple interactions control the intracellular localization of the herpes simplex virus type 1 capsid proteins.
about
HCF-dependent nuclear import of VP16Proteolytic cleavage of VP1-2 is required for release of herpes simplex virus 1 DNA into the nucleusWavelets filtering for classification of very noisy electron microscopic single particles images--application on structure determination of VP5-VP19C recombinantPrinciples of virus structural organizationImproper tagging of the non-essential small capsid protein VP26 impairs nuclear capsid egress of herpes simplex virus.Assembly of the herpes simplex virus procapsid from purified components and identification of small complexes containing the major capsid and scaffolding proteins.Assembly of the herpes simplex virus capsid: preformed triplexes bind to the nascent capsid.Ab initio modeling of the herpesvirus VP26 core domain assessed by CryoEM density.The herpes simplex virus type 1 DNA packaging protein UL17 is a virion protein that is present in both the capsid and the tegument compartmentsSilencing herpes simplex virus type 1 capsid protein encoding genes by siRNA: a promising antiviral therapeutic approach.Capsid assembly and DNA packaging in herpes simplex virus.Characterization of the subcellular localization of herpes simplex virus type 1 proteins in living cells.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.Analysis of HCF, the cellular cofactor of VP16, in herpes simplex virus-infected cells.A null mutation in the UL36 gene of herpes simplex virus type 1 results in accumulation of unenveloped DNA-filled capsids in the cytoplasm of infected cells.Phosphorylation of simian cytomegalovirus assembly protein precursor (pAPNG.5) and proteinase precursor (pAPNG1): multiple attachment sites identified, including two adjacent serines in a casein kinase II consensus sequence.Role of the UL25 gene product in packaging DNA into the herpes simplex virus capsid: location of UL25 product in the capsid and demonstration that it binds DNA.A hydrophobic domain within the small capsid protein of Kaposi's sarcoma-associated herpesvirus is required for assembly.HSV-1-based vectors for gene therapy of neurological diseases and brain tumors: part I. HSV-1 structure, replication and pathogenesis.Egress of HSV-1 capsid requires the interaction of VP26 and a cellular tetraspanin membrane proteinFunctional analysis of the triplex proteins (VP19C and VP23) of herpes simplex virus type 1Nuclear export of VP19C is not essential for replication of herpes simplex virus type 1Sequential localization of two herpes simplex virus tegument proteins to punctate nuclear dots adjacent to ICP0 domainsThe first identified nucleocytoplasmic shuttling herpesviral capsid protein: herpes simplex virus type 1 VP19C.Mutation of single hydrophobic residue I27, L35, F39, L58, L65, L67, or L71 in the N terminus of VP5 abolishes interaction with the scaffold protein and prevents closure of herpes simplex virus type 1 capsid shellsDNA binding and condensation properties of the herpes simplex virus type 1 triplex protein VP19CA domain in the herpes simplex virus 1 triplex protein VP23 is essential for closure of capsid shells into icosahedral structuresDNA methyltransferase DNMT3A associates with viral proteins and impacts HSV-1 infection.Assembly of Epstein-Barr Virus Capsid in Promyelocytic Leukemia Nuclear Bodies.Structural features of the scaffold interaction domain at the N terminus of the major capsid protein (VP5) of herpes simplex virus type 1.Identification of the sites of interaction between the scaffold and outer shell in herpes simplex virus-1 capsids by difference electron imaging.Herpes simplex virus 1 (HSV-1) for cancer treatment.Hexon-only binding of VP26 reflects differences between the hexon and penton conformations of VP5, the major capsid protein of herpes simplex virusLive visualization of herpes simplex virus type 1 compartment dynamicsSelf-assembly of Epstein-Barr virus capsids.The Marek's disease virus (MDV) protein encoded by the UL17 ortholog is essential for virus growth.Functional analysis of nuclear localization signals in VP1-2 homologues from all herpesvirus subfamiliesRelease of the herpes simplex virus 1 protease by self cleavage is required for proper conformation of the portal vertex.Cytomegalovirus assembly protein precursor and proteinase precursor contain two nuclear localization signals that mediate their own nuclear translocation and that of the major capsid protein.
P2860
Q24533545-4FDB5B93-27B6-4078-B19E-2FA511EFBE2DQ24652886-271977D9-CD3E-40BA-BD2A-76C6B3A95C27Q24805865-A16392B9-FB3D-4EFB-8781-28032ADC2F45Q27021684-6391991D-EE1F-4FF2-9A5A-E80BEA655B50Q28483224-661C7AF1-F4A9-4795-AF2E-F32585167AE8Q30303887-1B565F9C-9B09-4820-8C73-96A7F5C3D4AEQ30453526-72D3B7BB-EE8F-4DE1-AE96-13CD3D18395BQ33261808-F69E78E1-1339-47B9-957F-8548C5792C25Q33551408-C09958F9-C342-4F90-9A15-BE8723B438A4Q33560548-EC819C00-C921-49DC-BCF2-123112FA7331Q33682957-06195F5E-101F-40E8-AACA-997CEAAC9098Q33719606-CC49A67C-7D5F-4699-9403-D0DD1069150FQ33784001-23D9CE33-D95B-4D5E-8275-74C30030A21CQ33793651-C4159824-4064-4D1C-90BB-1D441606F3DDQ33794386-45525BC2-169B-4B3B-B3C6-20C4998D68F5Q33812522-F3AF73C1-7145-4F53-B009-444C4D50A8F2Q33822595-0463ED4A-3256-4032-85C2-264DD0AA5519Q33836521-BB36BD37-27AD-4E43-8EE1-20EE3CD0683DQ33918642-7BD8B054-37A9-4E19-BB00-C7C85873A34DQ33995747-9DB15587-EA26-42F3-827C-6D7F85E1D024Q34036057-3D5CA133-6991-4CD9-9EF3-460DBCDE334DQ34301854-FDD0B5D3-5CDC-411E-A1EF-AAE950CA00F4Q34308894-08AB2CF1-1C6E-4372-8742-EBD1842DBCCDQ34348658-CA82854F-0E58-4ED7-8684-B09F440F8E4AQ34395416-4DEE375A-7F82-496F-AD08-EF21E6D896A1Q34782106-D76C9483-A4AF-49CE-AF61-0A8D9AA2DC37Q35224426-E08E20E4-900E-4972-9B55-ABBC8402D4F4Q35531461-230ED393-78E5-4016-8368-9A5B6E0E29C2Q35574805-A2186AD8-8948-4083-9105-95C7504BF641Q35666747-DAF591F9-0AA2-4A4E-BC1B-71F43BE80B77Q35947874-5115DF9C-6B19-493F-8ED8-B2C977E4370CQ35970851-9386C53D-61FF-4DA1-B140-E33C216846B1Q36444443-06934348-BD23-4754-9094-74AE07D4C02CQ36548514-C7B6A1FC-56E1-46CF-8F72-06607F62C08AQ36594186-7536B8AE-F86E-440A-BDB9-A9454E7B506EQ37145249-7007E7F1-4F2C-43D2-9FA5-C61B206E495BQ37224343-5140168D-CBAB-4BB4-8FE8-002706AC0D68Q39020466-9FCD2345-F9DF-4E3F-837F-97768F79FE8AQ39356969-F2040BE1-35F9-423F-A0CE-7E4D4E249E7DQ39580849-5FC032E2-B8A3-41E3-8BBA-E9E635056995
P2860
Multiple interactions control the intracellular localization of the herpes simplex virus type 1 capsid proteins.
description
1996 nî lūn-bûn
@nan
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
1996年论文
@zh
1996年论文
@zh-cn
name
Multiple interactions control ...... virus type 1 capsid proteins.
@en
type
label
Multiple interactions control ...... virus type 1 capsid proteins.
@en
prefLabel
Multiple interactions control ...... virus type 1 capsid proteins.
@en
P2093
P1476
Multiple interactions control ...... virus type 1 capsid proteins.
@en
P2093
McGregor A
Nicholson P
Preston VG
P304
P356
10.1099/0022-1317-77-9-2251
P407
P478
77 ( Pt 9)
P577
1996-09-01T00:00:00Z