Microtubule reorganization during herpes simplex virus type 1 infection facilitates the nuclear localization of VP22, a major virion tegument protein
about
ICP0 dismantles microtubule networks in herpes simplex virus-infected cellsInteraction between Flavivirus and Cytoskeleton during Virus ReplicationHerpes simplex virus dances with amyloid precursor protein while exiting the cellConserved Tryptophan Motifs in the Large Tegument Protein pUL36 Are Required for Efficient Secondary Envelopment of Herpes Simplex Virus Capsids.Replication of herpes simplex virus: egress of progeny virus at specialized cell membrane sites.Nuclear egress and envelopment of herpes simplex virus capsids analyzed with dual-color fluorescence HSV1(17+)Dystonin/BPAG1 promotes plus-end-directed transport of herpes simplex virus 1 capsids on microtubules during entry.The major tegument structural protein VP22 targets areas of dispersed nucleolin and marginalized chromatin during productive herpes simplex virus 1 infection.Host cell targets of tegument protein VP22 of herpes simplex virus 1.Characterization of VP22 in herpes simplex virus-infected cells.DNA cleavage and packaging proteins encoded by genes U(L)28, U(L)15, and U(L)33 of herpes simplex virus type 1 form a complex in infected cells.Membrane association of VP22, a herpes simplex virus type 1 tegument protein.NF-kappaB is required for apoptosis prevention during herpes simplex virus type 1 infectionHerpes simplex virus 1 VP22 regulates translocation of multiple viral and cellular proteins and promotes neurovirulence.Replication-competent herpes simplex virus 1 isolates selected from cells transfected with a bacterial artificial chromosome DNA lacking only the UL49 gene vary with respect to the defect in the UL41 gene encoding host shutoff RNase.VP22 core domain from Herpes simplex virus 1 reveals a surprising structural conservation in both the Alpha- and Gammaherpesvirinae subfamiliesHistone deacetylase 6 inhibition enhances oncolytic viral replication in glioma.A microfluidic platform for real-time and in situ monitoring of virus infection process.Herpes simplex virus type 1 morphogenesis and virus-cell interactions: significance of cytoskeleton and methodological aspects.ORF9p phosphorylation by ORF47p is crucial for the formation and egress of varicella-zoster virus viral particles.The role of the cytoskeleton in the life cycle of viruses and intracellular bacteria: tracks, motors, and polymerization machines.VP22 of herpes simplex virus 1 promotes protein synthesis at late times in infection and accumulation of a subset of viral mRNAs at early times in infection.Kaposi's Sarcoma-Associated Herpesvirus Inhibitor of cGAS (KicGAS), Encoded by ORF52, Is an Abundant Tegument Protein and Is Required for Production of Infectious Progeny VirusesSynergy of a herpes oncolytic virus and paclitaxel for anaplastic thyroid cancer.Plus-end tracking proteins, CLASPs, and a viral Akt mimic regulate herpesvirus-induced stable microtubule formation and virus spread.Differing effects of herpes simplex virus 1 and pseudorabies virus infections on centrosomal function.Combination of vinblastine and oncolytic herpes simplex virus vector expressing IL-12 therapy increases antitumor and antiangiogenic effects in prostate cancer models.Varicella-zoster virus infection influences expression and organization of actin and alpha-tubulin but does not affect lamin A and vimentin.VP1, the major capsid protein of the mouse polyomavirus, binds microtubules, promotes their acetylation and blocks the host cell cycle.Purification of full-length VP22 from cells infected with HSV-1: A two-pronged approach for the solubilization and purification of viral proteins for use in biochemical studiesA conserved carboxy-terminal domain in the major tegument structural protein VP22 facilitates virion packaging of a chimeric protein during productive herpes simplex virus 1 infection.Herpes simplex virus 1 Us3 deletion mutant is infective despite impaired capsid translocation to the cytoplasm.Nuclear localizations of the herpes simplex virus type 1 tegument proteins VP13/14, vhs, and VP16 precede VP22-dependent microtubule reorganization and VP22 nuclear importImportin α1 is required for nuclear import of herpes simplex virus proteins and capsid assembly in fibroblasts and neurons.Cytoskeletons in the Closet-Subversion in Alphaherpesvirus Infections.The nuclear localization signal sequence of porcine circovirus type 2 ORF2 enhances intracellular delivery of plasmid DNA.
P2860
Q21136348-43C299AC-A9BD-4145-87AA-CBB280368C9FQ26782695-7CB14F9B-6210-40F0-A592-5C2875972D29Q27349482-07C809EC-BCBF-45EC-97DD-DDCBBF566E91Q30355292-04EEE0E5-DE97-40DF-8C8F-F6D348D14F36Q30423181-C2F72541-B61D-42BC-83E2-35E7AC1C5893Q30441453-96858F0E-AEB9-47FA-A8AD-083DCBE8F746Q30554266-4FAB0BD0-B534-4CB5-A9AD-BD2DFE4108F4Q33347221-F007202A-43A5-49E6-B257-B178F544E185Q33852011-D82747A5-D124-4FEA-982B-CC3077DA0490Q33984250-5B6B4A92-DC0B-4575-85E3-C02D81702DE0Q34338479-BBF34BEC-2251-490A-A061-BA7F41DB5DBAQ34860132-654A0B8B-257A-4D7B-B83F-D07F32BEB92EQ35149538-8D46197B-2D53-482C-B611-3098769B7BCCQ35943800-DB419EF1-E4AB-421A-A473-E393A21A179EQ36099301-242B5D3F-1F6C-4CC0-BAC3-3D90CEA8ADEAQ36255102-EDFA37E1-725F-4947-820B-39960DDE0B2FQ36266545-42B19EC8-BB49-4AFA-B063-E0B0AFA05258Q36315079-220CCCA2-B1A0-47B3-8BD4-AEDD183998D3Q36575899-8D953E0F-6645-47C4-BDAD-815521748BAFQ36607146-DE1A35FA-D239-4607-B6FB-51AE6D964E9BQ36739620-7847E591-FD4C-41AB-85A7-2EEB776586D0Q37033322-68029BAA-24C1-4F17-A71D-BFCB3ECE3F69Q37069828-3FFC37BC-15A6-4A4D-B7BA-9EA077AF091BQ37286038-0B4B4BCE-A2B4-44D5-A47E-FEE2F03D12D9Q37318197-EB0B866F-75F1-4D0E-9ECF-1BDF8B06F04BQ39164209-4A682BCF-48DA-4C1B-A54D-EAAD4934F9CDQ39247534-45886828-5BA4-40E2-89F5-09A0F42B5974Q40409449-5217DE9A-5C3C-4E6B-B236-8BDC0CDA1024Q40436326-78D10B6D-E189-4AB0-B2B5-2D4DD837EE11Q41774059-B9D50DE9-1C64-4C87-AC09-FB70AD64B501Q42065188-EFFE97A9-6F35-4A33-8BB5-A3699B8732CAQ42134883-BD9E2709-FDD0-447A-8054-B0C7493481DDQ42709865-E47DF0D8-8437-4AC2-8096-5620189A82F4Q47205447-E92F0FAF-39B5-44B2-B5A6-5DBEAE7CEBA4Q50042112-5CFEE55B-1126-418A-BB0E-14DAE04F3698Q50527092-B3B53BFB-093F-49B9-8A33-CE12F57D6F0B
P2860
Microtubule reorganization during herpes simplex virus type 1 infection facilitates the nuclear localization of VP22, a major virion tegument protein
description
2001 nî lūn-bûn
@nan
2001 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年学术文章
@wuu
2001年学术文章
@zh-cn
2001年学术文章
@zh-hans
2001年学术文章
@zh-my
2001年学术文章
@zh-sg
2001年學術文章
@yue
name
Microtubule reorganization dur ...... major virion tegument protein
@ast
Microtubule reorganization dur ...... major virion tegument protein
@en
type
label
Microtubule reorganization dur ...... major virion tegument protein
@ast
Microtubule reorganization dur ...... major virion tegument protein
@en
prefLabel
Microtubule reorganization dur ...... major virion tegument protein
@ast
Microtubule reorganization dur ...... major virion tegument protein
@en
P2093
P2860
P1433
P1476
Microtubule reorganization dur ...... major virion tegument protein
@en
P2093
P2860
P304
P356
10.1128/JVI.75.18.8697-8711.2001
P577
2001-09-01T00:00:00Z