Herpes simplex virus tegument protein US11 interacts with conventional kinesin heavy chain.
about
ICP0 dismantles microtubule networks in herpes simplex virus-infected cellsDetermination of interactions between tegument proteins of herpes simplex virus type 1Association of the herpes simplex virus type 1 Us11 gene product with the cellular kinesin light-chain-related protein PAT1 results in the redistribution of both polypeptidesBinding of herpes simplex virus-1 US11 to specific RNA sequencesCoupling viruses to dynein and kinesin-1Rotavirus viroplasm fusion and perinuclear localization are dynamic processes requiring stabilized microtubulesKaposi's sarcoma-associated herpesvirus ORF45 interacts with kinesin-2 transporting viral capsid-tegument complexes along microtubulesHerpes simplex virus type 1 capsid protein VP26 interacts with dynein light chains RP3 and Tctex1 and plays a role in retrograde cellular transportHeat-shock protein 90 promotes nuclear transport of herpes simplex virus 1 capsid protein by interacting with acetylated tubulinFunction of dynein and dynactin in herpes simplex virus capsid transport.The pseudorabies virus VP1/2 tegument protein is required for intracellular capsid transportReconstitution of herpes simplex virus microtubule-dependent trafficking in vitro.Three-dimensional structure of the human cytomegalovirus cytoplasmic virion assembly complex includes a reoriented secretory apparatus.Local modulation of plus-end transport targets herpesvirus entry and egress in sensory axonsTargeting of herpesvirus capsid transport in axons is coupled to association with specific sets of tegument proteins.Plus- and minus-end directed microtubule motors bind simultaneously to herpes simplex virus capsids using different inner tegument structuresViral trafficking violations in axons: the herpesvirus caseDirect interaction of baculovirus capsid proteins VP39 and EXON0 with kinesin-1 in insect cells determined by fluorescence resonance energy transfer-fluorescence lifetime imaging microscopy.Cryo electron tomography of herpes simplex virus during axonal transport and secondary envelopment in primary neurons.Identification of FEZ1 as a protein that interacts with JC virus agnoprotein and microtubules: role of agnoprotein-induced dissociation of FEZ1 from microtubules in viral propagation.Herpes simplex virus type 1 accumulation, envelopment, and exit in growth cones and varicosities in mid-distal regions of axonsThe taking of the cytoskeleton one two three: how viruses utilize the cytoskeleton during egress.In vivo replication of an ICP34.5 second-site suppressor mutant following corneal infection correlates with in vitro regulation of eIF2 alpha phosphorylation.Axonal transport and sorting of herpes simplex virus components in a mature mouse visual system.ICP22 is required for wild-type composition and infectivity of herpes simplex virus type 1 virions.Microtubule network facilitates nuclear targeting of human cytomegalovirus capsid.Nucleolin interacts with US11 protein of herpes simplex virus 1 and is involved in its traffickingN-terminal kinesins: many and various.Biophysical Characterization of Nucleophosmin Interactions with Human Immunodeficiency Virus Rev and Herpes Simplex Virus US11.Herpes simplex virus-based vectors.New insights into viral structure and virus-cell interactions through proteomics.Molecular motors hijacking by intracellular pathogens.Making the case: married versus separate models of alphaherpes virus anterograde transport in axons.Viral interactions with the cytoskeleton: a hitchhiker's guide to the cell.Determination of suitable housekeeping genes for normalisation of quantitative real time PCR analysis of cells infected with human immunodeficiency virus and herpes virusesThe cycle of human herpes simplex virus infection: virus transport and immune control.The role of the cytoskeleton in the life cycle of viruses and intracellular bacteria: tracks, motors, and polymerization machines.Directional spread of alphaherpesviruses in the nervous system.Effect of human apolipoprotein E genotype on the pathogenesis of experimental ocular HSV-1.Herpesvirus interactions with the host cytoskeleton.
P2860
Q21136348-A2D1F128-FE9B-499F-9992-917B385D2B8DQ24533075-CD996AAF-8D00-4C86-8B84-7989A56E6F89Q24683333-6087A15D-7674-4FC0-AF9F-18C958539F1FQ24816239-8AB11D9D-9C45-430F-9362-D83957C2860CQ26864993-4B7ABB4C-7C89-409B-94CF-742E1E5B58FDQ27313339-B88A9700-CE46-477B-862D-7A048FC19B9AQ27317383-DA8C5321-A61E-4B0F-A0AF-0724C4A5590BQ28259269-4F24459B-C10B-4CDD-B380-4AEDFBCB8A23Q28539444-B16CE72A-820E-4648-A24F-51FCD9DD7A6EQ30453354-9B0E5366-BAF5-4C97-B67B-D700B2648B6CQ30476546-CF8097D9-CF29-4020-A116-37681B369EF0Q30477354-0F64E31C-4984-443A-8DAF-F005A3AF53BBQ30480949-C3915D22-FBEF-4F55-8B1E-03E01C02C837Q30837157-5961A782-22D3-41A8-8495-F47735EF3FE2Q30856858-ED33A71F-42D5-43F5-A60D-2C508A5F3BB7Q33632158-52EEE8F3-B794-49F0-BC78-5F4587963D62Q33937007-230AC164-C9BE-43F7-A37E-01E6497B0356Q34071301-BF71F8F5-63ED-4F62-95DB-47A89F0EC4E6Q34109746-BA11EA3E-DAE7-41BC-B1F8-8296AD446E8DQ34412827-2D2C5BD7-D094-4AF2-B2FD-3588543F08AEQ34545675-1C64045B-FC96-4340-9490-FFD07D5949A3Q34629230-32229C27-A2CD-466A-A76F-886D29975CE3Q34858111-AEE8BEDE-3A2B-45A2-AD4E-5B8AFA7AEF8AQ34997133-AE7C1350-6FEA-48FB-96E6-FB6140A7E116Q35101439-45335354-8B91-4829-88DE-E9A4FE1118FAQ35155425-4771622A-A207-4A93-9D7D-014B22A1ED4DQ35689672-914061F2-5877-437E-AF22-02EA1960BE9AQ35760258-437BC933-EFFF-4034-8FB7-041F54D1D70FQ35857057-88CACD28-3CDD-4C0D-AD94-6DEDB2474F2CQ35863367-8C430563-36E0-4E22-91DA-9797169A4B2CQ36227964-5D6507D3-8E1A-43D6-B71B-87776A416D28Q36347858-8920B45D-609D-4220-8CF7-453C9C4B80ABQ36360714-66BCB871-DB8B-45FD-AFEB-17B86223F6D3Q36392210-329C37F4-0EE1-4C11-B097-370B863D09C9Q36409774-5719C1E7-3040-4451-AFF4-AF558307315FQ36572093-790E13BC-B9FE-4566-A308-0122540532ACQ36739620-0E355C49-3342-408B-9B8F-ED38D910EC6BQ36807145-CB9AE4ED-A05C-4702-9CC8-F2DE4F612D66Q36935652-6EBC6A45-A5E6-4CC8-85F3-B81C13DB7F1FQ37099692-A2967332-9923-47E8-A386-D0328FCB7BF5
P2860
Herpes simplex virus tegument protein US11 interacts with conventional kinesin heavy chain.
description
2002 nî lūn-bûn
@nan
2002 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Herpes simplex virus tegument ...... ventional kinesin heavy chain.
@ast
Herpes simplex virus tegument ...... ventional kinesin heavy chain.
@en
Herpes simplex virus tegument ...... ventional kinesin heavy chain.
@nl
type
label
Herpes simplex virus tegument ...... ventional kinesin heavy chain.
@ast
Herpes simplex virus tegument ...... ventional kinesin heavy chain.
@en
Herpes simplex virus tegument ...... ventional kinesin heavy chain.
@nl
prefLabel
Herpes simplex virus tegument ...... ventional kinesin heavy chain.
@ast
Herpes simplex virus tegument ...... ventional kinesin heavy chain.
@en
Herpes simplex virus tegument ...... ventional kinesin heavy chain.
@nl
P2093
P2860
P1433
P1476
Herpes simplex virus tegument ...... nventional kinesin heavy chain
@en
P2093
David J Holland
Eve Diefenbach
Monica Miranda-Saksena
Patricia J Armati
Ross A Boadle
Russell J Diefenbach
P2860
P304
P356
10.1128/JVI.76.7.3282-3291.2002
P407
P577
2002-04-01T00:00:00Z