Function of dynein and dynactin in herpes simplex virus capsid transport. - Wikidata - thesis-toulmin - TriplyDB

Function of dynein and dynactin in herpes simplex virus capsid transport.

Function of dynein and dynactin in herpes simplex virus capsid transport.

http://www.wikidata.org/entity/Q30453354

about

Involvement of microtubular network and its motors in productive endocytic trafficking of mouse polyomavirus Molecular biology of pseudorabies virus: impact on neurovirology and veterinary medicine.Formation of nuclear foci of the herpes simplex virus type 1 regulatory protein ICP4 at early times of infection: localization, dynamics, recruitment of ICP27, and evidence for the de novo induction of ND10-like complexes Association 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 polypeptides Tegument Assembly and Secondary Envelopment of Alphaherpesviruses Actin in herpesvirus infection Coupling viruses to dynein and kinesin-1 Microtubule plus end-associated CLIP-170 initiates HSV-1 retrograde transport in primary human cells Host cytoskeleton in respiratory syncytial virus assembly and budding The herpesvirus VP1/2 protein is an effector of dynein-mediated capsid transport and neuroinvasion.Herpes simplex virus type 1 capsid protein VP26 interacts with dynein light chains RP3 and Tctex1 and plays a role in retrograde cellular transport Improper tagging of the non-essential small capsid protein VP26 impairs nuclear capsid egress of herpes simplex virus.Prevention of herpes simplex virus induced stromal keratitis by a glycoprotein B-specific monoclonal antibody A role for cytoplasmic dynein and LIS1 in directed cell movement Genital Herpes: Insights into Sexually Transmitted Infectious Disease Conserved Tryptophan Motifs in the Large Tegument Protein pUL36 Are Required for Efficient Secondary Envelopment of Herpes Simplex Virus Capsids.Herpes simplex virus internalization into epithelial cells requires Na+/H+ exchangers and p21-activated kinases but neither clathrin- nor caveolin-mediated endocytosis.The C terminus of the large tegument protein pUL36 contains multiple capsid binding sites that function differently during assembly and cell entry of herpes simplex virus Uncoupling uncoating of herpes simplex virus genomes from their nuclear import and gene expression.Herpes simplex virus replication: roles of viral proteins and nucleoporins in capsid-nucleus attachment Nuclear egress and envelopment of herpes simplex virus capsids analyzed with dual-color fluorescence HSV1(17+)Eclipse phase of herpes simplex virus type 1 infection: Efficient dynein-mediated capsid transport without the small capsid protein VP26.A common mechanism for cytoplasmic dynein-dependent microtubule binding shared among adeno-associated virus and adenovirus serotypes.Cytoplasmic dynein mediates adenovirus binding to microtubules.ND10 components relocate to sites associated with herpes simplex virus type 1 nucleoprotein complexes during virus infection.The pseudorabies virus VP1/2 tegument protein is required for intracellular capsid transport Nuclear localization signal peptides induce molecular delivery along microtubules.Reconstitution of herpes simplex virus microtubule-dependent trafficking in vitro.The Herpesvirus capsid surface protein, VP26, and the majority of the tegument proteins are dispensable for capsid transport toward the nucleus.A motor neuron disease-associated mutation in p150Glued perturbs dynactin function and induces protein aggregation.Three-dimensional structure of the human cytomegalovirus cytoplasmic virion assembly complex includes a reoriented secretory apparatus.Native 3D intermediates of membrane fusion in herpes simplex virus 1 entry.Virus trafficking - learning from single-virus tracking Single-particle tracking as a quantitative microscopy-based approach to unravel cell entry mechanisms of viruses and pharmaceutical nanoparticles.Herpesvirus tegument protein pUL37 interacts with dystonin/BPAG1 to promote capsid transport on microtubules during egress.Fast anterograde transport of herpes simplex virus: role for the amyloid precursor protein of alzheimer's disease.Dystonin/BPAG1 promotes plus-end-directed transport of herpes simplex virus 1 capsids on microtubules during entry.HIV-1 capsids bind and exploit the kinesin-1 adaptor FEZ1 for inward movement to the nucleus.Local modulation of plus-end transport targets herpesvirus entry and egress in sensory axons Targeting of herpesvirus capsid transport in axons is coupled to association with specific sets of tegument proteins.

P2860

Q21558490-AF1EAC80-6193-46AB-9AF3-B49604854A02 Q24531303-801AC742-6B6A-4EC7-80C0-BFE62530D3BC Q24607261-2BB58712-3510-4F84-9E43-DF111DF4F23E Q24683333-301EC746-97CB-475D-B52E-DA67245090A3 Q26782247-3B92260B-07C8-45C1-9686-46F2D1B78A8D Q26823346-78EC90DF-C7A6-4613-B21B-D32B39C0E632 Q26864993-B203BFCA-B735-4CB6-914D-4DBCC2EAC3C7 Q27309233-24267B50-2B9F-4865-A4AE-685E1CF8B07E Q28067634-FFDD5E24-B094-418E-BD4D-BD2EC659A8A9 Q28116141-298230A5-CE9E-4D34-93C4-5363BE732BFA Q28259269-E8868253-8A66-4991-A92D-96C801D83A1C Q28483224-CBA8EED3-7572-424A-83F3-9F586DE81332 Q28543018-4E1C3714-5A6C-48AF-9301-7F7FEED5F88A Q28591271-EEAF2674-C777-40A0-8DC1-E8C111FEF0E8 Q30235026-C30AC101-0548-43E6-803C-B03BC220E369 Q30355292-2D551B3B-E02F-4562-9F77-4BD1936115DD Q30405542-C9957CA0-4BAB-4733-B818-BAF383A95B6B Q30424771-AD59201A-31FC-4FB7-A4D5-AAD22537EA3E Q30430017-B1D3071D-2C5E-4F87-B00E-637D805F1F3D Q30439071-85FA4A90-8355-44EC-AEEB-B79A8E52489C Q30441453-793E03DC-18D6-47FE-BAEF-A2C8E0B20CB1 Q30445612-5C1ACA42-58C1-4E4D-9F71-A405EA12D399 Q30445618-8C4CC0F1-D24B-47D1-A904-09333A771F33 Q30448880-51E68C65-59AA-4641-A232-4EF4454B2992 Q30475799-7DD7F7F2-4D79-41AC-B433-A49F0E946C58 Q30476546-A96E6870-35EF-4477-8771-F096B501F17C Q30476771-3807FB92-9ED4-42AB-8D82-75DAE64C54A0 Q30477354-FF041964-E3E1-424C-A38E-CCD479BCC99B Q30477358-F153FCE0-DA13-4662-93C5-BCB8971EAB9F Q30480370-119DB2BB-C5A5-4E79-BB4A-D6D0CFAFFA7F Q30480949-5D92E3A6-1FFA-4BE9-88EF-0C003773027B Q30482898-67F7EFBF-FAFD-4B9A-8A3B-CFA04BDDDEA6 Q30490068-62699E07-A4BD-4FFA-AE1A-03065708DDF9 Q30502104-26422F9E-A42B-4DBC-AB75-5B2DCE382BB4 Q30535712-531E45C6-B562-4F67-B104-8ACC1C375C82 Q30538684-D8ACD4DC-F89C-4E59-9697-86517E84BD13 Q30554266-AFCDF36D-9596-43DA-A713-2A7B17929ECB Q30634144-E3B0D8F4-C055-4266-99E5-8C444A5CA8C2 Q30837157-5FFC8F5C-0F5B-4B94-B3BB-6429096633EA Q30856858-0AA124C8-9BFA-4C09-B95A-80C83CFE4586

P2860

Function of dynein and dynactin in herpes simplex virus capsid transport.

http://www.wikidata.org/entity/Q30453354

description

2002 nî lūn-bûn

@nan

2002 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2002 թվականի օգոստոսին 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

Function of dynein and dynactin in herpes simplex virus capsid transport.

@ast

Function of dynein and dynactin in herpes simplex virus capsid transport.

@en

type

label

Function of dynein and dynactin in herpes simplex virus capsid transport.

@ast

Function of dynein and dynactin in herpes simplex virus capsid transport.

@en

prefLabel

Function of dynein and dynactin in herpes simplex virus capsid transport.

@ast

Function of dynein and dynactin in herpes simplex virus capsid transport.

@en

P1433

Q30453354-3275F9A7-536C-4606-9E05-F26AED4ED8F0

P1476

Q30453354-E0B30DDA-8D1C-4357-826B-77DA8F8DDB23

P2093

Q30453354-52B53CD7-E356-4C6E-BF7D-EED2ED26E441

Q30453354-5733C083-C2CB-48BA-8F18-58490E63AEFA

Q30453354-7E997B92-8B94-4CB9-A2EF-538022BFD989

Q30453354-7F34CA7F-9E6E-49EC-8421-32A7C01A0A61

Q30453354-A5D6293A-1B31-4E0B-BC26-ACB937481713

Q30453354-C450361E-0FB1-4BEA-ABB7-7F942E5E23AB

Q30453354-F0394C22-097C-4858-AD95-62A184605D72

P2860

Q30453354-0B1BAB28-AE59-4E2C-93C6-C6B7D29A6BAA

Q30453354-0DCA2F4A-0AD8-4012-B772-D75F5E546C72

Q30453354-127F12C2-77EC-453E-9C7A-9F8422A2E6A7

Q30453354-181AB902-6FB0-40D3-B721-D0D53723FC65

Q30453354-19207BD8-BBBB-4A02-A100-F4FB8C6591EE

Q30453354-21C44533-2813-4A40-A317-11CEBE6C1E3C

Q30453354-22DECA6C-1556-4D05-8574-CEE9BD48C6DF

Q30453354-2550F154-FE8F-45B1-ADE7-19A6F5E5AD43

Q30453354-296AAD98-99E4-4795-A2AD-B6F43F0F02A8

Q30453354-2AF49690-5C1A-492A-97C3-D9EFBF81A03D

P304

Q30453354-8C49E9DA-57F7-416C-B5DB-22F071D526CE

P31

Q30453354-4F03B680-F9D2-43EE-9F68-9F36B10EECA0

P356

Q30453354-BDF9197B-DF90-4B83-BE29-FF5762DE9D7D

P433

Q30453354-2C4067F8-D698-4708-8BFC-1AA4182AD7B2

P478

Q30453354-A4C29565-6010-4949-B519-BD647D169539

P577

Q30453354-23E8816E-157C-4329-A6A5-0C7AE3723419

P5875

Q30453354-A32C67D0-09FD-4735-9F27-FA2B817DF219

P698

Q30453354-425564B0-4D46-4CF9-9D56-3819ACB9E41E

P932

Q30453354-E212FBBA-7B35-4853-BF8C-F0C3EAE6B5AB

P356

P1433

Molecular Biology of the Cell

P1476

Function of dynein and dynactin in herpes simplex virus capsid transport.

@en

P2093

André Wolfstein

http://www.w3.org/2001/XMLSchema#string

Beate Sodeik

http://www.w3.org/2001/XMLSchema#string

Christophe Echeverri

http://www.w3.org/2001/XMLSchema#string

Denis Dujardin

http://www.w3.org/2001/XMLSchema#string

Katinka Döhner

http://www.w3.org/2001/XMLSchema#string

Richard Vallee

http://www.w3.org/2001/XMLSchema#string

Ute Prank

http://www.w3.org/2001/XMLSchema#string

P2860

Cytoplasmic dynein-mediated assembly of pericentrin and gamma tubulin onto centrosomes

Cytoplasmic dynein binds dynactin through a direct interaction between the intermediate chains and p150Glued

A cell surface protein with herpesvirus entry activity (HveB) confers susceptibility to infection by mutants of herpes simplex virus type 1, herpes simplex virus type 2, and pseudorabies virus

Molecular characterization of the 50-kD subunit of dynactin reveals function for the complex in chromosome alignment and spindle organization during mitosis

Cytoplasmic dynein plays a role in mammalian mitotic spindle formation

Two activators of microtubule-based vesicle transport

Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmic dynein

Ultrastructural analysis of the dynactin complex: an actin-related protein is a component of a filament that resembles F-actin

Dynactin is required for microtubule anchoring at centrosomes

Analysis of dynactin subcomplexes reveals a novel actin-related protein associated with the arp1 minifilament pointed end

P304

2795-2809

http://www.w3.org/2001/XMLSchema#string

P31

scholarly article

P356

10.1091/MBC.01-07-0348

http://www.w3.org/2001/XMLSchema#string

P433

8

http://www.w3.org/2001/XMLSchema#string

P478

13

http://www.w3.org/2001/XMLSchema#string

P577

2002-08-01T00:00:00Z

http://www.w3.org/2001/XMLSchema#dateTime

P5875

11206719

http://www.w3.org/2001/XMLSchema#string

P698

12181347

http://www.w3.org/2001/XMLSchema#string

P932

117943

http://www.w3.org/2001/XMLSchema#string