Structure of bluetongue virus particles by cryoelectron microscopy.
about
Intermediates in the assembly pathway of the double-stranded RNA virus phi6The membrane trafficking protein calpactin forms a complex with bluetongue virus protein NS3 and mediates virus releaseRGD tripeptide of bluetongue virus VP7 protein is responsible for core attachment to Culicoides cells.Bluetongue virus: dissection of the polymerase complexAdding the Third Dimension to Virus Life Cycles: Three-Dimensional Reconstruction of Icosahedral Viruses from Cryo-Electron MicrographsDetection of a fourth orbivirus non-structural proteinVP1, the putative RNA-dependent RNA polymerase of infectious bursal disease virus, forms complexes with the capsid protein VP3, leading to efficient encapsidation into virus-like particlesRT-PCR assays for seven serotypes of epizootic haemorrhagic disease virus & their use to type strains from the Mediterranean region and North America.Expression and functional characterization of bluetongue virus VP5 protein: role in cellular permeabilization.Role of an arbovirus nonstructural protein in cellular pathogenesis and virus release.Oncolytic bluetongue viruses: promise, progress, and perspectivesStructural insight into African horsesickness virus infection.Early steps in reovirus infection are associated with dramatic changes in supramolecular structure and protein conformation: analysis of virions and subviral particles by cryoelectron microscopy and image reconstructionA Dual Laser Scanning Confocal and Transmission Electron Microscopy Analysis of the Intracellular Localization, Aggregation and Particle Formation of African Horse Sickness Virus Major Core Protein VP7.A capsid protein of nonenveloped Bluetongue virus exhibits membrane fusion activityStructure of a neutralizing antibody bound bivalently to human rhinovirus 2.Manipulation of the bluetongue virus tubules for immunogen delivery.Role of lipids on entry and exit of bluetongue virus, a complex non-enveloped virusExpression and functional characterization of bluetongue virus VP2 protein: role in cell entry.Identification of domains in bluetongue virus VP3 molecules essential for the assembly of virus cores.A single point mutation in the VP7 major core protein of bluetongue virus prevents the formation of core-like particles.The Aedes albopictus inhibitor of apoptosis 1 gene protects vertebrate cells from bluetongue virus-induced apoptosis.Development of baculovirus triple and quadruple expression vectors: co-expression of three or four bluetongue virus proteins and the synthesis of bluetongue virus-like particles in insect cells.Structural Protein VP2 of African Horse Sickness Virus Is Not Essential for Virus Replication In Vitro.Interactions between the inner and outer capsids of bluetongue virus.Adenovirus 3 penton dodecahedron exhibits structural changes of the base on fibre binding.Multiple gene expression in baculovirus system. Third generation vaccines for bluetongue disease and African horsesickness disease.In Silico Studies on Development of Novel Virostatic Agents against Bluetongue Virus
P2860
Q24532454-84A7EABC-0F26-4E69-9B31-B30112EFB27CQ24538680-B5EA27AB-DA93-4C75-8A81-0E69E5D63633Q27469906-94CFBC29-0483-41F0-8546-CC04F24E5DD0Q27489424-78F8D41B-53BD-428F-BFD0-9768ED640D7FQ27702159-603B3FB3-12C7-4B0E-8315-3EEE66BB58E5Q28743968-A05672CD-2B4A-4EA2-83F4-45A301877B24Q30731540-DF14C67D-8F22-469D-BDBD-72A0DCA121DDQ33700346-D617655C-4E45-446B-ADA7-32BF242060FDQ33853828-695A2D33-22C2-4817-8C1C-C1A12F7445C6Q34186230-00D4DE41-55C1-4479-B057-3E4DE5841A4CQ35084491-12D2995C-A553-4DCC-A641-4809DDD3F68EQ36171865-2FF7F931-5EC5-4BC2-A17F-BEA0EA8FBC61Q36232691-D5743374-0BBE-4188-B980-E9B37E8CEF5CQ36256933-92F9FA87-BFD8-40B9-B97D-814A6707DC43Q36604788-FF12E4A4-7AF6-4C1B-B673-5326A268BA9CQ36797072-100935F4-8244-4A6C-A5B0-C143C6834633Q37174137-77E13164-B842-4FB1-ABC7-5A63A5CB86D0Q37945206-F87374B8-8A6C-44CB-AD52-9B63DC58E0BFQ39596872-02FCE000-87CD-4D27-A3DC-2FA9833382D9Q40040402-077C061A-2A48-401C-A0A7-F6E7E0D2C668Q40043569-EDBE9EAE-C60F-423B-AFB5-2CAF1E2E48BBQ40178447-21D53326-5F0F-478F-BBDF-13B488DE1962Q40405794-1F6914E3-3DCC-4802-9E43-27DC947468CAQ40448117-8320EEEF-8A6E-47C9-BD03-3BB2113204D6Q41039228-08FAEE91-E30C-4DD0-A8E5-9E7DA048509FQ41078950-25294DE1-F485-46E6-B078-E3F2AC9779ACQ41183186-3C024F39-0564-4DB1-94B7-E793B1CCDC34Q59048200-0016D9F4-A592-4AD8-A85F-C1B2B506EAEF
P2860
Structure of bluetongue virus particles by cryoelectron microscopy.
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年学术文章
@wuu
1992年学术文章
@zh
1992年学术文章
@zh-cn
1992年学术文章
@zh-hans
1992年学术文章
@zh-my
1992年学术文章
@zh-sg
1992年學術文章
@yue
1992年學術文章
@zh-hant
name
Structure of bluetongue virus particles by cryoelectron microscopy.
@en
Structure of bluetongue virus particles by cryoelectron microscopy.
@nl
type
label
Structure of bluetongue virus particles by cryoelectron microscopy.
@en
Structure of bluetongue virus particles by cryoelectron microscopy.
@nl
prefLabel
Structure of bluetongue virus particles by cryoelectron microscopy.
@en
Structure of bluetongue virus particles by cryoelectron microscopy.
@nl
P2093
P1476
Structure of bluetongue virus particles by cryoelectron microscopy.
@en
P2093
P356
10.1016/1047-8477(92)90068-L
P577
1992-07-01T00:00:00Z