Membrane association of VP22, a herpes simplex virus type 1 tegument protein.
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Trafficking of Sendai virus nucleocapsids is mediated by intracellular vesiclesThe Us2 gene product of herpes simplex virus 2 is a membrane-associated ubiquitin-interacting proteinThe major tegument structural protein VP22 targets areas of dispersed nucleolin and marginalized chromatin during productive herpes simplex virus 1 infection.Actin is a component of the compensation mechanism in pseudorabies virus virions lacking the major tegument protein VP22.Host cell targets of tegument protein VP22 of herpes simplex virus 1.Characterization of VP22 in herpes simplex virus-infected cells.Herpes simplex virus glycoproteins gB and gD function in a redundant fashion to promote secondary envelopmentInteraction and interdependent packaging of tegument protein UL11 and glycoprotein e of herpes simplex virus.Cytoplasmic residues of herpes simplex virus glycoprotein gE required for secondary envelopment and binding of tegument proteins VP22 and UL11 to gE and gDPackaging of the virion host shutoff (Vhs) protein of herpes simplex virus: two forms of the Vhs polypeptide are associated with intranuclear B and C capsids, but only one is associated with enveloped virionsHerpes 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 subfamiliesHerpes Simplex Virus Capsid-Organelle Association in the Absence of the Large Tegument Protein UL36pVirion incorporation of the herpes simplex virus type 1 tegument protein VP22 is facilitated by trans-Golgi network localization and is independent of interaction with glycoprotein E.Binding partners for the UL11 tegument protein of herpes simplex virus type 1.Serological Evaluation of Immunity to the Varicella-Zoster Virus Based on a Novel Competitive Enzyme-Linked Immunosorbent AssayKaposi's Sarcoma-Associated Herpesvirus Inhibitor of cGAS (KicGAS), Encoded by ORF52, Is an Abundant Tegument Protein and Is Required for Production of Infectious Progeny VirusesHerpes simplex virus type 1 glycoprotein K and the UL20 protein are interdependent for intracellular trafficking and trans-Golgi network localizationHerpesviruses remodel host membranes for virus egress.Insights into the function of tegument proteins from the varicella zoster virus.Expression and characterization of UL16 gene from duck enteritis virus.Evasion of the STING DNA-Sensing Pathway by VP11/12 of Herpes Simplex Virus 1.The amino terminus of the herpes simplex virus 1 protein Vhs mediates membrane association and tegument incorporation.Analysis of viral and cellular factors influencing herpesvirus-induced nuclear envelope breakdownComplex mechanisms for the packaging of the UL16 tegument protein into herpes simplex virusRedistribution of cellular and herpes simplex virus proteins from the trans-golgi network to cell junctions without enveloped capsids.Herpes simplex virus tegument protein VP22 contains an internal VP16 interaction domain and a C-terminal domain that are both required for VP22 assembly into the virus particle.An acidic cluster of human cytomegalovirus UL99 tegument protein is required for trafficking and function.Compartmentalization of VP16 in cells infected with recombinant herpes simplex virus expressing VP16-green fluorescent protein fusion proteins.A 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.Evidence that insertion of Tomato ringspot nepovirus NTB-VPg protein in endoplasmic reticulum membranes is directed by two domains: a C-terminal transmembrane helix and an N-terminal amphipathic helix.Heterogeneity of a fluorescent tegument component in single pseudorabies virus virions and enveloped axonal assemblies.Nuclear localizations of the herpes simplex virus type 1 tegument proteins VP13/14, vhs, and VP16 precede VP22-dependent microtubule reorganization and VP22 nuclear import
P2860
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P2860
Membrane association of VP22, a herpes simplex virus type 1 tegument protein.
description
2003 nî lūn-bûn
@nan
2003 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年学术文章
@wuu
2003年学术文章
@zh-cn
2003年学术文章
@zh-hans
2003年学术文章
@zh-my
2003年学术文章
@zh-sg
2003年學術文章
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name
Membrane association of VP22, a herpes simplex virus type 1 tegument protein.
@ast
Membrane association of VP22, a herpes simplex virus type 1 tegument protein.
@en
Membrane association of VP22, a herpes simplex virus type 1 tegument protein.
@nl
type
label
Membrane association of VP22, a herpes simplex virus type 1 tegument protein.
@ast
Membrane association of VP22, a herpes simplex virus type 1 tegument protein.
@en
Membrane association of VP22, a herpes simplex virus type 1 tegument protein.
@nl
prefLabel
Membrane association of VP22, a herpes simplex virus type 1 tegument protein.
@ast
Membrane association of VP22, a herpes simplex virus type 1 tegument protein.
@en
Membrane association of VP22, a herpes simplex virus type 1 tegument protein.
@nl
P2093
P2860
P1433
P1476
Membrane association of VP22, a herpes simplex virus type 1 tegument protein.
@en
P2093
John W Wills
Joshua S Loomis
Michael J Brignati
Richard J Courtney
P2860
P304
P356
10.1128/JVI.77.8.4888-4898.2003
P407
P577
2003-04-01T00:00:00Z