Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro

Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro

Item
http://www.wikidata.org/entity/Q27480321
Signal peptidase cleavage at the flavivirus C-prM junction: dependence on the viral NS2B-3 protease for efficient processing requires determinants in C, the signal peptide, and prMEncapsidation of the flavivirus kunjin replicon RNA by using a complementation system providing Kunjin virus structural proteins in transAlpha-glucosidase inhibitors reduce dengue virus production by affecting the initial steps of virion morphogenesis in the endoplasmic reticulumMutagenesis of the NS2B-NS3-mediated cleavage site in the flavivirus capsid protein demonstrates a requirement for coordinated processingMutations in the Yellow Fever Virus Nonstructural Protein NS2A Selectively Block Production of Infectious ParticlesFolding and dimerization of tick-borne encephalitis virus envelope proteins prM and E in the endoplasmic reticulumHuman isolates of dengue type 1 virus induce apoptosis in mouse neuroblastoma cellsUpregulation of signalase processing and induction of prM-E secretion by the flavivirus NS2B-NS3 protease: roles of protease componentsFunctional Analysis of Potential Carboxy-Terminal Cleavage Sites of Tick-Borne Encephalitis Virus Capsid ProteinExtension of Flavivirus Protein C Differentially Affects Early RNA Synthesis and Growth in Mammalian and Arthropod Host CellsAn internal signal sequence directs intramembrane proteolysis of a cellular immunoglobulin domain proteinHighly efficient production of a dengue pseudoinfectious virus.Inefficient signalase cleavage promotes efficient nucleocapsid incorporation into budding flavivirus membranes.Internal ribosome entry site-based attenuation of a flavivirus candidate vaccine and evaluation of the effect of beta interferon coexpression on vaccine propertiesUncleaved NS2-3 is required for production of infectious bovine viral diarrhea virus.NS2B/3 proteolysis at the C-prM junction of the tick-borne encephalitis virus polyprotein is highly membrane dependent
P2860

Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro

Item
http://www.wikidata.org/entity/Q27480321
description
1995 nî lūn-bûn
@nan
1995 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1995 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1995年の論文
@ja
1995年論文
@yue
1995年論文
@zh-hant
1995年論文
@zh-hk
1995年論文
@zh-mo
1995年論文
@zh-tw
1995年论文
@wuu
name
Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro
@ast
Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro
@en
Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro
@nl
type
label
Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro
@ast
Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro
@en
Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro
@nl
prefLabel
Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro
@ast
Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro
@en
Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro
@nl
P1433
P1476
P2093
P2860
P304
P31
P433
P478
P577
P698
P932
P1433
P1476
Posttranslational signal peptidase cleavage at the flavivirus C-prM junction in vitro
@en
P2093
P2860
P304
P31
P433
P478
P577
P698
P932