Targeting of a heterodimeric membrane protein complex to the Golgi: rubella virus E2 glycoprotein contains a transmembrane Golgi retention signal.
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Role of rubella virus glycoprotein domains in assembly of virus-like particles.Rubella virus replication and links to teratogenicityAn investigation of the role of transmembrane domains in Golgi protein retentionThe transmembrane domain of hepatitis C virus glycoprotein E1 is a signal for static retention in the endoplasmic reticulum.A retention signal necessary and sufficient for endoplasmic reticulum localization maps to the transmembrane domain of hepatitis C virus glycoprotein E2.cDNA cloning and expression of bovine UDP-N-acetylglucosamine: alpha1, 3-D-mannoside beta1,4-N-acetylglucosaminyltransferase IV.The cytoplasmic tail of infectious bronchitis virus E protein directs Golgi targeting.Cryo-electron tomography of rubella virus.Rubella virus: first calcium-requiring viral fusion protein.An N-terminal polybasic domain and cell surface localization are required for mutant prion protein toxicity.Immunoisolation and characterization of a subdomain of the endoplasmic reticulum that concentrates proteins involved in COPII vesicle biogenesis.Rubella virus capsid protein: a small protein with big functions.Class II enveloped viruses.Effects of mutations in the rubella virus E1 glycoprotein on E1-E2 interaction and membrane fusion activity.Targeting of a short peptide derived from the cytoplasmic tail of the G1 membrane glycoprotein of Uukuniemi virus (Bunyaviridae) to the Golgi complexRubella virus E2 signal peptide is required for perinuclear localization of capsid protein and virus assembly.Characterization of the Golgi retention motif of Rift Valley fever virus G(N) glycoprotein.A retention signal necessary and sufficient for Golgi localization maps to the cytoplasmic tail of a Bunyaviridae (Uukuniemi virus) membrane glycoprotein.Characterization of an endoplasmic reticulum retention signal in the rubella virus E1 glycoprotein.Analysis of the selective advantage conferred by a C-E1 fusion protein synthesized by rubella virus DI RNAs.The transmembrane domains of the prM and E proteins of yellow fever virus are endoplasmic reticulum localization signals.Hepatitis C virus glycoprotein complex localization in the endoplasmic reticulum involves a determinant for retention and not retrieval.Localization of a yeast early Golgi mannosyltransferase, Och1p, involves retrograde transport.Intracellular transport of the glycoproteins gE and gI of the varicella-zoster virus. gE accelerates the maturation of gI and determines its accumulation in the trans-Golgi network.
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P2860
Targeting of a heterodimeric membrane protein complex to the Golgi: rubella virus E2 glycoprotein contains a transmembrane Golgi retention signal.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on January 1995
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Targeting of a heterodimeric m ...... mbrane Golgi retention signal.
@en
Targeting of a heterodimeric m ...... mbrane Golgi retention signal.
@nl
type
label
Targeting of a heterodimeric m ...... mbrane Golgi retention signal.
@en
Targeting of a heterodimeric m ...... mbrane Golgi retention signal.
@nl
prefLabel
Targeting of a heterodimeric m ...... mbrane Golgi retention signal.
@en
Targeting of a heterodimeric m ...... mbrane Golgi retention signal.
@nl
P2093
P2860
P356
P1476
Targeting of a heterodimeric m ...... mbrane Golgi retention signal.
@en
P2093
L Woodward
M G Farquhar
T C Hobman
P2860
P356
10.1091/MBC.6.1.7
P577
1995-01-01T00:00:00Z