A dramatic shift in the transmembrane topology of a viral envelope glycoprotein accompanies hepatitis B viral morphogenesis.
about
Protein N-myristoylation plays a critical role in the endoplasmic reticulum morphological change induced by overexpression of protein Lunapark, an integral membrane protein of the endoplasmic reticulumHepatitis B virus large envelope protein interacts with gamma2-adaptin, a clathrin adaptor-related proteinHepatitis B virus morphogenesisProperties of subviral particles of hepatitis B virusTopology of the Membrane-Associated Hepatitis C Virus Protein NS4BMolecular biology of hepatitis B virus infectionIdentification and characterization of peptides that interact with hepatitis B virus via the putative receptor binding siteInfection process of the hepatitis B virus depends on the presence of a defined sequence in the pre-S1 domainRole of the pre-S2 domain of the large envelope protein in hepatitis B virus assembly and infectivityHepatitis B virus-induced oncogenesis.Initiation of duck hepatitis B virus infection requires cleavage by a furin-like proteaseA short N-proximal region in the large envelope protein harbors a determinant that contributes to the species specificity of human hepatitis B virus.The emerging role of hepatitis B virus pre-S2 deletion mutant proteins in HBV tumorigenesis.Role of human sec63 in modulating the steady-state levels of multi-spanning membrane proteins.Inefficient signalase cleavage promotes efficient nucleocapsid incorporation into budding flavivirus membranes.Selection of peptide inhibitors of interactions involved in complex protein assemblies: association of the core and surface antigens of hepatitis B virus.Chaperone action in the posttranslational topological reorientation of the hepatitis B virus large envelope protein: Implications for translocational regulation.HBV life cycle: entry and morphogenesis.Roles of the envelope proteins in the amplification of covalently closed circular DNA and completion of synthesis of the plus-strand DNA in hepatitis B virus.Topology of the large envelope protein of duck hepatitis B virus suggests a mechanism for membrane translocation during particle morphogenesis.The small envelope protein is required for secretion of a naturally occurring hepatitis B virus mutant with pre-S1 deleted.Molecular virology of hepatitis B virus for clinicians.Epimorphin mediates mammary luminal morphogenesis through control of C/EBPbeta.The large surface protein of duck hepatitis B virus is phosphorylated in the pre-S domainPosttranslational modifications and secretion efficiency of immunogenic hepatitis B virus L protein deletion variants.Incorporation of hepatitis C virus E1 and E2 glycoproteins: the keystones on a peculiar virion.Functions of the internal pre-S domain of the large surface protein in hepatitis B virus particle morphogenesis.Role for calnexin and N-linked glycosylation in the assembly and secretion of hepatitis B virus middle envelope protein particles.Snow goose hepatitis B virus (SGHBV) envelope and capsid proteins independently contribute to the ability of SGHBV to package capsids containing single-stranded DNA in virions.Mutational analysis of glycosylation, membrane translocation, and cell surface expression of the hepatitis E virus ORF2 protein.Structure and glycosylation patterns of surface proteins from woodchuck hepatitis virus.Hepadnavirus envelope topology: insertion of a loop region in the membrane and role of S in L protein translocation.Molecular chaperone GRP78/BiP interacts with the large surface protein of hepatitis B virus in vitro and in vivo.Phenotypic mixing of rodent but not avian hepadnavirus surface proteins into human hepatitis B virus particlesFormation of intracellular particles by hepatitis B virus large surface protein.A short linear sequence in the pre-S domain of the large hepatitis B virus envelope protein required for virion formation.Dual topology of the large envelope protein of duck hepatitis B virus: determinants preventing pre-S translocation and glycosylation.Assembly of hepatitis B virus envelope proteins onto a lentivirus pseudotype that infects primary human hepatocytes.Infectivity determinants of the hepatitis B virus pre-S domain are confined to the N-terminal 75 amino acid residues.Immunoadhesins containing pre-S domains of hepatitis B virus large envelope protein are secreted and inhibit virus infection.
P2860
Q24339575-6FE17E83-0541-4059-B0C6-FB1F5AA9BBA3Q24529521-B9971E03-A7EB-481D-90CD-CD6B7097098EQ24563883-C8F7FC6B-4DB2-4E5B-9CEF-0565DB2DD2B6Q24658234-E4D34569-9BC3-4ED2-B8B2-4E62560369A1Q27473470-6D438306-C47D-45C2-BD88-2FA749F2C41DQ28083478-21C5C01D-0CBA-421B-877F-AC0F4AD9522FQ33267760-68CF97A6-FCF4-44A9-90CB-0BF4AD36DDBDQ33653137-921F17CA-2F1E-4E71-A44F-D2F64C1DBBA5Q33785018-937FA832-75C2-4266-B8F9-AF0D5D710492Q33787553-DC571941-A98B-4392-A77B-E53457D9EE3EQ33826761-0F8B6F97-5DB6-4D62-BB48-962BE02EC7DEQ33849892-51FE87D1-4211-496D-BC21-24952DB6770BQ34354947-C75C516A-9457-4ABD-982A-870D7961B0BEQ34482113-ECFD22EF-F7E6-4439-881F-8CEBAFDB5AC4Q34553454-39552DC9-1993-4603-AC08-54FCFA07FBE2Q34575501-1E744451-A365-4CD3-BEEE-CA5237C62B1AQ34982391-FA17043E-93BE-4338-99D8-3E0418A3FD98Q35259698-5F5975B5-56D8-458D-A762-69ECC7795D6CQ35531299-DA34843F-61D2-4E59-92A0-FFFAA2F4BE3EQ35876475-113ADB31-2C74-48FC-9C22-ED301E7CF2E3Q35888546-9DC02BB4-512C-402F-A3BB-8A60A7B6B001Q36282234-B5FAEB19-E101-49F0-A91A-925E1FBC45D1Q36366027-8024412B-B780-4D3A-83F2-F6E44DAA3D39Q36637159-496A91C7-211C-41DA-916A-07880A72589AQ36688211-0C84F94B-6E7B-4DFD-835E-56F4E35C008AQ38195180-E4E37DA9-633D-40BB-A702-8216B00CA3B1Q38290035-C8A956AB-C292-4683-B6A6-A88A12A04A3BQ38341008-0C7BC1B2-49BE-4470-AC42-A77960C6E63AQ39127774-4AC99BB7-7E4D-4F12-A6FB-AB388F134C18Q39550533-DAF3BC23-CC3C-485D-8CD9-0A82D189CE1DQ39583127-E816CE27-77E1-4A8F-A2DA-ABB0179FE4A8Q39589692-AA9BBB4C-5382-42E7-9507-CEE10487E0C3Q39700295-7976C698-8AB3-4DE9-86E9-707045C9C108Q39868858-9C2CC85C-0FC2-474A-A1C4-D91492FB49D8Q39880339-FF5F4652-DCE7-4BF5-BC52-8C66AE969379Q40015390-AAC89810-B746-4CB5-9271-9C2A258B77B2Q40015431-33C61DC3-5404-43DD-BC7F-7A04A48F1306Q40099387-CB463087-3A4C-4266-BACE-5EC0C766166DQ40155796-B76237A5-CAD6-4304-AF2A-621E80446CACQ40165285-F73E8DD7-F07A-4869-AF94-6BB4E97CB70F
P2860
A dramatic shift in the transmembrane topology of a viral envelope glycoprotein accompanies hepatitis B viral morphogenesis.
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on March 1994
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
A dramatic shift in the transm ...... patitis B viral morphogenesis.
@en
A dramatic shift in the transm ...... patitis B viral morphogenesis.
@nl
type
label
A dramatic shift in the transm ...... patitis B viral morphogenesis.
@en
A dramatic shift in the transm ...... patitis B viral morphogenesis.
@nl
prefLabel
A dramatic shift in the transm ...... patitis B viral morphogenesis.
@en
A dramatic shift in the transm ...... patitis B viral morphogenesis.
@nl
P2860
P1433
P1476
A dramatic shift in the transm ...... patitis B viral morphogenesis.
@en
P2093
Ostapchuk P
P2860
P304
P407
P50
P577
1994-03-01T00:00:00Z