Functional analysis of cell surface-expressed hepatitis C virus E2 glycoprotein.
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Characterization of hepatitis C virus E2 glycoprotein interaction with a putative cellular receptor, CD81.Hepatitis C virus glycoproteins interact with DC-SIGN and DC-SIGNRScavenger receptor BI and BII expression levels modulate hepatitis C virus infectivityInfectious hepatitis C virus pseudo-particles containing functional E1-E2 envelope protein complexesGenetic Diversity Underlying the Envelope Glycoproteins of Hepatitis C Virus: Structural and Functional Consequences and the Implications for Vaccine DesignThe hepatitis C virus glycan shield and evasion of the humoral immune responseCharacterization of hepatitis C virus (HCV) and HCV E2 interactions with CD81 and the low-density lipoprotein receptorCell fusion activity of hepatitis C virus envelope proteinsFunctional characterization of intracellular and secreted forms of a truncated hepatitis C virus E2 glycoproteinBinding of hepatitis C virus E2 glycoprotein to CD81 does not correlate with species permissiveness to infectionAnalysis of antigenicity and topology of E2 glycoprotein present on recombinant hepatitis C virus-like particles.Functional analysis of hepatitis C virus envelope proteins, using a cell-cell fusion assay.Different Domains of CD81 Mediate Distinct Stages of Hepatitis C Virus Pseudoparticle EntryL-SIGN (CD 209L) is a liver-specific capture receptor for hepatitis C virusHepatitis C virus glycoproteins mediate pH-dependent cell entry of pseudotyped retroviral particlesCharacterization of Fusion Determinants Points to the Involvement of Three Discrete Regions of Both E1 and E2 Glycoproteins in the Membrane Fusion Process of Hepatitis C VirusStudying Hepatitis C Virus: Making the Best of a Bad VirusDissecting the role of putative CD81 binding regions of E2 in mediating HCV entry: Putative CD81 binding region 1 is not involved in CD81 bindingCD81 and Claudin 1 Coreceptor Association: Role in Hepatitis C Virus EntryA computational approach identifies two regions of Hepatitis C Virus E1 protein as interacting domains involved in viral fusion processHepatitis C Virus NS2 Protein Contributes to Virus Particle Assembly via Opposing Epistatic Interactions with the E1-E2 Glycoprotein and NS3-NS4A Enzyme ComplexesMutagenesis of the fusion peptide-like domain of hepatitis C virus E1 glycoprotein: involvement in cell fusion and virus entryMutational analysis of the hepatitis C virus E1 glycoprotein in retroviral pseudoparticles and cell-culture-derived H77/JFH1 chimeric infectious virus particlesThe Disulfide Bonds in Glycoprotein E2 of Hepatitis C Virus Reveal the Tertiary Organization of the MoleculeThe impact of hepatitis C virus entry on viral tropismA novel small molecule inhibitor of hepatitis C virus entryCD81 is an entry coreceptor for hepatitis C virusUnexpected structural features of the hepatitis C virus envelope protein 2 ectodomain.Capitalizing on knowledge of hepatitis C virus neutralizing epitopes for rational vaccine designNA proteins of influenza A viruses H1N1/2009, H5N1, and H9N2 show differential effects on infection initiation, virus release, and cell-cell fusion.The missing pieces of the HCV entry puzzle.NS2 is dispensable for efficient assembly of hepatitis C virus-like particles in a bipartite trans-encapsidation system.Interacting regions of CD81 and two of its partners, EWI-2 and EWI-2wint, and their effect on hepatitis C virus infectionHepatitis C virus is primed by CD81 protein for low pH-dependent fusionCyclic adenosine monophosphate response element-binding protein transcriptionally regulates CHCHD2 associated with the molecular pathogenesis of hepatocellular carcinoma.Flunarizine prevents hepatitis C virus membrane fusion in a genotype-dependent manner by targeting the potential fusion peptide within E1.Specialization of Hepatitis C Virus Envelope Glycoproteins for B Lymphocytes in Chronically Infected Patients.Hepatitis C Virus Envelope Glycoprotein E1 Forms Trimers at the Surface of the Virion.Broadly neutralizing immune responses against hepatitis C virus induced by vectored measles viruses and a recombinant envelope protein boosterIdentification of a New Benzimidazole Derivative as an Antiviral against Hepatitis C Virus
P2860
Q22010245-FCD7E555-3EFD-4101-8CD6-90580B2765F1Q24551041-5AC1344F-6081-4E10-833C-561DE05A5AB6Q24672232-FBF2FE49-67D1-4AC2-9DFA-E204EAD84139Q24673768-5A0CFB12-E0C9-4A3D-A003-08753A40FA9DQ26801759-1BA6F8DD-343C-4385-A648-80E4EC9B8608Q27023390-BD52896E-0D13-407C-AF9C-AD024ACE99B0Q27469307-EE707F3B-80CA-405C-B42A-221872C9B7D5Q27469594-7C57765E-E9E7-4522-88F8-1BF942BA8DD5Q27469621-EFF66724-345A-4BAD-B22C-01228AD89826Q27469669-2F439DDF-9F75-4B78-BC20-5DF63636949EQ27472891-E3B6DC13-9BFD-497B-A38C-D3AB2E2730ECQ27472928-97BB5F5B-04D1-47E6-97F0-9E1F34E3803AQ27473222-161DA7E8-3B3B-4BAB-BBD5-8565864E097EQ27473455-B6BD6505-6424-4004-97B4-58097712DAC6Q27477687-17F4F0D7-3E01-498A-8FDD-01D5B3C3B2B9Q27481024-090DAD88-DEC5-4642-AF31-D97DA1A3B7F2Q27481034-11E70DFA-D0DA-4EBB-8BF6-1CFAE2FD4409Q27485638-BD5465C6-C5C8-42F0-B5A1-7B01B520A34DQ27485899-5F540CA8-BA8D-40AC-B766-55B3E0D3866BQ27489412-4DD70CC0-064A-413E-9466-255F663203A8Q27489514-373CF189-A3A6-49CE-A580-936F561DA1DAQ27489898-499B682E-3BB1-4610-9C12-BCC488DB6D8CQ27490271-C0B51E8D-461C-4CCE-920D-1ABAAFE4C5FEQ27490948-E8293864-3EDB-47F7-B145-8A0689F8030DQ27693297-CDC17A53-CA3F-4D43-B1FB-6D5372650ED0Q28475468-D7AC6798-F4F0-45DD-929C-A743F8D97C24Q29614812-D7F534E1-3201-42A8-A62B-CE75CFD6AF6FQ30364309-164E037C-FCC2-42ED-B9CE-CF3D32837284Q30374314-4DCA5683-95C3-4231-B3E2-FDFCE3D04F1CQ30426345-E45FC206-1E5E-40CD-9738-80CDF3E8AB81Q33360674-64AE28CE-2832-44D7-B251-8B0419387DDBQ34366406-A3D70513-7525-40CB-82F3-E3B6B50FF3A4Q34799950-356109C7-9D81-45F4-A3E8-97234109D75AQ35182834-92F709B0-071B-45AB-932A-EE57919483B4Q35387526-4412EEF3-C6D0-4085-91C2-203971162737Q35739094-31357DCA-1D77-48CF-B194-031BE3E18B7CQ35832687-7CA29073-1BCB-43FE-B4EC-47605827DB4BQ36086218-DC7408A0-87D2-4741-9E0F-28A53DB1EC65Q36363203-6F94CF2D-9E25-4386-9E24-4B2FD763C44DQ37252935-6ECEAFAB-3794-453C-909D-D623C0BEAA57
P2860
Functional analysis of cell surface-expressed hepatitis C virus E2 glycoprotein.
description
1999 nî lūn-bûn
@nan
1999 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1999 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
name
Functional analysis of cell surface-expressed hepatitis C virus E2 glycoprotein
@nl
Functional analysis of cell surface-expressed hepatitis C virus E2 glycoprotein.
@ast
Functional analysis of cell surface-expressed hepatitis C virus E2 glycoprotein.
@en
type
label
Functional analysis of cell surface-expressed hepatitis C virus E2 glycoprotein
@nl
Functional analysis of cell surface-expressed hepatitis C virus E2 glycoprotein.
@ast
Functional analysis of cell surface-expressed hepatitis C virus E2 glycoprotein.
@en
prefLabel
Functional analysis of cell surface-expressed hepatitis C virus E2 glycoprotein
@nl
Functional analysis of cell surface-expressed hepatitis C virus E2 glycoprotein.
@ast
Functional analysis of cell surface-expressed hepatitis C virus E2 glycoprotein.
@en
P2093
P2860
P1433
P1476
Functional analysis of cell surface-expressed hepatitis C virus E2 glycoprotein.
@en
P2093
C M Maidens
J A McKeating
J M Thomas
W S Barclay
P2860
P304
P577
1999-08-01T00:00:00Z