about
Modes of paramyxovirus fusion: a Henipavirus perspectiveHenipavirus mediated membrane fusion, virus entry and targeted therapeuticsSynthetic protocells interact with viral nanomachinery and inactivate pathogenic human virusA general strategy to endow natural fusion-protein-derived peptides with potent antiviral activitySimulating henipavirus multicycle replication in a screening assay leads to identification of a promising candidate for therapy.Antiviral activity of gliotoxin, gentian violet and brilliant green against Nipah and Hendra virus in vitroInhibition of Nipah virus infection in vivo: targeting an early stage of paramyxovirus fusion activation during viral entryViral entry inhibitors targeted to the membrane site of action.Off Label Antiviral Therapeutics for Henipaviruses: New Light Through Old Windows.Henipavirus outbreaks to antivirals: the current status of potential therapeutics.Premature activation of the paramyxovirus fusion protein before target cell attachment with corruption of the viral fusion machineryCapturing a fusion intermediate of influenza hemagglutinin with a cholesterol-conjugated peptide, a new antiviral strategy for influenza virus.Hendra and nipah infection: pathology, models and potential therapies.Emerging paramyxoviruses: molecular mechanisms and antiviral strategiesSpring-loaded heptad repeat residues regulate the expression and activation of paramyxovirus fusion protein.A second receptor binding site on human parainfluenza virus type 3 hemagglutinin-neuraminidase contributes to activation of the fusion mechanism.Molecular determinants of antiviral potency of paramyxovirus entry inhibitors.Identification and evaluation of a highly effective fusion inhibitor for human metapneumovirusDevelopment of Small-molecule HIV Entry Inhibitors Specifically Targeting gp120 or gp41Development and validation of a chemiluminescent immunodetection assay amenable to high throughput screening of antiviral drugs for Nipah and Hendra virus.Kinetic dependence of paramyxovirus entry inhibition.Recent advances in diagnosis, prevention, and treatment of human respiratory syncytial virus.Hendra virus: a one health tale of flying foxes, horses and humans.Cholesterol-conjugated peptide antivirals: a path to a rapid response to emerging viral diseases.Henipavirus pathogenesis and antiviral approaches.Antiviral Lipopeptide-Cell Membrane Interaction Is Influenced by PEG Linker Length.Infectivity inhibition by overlapping synthetic peptides derived from the gH/gL heterodimer of herpes simplex virus type 1.Regulation of paramyxovirus fusion activation: the hemagglutinin-neuraminidase protein stabilizes the fusion protein in a pretriggered state.Spring-loaded model revisited: paramyxovirus fusion requires engagement of a receptor binding protein beyond initial triggering of the fusion protein.A quantitative and kinetic fusion protein-triggering assay can discern distinct steps in the nipah virus membrane fusion cascadeCholesterol conjugation potentiates the antiviral activity of an HIV immunoadhesin.Differential rates of protein folding and cellular trafficking for the Hendra virus F and G proteins: implications for F-G complex formation.Fusion Inhibitory Lipopeptides Engineered for Prophylaxis of Nipah Virus in Primates.Inhibition of Flaviviruses by Targeting a Conserved Pocket on the Viral Envelope ProteinInterface Peptides
P2860
Q24604089-BC80C017-C1F3-4D68-B1F3-AE9D4FCDCA3BQ27002511-343A43DD-57B0-4D22-93DE-A2D365434072Q27430064-D1925094-39AA-4B4D-A5EC-B276C6065CE5Q28729918-D3899DA4-5A76-4204-969D-4CE4E8AD90C5Q33415278-F88180C9-74A4-4241-A727-0FB8F2E9F927Q33514948-4441B0B0-50E4-4F4C-AFDE-9B240322F248Q33741962-10048468-8776-423D-B039-6051BF9D082BQ33990602-69169155-CEB5-4406-972F-F8A64CE0208BQ34021811-F150C432-9E07-47AC-8365-4EA1B916BFCFQ35141580-0E6B51CA-4AB1-41F6-8842-B422431CAE11Q35515383-C0078130-F281-4AE8-9511-A175F5D11A2BQ35604856-F81FF4BD-CDCB-49F7-B43F-02530D80A2E3Q35658146-F3B8285E-C53B-4D4A-A7ED-778AD1CABAA1Q35658152-AE19B006-2BCC-4C5F-90E3-34C97AB96943Q35785110-2CD3CB46-26A1-45DF-8BF0-57287E6456B4Q35785169-17979A46-2820-4362-93FB-608D81DE2761Q36099124-EFB234C6-6F04-42F6-94A4-6E559E88A042Q36422618-04877FE5-FCA4-412E-91F6-F7CCAE4E21F8Q36643050-C82E75C8-8CB8-4E90-96CD-F6C96298FE59Q37121907-FB74EC92-9836-4ECC-9DDC-EF0CCCE910CBQ37232863-B32ADD07-1DBA-4BCE-8488-8F7007285790Q37412509-833BAE60-00E5-4346-91FB-8CFDB514A840Q38093644-EECEC0CA-53B7-4941-976C-6FCBB50EB7C3Q38261556-FDA2608B-CA1C-4DEE-839A-E2BDFFC27801Q38337204-2E6FF920-D58D-41A7-80F0-0B38E10CF388Q38675925-20649C63-5A24-4CBF-BA21-EFDFC8808D7CQ38962811-D9CD95E9-054C-4AC3-BAE5-88664A4481ACQ39275444-31C91F39-5E99-4A09-9322-7788BA79FBB0Q39462591-1B7CEFDF-63C1-428A-88BE-3A0D595EE2D1Q39697289-334CFD21-984E-4479-ACF4-64E2BC3720BFQ41041346-FD428423-3FA0-4BF1-9C89-DB2D818E59B7Q42546299-F005C5A4-34F0-40B2-B9C5-D7FC740F9221Q51783167-C8502A43-C21E-47C7-9CAE-D7983049DBFAQ56339834-7BE3A4F2-3597-483C-8E27-9655BA7B2AB6Q57721879-D15AB951-F801-4D41-A52D-B5F8C6E953B9
P2860
description
2006 nî lūn-bûn
@nan
2006 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Inhibition of hendra virus fusion.
@ast
Inhibition of hendra virus fusion.
@en
type
label
Inhibition of hendra virus fusion.
@ast
Inhibition of hendra virus fusion.
@en
prefLabel
Inhibition of hendra virus fusion.
@ast
Inhibition of hendra virus fusion.
@en
P2093
P2860
P356
P1433
P1476
Inhibition of hendra virus fusion
@en
P2093
P2860
P304
P356
10.1128/JVI.00736-06
P407
P577
2006-10-01T00:00:00Z