Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins.
about
Genetic variability of the envelope gene of Type D simian retrovirus-2 (SRV-2) subtypes associated with SAIDS-related retroperitoneal fibromatosis in different macaque speciesMechanisms of viral entry: sneaking in the front doorMutational analysis of the subgroup A avian sarcoma and leukosis virus putative fusion peptide domain.The C terminus of the B5 receptor for herpes simplex virus contains a functional region important for infection.The viral transmembrane superfamily: possible divergence of Arenavirus and Filovirus glycoproteins from a common RNA virus ancestorInhibition of Henipavirus fusion and infection by heptad-derived peptides of the Nipah virus fusion glycoprotein.Mechanisms of coronavirus cell entry mediated by the viral spike proteinThe Coronavirus Spike Protein Is a Class I Virus Fusion Protein: Structural and Functional Characterization of the Fusion Core ComplexStructural requirements for low-pH-induced rearrangements in the envelope glycoprotein of tick-borne encephalitis virusMembrane and protein interactions of a soluble form of the Semliki Forest virus fusion proteinInhibition of human immunodeficiency virus type 1 infectivity by the gp41 core: role of a conserved hydrophobic cavity in membrane fusionStructural characterization of the human respiratory syncytial virus fusion protein coreStructural and functional analysis of interhelical interactions in the human immunodeficiency virus type 1 gp41 envelope glycoprotein by alanine-scanning mutagenesis.Mutations that destabilize the gp41 core are determinants for stabilizing the simian immunodeficiency virus-CPmac envelope glycoprotein complexDesign of an engineered N-terminal HIV-1 gp41 trimer with enhanced stability and potencyStructure of the Fusion Core and Inhibition of Fusion by a Heptad Repeat Peptide Derived from the S Protein of Middle East Respiratory Syndrome CoronavirusBioinformatic analysis of HIV-1 entry and pathogenesis.Atomic structure of a thermostable subdomain of HIV-1 gp41Mutations in the leucine zipper of the human immunodeficiency virus type 1 transmembrane glycoprotein affect fusion and infectivityThe ectodomain of HIV-1 env subunit gp41 forms a soluble, alpha-helical, rod-like oligomer in the absence of gp120 and the N-terminal fusion peptideMolecular basis of the structure and function of H1 hemagglutinin of influenza virus.Specific single or double proline substitutions in the "spring-loaded" coiled-coil region of the influenza hemagglutinin impair or abolish membrane fusion activity.Identification of a domain within the human T-cell leukemia virus type 2 envelope required for syncytium induction and replicationSIRE-1, a copia/Ty1-like retroelement from soybean, encodes a retroviral envelope-like protein.Structure of a proteolytically resistant core from the severe acute respiratory syndrome coronavirus S2 fusion proteinMutational analysis of heptad repeats in the membrane-proximal region of Newcastle disease virus HN protein.Subdomain folding and biological activity of the core structure from human immunodeficiency virus type 1 gp41: implications for viral membrane fusion.RhoA signaling is required for respiratory syncytial virus-induced syncytium formation and filamentous virion morphology.Biochemical analysis of the secreted and virion glycoproteins of Ebola virus.Mutations in the leucine zipper-like heptad repeat sequence of human immunodeficiency virus type 1 gp41 dominantly interfere with wild-type virus infectivity.Targeted recombination within the spike gene of murine coronavirus mouse hepatitis virus-A59: Q159 is a determinant of hepatotropism.A single amino acid change in the Newcastle disease virus fusion protein alters the requirement for HN protein in fusionRecognition by human monoclonal antibodies of free and complexed peptides representing the prefusogenic and fusogenic forms of human immunodeficiency virus type 1 gp41Interaction of peptides with sequences from the Newcastle disease virus fusion protein heptad repeat regions.Identification, phylogeny, and evolution of retroviral elements based on their envelope genes.Murine coronavirus spike protein determines the ability of the virus to replicate in the liver and cause hepatitis.Mutations in the fusion peptide and adjacent heptad repeat inhibit folding or activity of the Newcastle disease virus fusion proteinActivity of the Mason-Pfizer monkey virus fusion protein is modulated by single amino acids in the cytoplasmic tail.Identification of novel functional regions within the spike glycoprotein of MHV-A59 based on a bioinformatics approachSevere acute respiratory syndrome coronavirus (SARS-CoV) infection inhibition using spike protein heptad repeat-derived peptides.
P2860
Q21093217-9EEE8A54-D878-45A7-BCFD-C069529E2C7BQ22252690-F2BDD032-1B46-416C-9762-769F8FA651A9Q24524815-2AAE93F4-3780-4E31-81D7-76C9B42D3DCAQ24529146-2897ABA1-FB36-412B-8DF0-D0F222CE9E89Q24796207-78FEF04D-03BB-46B3-91B8-ACAC66BA034AQ24814238-2533EA1D-DF34-4B86-A800-ED85326C562AQ27027678-3099D735-65E5-4CB1-8FAD-CEF16AC01CF8Q27477706-099949BD-9077-472B-AE53-8DD3AA396D4DQ27480753-A6E23182-1C29-4868-BB32-AB7B07F9E071Q27485999-10539F80-A2A7-427D-8B51-88F2AD25A827Q27619600-43178937-870A-46F6-8EC6-19880C0C806DQ27628799-65DEF623-36CF-4F98-8330-91FFACFA0FFCQ27635422-1B0EA9C5-8E94-4900-BEB2-6C2F6AF5D63BQ27637675-5DA3A6FE-D444-45E9-9A0D-2575F31FCD3CQ27650133-F65A77F0-BE18-4E10-872F-C0658F5D6D31Q27680061-8BE19324-6BA2-4625-B7C8-4D1368BFD955Q27693321-FE6DBB7B-0162-4E1C-9388-641D0ADC923FQ27746904-DACE87FC-7B40-48A8-AD46-A8169FFDB0CDQ28646740-B8874BC6-E20E-433E-9373-E3FB2CA4D52BQ28646857-9A001E56-BA9B-462A-87FA-047A6E4372F4Q30418463-23B8A6DC-090D-43F5-AEA3-9D76CE18C12EQ30442103-4B5C9C7C-0A3B-4089-A7F3-8D434298ECF7Q30453537-66E27365-DC07-4305-848B-0C4FCFF2A355Q32061666-35104969-3D45-4E70-BFDD-43589C724AB9Q33581892-EE133C50-77E9-4A6C-BAE0-1FEFDAC87FDFQ33646121-30D23BDC-C92B-4A3D-9FB6-04D871559527Q33648376-920C469E-4197-45F9-A8D2-B309FF3BEF98Q33754914-28009E6F-6862-49B4-869B-4382F11A236CQ33783398-E5216F5B-FFCE-46F7-91BE-69E2562094E0Q33784040-C6A538C1-DFAC-4BA5-B68B-2560EEB1F7C8Q33785982-9F988801-F78B-45ED-80BD-3937F046E5FAQ33787073-8AC6233D-79E8-42CC-90C1-0644731A2AF3Q33807129-141A11DF-8897-4464-942B-C58204EB5F10Q33815821-D3A412C6-BE5D-4F54-8126-133D64447DEDQ33850069-1645ABBD-E8A1-426C-B905-6E7BD215F4DAQ33850858-F16B7672-FE40-44C1-8A14-4FEC68A3A667Q33853545-7B6F9B3F-B88F-4C80-8B2B-D9985F5BEB04Q33987377-CF4272F1-25E7-437A-A610-3F2195585039Q34053783-5874AFD9-DA1C-4294-8493-CE2A91A47108Q34376025-B5F69FFB-6A24-4C76-81B0-721683CB3BEB
P2860
Heptad repeat sequences are located adjacent to hydrophobic regions in several types of virus fusion glycoproteins.
description
1990 nî lūn-bûn
@nan
1990 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年論文
@yue
1990年論文
@zh-hant
1990年論文
@zh-hk
1990年論文
@zh-mo
1990年論文
@zh-tw
1990年论文
@wuu
name
Heptad repeat sequences are lo ...... of virus fusion glycoproteins.
@ast
Heptad repeat sequences are lo ...... of virus fusion glycoproteins.
@en
Heptad repeat sequences are lo ...... of virus fusion glycoproteins.
@nl
type
label
Heptad repeat sequences are lo ...... of virus fusion glycoproteins.
@ast
Heptad repeat sequences are lo ...... of virus fusion glycoproteins.
@en
Heptad repeat sequences are lo ...... of virus fusion glycoproteins.
@nl
prefLabel
Heptad repeat sequences are lo ...... of virus fusion glycoproteins.
@ast
Heptad repeat sequences are lo ...... of virus fusion glycoproteins.
@en
Heptad repeat sequences are lo ...... of virus fusion glycoproteins.
@nl
P2093
P1476
Heptad repeat sequences are lo ...... of virus fusion glycoproteins.
@en
P2093
P304
P356
10.1099/0022-1317-71-12-3075
P407
P478
71 ( Pt 12)
P577
1990-12-01T00:00:00Z