A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity
about
Functional interaction of human immunodeficiency virus type 1 Vpu and Gag with a novel member of the tetratricopeptide repeat protein family.Pathogenesis of human immunodeficiency virus infectionNovel approaches to inhibit HIV entryIon-abrasion scanning electron microscopy reveals surface-connected tubular conduits in HIV-infected macrophagesReal-time visualization of HIV-1 GAG trafficking in infected macrophagesMembrane interface-interacting sequences within the ectodomain of the human immunodeficiency virus type 1 envelope glycoprotein: putative role during viral fusionEngineering T Cells to Functionally Cure HIV-1 InfectionCell type-dependence for Vpu functionCrystal Structure of the Pre-fusion Nipah Virus Fusion Glycoprotein Reveals a Novel Hexamer-of-Trimers AssemblyRequirement of N-terminal amino acid residues of gp41 for human immunodeficiency virus type 1-mediated cell fusionC-terminal tail of human immunodeficiency virus gp41: functionally rich and structurally enigmatic.Membrane fusion mediated by the influenza virus hemagglutinin requires the concerted action of at least three hemagglutinin trimers.Stoichiometry of envelope glycoprotein trimers in the entry of human immunodeficiency virus type 1Biophysical characterization of the structure of the amino-terminal region of gp41 of HIV-1. Implications on viral fusion mechanism.Mode of action of an antiviral peptide from HIV-1. Inhibition at a post-lipid mixing stage.Hexapeptides that interfere with HIV-1 fusion peptide activity in liposomes block GP41-mediated membrane fusion.The HIV envelope but not VSV glycoprotein is capable of mediating HIV latent infection of resting CD4 T cellsEffect of cleavage mutants on syncytium formation directed by the wild-type fusion protein of Newcastle disease virusRole of matrix in an early postentry step in the human immunodeficiency virus type 1 life cycle.Mutations in the leucine zipper-like heptad repeat sequence of human immunodeficiency virus type 1 gp41 dominantly interfere with wild-type virus infectivity.Cleavage of the murine leukemia virus transmembrane env protein by human immunodeficiency virus type 1 protease: transdominant inhibition by matrix mutations.Effect of polypurine tract (PPT) mutations on human immunodeficiency virus type 1 replication: a virus with a completely randomized PPT retains low infectivity.Identification and characterization of the putative fusion peptide of the severe acute respiratory syndrome-associated coronavirus spike proteinExpanded host cell tropism and cytopathic properties of feline immunodeficiency virus strain PPR subsequent to passage through interleukin-2-independent T cellsGlycosphingolipids promote entry of a broad range of human immunodeficiency virus type 1 isolates into cell lines expressing CD4, CXCR4, and/or CCR5.Reversion of a human immunodeficiency virus type 1 matrix mutation affecting Gag membrane binding, endogenous reverse transcriptase activity, and virus infectivity.trans-dominant interference with human immunodeficiency virus type 1 replication and transmission in CD4(+) cells by an envelope double mutant.Human immunodeficiency virus type 1 N-terminal capsid mutants that exhibit aberrant core morphology and are blocked in initiation of reverse transcription in infected cells.Cellular membrane-binding ability of the C-terminal cytoplasmic domain of human immunodeficiency virus type 1 envelope transmembrane protein gp41.Restoration of wild-type infectivity to human immunodeficiency virus type 1 strains lacking nef by intravirion reverse transcription.Identification and characterization of fusion and processing domains of the human immunodeficiency virus type 2 envelope glycoprotein.Mutation-directed chemical cross-linking of human immunodeficiency virus type 1 gp41 oligomers.HIV fusion peptide penetrates, disorders, and softens T-cell membrane mimics.TIM-family proteins inhibit HIV-1 release.Conformational partitioning of the fusion peptide of HIV-1 gp41 and its structural analogs in bilayer membranes.Oligomerization of fusogenic peptides promotes membrane fusion by enhancing membrane destabilizationOligomeric beta-structure of the membrane-bound HIV-1 fusion peptide formed from soluble monomers.Regional clustering of shared neutralization determinants on primary isolates of clade C human immunodeficiency virus type 1 from South Africa.Folded monomers and hexamers of the ectodomain of the HIV gp41 membrane fusion protein: potential roles in fusion and synergy between the fusion peptide, hairpin, and membrane-proximal external regionHIV-1 pathogenicity and virion production are dependent on the metabolic phenotype of activated CD4+ T cells
P2860
Q24523647-F0BA26B4-80E7-48A8-BD0A-E258B0F50DECQ24634681-727BAD05-88D0-4F1C-A50A-FC7700E42A39Q27013957-B0E8EFE1-3695-47A9-892C-1128CF9343AAQ27316251-C8383591-8514-4686-B9B8-A6377B19BB43Q27318996-D7C2C7AA-BF06-4F5F-BB1B-3496AE34B1E9Q27469690-02AA2D1E-E2F5-4D8A-AABC-0DFADE02FDF9Q28086801-2FD3122B-5067-464B-8E6D-27E105476E99Q28241247-DFE007C6-33BF-4014-8DDB-E13BF149AB86Q28551413-D9B984C0-97D5-4AF6-9178-59F901ADDD1DQ28646837-80FA964F-26C4-4600-A818-E69E090A1B0DQ30422545-3031F2D7-4243-4B87-898E-A5A1ADA616BDQ30442203-6D7E4D7F-EECA-4418-94C2-0DAC6DACC9C3Q30447936-A9AAF541-4696-48DE-A9D4-80F0988BAAFCQ30558462-A9747ADA-49EE-4C20-A696-8C70410A3A10Q31454800-6FF7F06D-FDA9-46EB-AC05-42D80E01A89AQ33241568-DF7774EB-A0CA-459F-B076-044AAD5912AEQ33511958-A506A3A3-EE84-4BFF-9936-14DC1D5877BDQ33782657-CFC57499-11FF-46C3-8351-28411FE8ADF6Q33782781-AF3A1199-24DF-4A01-992A-3685182C2806Q33784040-B87A3F19-16CA-4AA0-A2B8-1C8238B8499CQ33785977-49258D3D-88F4-46F7-875C-AA9466B4931DQ33788773-697DBD74-3959-4ADC-9855-8E07398BC787Q33788831-34A31B99-1057-4676-A6C8-F23F1C26A553Q33797700-3F1C1D78-8660-46F5-BBC7-D776581916D7Q33807605-645A952C-9605-4FE2-921B-E48AA4B210EFQ33813747-0B65D1BE-2259-488A-B025-7081E36581ECQ33819782-705F3B39-C45C-4E04-AFBC-5700D9870366Q33845811-01358902-05B9-4996-9DA9-A9F9E7C4AB2CQ33847059-B9CC396E-E7A8-49AE-A81A-340AD837215AQ33869997-E64CC78C-FF1C-4810-B461-FE9A08C1521AQ33935988-CBCCA364-822E-4EAA-B8DE-C0B0DF594AFEQ34070049-C9401A11-6A8D-477B-9AE1-A31E62C89943Q34131438-361E1FE2-CD63-488C-8EE8-1D0532A73664Q34144143-617F4C5A-14CA-46C5-81EE-81FFD821F95CQ34179319-9DDB7931-0383-4ADE-A7CD-C93ACD601A87Q34184290-2D3FD739-8D34-4E45-AC21-25750AB5A542Q34187142-9B6A405E-4F58-4256-AC77-4174F6A3CC38Q34332009-413FD049-28A8-4D5B-BF2F-9C2A20607DB2Q34579843-6556B983-09C1-4003-8BEE-03406F66C0DCQ34617099-627590B7-44E4-4736-992E-A3C901BE48D9
P2860
A mutation in the human immunodeficiency virus type 1 transmembrane glycoprotein gp41 dominantly interferes with fusion and infectivity
description
1992 nî lūn-bûn
@nan
1992年の論文
@ja
1992年論文
@yue
1992年論文
@zh-hant
1992年論文
@zh-hk
1992年論文
@zh-mo
1992年論文
@zh-tw
1992年论文
@wuu
1992年论文
@zh
1992年论文
@zh-cn
name
A mutation in the human immuno ...... es with fusion and infectivity
@ast
A mutation in the human immuno ...... es with fusion and infectivity
@en
type
label
A mutation in the human immuno ...... es with fusion and infectivity
@ast
A mutation in the human immuno ...... es with fusion and infectivity
@en
prefLabel
A mutation in the human immuno ...... es with fusion and infectivity
@ast
A mutation in the human immuno ...... es with fusion and infectivity
@en
P2093
P2860
P356
P1476
A mutation in the human immuno ...... es with fusion and infectivity
@en
P2093
A T Panganiban
E L Delwart
G L Buchschacher
P2860
P356
10.1073/PNAS.89.1.70
P407
P577
1992-01-01T00:00:00Z