Interaction between the human T-cell lymphotropic virus type IIIB envelope glycoprotein gp120 and the surface antigen CD4: role of carbohydrate in binding and cell fusion.
about
Sequence and expression of a membrane-associated C-type lectin that exhibits CD4-independent binding of human immunodeficiency virus envelope glycoprotein gp120Role of oligosaccharides in the processing and maturation of envelope glycoproteins of human immunodeficiency virus type 1Human immunodeficiency virus-1 glycoproteins gp120 and gp160 specifically inhibit the CD3/T cell-antigen receptor phosphoinositide transduction pathwayA lectin isolated from bananas is a potent inhibitor of HIV replicationPathogenesis of human immunodeficiency virus infectionRole of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1Glycosylation is necessary for the correct folding of human immunodeficiency virus gp120 in CD4 bindingBiosynthesis and processing of human immunodeficiency virus type 1 envelope glycoproteins: effects of monensin on glycosylation and transportSulfation of the human immunodeficiency virus envelope glycoproteinEffect of various glycosidase treatments on the resistance of the HIV-1 envelope to degradationA synthetic peptide inhibitor of human immunodeficiency virus replication: correlation between solution structure and viral inhibitionHuman immunodeficiency virus type 1 protease inhibitors irreversibly block infectivity of purified virions from chronically infected cellsAlpha-(1-3)- and alpha-(1-6)-D-mannose-specific plant lectins are markedly inhibitory to human immunodeficiency virus and cytomegalovirus infections in vitroInhibition of human immunodeficiency virus (HIV) infection in vitro by anticarbohydrate monoclonal antibodies: peripheral glycosylation of HIV envelope glycoprotein gp120 may be a target for virus neutralizationNonrandom distribution of gp120 N-linked glycosylation sites important for infectivity of human immunodeficiency virus type 1A molecular clasp in the human immunodeficiency virus (HIV) type 1 TM protein determines the anti-HIV activity of gp41 derivatives: implication for viral fusionImpact of HIV on cell survival and antiviral activity of plasmacytoid dendritic cellsVertical transmission of human immunodeficiency virus is correlated with the absence of high-affinity/avidity maternal antibodies to the gp120 principal neutralizing domain.A soluble recombinant polypeptide comprising the amino-terminal half of the extracellular region of the CD4 molecule contains an active binding site for human immunodeficiency virus.Binding site for human immunodeficiency virus coat protein gp120 is located in the NH2-terminal region of T4 (CD4) and requires the intact variable-region-like domain.95- and 25-kDa fragments of the human immunodeficiency virus envelope glycoprotein gp120 bind to the CD4 receptorAminosugar derivatives as potential anti-human immunodeficiency virus agents.Specific interaction of aurintricarboxylic acid with the human immunodeficiency virus/CD4 cell receptor.The human and simian immunodeficiency virus envelope glycoprotein transmembrane subunits are palmitoylated.Influence of carbohydrate moieties on the immunogenicity of human immunodeficiency virus type 1 recombinant gp160.An aptamer that neutralizes R5 strains of human immunodeficiency virus type 1 blocks gp120-CCR5 interaction.Vaccine and antiviral strategies against infections caused by human immunodeficiency virus.Stapled HIV-1 peptides recapitulate antigenic structures and engage broadly neutralizing antibodies.How does HIV-1 infect a susceptible human cell?: Current thinkingNoninfectious entry of HIV-1 into peripheral and brain macrophages mediated by the mannose receptorThe majority of cells are superinfected in a cloned cell line that produces high levels of human immunodeficiency virus type 1 strain MN.Oligomerization of the hydrophobic heptad repeat of gp41.N-butyldeoxynojirimycin-mediated inhibition of human immunodeficiency virus entry correlates with changes in antibody recognition of the V1/V2 region of gp120Mutation of a Single Envelope N-Linked Glycosylation Site Enhances the Pathogenicity of Bovine Leukemia Virus.Strategies in the treatment of AIDS and related diseases: the lessons of cancer chemotherapy.Viral cell recognition and entry.Antibody raised against soluble CD4-rgp120 complex recognizes the CD4 moiety and blocks membrane fusion without inhibiting CD4-gp120 binding.Phenotypic variation in the response to the human immunodeficiency virus among derivatives of the CEM T and WIL-2 B cell linesA human serum mannose-binding protein inhibits in vitro infection by the human immunodeficiency virusRole of N-linked glycans in the interaction between the envelope glycoprotein of human immunodeficiency virus and its CD4 cellular receptor. Structural enzymatic analysis
P2860
Q24296281-F51F5124-0FE7-4825-A4CA-5737091DD699Q24615670-BAA033A6-A4E6-4D8D-AD7E-B88B1DC47830Q24619935-038216C4-8641-483D-9EC7-5BA2C7762282Q24629155-DB2A717B-D2C2-4B90-9315-1FE4D3E87ED2Q24634681-7C1CC633-0495-49FB-A11A-DCF727B21458Q24643931-1DAEDE40-32A4-4EEA-A499-88F97C5C5BB9Q24644617-7EE4D904-A312-4A4D-BC8A-E74C263FC02DQ24646043-BA64B1DB-940D-40F8-BDCF-A12673480D6FQ24647955-E33DDE57-7019-4A19-B652-1FC69BF12A68Q28235367-ADC4D3BA-7A01-42A6-9843-30B2CA73749BQ28317348-E0ACA2B0-CD6D-464B-BA01-656D77FD0437Q28318483-958B5C92-4D8D-4D77-846E-6695C39535A8Q28321244-2DFADD48-8DFF-4AC6-A833-32667E0B6B28Q28323332-8C860666-3A47-45A7-B1AD-B7751B4707FBQ28646731-15AA282F-B687-4C10-8BF5-14D21D99EF4FQ28646828-79994EE7-F9FF-4809-A963-F9381EB07848Q33285471-AE3F3DFE-59A0-40EB-AC6B-69B154271F1AQ33564746-595CF3F0-684C-4921-9597-4DC4D612984AQ33564946-3FC58A48-929C-4796-8A11-CCE6D1249F4AQ33641132-94F567DD-50BA-4ADA-B4F7-AB3D98E66841Q33645518-5B798331-D144-47F3-95C1-6C0C6F472765Q33681820-A72811BD-8836-459C-8781-4C24B2DACAF9Q33854208-0B79BE8B-86BE-43A0-B0FC-01F700452A0CQ33876152-A5E5D311-7A38-4506-B03C-19DC34EA0F5BQ33933098-E5421719-BB46-4C32-B057-04A9C4E88843Q34092668-31E0D58C-D2E1-486C-8806-3FAD4BB586EBQ34101462-475300E3-08F9-4478-9754-DFA0FC3C942FQ35007412-AE80D0C1-11DD-4762-8492-7C7D00675EB2Q35217312-7EC92B00-A0F8-4D2F-9187-4A72D4A93CB8Q35677825-F9F8B85E-D42B-4B9D-8D32-FF5DFF47A0FEQ35837877-AE98C9B6-73E3-4E23-99E1-124DC337F9A1Q35838506-E9C6E2E2-6D85-4419-B651-C4F1CA15CEB8Q35870879-AF6638B9-DE47-4CDB-801A-48452F38FD39Q35913955-6C63E109-3CC4-4EC1-B9D6-A29D6A4DE9B5Q35930774-3F148CE2-3591-4C9F-ABBA-270905A2F5EEQ36278326-DADC5B2C-6812-458D-A664-9421C0907421Q36353645-110DE61D-DD13-4D3E-88B8-7C5C68814C25Q36355185-A7945EB7-7786-47BF-AEE6-C23C27E3AA51Q36355881-D361EEB3-B2D2-4FDE-87C7-C41D98B98D21Q36356138-E502729A-538C-4C9C-9D96-51C125FD2685
P2860
Interaction between the human T-cell lymphotropic virus type IIIB envelope glycoprotein gp120 and the surface antigen CD4: role of carbohydrate in binding and cell fusion.
description
1987 nî lūn-bûn
@nan
1987 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
1987 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
1987年の論文
@ja
1987年論文
@yue
1987年論文
@zh-hant
1987年論文
@zh-hk
1987年論文
@zh-mo
1987年論文
@zh-tw
1987年论文
@wuu
name
Interaction between the human ...... te in binding and cell fusion.
@ast
Interaction between the human ...... te in binding and cell fusion.
@en
Interaction between the human ...... te in binding and cell fusion.
@nl
type
label
Interaction between the human ...... te in binding and cell fusion.
@ast
Interaction between the human ...... te in binding and cell fusion.
@en
Interaction between the human ...... te in binding and cell fusion.
@nl
prefLabel
Interaction between the human ...... te in binding and cell fusion.
@ast
Interaction between the human ...... te in binding and cell fusion.
@en
Interaction between the human ...... te in binding and cell fusion.
@nl
P2093
P2860
P356
P1476
Interaction between the human ...... te in binding and cell fusion.
@en
P2093
A J Langlois
D P Bolognesi
H K Lyerly
K J Weinhold
T J Matthews
P2860
P304
P356
10.1073/PNAS.84.15.5424
P407
P50
P577
1987-08-01T00:00:00Z