Crystal structure of the principal neutralization site of HIV-1
about
Hyperglycosylated mutants of human immunodeficiency virus (HIV) type 1 monomeric gp120 as novel antigens for HIV vaccine designAssembly of a polytopic membrane protein structure from the solution structures of overlapping peptide fragments of bacteriorhodopsin.Structure of Antibody F425-B4e8 in Complex with a V3 Peptide Reveals a New Binding Mode for HIV-1 NeutralizationStructure determination of an anti-HIV-1 Fab 447-52D–peptide complex from an epitaxially twinned data setCrystal Structure of the HIV-2 Neutralizing Fab Fragment 7C8 with High Specificity to the V3 Region of gp125Rabbit Anti-HIV-1 Monoclonal Antibodies Raised by Immunization Can Mimic the Antigen-Binding Modes of Antibodies Derived from HIV-1-Infected HumansThe complete Consensus V3 loop peptide of the envelope protein gp120 of HIV-1 shows pronounced helical character in solutionPrimary and tertiary structures of the Fab fragment of a monoclonal anti-E-selectin 7A9 antibody that inhibits neutrophil attachment to endothelial cellsMode of binding of anti-P-glycoprotein antibody MRK-16 to its antigen. A crystallographic and molecular modeling studyBactericidal antibody recognition of meningococcal PorA by induced fit. Comparison of liganded and unliganded Fab structuresSynthetic multimeric peptides derived from the principal neutralization domain (V3 loop) of human immunodeficiency virus type 1 (HIV-1) gp120 bind to galactosylceramide and block HIV-1 infection in a human CD4-negative mucosal epithelial cell lineTargeting of HIV gp120 by oligonucleotide-photosensitizer conjugates. Light-induced damages.3D structure model of the principal neutralizing epitope of Minnesota HIV-1 isolate.Dual spatial folds and different local structures of the HIV-1 immunogenic crown in various virus isolates.Conformational preferences of the HIV-1 principal neutralizing determinant.Structural analysis of the HIV-1 gp120 V3 loop: application to the HIV-Haiti isolates.Conformational model for the consensus V3 loop of the envelope protein gp120 of HIV-1 in a 20% trifluoroethanol/water solution.Human rhinovirus type 14:human immunodeficiency virus type 1 (HIV-1) V3 loop chimeras from a combinatorial library induce potent neutralizing antibody responses against HIV-1.Overview on concepts and applications of Fab antibody fragments.Nuclear magnetic resonance analysis of solution conformations in C4-V3 hybrid peptides derived from human immunodeficiency virus (HIV) type 1 gp120: relation to specificity of peptide-induced anti-HIV neutralizing antibodiesVaccination of rhesus macaques with recombinant Mycobacterium bovis bacillus Calmette-Guérin Env V3 elicits neutralizing antibody-mediated protection against simian-human immunodeficiency virus with a homologous but not a heterologous V3 motif.Extent of antigenic diversity in the V3 region of the surface glycoprotein, gp120, of human immunodeficiency virus type 1 group M and consequences for serotypingExpression, glycoform characterization, and antibody-binding of HIV-1 V3 glycopeptide domain fused with human IgG1-FcHigh resolution structures of the 4-4-20 Fab-fluorescein complex in two solvent systems: effects of solvent on structure and antigen-binding affinityHuman monoclonal antibodies specific for conformation-sensitive epitopes of V3 neutralize human immunodeficiency virus type 1 primary isolates from various clades.Identification of conserved and variable structures in the human immunodeficiency virus gp120 glycoprotein of importance for CXCR4 bindingHuman immunodeficiency virus (HIV) antigens: structure and serology of multivalent human mucin MUC1-HIV V3 chimeric proteins.Synthetic peptide vaccine and antibody therapeutic development: prevention and treatment of Pseudomonas aeruginosa.A human monoclonal antibody to a complex epitope in the V3 region of gp120 of human immunodeficiency virus type 1 has broad reactivity within and outside clade B.Chimeras from a human rhinovirus 14-human immunodeficiency virus type 1 (HIV-1) V3 loop seroprevalence library induce neutralizing responses against HIV-1.Curcumin improves synaptic plasticity impairment induced by HIV-1gp120 V3 loop.A role for urokinase-type plasminogen activator in human immunodeficiency virus type 1 infection of macrophages.Autoantibodies to the alpha/beta T-cell receptors in human immunodeficiency virus infection: dysregulation and mimicry.Evolutionary mechanisms and population dynamics of the third variable envelope region of HIV within single hosts.Crystal Structure of the Conserved Amino Terminus of the Extracellular Domain of Matrix Protein 2 of Influenza A Virus Gripped by an AntibodyGenetic and phenotypic analyses of human immunodeficiency virus type 1 escape from a small-molecule CCR5 inhibitor.Structure of a malaria parasite antigenic determinant displayed on filamentous bacteriophage determined by NMR spectroscopy: implications for the structure of continuous peptide epitopes of proteins.Structure and polymorphism of HIV-1 third variable loops.The sclerostin-neutralizing antibody AbD09097 recognizes an epitope adjacent to sclerostin's binding site for the Wnt co-receptor LRP6Tyrosine sulfation in the second variable loop (V2) of HIV-1 gp120 stabilizes V2-V3 interaction and modulates neutralization sensitivity
P2860
Q24679395-1823E4DB-4731-4B32-AA23-1871237D238EQ27633379-F1820F19-CEB4-4798-A748-013C76604D17Q27649247-DD3985C2-7230-469F-AE98-1011C1E489F9Q27650903-06541F9E-43FF-4549-85FF-83458D430C43Q27667679-C5B7511F-151D-488F-83A0-227FC797C0FCQ27679123-94270F90-625C-4799-BC9D-0247FF0839C7Q27729741-603ECA4F-A9AE-4811-BEEF-19084A96FBCCQ27756637-5B1087B1-B309-4E9C-B2C6-7C54D7D66A00Q27765326-0103334C-E4B6-42E9-8987-D6F0F99BCB3BQ27766459-DE26D289-6D39-4DD1-9185-70D94D9D702EQ28369122-72B3E8A8-D22D-403C-94F9-B56A6B1EB2B5Q30830795-2A1485D8-C9AE-49C0-915C-7984733432EAQ30886684-339B9AA0-26AE-4395-977A-E73E6A09E2A1Q30952700-8A252EC5-6F83-4BEB-B852-AB3CE496F5AFQ31010762-C555D81F-726A-44DF-9FD1-34F33CEEA5EDQ31112947-56E0B45A-BEC5-4925-B630-2FB1E60E7862Q31911259-8E600193-E314-4FA0-A254-CF4A73A5265EQ32157115-59628017-8B66-490D-85A1-909DD2BE606DQ33411367-71D3BB1A-F62A-413D-91D1-20177A0C1ADAQ33639792-AC3F28DD-2FEB-43F1-8FE9-674D69AE2FA6Q33717525-593113CC-E06A-47ED-8F29-36D47C64DFA6Q33782134-BBE1E166-CD9F-40C9-B47E-92867D16A8B6Q33984231-45362E7B-CC9D-4F7D-8E70-0F112C5675E0Q34018972-6CFC514F-1FDC-4228-A58D-AA0505ACDE8FQ34145199-C9A50E1D-3223-4903-81F5-1B4AB1C0C127Q34349528-0D0DF1CD-A4E0-4473-A14A-5B5C86C8B05FQ34867076-508AFB1E-C1B5-40DA-8414-A9E659C88333Q35136110-73BA936C-4BCC-4119-A56C-E304AAF923D0Q35828898-09BDB621-4256-4EF5-886A-BE083E7095F7Q35837816-4EF11566-3428-4B00-B915-5E35EC369314Q35837978-A2B491B7-F5EC-4EBD-88CD-54905C6C9B27Q35864006-AB851BAC-16BD-4B20-95E5-422EA376202FQ35882020-98D1E50E-6E62-4350-A4E6-BF14984A2E35Q35994354-49EDA662-3389-4CBA-8F28-DA7AD2F7B952Q36433887-E0905E9E-E573-4934-A43E-2C28AF5837A9Q36509765-0BCB634B-0D4C-4D4B-AB93-FC7AA78EC571Q36640407-64E616CF-6F9F-431C-928D-C2A5CCB481A1Q36798525-55A64CD5-F30B-4935-B282-8843C42E2594Q37224687-67FC9F5D-9044-4AE8-9526-3604AEE17BAEQ37612615-4D0F11C5-C61E-470D-A79B-FFC628108716
P2860
Crystal structure of the principal neutralization site of HIV-1
description
1994 nî lūn-bûn
@nan
1994 թուականի Ապրիլին հրատարակուած գիտական յօդուած
@hyw
1994 թվականի ապրիլին հրատարակված գիտական հոդված
@hy
1994年の論文
@ja
1994年論文
@yue
1994年論文
@zh-hant
1994年論文
@zh-hk
1994年論文
@zh-mo
1994年論文
@zh-tw
1994年论文
@wuu
name
Crystal structure of the principal neutralization site of HIV-1
@ast
Crystal structure of the principal neutralization site of HIV-1
@en
Crystal structure of the principal neutralization site of HIV-1
@nl
type
label
Crystal structure of the principal neutralization site of HIV-1
@ast
Crystal structure of the principal neutralization site of HIV-1
@en
Crystal structure of the principal neutralization site of HIV-1
@nl
prefLabel
Crystal structure of the principal neutralization site of HIV-1
@ast
Crystal structure of the principal neutralization site of HIV-1
@en
Crystal structure of the principal neutralization site of HIV-1
@nl
P2093
P3181
P356
P1433
P1476
Crystal structure of the principal neutralization site of HIV-1
@en
P2093
I A Wilson
J B Ghiara
R L Stanfield
P3181
P356
10.1126/SCIENCE.7511253
P407
P577
1994-04-01T00:00:00Z