about
The HIV glycan shield as a target for broadly neutralizing antibodiesAntibody 2G12 Recognizes Di-Mannose Equivalently in Domain- and Nondomain-Exchanged Forms but Only Binds the HIV-1 Glycan Shield if Domain ExchangedA nonself sugar mimic of the HIV glycan shield shows enhanced antigenicityA Potent and Broad Neutralizing Antibody Recognizes and Penetrates the HIV Glycan ShieldBroadly Neutralizing Antibody PGT121 Allosterically Modulates CD4 Binding via Recognition of the HIV-1 gp120 V3 Base and Multiple Surrounding GlycansSupersite of immune vulnerability on the glycosylated face of HIV-1 envelope glycoprotein gp120Targeting host-derived glycans on enveloped viruses for antibody-based vaccine designStructural Constraints Determine the Glycosylation of HIV-1 Envelope TrimersCell- and Protein-Directed Glycosylation of Native Cleaved HIV-1 EnvelopeGlycan clustering stabilizes the mannose patch of HIV-1 and preserves vulnerability to broadly neutralizing antibodiesBroad neutralization coverage of HIV by multiple highly potent antibodiesHIV-1 Glycan Density Drives the Persistence of the Mannose Patch within an Infected Individual.Ligand amplification in a dynamic combinatorial glycopeptide library.Envelope glycans of immunodeficiency virions are almost entirely oligomannose antigens.Analysis of the dispersity in carbohydrate loading of synthetic glycoproteins using MALDI-TOF mass spectrometry.The glycan shield of HIV is predominantly oligomannose independently of production system or viral clade.Variable loop glycan dependency of the broad and potent HIV-1-neutralizing antibodies PG9 and PG16.Very few substitutions in a germ line antibody are required to initiate significant domain exchange.Incomplete Neutralization and Deviation from Sigmoidal Neutralization Curves for HIV Broadly Neutralizing Monoclonal AntibodiesFolding of an MHC class II-restricted tumor antigen controls its antigenicity via MHC-guided processing.Mechanisms of escape from the PGT128 family of anti-HIV broadly neutralizing antibodiesB cells from knock-in mice expressing broadly neutralizing HIV antibody b12 carry an innocuous B cell receptor responsive to HIV vaccine candidatesResistance of Transmitted Founder HIV-1 to IFITM-Mediated Restriction.Rewritable glycochips.Convergent immunological solutions to Argentine hemorrhagic fever virus neutralization.Determination of N-linked Glycosylation in Viral Glycoproteins by Negative Ion Mass Spectrometry and Ion Mobility.Broadly neutralizing HIV antibodies define a glycan-dependent epitope on the prefusion conformation of gp41 on cleaved envelope trimers.The Tetrameric Plant Lectin BanLec Neutralizes HIV through Bidentate Binding to Specific Viral Glycans.Glycan Microheterogeneity at the PGT135 Antibody Recognition Site on HIV-1 gp120 Reveals a Molecular Mechanism for Neutralization ResistancePromiscuous glycan site recognition by antibodies to the high-mannose patch of gp120 broadens neutralization of HIV.Polysaccharide mimicry of the epitope of the broadly neutralizing anti-HIV antibody, 2G12, induces enhanced antibody responses to self oligomannose glycans.Correction for Doores et al., Two Classes of Broadly Neutralizing Antibodies within a Single Lineage Directed to the High-Mannose Patch of HIV Envelope.P19-03. Molecular mechanisms for enhancing the antigenicity of the carbohydrate epitope of the broadly neutralizing anti-HIV-1 antibody 2G12.P04-05. Requirements for antibody domain exchange explored through mutation of the germline 2G12 antibody.Reagent switchable stereoselective beta(1,2) mannoside mannosylation: OH-2 of mannose is a privileged acceptor.Engineered mice and B cell lines expressing broadly neutralizing antibodies and their unmutated precursors: tools for HIV vaccinology.Atomic-scale detection of organic molecules coupled to single-walled carbon nanotubes.P12-06. A 'non-self' mimic of the natural epitope of anti-HIV antibody 2G12 shows enhanced antigenicityP05-11. Yeast mannan genetics controls the molecular specificity of anti-carbohydrate antibodies cross-reactive to the HIV envelopeRecognition and penetration of the HIV-1 Env glycan shield by potent broadly neutralizing antibodies
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description
hulumtuese
@sq
onderzoeker
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researcher
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հետազոտող
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name
Katie J Doores
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Katie J Doores
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Katie J Doores
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Katie J Doores
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Katie J Doores
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Katie J Doores
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Katie J Doores
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Katie J Doores
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Katie J Doores
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Katie J Doores
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prefLabel
Katie J Doores
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Katie J Doores
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Katie J Doores
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Katie J Doores
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Katie J Doores
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P106
P21
P31
P496
0000-0002-5507-1725