Partial enzymatic deglycosylation preserves the structure of cleaved recombinant HIV-1 envelope glycoprotein trimers. - Wikidata - awgldk - TriplyDB

Partial enzymatic deglycosylation preserves the structure of cleaved recombinant HIV-1 envelope glycoprotein trimers.

Partial enzymatic deglycosylation preserves the structure of cleaved recombinant HIV-1 envelope glycoprotein trimers.

http://www.wikidata.org/entity/Q34285680

about

Dynamic Viral Glycoprotein Machines: Approaches for Probing Transient States That Drive Membrane Fusion Rational HIV Immunogen Design to Target Specific Germline B Cell Receptors Broadly Neutralizing Antibody PGT121 Allosterically Modulates CD4 Binding via Recognition of the HIV-1 gp120 V3 Base and Multiple Surrounding Glycans Crystal Structure of a Soluble Cleaved HIV-1 Envelope Trimer Structure and Immunogenicity of a Peptide Vaccine, Including the Complete HIV-1 gp41 2F5 Epitope A next-generation cleaved, soluble HIV-1 Env trimer, BG505 SOSIP.664 gp140, expresses multiple epitopes for broadly neutralizing but not non-neutralizing antibodies HIV-1 VACCINES. HIV-1 neutralizing antibodies induced by native-like envelope trimers Structure of 2G12 Fab2 in complex with soluble and fully glycosylated HIV-1 Env by negative-stain single-particle electron microscopy Composition and Antigenic Effects of Individual Glycan Sites of a Trimeric HIV-1 Envelope Glycoprotein Recent advances on the use of structural biology for the design of novel envelope immunogens of HIV-1 The influence of N-linked glycans on the molecular dynamics of the HIV-1 gp120 V3 loop.Influenza Virus Hemagglutinin Glycoproteins with Different N-Glycan Patterns Activate Dendritic Cells In Vitro.Antigenic and 3D structural characterization of soluble X4 and hybrid X4-R5 HIV-1 Env trimers Analysis of carbohydrates and glycoconjugates by matrix-assisted laser desorption/ionization mass spectrometry: An update for 2011-2012.Increased functional stability and homogeneity of viral envelope spikes through directed evolution.Structural evolution of glycan recognition by a family of potent HIV antibodies.Comparative Immunogenicity of Evolved V1V2-Deleted HIV-1 Envelope Glycoprotein Trimers Well-ordered trimeric HIV-1 subtype B and C soluble spike mimetics generated by negative selection display native-like properties Immunogenic Display of Purified Chemically Cross-Linked HIV-1 Spikes.A New Approach to Produce HIV-1 Envelope Trimers: BOTH CLEAVAGE AND PROPER GLYCOSYLATION ARE ESSENTIAL TO GENERATE AUTHENTIC TRIMERS Antibodies to a conformational epitope on gp41 neutralize HIV-1 by destabilizing the Env spike.Minimally Mutated HIV-1 Broadly Neutralizing Antibodies to Guide Reductionist Vaccine Design.Asymmetric recognition of the HIV-1 trimer by broadly neutralizing antibody PG9.Structural characterization of cleaved, soluble HIV-1 envelope glycoprotein trimers.Influences on trimerization and aggregation of soluble, cleaved HIV-1 SOSIP envelope glycoprotein.High-sensitivity analytical approaches for the structural characterization of glycoproteins.Structural insights into key sites of vulnerability on HIV-1 Env and influenza HA.Conserved immunogens in prime-boost strategies for the next-generation HIV-1 vaccines.Stable 293 T and CHO cell lines expressing cleaved, stable HIV-1 envelope glycoprotein trimers for structural and vaccine studies.Global site-specific N-glycosylation analysis of HIV envelope glycoprotein.Model Building and Refinement of a Natively Glycosylated HIV-1 Env Protein by High-Resolution Cryoelectron Microscopy.Immunosilencing a highly immunogenic protein trimerization domain.Guiding the immune response against influenza virus hemagglutinin toward the conserved stalk domain by hyperglycosylation of the globular head domain

P2860

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P2860

Partial enzymatic deglycosylation preserves the structure of cleaved recombinant HIV-1 envelope glycoprotein trimers.

http://www.wikidata.org/entity/Q34285680

description

2012 nî lūn-bûn

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2012 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2012 թվականի մայիսին հրատարակված գիտական հոդված

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2012年の論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年論文

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2012年论文

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name

Partial enzymatic deglycosylat ...... envelope glycoprotein trimers.

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Partial enzymatic deglycosylat ...... envelope glycoprotein trimers.

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Partial enzymatic deglycosylat ...... envelope glycoprotein trimers.

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type

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Partial enzymatic deglycosylat ...... envelope glycoprotein trimers.

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Partial enzymatic deglycosylat ...... envelope glycoprotein trimers.

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Partial enzymatic deglycosylat ...... envelope glycoprotein trimers.

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Partial enzymatic deglycosylat ...... envelope glycoprotein trimers.

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Partial enzymatic deglycosylat ...... envelope glycoprotein trimers.

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Partial enzymatic deglycosylat ...... envelope glycoprotein trimers.

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JBC.M112.371898

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Journal of Biological Chemistry

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Partial enzymatic deglycosylat ...... envelope glycoprotein trimers.

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Albert Cupo

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Andre J Marozsan

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Andrew B Ward

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Evan Massi

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John P Moore

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Kathryn B David

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Milind Kachare

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Nicolette Cocco

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Rafael S Depetris

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Reza Khayat

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P2860

Role of protein N-glycosylation in pathogenesis of human immunodeficiency virus type 1

Structural definition of a conserved neutralization epitope on HIV-1 gp120

Structural rationale for the broad neutralization of HIV-1 by human monoclonal antibody 447-52D

Structure of HIV-1 gp120 V1/V2 domain with broadly neutralizing antibody PG9

Structures of the CCR5 N Terminus and of a Tyrosine-Sulfated Antibody with HIV-1 gp120 and CD4

A Potent and Broad Neutralizing Antibody Recognizes and Penetrates the HIV Glycan Shield

EMAN: semiautomated software for high-resolution single-particle reconstructions

Accurate determination of local defocus and specimen tilt in electron microscopy

EMAN2: an extensible image processing suite for electron microscopy

Fine mapping of the interaction of neutralizing and nonneutralizing monoclonal antibodies with the CD4 binding site of human immunodeficiency virus type 1 gp120.

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24239-24254

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scholarly article

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10.1074/JBC.M112.371898

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29

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287

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Jean-Philippe Julien

Ian Andrew Wilson

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2012-05-29T00:00:00Z

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22645128

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3397850

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