The 1.25 A resolution refinement of the cholera toxin B-pentamer: evidence of peptide backbone strain at the receptor-binding site
about
Rapid and scalable plant-based production of a cholera toxin B subunit variant to aid in mass vaccination against cholera outbreaksA mutant cholera toxin B subunit that binds GM1- ganglioside but lacks immunomodulatory or toxic activityComplement Factor H and Simian Virus 40 bind the GM1 ganglioside in distinct conformationsLocalizing Carbohydrate Binding Sites in Proteins Using Hydrogen/Deuterium Exchange Mass Spectrometry.Protein Geometry Database: a flexible engine to explore backbone conformations and their relationships to covalent geometry.Nonplanar peptide bonds in proteins are common and conserved but not biased toward active sites.Identification of mycobacterial lectins from genomic data.Using a galactose library for exploration of a novel hydrophobic pocket in the receptor binding site of the Escherichia coli heat-labile enterotoxin.Comprehensive analysis of blood group antigen binding to classical and El Tor cholera toxin B-pentamers by NMR.Glycoblocks: a schematic three-dimensional representation for glycans and their interactions.Combining 3D structure with glycan array data provides insight into the origin of glycan specificityGas phase characterization of the noncovalent quaternary structure of cholera toxin and the cholera toxin B subunit pentamer.Presentation of membrane-anchored glycosphingolipids determined from molecular dynamics simulations and NMR paramagnetic relaxation rate enhancement.NMR characterization of the interactions between lyso-GM1 aqueous micelles and amyloid beta.Molecular basis of cholera blood-group dependence and implications for a world characterized by climate change.Characterization of receptor-mediated signal transduction by Escherichia coli type IIa heat-labile enterotoxin in the polarized human intestinal cell line T84.Structure-guided design and immunological characterization of immunogens presenting the HIV-1 gp120 V3 loop on a CTB scaffold.Structural and Functional Analysis of Murine Polyomavirus Capsid Proteins Establish the Determinants of Ligand Recognition and Pathogenicity.Recognition of human milk oligosaccharides by bacterial exotoxins.High-Resolution Crystal Structures Elucidate the Molecular Basis of Cholera Blood Group Dependence.N-glycolyl GM1 ganglioside as a receptor for simian virus 40.Rafting with cholera toxin: endocytosis and trafficking from plasma membrane to ER.Synthetic cell surface receptors for delivery of therapeutics and probes.Targeting bacterial toxins.Bacterial toxin inhibitors based on multivalent scaffolds.Design and in silico screening of inhibitors of the cholera toxin.Bridging lectin binding sites by multivalent carbohydrates.Mutational analysis of ganglioside GM(1)-binding ability, pentamer formation, and epitopes of cholera toxin B (CTB) subunits and CTB/heat-labile enterotoxin B subunit chimeras.Siglec-7 undergoes a major conformational change when complexed with the alpha(2,8)-disialylganglioside GT1b.BOF: a novel family of bacterial OB-fold proteins.Towards new cholera prophylactics and treatment: Crystal structures of bacterial enterotoxins in complex with GM1 mimics.Glycoscience@Synchrotron: Synchrotron radiation applied to structural glycoscience.Ganglioside-dependent cell attachment and endocytosis of murine polyomavirus-like particles.Molecular dynamics of sialic acid analogues complex with cholera toxin and DFT optimization of ethylene glycol-mediated zinc nanocluster conjugation.A protein-based pentavalent inhibitor of the cholera toxin B-subunit.Cloning, expression, purification, crystallization and preliminary X-ray studies of a secreted lectin (Rv1419) from Mycobacterium tuberculosisMolecular modeling of methyl-α-Neu5Ac analogues docked against cholera toxin--a molecular dynamics study.A Self-Assembled Spherical Complex Displaying a Gangliosidic Glycan Cluster Capable of Interacting with Amyloidogenic Proteins.Synthetic glycopeptides and glycoproteins with applications in biological research.Towards a structural basis for the relationship between blood group and the severity of El Tor cholera.
P2860
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P2860
The 1.25 A resolution refinement of the cholera toxin B-pentamer: evidence of peptide backbone strain at the receptor-binding site
description
1998 nî lūn-bûn
@nan
1998 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1998 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1998年の論文
@ja
1998年論文
@yue
1998年論文
@zh-hant
1998年論文
@zh-hk
1998年論文
@zh-mo
1998年論文
@zh-tw
1998年论文
@wuu
name
The 1.25 A resolution refineme ...... n at the receptor-binding site
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The 1.25 A resolution refineme ...... n at the receptor-binding site
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The 1.25 A resolution refineme ...... n at the receptor-binding site
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type
label
The 1.25 A resolution refineme ...... n at the receptor-binding site
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The 1.25 A resolution refineme ...... n at the receptor-binding site
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The 1.25 A resolution refineme ...... n at the receptor-binding site
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The 1.25 A resolution refineme ...... n at the receptor-binding site
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The 1.25 A resolution refineme ...... n at the receptor-binding site
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The 1.25 A resolution refineme ...... n at the receptor-binding site
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P2093
P3181
P356
P1476
The 1.25 A resolution refineme ...... n at the receptor-binding site
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P2093
P304
P3181
P356
10.1006/JMBI.1998.2076
P407
P577
1998-10-09T00:00:00Z