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Interaction of human complement with Sbi, a staphylococcal immunoglobulin-binding protein: indications of a novel mechanism of complement evasion by Staphylococcus aureusStructure-function analysis of the C3 binding region of Staphylococcus aureus immune subversion protein SbiFrom Insect to Man: Photorhabdus Sheds Light on the Emergence of Human PathogenicityAdhesion mechanism of human beta(2)-glycoprotein I to phospholipids based on its crystal structure.Structure of Golgi alpha-mannosidase II: a target for inhibition of growth and metastasis of cancer cellsA structural basis for Staphylococcal complement subversion: X-ray structure of the complement-binding domain of Staphylococcus aureus protein Sbi in complex with ligand C3dA crystal structure of the complex between human complement receptor 2 and its ligand C3dThe catalytic core of an archaeal 2-oxoacid dehydrogenase multienzyme complex is a 42-mer protein assemblyWhy are the 2-oxoacid dehydrogenase complexes so large? Generation of an active trimeric complexBactericidal antibody recognition of a PorA epitope of Neisseria meningitidis: crystal structure of a Fab fragment in complex with a fluorescein-conjugated peptidePredicting the virulence of MRSA from its genome sequence.Staphylococcus aureus proteins Sbi and Efb recruit human plasmin to degrade complement C3 and C3b.Macrophage Migration Inhibitory Factor is subjected to glucose modification and oxidation in Alzheimer's Disease.Mutational analyses reveal that the staphylococcal immune evasion molecule Sbi and complement receptor 2 (CR2) share overlapping contact residues on C3d: implications for the controversy regarding the CR2/C3d cocrystal structure.The red edge excitation shift phenomenon can be used to unmask protein structural ensembles: implications for NEMO-ubiquitin interactions.Thermal stability, storage and release of proteins with tailored fit in silica.Corrigendum: Macrophage Migration Inhibitory Factor is subjected to glucose modification and oxidation in Alzheimer's Disease.Analysis of protein glycation using phenylboronate acrylamide gel electrophoresis.Dye displacement assay for saccharide detection with boronate hydrogels.Exploiting the reversible covalent bonding of boronic acids: recognition, sensing, and assembly.Structural analysis of Salmonella enterica effector protein SopD.Analysis of protein glycation using phenylboronate acrylamide gel electrophoresis.Investigating the lytic activity and structural properties of Staphylococcus aureus phenol soluble modulin (PSM) peptide toxins.From genotype to phenotype: can systems biology be used to predict Staphylococcus aureus virulence?The synthesis and kinetic evaluation of aryl α-aminophosphonates as novel inhibitors of T. cruzi trans-sialidaseGlycation Alters Ligand Binding, Enzymatic, and Pharmacological Properties of Human AlbuminUtilization of Staphylococcal Immune Evasion Protein Sbi as a Novel Vaccine AdjuvantOn the interaction between a bactericidal antibody and a PorA epitope of Neisseria meningitidis in outer membrane vesicles: a competitive fluorescence polarization immunoassayThermodynamic analysis of the interaction between a bactericidal antibody and a PorA epitope of Neisseria meningitidisEvolution of the genetic triplet code via two types of doublet codonsThe rational design of affinity-attenuated OmCI for the purification of complement C5Ensilication Improves the Thermal Stability of the Tuberculosis Antigen Ag85b and an Sbi-Ag85b Vaccine ConjugateAnalysis of Protein Glycation Using Phenylboronate Acrylamide Gel Electrophoresis
P50
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P50
description
researcher ORCID ID = 0000-0002-0367-1956
@en
wetenschapper
@nl
name
Jean van den Elsen
@ast
Jean van den Elsen
@en
Jean van den Elsen
@es
Jean van den Elsen
@nl
type
label
Jean van den Elsen
@ast
Jean van den Elsen
@en
Jean van den Elsen
@es
Jean van den Elsen
@nl
prefLabel
Jean van den Elsen
@ast
Jean van den Elsen
@en
Jean van den Elsen
@es
Jean van den Elsen
@nl
P108
P106
P2798
P31
P496
0000-0002-0367-1956