about
sameAs
The structural modifications induced by the M339F substitution in PBP2x from Streptococcus pneumoniae further decreases the susceptibility to beta-lactams of resistant strainsCommon alterations in PBP1a from resistant Streptococcus pneumoniae decrease its reactivity toward beta-lactams: structural insightsResistance to β-Lactams in Neisseria ssp Due to Chromosomally Encoded Penicillin-Binding ProteinsPenicillin-binding proteins and beta-lactam resistanceAutomated high-throughput process for site-directed mutagenesis, production, purification, and kinetic characterization of enzymes.Membrane topology of the Streptococcus pneumoniae FtsW division proteinIdentification of FtsW as a transporter of lipid-linked cell wall precursors across the membraneThe reactive and destabilizing disulfide bond of DsbA, a protein required for protein disulfide bond formation in vivo.Reconstitution of membrane protein complexes involved in pneumococcal septal cell wall assemblyInhibition of Streptococcus pneumoniae penicillin-binding protein 2x and Actinomadura R39 DD-peptidase activities by ceftaroline.The different shapes of cocci.Peptidoglycan assembly machines: the biochemical evidence.The elongation of ovococciIdentification and crystallization of a protease-resistant core of calnexin that retains biological activity.Roles of pneumococcal DivIB in cell divisionThe D,D-carboxypeptidase PBP3 organizes the division process of Streptococcus pneumoniae.The role of the lectin calnexin in conformation independent binding to N-linked glycoproteins and quality control.Mechanism of β-lactam action in Streptococcus pneumoniae: the piperacillin paradox.Central domain of DivIB caps the C-terminal regions of the FtsL/DivIC coiled-coil rod.Identical penicillin-binding domains in penicillin-binding proteins of Streptococcus pneumoniae clinical isolates with different levels of beta-lactam resistance.Expression and purification of FtsW and RodA from Streptococcus pneumoniae, two membrane proteins involved in cell division and cell growth, respectively.In vitro reconstitution of a trimeric complex of DivIB, DivIC and FtsL, and their transient co-localization at the division site in Streptococcus pneumoniae.Pneumococcal beta-lactam resistance due to a conformational change in penicillin-binding protein 2x.Cooperativity of peptidoglycan synthases active in bacterial cell elongation.Crystallization of DsbC, the disulfide bond isomerase of Escherichia coli.Substitutions in PBP2b from β-Lactam-resistant Streptococcus pneumoniae Have Different Effects on Enzymatic Activity and Drug Reactivity.Increase of the deacylation rate of PBP2x from Streptococcus pneumoniae by single point mutations mimicking the class A beta-lactamases.The membrane anchor of penicillin-binding protein PBP2a from Streptococcus pneumoniae influences peptidoglycan chain length.Optimization of conditions for the glycosyltransferase activity of penicillin-binding protein 1a from Thermotoga maritima.Structural and functional characterization of DsbC, a protein involved in disulfide bond formation in Escherichia coli.Effects of DsbA on the disulfide folding of bovine pancreatic trypsin inhibitor and alpha-lactalbumin.Replacement of the active-site cysteine residues of DsbA, a protein required for disulfide bond formation in vivo.Enhanced Catalysis of Ribonuclease B Folding by the Interaction of Calnexin or Calreticulin with ERp57In vitro Reconstitution of Peptidoglycan Assembly from the Gram-Positive Pathogen Streptococcus pneumoniaeOne-Pot Two-Step Metabolic Labeling of Teichoic Acids and Direct Labeling of Peptidoglycan Reveals Tight Coordination of Both Polymers Inserted into Pneumococcus Cell WallFolding in vitro of bovine pancreatic trypsin inhibitor in the presence of proteins of the endoplasmic reticulum
P50
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P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
André Zapun
@ast
André Zapun
@en
André Zapun
@es
André Zapun
@fr
André Zapun
@nl
André Zapun
@sl
type
label
André Zapun
@ast
André Zapun
@en
André Zapun
@es
André Zapun
@fr
André Zapun
@nl
André Zapun
@sl
prefLabel
André Zapun
@ast
André Zapun
@en
André Zapun
@es
André Zapun
@fr
André Zapun
@nl
André Zapun
@sl
P106
P21
P31
P496
0000-0001-8953-4399