about
Structural basis for the growth factor activity of human adenosine deaminase ADA2Structure and biogenesis of the capsular F1 antigen from Yersinia pestis: preserved folding energy drives fiber formationA novel self-capping mechanism controls aggregation of periplasmic chaperone Caf1MCaf1A usher possesses a Caf1 subunit-like domain that is crucial for Caf1 fibre secretionAllosteric mechanism controls traffic in the chaperone/usher pathwayCrystal structure of enterotoxigenic Escherichia coli colonization factor CS6 reveals a novel type of functional assemblyStructural basis for Myf and Psa fimbriae-mediated tropism of pathogenic strains of Yersinia for host tissuesStructural insight into host recognition by aggregative adherence fimbriae of enteroaggregative Escherichia coliEarly-onset stroke and vasculopathy associated with mutations in ADA2A posttermination ribosomal complex is the guanine nucleotide exchange factor for peptide release factor RF3.Crystallization and sulfur SAD phasing of AggA, the major subunit of aggregative adherence fimbriae type I from the Escherichia coli strain that caused an outbreak of haemolytic-uraemic syndrome in Germany.Structural and functional significance of the FGL sequence of the periplasmic chaperone Caf1M of Yersinia pestis.Large is fast, small is tight: determinants of speed and affinity in subunit capture by a periplasmic chaperone.The affinity of the FimH fimbrial adhesin is receptor-driven and quasi-independent of Escherichia coli pathotypes.Metacaspases.Structural Insight into Archaic and Alternative Chaperone-Usher Pathways Reveals a Novel Mechanism of Pilus Biogenesis.YopN and TyeA Hydrophobic Contacts Required for Regulating Ysc-Yop Type III Secretion Activity by Yersinia pseudotuberculosis.Crystallization and preliminary X-ray diffraction analysis of the Csu pili CsuC-CsuA/B chaperone-major subunit pre-assembly complex from Acinetobacter baumannii.Resolving the energy paradox of chaperone/usher-mediated fibre assembly.Mutagenesis elucidates the assembly pathway and structure of Yersinia pestis F1 polymer.Overexpression, purification, crystallization and preliminary X-ray diffraction analysis of the F1 antigen Caf1M-Caf1 chaperone-subunit pre-assembly complex from Yersinia pestis.Donor strand complementation mechanism in the biogenesis of non-pilus systems.Influence of the conserved disulphide bond, exposed to the putative binding pocket, on the structure and function of the immunoglobulin-like molecular chaperone Caf1M of Yersinia pestis.Tudor staphylococcal nuclease is an evolutionarily conserved component of the programmed cell death degradome.The effect of the intersubunit disulfide bond on the structural and functional properties of the small heat shock protein Hsp25.Methylation, crystallization and SAD phasing of the Csu pilus CsuC-CsuE chaperone-adhesin subunit pre-assembly complex from Acinetobacter baumannii.Heterologous Complementation Studies With the YscX and YscY Protein Families Reveals a Specificity for Yersinia pseudotuberculosis Type III Secretion.Structural basis for Acinetobacter baumannii biofilm formation.Thiol/disulfide exchange between small heat shock protein 25 and glutathioneArchaic and alternative chaperones preserve pilin folding energy by providing incomplete structural informationReceptor binding studies disclose a novel class of high-affinity inhibitors of the Escherichia coli FimH adhesinNovel fusion proteins in the analysis of diabetes-associated autoantibodies to GAD65 and IA-2A new human challenge model for testing heat-stable toxin-based vaccine candidates for enterotoxigenic Escherichia coli diarrhea - dose optimization, clinical outcomes, and CD4+ T cell responsesGlycosphingolipids Recognized by Acinetobacter baumannii
P50
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P50
description
hulumtues
@sq
onderzoeker
@nl
researcher
@en
հետազոտող
@hy
name
Anton V Zavialov
@ast
Anton V Zavialov
@en
Anton V Zavialov
@es
type
label
Anton V Zavialov
@ast
Anton V Zavialov
@en
Anton V Zavialov
@es
prefLabel
Anton V Zavialov
@ast
Anton V Zavialov
@en
Anton V Zavialov
@es
P1053
C-7664-2015
P106
P21
P31
P3829
P496
0000-0001-6191-5931