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Neutrophil Attack Triggers Extracellular Trap-Dependent Candida Cell Wall Remodeling and Altered Immune RecognitionImmobilization of the glycosylphosphatidylinositol-anchored Gas1 protein into the chitin ring and septum is required for proper morphogenesis in yeast.The genetic interaction network of CCW12, a Saccharomyces cerevisiae gene required for cell wall integrity during budding and formation of mating projections.The Gas family of proteins of Saccharomyces cerevisiae: characterization and evolutionary analysis.Characterization of recombinant forms of the yeast Gas1 protein and identification of residues essential for glucanosyltransferase activity and folding.GAS2 and GAS4, a pair of developmentally regulated genes required for spore wall assembly in Saccharomyces cerevisiae.Control of the yeast cell cycle by protein synthesis.Expression and phylogenetic analyses of the Gel/Gas proteins of Tuber melanosporum provide insights into the function and evolution of glucan remodeling enzymes in fungi.Expression, stability, and replacement of glucan-remodeling enzymes during developmental transitions in Saccharomyces cerevisiae.Genomic and functional analyses unveil the response to hyphal wall stress in Candida albicans cells lacking β(1,3)-glucan remodeling.An improved expression system for the VC1 ligand binding domain of the receptor for advanced glycation end products in Pichia pastoris.Increase of external osmolarity reduces morphogenetic defects and accumulation of chitin in a gas1 mutant of Saccharomyces cerevisiae.A capture method based on the VC1 domain reveals new binding properties of the human receptor for advanced glycation end products (RAGE).GAS3, a developmentally regulated gene, encodes a highly mannosylated and inactive protein of the Gas family of Saccharomyces cerevisiae.Immunological cross-reactivity of fungal and yeast plasma membrane H+-ATPase.Disulfide bond structure and domain organization of yeast beta(1,3)-glucanosyltransferases involved in cell wall biogenesis.Cloning, sequencing and regulation of a cDNA encoding a small heat-shock protein from Schizosaccharomyces pombe.The PHR Family: The Role of Extracellular Transglycosylases in Shaping Candida albicans Cells.Imine Deaminase Activity and Conformational Stability of UK114, the Mammalian Member of the Rid Protein Family Active in Amino Acid Metabolism.Evolutionary conservation of genomic sequences related to the GGP1 gene encoding a yeast GPI-anchored glycoproteinMaintenance of cell integrity in thegas1 mutant ofSaccharomyces cerevisiae requires the Chs3p-targeting and activation pathway and involves an unusual Chs3p localizationTranscript accumulation of the GGP1 gene, encoding a yeast GPI-anchored glycoprotein, is inhibited during arrest in the G1 phase and during sporulationChanges in the protein synthesis pattern during a nutritional shift-down transition in Saccharomyces cerevisiaeReduction of ribosome activity and synthesis of stable RNA in Neurospora crassaThe GPI-anchored Gas and Crh families are fungal antigensThe Gas1 glycoprotein, a putative wall polymer cross-linkerTranscriptome profiling of a Saccharomyces cerevisiae mutant with a constitutively activated Ras/cAMP pathwayPHR1, a pH-regulated gene of Candida albicans encoding a glucan-remodelling enzyme, is required for adhesion and invasionCatalytic properties of the Gas family β-(1,3)-glucanosyltransferases active in fungal cell-wall biogenesis as determined by a novel fluorescent assayGeneration of an evolved Saccharomyces cerevisiae strain with a high freeze tolerance and an improved ability to grow on glycerolCatalytic properties of Phr family members of cell wall glucan remodeling enzymes: implications for the adaptation of Candida albicans to ambient pHAdvanced lipoxidation end products (ALEs) as RAGE binders: Mass spectrometric and computational studies to explain the reasons whyInsights into the effects of N-glycosylation on the characteristics of the VC1 domain of the human receptor for advanced glycation end products (RAGE) secreted by Pichia pastoris
P50
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P50
description
researcher ORCID ID = 0000-0002-5590-0167
@en
wetenschapper
@nl
name
Laura Popolo
@ast
Laura Popolo
@en
Laura Popolo
@es
Laura Popolo
@nl
type
label
Laura Popolo
@ast
Laura Popolo
@en
Laura Popolo
@es
Laura Popolo
@nl
prefLabel
Laura Popolo
@ast
Laura Popolo
@en
Laura Popolo
@es
Laura Popolo
@nl
P106
P1153
7004183702
P21
P31
P496
0000-0002-5590-0167