Glyceraldehyde-3-phosphate dehydrogenase of Paracoccidioides brasiliensis is a cell surface protein involved in fungal adhesion to extracellular matrix proteins and interaction with cells.
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Extracellular Vesicle-Associated Transitory Cell Wall Components and Their Impact on the Interaction of Fungi with Host CellsParacoccidioides-host Interaction: An Overview on Recent Advances in the ParacoccidioidomycosisSurface-associated plasminogen binding of Cryptococcus neoformans promotes extracellular matrix invasionPhysical Features of Intracellular Proteins that Moonlight on the Cell SurfaceWhy study moonlighting proteins?The transcriptome analysis of early morphogenesis in Paracoccidioides brasiliensis mycelium reveals novel and induced genes potentially associated to the dimorphic processThe malate synthase of Paracoccidioides brasiliensis is a linked surface protein that behaves as an anchorless adhesin.Transcriptional profiling reveals the expression of novel genes in response to various stimuli in the human dermatophyte Trichophyton rubrum.Interaction of the heterotrimeric G protein alpha subunit SSG-1 of Sporothrix schenckii with proteins related to stress response and fungal pathogenicity using a yeast two-hybrid assay.Paracoccidioides brasiliensis enolase is a surface protein that binds plasminogen and mediates interaction of yeast forms with host cells.Ss-Sl2, a novel cell wall protein with PAN modules, is essential for sclerotial development and cellular integrity of Sclerotinia sclerotiorum.A 32-kilodalton hydrolase plays an important role in Paracoccidioides brasiliensis adherence to host cells and influences pathogenicity.Paracoccidioides species complex: ecology, phylogeny, sexual reproduction, and virulence.Analysis of the secretomes of Paracoccidioides mycelia and yeast cells.Paracoccidoides brasiliensis 30 kDa adhesin: identification as a 14-3-3 protein, cloning and subcellular localization in infection models.Intermolecular interactions of the malate synthase of Paracoccidioides sppQuantitative proteomic analysis of cell cycle of the dinoflagellate Prorocentrum donghaiense (Dinophyceae).Characterization of Alternaria infectoria extracellular vesicles.Alterations of protein expression in conditions of copper-deprivation for Paracoccidioides lutzii in the presence of extracellular matrix components.Proteome profiling of the dimorphic fungus Penicillium marneffei extracellular proteins and identification of glyceraldehyde-3-phosphate dehydrogenase as an important adhesion factor for conidial attachment.Analysis of Paracoccidioides secreted proteins reveals fructose 1,6-bisphosphate aldolase as a plasminogen-binding proteinIn vitro Paracoccidioides brasiliensis biofilm and gene expression of adhesins and hydrolytic enzymes.Functional analysis of Paracoccidioides brasiliensis 14-3-3 adhesin expressed in Saccharomyces cerevisiaeVesicle and vesicle-free extracellular proteome of Paracoccidioides brasiliensis: comparative analysis with other pathogenic fungi.Comparative Proteomics Analyses of Two Races of Fusarium oxysporum f. sp. conglutinans that Differ in Pathogenicity.Novel candidate virulence factors in rice pathogen Xanthomonas oryzae pv. oryzicola as revealed by mutational analysis.Immune Response Induced by an Immunodominant 60 kDa Glycoprotein of the Cell Wall of Sporothrix schenckii in Two Mice Strains with Experimental SporotrichosisComparison of virulence between Paracoccidioides brasiliensis and Paracoccidioides lutzii using Galleria mellonella as a host modelInsights into the pathogenicity of Penicillium marneffei.Decreased expression of 14-3-3 in Paracoccidioides brasiliensis confirms its involvement in fungal pathogenesis.Adherence mechanisms in human pathogenic fungi.Glyceraldehyde-3-phosphate dehydrogenase acts as an adhesin in Erysipelothrix rhusiopathiae adhesion to porcine endothelial cells and as a receptor in recruitment of host fibronectin and plasminogen.Human pathogens utilize host extracellular matrix proteins laminin and collagen for adhesion and invasion of the host.Where do they come from and where do they go: candidates for regulating extracellular vesicle formation in fungi.Moonlighting proteins as virulence factors of pathogenic fungi, parasitic protozoa and multicellular parasites.The multifaceted roles of metabolic enzymes in the Paracoccidioides species complex.The paracoccidioides cell wall: past and present layers toward understanding interaction with the host.New insights into a complex fungal pathogen: the case of Paracoccidioides spp.Anti-GAPDH Autoantibodies as a Pathogenic Determinant and Potential Biomarker of Neuropsychiatric Diseases.Paracoccidioides Spp.: Virulence Factors and Immune-Evasion Strategies.
P2860
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P2860
Glyceraldehyde-3-phosphate dehydrogenase of Paracoccidioides brasiliensis is a cell surface protein involved in fungal adhesion to extracellular matrix proteins and interaction with cells.
description
2006 nî lūn-bûn
@nan
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
2006年论文
@zh
2006年论文
@zh-cn
name
Glyceraldehyde-3-phosphate deh ...... ns and interaction with cells.
@en
type
label
Glyceraldehyde-3-phosphate deh ...... ns and interaction with cells.
@en
prefLabel
Glyceraldehyde-3-phosphate deh ...... ns and interaction with cells.
@en
P2093
P2860
P1476
Glyceraldehyde-3-phosphate deh ...... ns and interaction with cells.
@en
P2093
Fabrícia P de Faria
Luciano dos Santos Feitosa
Maria José Soares Mendes-Giannini
Maria Sueli S Felipe
Mônica Santiago Barbosa
Patrícia Ferrari Andreotti
Sônia Nair Báo
P2860
P304
P356
10.1128/IAI.74.1.382-389.2006
P407
P577
2006-01-01T00:00:00Z