RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion.
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Pertussis toxin and adenylate cyclase toxin: key virulence factors of Bordetella pertussis and cell biology toolsStructural models of intrinsically disordered and calcium-bound folded states of a protein adapted for secretionMARTX toxins as effector delivery platformsDisorder-to-order transition in the CyaA toxin RTX domain: implications for toxin secretionFunctional roles of transiently and intrinsically disordered regions within proteinsInterdomain Contacts and the Stability of Serralysin Protease from Serratia marcescensCalcium-dependent conformational flexibility of a CUB domain controls activation of the complement serine protease C1rCharge-dependent secretion of an intrinsically disordered protein via the autotransporter pathway.Albumin, in the Presence of Calcium, Elicits a Massive Increase in Extracellular Bordetella Adenylate Cyclase Toxin.The Bordetella adenylate cyclase repeat-in-toxin (RTX) domain is immunodominant and elicits neutralizing antibodies.Monitoring the conformational changes of an intrinsically disordered peptide using a quartz crystal microbalance.Order and disorder in the domain organization of the plasmid partition protein KorB.Structural features of the Pseudomonas fluorescens biofilm adhesin LapA required for LapG-dependent cleavage, biofilm formation, and cell surface localizationExpanding the proteome: disordered and alternatively folded proteins.Inducible polymerization and two-dimensional assembly of the repeats-in-toxin (RTX) domain from the Pseudomonas aeruginosa alkaline protease.Calcium-induced folding and stabilization of the intrinsically disordered RTX domain of the CyaA toxinModulation of the epithelial sodium channel (ENaC) by bacterial metalloproteases and protease inhibitors.Calcium, acylation, and molecular confinement favor folding of Bordetella pertussis adenylate cyclase CyaA toxin into a monomeric and cytotoxic formOuter membrane targeting of secretin PulD protein relies on disordered domain recognition by a dedicated chaperone.Membrane-Pore Forming Characteristics of the Bordetella pertussis CyaA-Hemolysin Domain.Distinct roles of the repeat-containing regions and effector domains of the Vibrio vulnificus multifunctional-autoprocessing repeats-in-toxin (MARTX) toxin.Calcium-induced folding and stabilization of the Pseudomonas aeruginosa alkaline protease.Identification of the minimal region in lipase ABC transporter recognition domain of Pseudomonas fluorescens for secretion and fluorescence of green fluorescent proteinStructural and functional dissection reveals distinct roles of Ca2+-binding sites in the giant adhesin SiiE of Salmonella enterica.Autotransporters: The Cellular Environment Reshapes a Folding Mechanism to Promote Protein TransportToxins from bacteria.Mutual effects of disorder and order in fusion proteins between intrinsically disordered domains and fluorescent proteins.Repeat protein engineering: creating functional nanostructures/biomaterials from modular building blocks.Tetra detector analysis of membrane proteinsAggregating tags for column-free protein purification.Identification of a region that assists membrane insertion and translocation of the catalytic domain of Bordetella pertussis CyaA toxin.Rearranging and concatenating a native RTX domain to understand sequence modularity.Negatively charged residues of the segment linking the enzyme and cytolysin moieties restrict the membrane-permeabilizing capacity of adenylate cyclase toxin.In vivo quantification of the secretion rates of the hemolysin A Type I secretion system.A vector system for ABC transporter-mediated secretion and purification of recombinant proteins in Pseudomonas species.Block V RTX Domain of Adenylate Cyclase from Bordetella pertussis: A Conformationally Dynamic Scaffold for Protein Engineering Applications.The C terminus of tubulin, a versatile partner for cationic molecules: binding of Tau, polyamines, and calcium.Stability, structural and functional properties of a monomeric, calcium-loaded adenylate cyclase toxin, CyaA, from Bordetella pertussis.Calcium-induced folding of intrinsically disordered repeat-in-toxin (RTX) motifs via changes of protein charges and oligomerization states.Characterization of a membrane-active peptide from the Bordetella pertussis CyaA toxin.
P2860
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P2860
RTX calcium binding motifs are intrinsically disordered in the absence of calcium: implication for protein secretion.
description
2008 nî lūn-bûn
@nan
2008年の論文
@ja
2008年学术文章
@wuu
2008年学术文章
@zh
2008年学术文章
@zh-cn
2008年学术文章
@zh-hans
2008年学术文章
@zh-my
2008年学术文章
@zh-sg
2008年學術文章
@yue
2008年學術文章
@zh-hant
name
RTX calcium binding motifs are ...... ication for protein secretion.
@en
RTX calcium binding motifs are ...... ication for protein secretion.
@nl
type
label
RTX calcium binding motifs are ...... ication for protein secretion.
@en
RTX calcium binding motifs are ...... ication for protein secretion.
@nl
prefLabel
RTX calcium binding motifs are ...... ication for protein secretion.
@en
RTX calcium binding motifs are ...... ication for protein secretion.
@nl
P2093
P2860
P356
P1476
RTX calcium binding motifs are ...... lication for protein secretion
@en
P2093
Bertrand Raynal
J Iñaki Guijarro
Muriel Delepierre
P2860
P304
P356
10.1074/JBC.M807312200
P407
P577
2008-11-17T00:00:00Z