about
Crystal structures of two Bordetella pertussis periplasmic receptors contribute to defining a novel pyroglutamic acid binding DctP subfamilyStructure-based mechanism of ligand binding for periplasmic solute-binding protein of the Bug familyPeriplasmic domain of the sensor-kinase BvgS reveals a new paradigm for the Venus flytrap mechanismProbing the conformation of FhaC with small-angle neutron scattering and molecular modeling.First structural insights into the TpsB/Omp85 superfamily.Influence of the passenger domain of a model autotransporter on the properties of its translocator domain.Structure of the membrane protein FhaC: a member of the Omp85-TpsB transporter superfamily.Beta-helix model for the filamentous haemagglutinin adhesin of Bordetella pertussis and related bacterial secretory proteins.Characterization of the PAS domain in the sensor-kinase BvgS: mechanical role in signal transmissionLack of functional complementation between Bordetella pertussis filamentous hemagglutinin and Proteus mirabilis HpmA hemolysin secretion machineriesPapD chaperone function in pilus biogenesis depends on oxidant and chaperone-like activities of DsbAOuter-membrane PapC molecular usher discriminately recognizes periplasmic chaperone-pilus subunit complexes.Crystallization and preliminary X-ray diffraction analysis of two extracytoplasmic solute receptors of the DctP family from Bordetella pertussis.Development of pilus organelle subassemblies in vitro depends on chaperone uncapping of a beta zipper.Balance between Coiled-Coil Stability and Dynamics Regulates Activity of BvgS Sensor Kinase in Bordetella.Current challenges in autotransport and two-partner protein secretion pathways.New virulence-activated and virulence-repressed genes identified by systematic gene inactivation and generation of transcriptional fusions in Bordetella pertussis.A novel secretion apparatus for the assembly of adhesive bacterial pili.PapD and superfamily of periplasmic immunoglobulin-like pilus chaperones.Structure and plasticity of the peptidyl-prolyl isomerase Par27 of Bordetella pertussis revealed by X-ray diffraction and small-angle X-ray scattering.Differential modulation of Bordetella pertussis virulence genes as evidenced by DNA microarray analysis.Surface anchoring of bacterial subtilisin important for maturation function.The periplasmic binding protein of a tripartite tricarboxylate transporter is involved in signal transduction.N-terminal characterization of the Bordetella pertussis filamentous haemagglutinin.Molecular characterization of Bordetella bronchiseptica filamentous haemagglutinin and its secretion machinery.Amino-terminal maturation of the Bordetella pertussis filamentous haemagglutinin.Distinct virulence ranges for infection of mice by Bordetella pertussis revealed by engineering of the sensor-kinase BvgSThe Peptidyl–Prolyl Isomerase and Chaperone Par27 of Bordetella pertussis as the Prototype for a New Group of ParvulinsStructural insights into the signalling mechanisms of two-component systemsArginine 220 is a critical residue for the catalytic mechanism of the Streptomyces albus G beta-lactamaseAutotransporter proteins, evolution and redefining protein secretion: responseEvidence that a globular conformation is not compatible with FhaC-mediated secretion of the Bordetella pertussis filamentous haemagglutininTetanus toxin fragment C-specific priming by intranasal infection with recombinant Bordetella pertussisStructural analysis of Bordetella pertussis BugE solute receptor in a bound conformationSecretion signal of the filamentous haemagglutinin, a model two-partner secretion substrate
P50
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P50
description
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F Jacob-Dubuisson
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P31
P496
0000-0002-5102-1704