Novel topological features of FhaC, the outer membrane transporter involved in the secretion of the Bordetella pertussis filamentous hemagglutinin. - Wikidata - awgldk - TriplyDB

Novel topological features of FhaC, the outer membrane transporter involved in the secretion of the Bordetella pertussis filamentous hemagglutinin.

Novel topological features of FhaC, the outer membrane transporter involved in the secretion of the Bordetella pertussis filamentous hemagglutinin.

http://www.wikidata.org/entity/Q30168887

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Molecular pathogenesis, epidemiology, and clinical manifestations of respiratory infections due to Bordetella pertussis and other Bordetella subspecies.Mechanisms of protein export across the bacterial outer membrane Prediction of beta-barrel membrane proteins by searching for restricted domains.Functional importance of a conserved sequence motif in FhaC, a prototypic member of the TpsB/Omp85 superfamily Current progress with Moraxella catarrhalis antigens as vaccine candidates Molecular basis of bacterial outer membrane permeability revisited Relative Orientation of POTRA Domains from Cyanobacterial Omp85 Studied by Pulsed EPR Spectroscopy.Dynamic interplay of membrane-proximal POTRA domain and conserved loop L6 in Omp85 transporter FhaC.Translocation path of a substrate protein through its Omp85 transporter.Probing the conformation of FhaC with small-angle neutron scattering and molecular modeling.Conformational dynamics of protein transporter FhaC: large-scale motions of plug helix.Predicting functionally informative mutations in Escherichia coli BamA using evolutionary covariance analysis.Conformation-specific labeling of BamA and suppressor analysis suggest a cyclic mechanism for β-barrel assembly in Escherichia coli Assembly of Outer Membrane β-Barrel Proteins: the Bam Complex.Substrate recognition by the POTRA domains of TpsB transporter FhaC.The complex that inserts lipopolysaccharide into the bacterial outer membrane forms a two-protein plug-and-barrel Type V Secretion: the Autotransporter and Two-Partner Secretion Pathways First structural insights into the TpsB/Omp85 superfamily.Omp85(Tt) from Thermus thermophilus HB27: an ancestral type of the Omp85 protein family.Structure of the Haemophilus influenzae HMW1B translocator protein: evidence for a twin pore.Translocator proteins in the two-partner secretion family have multiple domains.Channel properties of TpsB transporter FhaC point to two functional domains with a C-terminal protein-conducting pore.Topology of the outer membrane usher PapC determined by site-directed fluorescence labeling.Topology of the Erwinia chrysanthemi oligogalacturonate porin KdgM.Two-partner secretion in Gram-negative bacteria: a thrifty, specific pathway for large virulence proteins.Identification and regulation of expression of a gene encoding a filamentous hemagglutinin-related protein in Bordetella holmesii Virulence determinants involved in differential host niche adaptation of Neisseria meningitidis and Neisseria gonorrhoeae.Type V protein secretion pathway: the autotransporter story Two-Partner Secretion: Combining Efficiency and Simplicity in the Secretion of Large Proteins for Bacteria-Host and Bacteria-Bacteria Interactions Transport proteins promoting Escherichia coli pathogenesis.Protein secretion in the absence of ATP: the autotransporter, two-partner secretion and chaperone/usher pathways of gram-negative bacteria (review).Sequential translocation of an Escherchia coli two-partner secretion pathway exoprotein across the inner and outer membranes Autotransporter and two-partner secretion: delivery of large-size virulence factors by gram-negative bacterial pathogens.Vaccine targets against Moraxella catarrhalis.Balance between Coiled-Coil Stability and Dynamics Regulates Activity of BvgS Sensor Kinase in Bordetella.The LspB protein is involved in the secretion of the LspA1 and LspA2 proteins by Haemophilus ducreyi.Toxins from bacteria.The β-Barrel Assembly Machinery Complex.Role of HrpA in biofilm formation of Neisseria meningitidis and regulation of the hrpBAS transcripts.Moraxella catarrhalis strain O35E expresses two filamentous hemagglutinin-like proteins that mediate adherence to human epithelial cells.

P2860

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P2860

Novel topological features of FhaC, the outer membrane transporter involved in the secretion of the Bordetella pertussis filamentous hemagglutinin.

http://www.wikidata.org/entity/Q30168887

description

2000 nî lūn-bûn

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2000 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած

@hyw

2000 թվականի սեպտեմբերին հրատարակված գիտական հոդված

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2000年の論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年论文

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Novel topological features of ...... sis filamentous hemagglutinin.

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Novel topological features of ...... sis filamentous hemagglutinin.

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Novel topological features of ...... sis filamentous hemagglutinin.

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Novel topological features of ...... sis filamentous hemagglutinin.

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P1433

Journal of Biological Chemistry

P1476

Novel topological features of ...... sis filamentous hemagglutinin.

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P2093

Drobecq H

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Fort E

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Guédin S

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Jacob-Dubuisson F

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Locht C

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Tommassen J

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Willery E

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P2860

Crystal structures explain functional properties of two E. coli porins

Structural basis for sugar translocation through maltoporin channels at 3.1 A resolution

Structure of the outer membrane protein A transmembrane domain

Crystal structure of the outer membrane active transporter FepA from Escherichia coli

Channel formation by FhaC, the outer membrane protein involved in the secretion of the Bordetella pertussis filamentous hemagglutinin.

The three-dimensional structure of porin from Rhodobacter capsulatus at 3 A resolution.

Genetic insertion and exposure of a reporter epitope in the ferrichrome-iron receptor of Escherichia coli K-12.

Surface topology of the Escherichia coli K-12 ferric enterobactin receptor

Three-dimensional structure of membrane and surface proteins.

Topological analysis of the Escherichia coli ferrichrome-iron receptor by using monoclonal antibodies.

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30202-30210

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scholarly article

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10.1074/JBC.M005515200

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P433

39

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P478

275

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2000-09-01T00:00:00Z

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10906141

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P921

Bordetella pertussis