Substrate specificity classes and the recognition signal for Salmonella type III flagellar export. - Wikidata - awgldk - TriplyDB

Substrate specificity classes and the recognition signal for Salmonella type III flagellar export.

Substrate specificity classes and the recognition signal for Salmonella type III flagellar export.

http://www.wikidata.org/entity/Q39743825

about

Inhibition of a type III secretion system by the deletion of a short loop in one of its membrane proteins Interaction of FliK with the bacterial flagellar hook is required for efficient export specificity switching Straight and rigid flagellar hook made by insertion of the FlgG specific sequence into FlgE.Application of a short, disordered N-terminal flagellin segment, a fully functional flagellar type III export signal, to expression of secreted proteins.High-throughput comparison of gene fitness among related bacteria.Identification of new flagellar genes of Salmonella enterica serovar Typhimurium.Posttranscriptional control of the Salmonella enterica flagellar hook protein FlgE Function of FlhB, a membrane protein implicated in the bacterial flagellar type III secretion system Theoretical and computational investigation of flagellin translocation and bacterial flagellum growth Self-assembly and type III protein export of the bacterial flagellum.The mechanism of outer membrane penetration by the eubacterial flagellum and implications for spirochete evolution.Flk prevents premature secretion of the anti-sigma factor FlgM into the periplasm.Mutations in flk, flgG, flhA, and flhE that affect the flagellar type III secretion specificity switch in Salmonella enterica.Comparative analysis of the secretion capability of early and late flagellar type III secretion substrates.Extracellular secretion of a recombinant therapeutic peptide by Bacillus halodurans utilizing a modified flagellin type III secretion system.Role of the Dc domain of the bacterial hook protein FlgE in hook assembly and function.Use of a Novel Report Protein to Study the Secretion Signal of Flagellin in Bacillus subtilis.Xenocin export by the flagellar type III pathway in Xenorhabdus nematophila.Biochemical Characterization of the Flagellar Rod Components of Rhodobacter sphaeroides: Properties and Interactions.Secretome analysis of diarrhea-inducing strains of Escherichia coli Yersinia enterocolitica type III secretion depends on the proton motive force but not on the flagellar motor components MotA and MotB Secretion of YscP from Yersinia enterocolitica is essential to control the length of the injectisome needle but not to change the type III secretion substrate specificity.MotD of Sinorhizobium meliloti and related alpha-proteobacteria is the flagellar-hook-length regulator and therefore reassigned as FliK.A regulatory checkpoint during flagellar biogenesis in Campylobacter jejuni initiates signal transduction to activate transcription of flagellar genes.Functional Activation of the Flagellar Type III Secretion Export Apparatus Sorting of early and late flagellar subunits after docking at the membrane ATPase of the type III export pathway.Identification of a putative glycosyltransferase responsible for the transfer of pseudaminic acid onto the polar flagellin of Aeromonas caviae Sch3N.Weak Interactions between Salmonella enterica FlhB and Other Flagellar Export Apparatus Proteins Govern Type III Secretion Dynamics.A Naturally Occurring Deletion in FliE from Salmonella enterica Serovar Dublin Results in an Aflagellate Phenotype and Defective Proinflammatory Properties.Extracellular secretion of polypeptides using a modified Escherichia coli flagellar secretion apparatus.Novel insights into the mechanism of well-ordered assembly of bacterial flagellar proteins in Salmonella.Fuel of the Bacterial Flagellar Type III Protein Export Apparatus.Interactions of bacterial flagellar chaperone-substrate complexes with FlhA contribute to co-ordinating assembly of the flagellar filament.In Vitro Reconstitution of Functional Type III Protein Export and Insights into Flagellar Assembly.

P2860

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P2860

Substrate specificity classes and the recognition signal for Salmonella type III flagellar export.

http://www.wikidata.org/entity/Q39743825

description

2003 nî lūn-bûn

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2003年の論文

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

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2003年学术文章

@zh-sg

2003年學術文章

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2003年學術文章

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2003年學術文章

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name

Substrate specificity classes ...... lla type III flagellar export.

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Substrate specificity classes ...... lla type III flagellar export.

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type

label

Substrate specificity classes ...... lla type III flagellar export.

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Substrate specificity classes ...... lla type III flagellar export.

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prefLabel

Substrate specificity classes ...... lla type III flagellar export.

@en

Substrate specificity classes ...... lla type III flagellar export.

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P356

JB.185.8.2485-2492.2003

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Journal of Bacteriology

P1476

Substrate specificity classes ...... lla type III flagellar export.

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P2093

Keiichi Namba

http://www.w3.org/2001/XMLSchema#string

Robert M Macnab

http://www.w3.org/2001/XMLSchema#string

Takanori Hirano

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Tohru Minamino

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P2860

Functional insights from the structure of the 30S ribosomal subunit and its interactions with antibiotics

Identification of the YopE and YopH domains required for secretion and internalization into the cytosol of macrophages, using the cyaA gene fusion approach.

Export of an N-terminal fragment of Escherichia coli flagellin by a flagellum-specific pathway.

Flagellar assembly in Salmonella typhimurium: analysis with temperature-sensitive mutants.

Incomplete flagellar structures in Escherichia coli mutants.

Examination of bacterial flagellation by dark-field microscopy.

Quick transformation in Salmonella typhimurium LT2.

Components of the Salmonella flagellar export apparatus and classification of export substrates.

Interaction between FliE and FlgB, a proximal rod component of the flagellar basal body of Salmonella.

Intergenic suppression between the flagellar MS ring protein FliF of Salmonella and FlhA, a membrane component of its export apparatus.

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2485-2492

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scholarly article

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10.1128/JB.185.8.2485-2492.2003

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8

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152621

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