Results 281 to 290 of about 61,644 (304)
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Experimental Lung Research, 2019
Background and purpose of the study: Pseudomonas aeruginosa commonly colonizes the airway of patients with chronic obstructive pulmonary disease (COPD) and exacerbates their symptoms. P.
Keitaro Nakamoto +8 more
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Background and purpose of the study: Pseudomonas aeruginosa commonly colonizes the airway of patients with chronic obstructive pulmonary disease (COPD) and exacerbates their symptoms. P.
Keitaro Nakamoto +8 more
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Molecular Microbiology, 2016
SummaryFliS chaperone binds to flagellin FliC in the cytoplasm and transfers FliC to a sorting platform of the flagellar type III export apparatus through the interaction between FliS and FlhA for rapid and efficient protein export during flagellar filament assembly. FliS also suppresses the secretion of an anti‐σ factor, FlgM.
Yumi Inoue +7 more
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SummaryFliS chaperone binds to flagellin FliC in the cytoplasm and transfers FliC to a sorting platform of the flagellar type III export apparatus through the interaction between FliS and FlhA for rapid and efficient protein export during flagellar filament assembly. FliS also suppresses the secretion of an anti‐σ factor, FlgM.
Yumi Inoue +7 more
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The flagellin-TLR5 axis: Therapeutic opportunities
Drug News & Perspectives, 2002Motile bacteria synthesize large-sized surface structures known as flagella through the ordered polymerization of protein subunits. Flagellin, a protein of 40-60 kDa, is the principal constituent of the flagellum; each flagellum consists of approximately 20,000 flagellin molecules.
Liaudet, L. +6 more
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Flagellin Signalling in Plant Immunity
2007Like all higher living organisms, plants are constantly exposed to microbes that either grow epiphytically on the organ surface, establish beneficial interactions in specific tissues, or infect host tissues as pathogens and cause disease. In order to infect, pathogens must attach to the plant surface and break physical barriers to enter the tissue ...
Delphine Chinchilla +2 more
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Bioscience, Biotechnology, and Biochemistry, 2009
Flagellin glycosylation was identified in Bacillus sp. PS3 and Geobacillus stearothermophilus. In vivo complementation showed that these flagellin genes did not restore the motility of a Bacillus subtilis flagellin mutant, whereas the genes encoding non-glycosylated flagellin from Geobacillus kaustophilus and Bacillus sp.
Morio Ishizuka +2 more
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Flagellin glycosylation was identified in Bacillus sp. PS3 and Geobacillus stearothermophilus. In vivo complementation showed that these flagellin genes did not restore the motility of a Bacillus subtilis flagellin mutant, whereas the genes encoding non-glycosylated flagellin from Geobacillus kaustophilus and Bacillus sp.
Morio Ishizuka +2 more
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Divergence of a flagellin protein in Serratia marcescens
Gene, 1995A gene (hag) encoding the flagellin (Fla) protein was cloned from Serratia marcescens (Sm) 8000, the wild-type strain of Sr41. The hag gene codes for a 348-amino-acid (aa) protein of 36.7 kDa. The predicted aa sequence showed 79% homology compared with the Fla of Sm 274 which has been reported previously [Harshey et al., Gene 79 (1989) 1-8]. Dot-matrix
Eri Kawai +3 more
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Current Opinion in Structural Biology, 1992
Abstract Flagellin is the protein that makes up the filament or propeller of the bacterial flagellum. Structural studies have revealed that this protein has a disordered domain which becomes ordered upon polymerization. This part of the structure may be the key to understanding flagellin export from the cell and assembly into the filament.
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Abstract Flagellin is the protein that makes up the filament or propeller of the bacterial flagellum. Structural studies have revealed that this protein has a disordered domain which becomes ordered upon polymerization. This part of the structure may be the key to understanding flagellin export from the cell and assembly into the filament.
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Significance of Duplicated Flagellin Genes in Campylobacter
Journal of Molecular Biology, 1993The complex flagellum of Campylobacter coli VC167 contains two highly related (98%) flagellin subunit proteins which are produced from two 92% homologous, tandemly orientated genes, flaA and flaB. Mutants expressing only flaA form a full-length flagellar filament that confers slightly less than wild-type motility to the bacterium.
P Guerry, R A Alm, Trevor J. Trust
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Bacterial flagellar filaments and their component flagellins
Canadian Journal of Microbiology, 1993Introduction: the basic design . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 45 1 Variation in filament form and function . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . . 452 Mechanisms of motility . . . . . . . . . . . . . . . .
Dan R. Wilson, Terry J. Beveridge
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Terminal regions of flagellin are disordered in solution
Journal of Molecular Biology, 1989Limited proteolysis of flagellin from Salmonella typhimurium SJW1103 by subtilisin, trypsin and thermolysin results in homologous degradation patterns. The terminal regions of flagellin are very sensitive to proteolysis. These parts are degraded into small oligopeptides at the very early stage of a mild digestion that yields a relatively stable ...
Keiichi Namba +3 more
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