| scholarly article | Q13442814 |
| P356 | DOI | 10.1016/J.FEBSLET.2009.01.026 |
| P698 | PubMed publication ID | 19174164 |
| P50 | author | Masaru Okabe | Q37379874 |
| Katsumi Imada | Q59662528 | ||
| P2093 | author name string | Tohru Minamino | |
| Keiichi Namba | |||
| May Kihara | |||
| P2860 | cites work | Structural similarity between the flagellar type III ATPase FliI and F1-ATPase subunits | Q27641045 |
| Structure at 2.8 A resolution of F1-ATPase from bovine heart mitochondria | Q27730864 | ||
| The crystal structure of the nucleotide-free alpha 3 beta 3 subcomplex of F1-ATPase from the thermophilic Bacillus PS3 is a symmetric trimer | Q27741925 | ||
| Molecular basis of the interaction between the flagellar export proteins FliI and FliH from Helicobacter pylori | Q28484801 | ||
| An improved assay for nanomole amounts of inorganic phosphate | Q29620585 | ||
| Proteolytic analysis of the FliH/FliI complex, the ATPase component of the type III flagellar export apparatus of Salmonella | Q31012487 | ||
| Mechanisms of type III protein export for bacterial flagellar assembly. | Q34860251 | ||
| Self-assembly and type III protein export of the bacterial flagellum | Q35788077 | ||
| The ATPase FliI can interact with the type III flagellar protein export apparatus in the absence of its regulator, FliH. | Q39775119 | ||
| Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly. | Q41817833 | ||
| Interactions among components of the Salmonella flagellar export apparatus and its substrates | Q42484827 | ||
| Energy source of flagellar type III secretion | Q46793602 | ||
| Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein export | Q46793605 | ||
| Oligomerization of the bacterial flagellar ATPase FliI is controlled by its extreme N-terminal region | Q50079660 | ||
| FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activity | Q50119364 | ||
| Enzymatic characterization of FliI. An ATPase involved in flagellar assembly in Salmonella typhimurium | Q50136458 | ||
| P433 | issue | 4 | |
| P407 | language of work or name | English | Q1860 |
| P921 | main subject | biophysics | Q7100 |
| cell biology | Q7141 | ||
| structural biology | Q908902 | ||
| molecular biology | Q7202 | ||
| P304 | page(s) | 743-748 | |
| P577 | publication date | 2009-01-25 | |
| P1433 | published in | FEBS Letters | Q1388051 |
| P1476 | title | Role of the N-terminal domain of FliI ATPase in bacterial flagellar protein export | |
| P478 | volume | 583 |
| Q34142106 | Bacterial nanomachines: the flagellum and type III injectisome. |
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| Q40600401 | EscO, a functional and structural analog of the flagellar FliJ protein, is a positive regulator of EscN ATPase activity of the enteropathogenic Escherichia coli injectisome |
| Q39235366 | Functional Characterization of EscK (Orf4), a Sorting Platform Component of the Enteropathogenic Escherichia coli Injectisome |
| Q28534112 | Identification and molecular characterization of YsaL (Ye3555): a novel negative regulator of YsaN ATPase in type three secretion system of enteropathogenic bacteria Yersinia enterocolitica |
| Q36770466 | Insight into the flagella type III export revealed by the complex structure of the type III ATPase and its regulator |
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| Q33526048 | Interactions between flagellar and type III secretion proteins in Chlamydia pneumoniae |
| Q47254500 | Novel insights into the mechanism of SepL-mediated control of effector secretion in enteropathogenic Escherichia coli. |
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