Role of the C-terminal cytoplasmic domain of FlhA in bacterial flagellar type III protein export

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Role of the C-terminal cytoplasmic domain of FlhA in bacterial flagellar type III protein export is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1128/JB.01328-09
P3181OpenCitations bibliographic resource ID1694664
P932PMC publication ID2838044
P698PubMed publication ID20118266
P5875ResearchGate publication ID41191322

P2093author name stringKatsumi Imada
Tohru Minamino
Keiichi Namba
Masafumi Shimada
May Kihara
Mayuko Okabe
Yumiko Saijo-Hamano
P2860cites workStructure of the cytoplasmic domain of FlhA and implication for flagellar type III protein exportQ27660101
One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR productsQ27860842
Analysis of the cytoplasmic domains of Salmonella FlhA and interactions with components of the flagellar export machineryQ28770106
How Bacteria Assemble FlagellaQ34194719
Mechanisms of type III protein export for bacterial flagellar assembly.Q34860251
An escort mechanism for cycling of export chaperones during flagellum assemblyQ35768702
Self-assembly and type III protein export of the bacterial flagellumQ35788077
Genetic evidence for a switching and energy-transducing complex in the flagellar motor of Salmonella typhimuriumQ36261949
Mutations in flk, flgG, flhA, and flhE that affect the flagellar type III secretion specificity switch in Salmonella entericaQ37232486
Components of the Salmonella flagellar export apparatus and classification of export substratesQ39494402
Intergenic suppression between the flagellar MS ring protein FliF of Salmonella and FlhA, a membrane component of its export apparatusQ39502769
Role of FliJ in flagellar protein export in SalmonellaQ39538800
Domain structure of Salmonella FlhB, a flagellar export component responsible for substrate specificity switchingQ39587747
The ATPase FliI can interact with the type III flagellar protein export apparatus in the absence of its regulator, FliH.Q39775119
The FliO, FliP, FliQ, and FliR proteins of Salmonella typhimurium: putative components for flagellar assemblyQ39847377
Interactions of FliJ with the Salmonella type III flagellar export apparatusQ39887119
Molecular characterization of the Salmonella typhimurium flhB operon and its protein productsQ39899611
FlgD is a scaffolding protein needed for flagellar hook assembly in Salmonella typhimuriumQ39931449
Analysis of an engineered Salmonella flagellar fusion protein, FliR-FlhB.Q40867738
Oligomerization and activation of the FliI ATPase central to bacterial flagellum assembly.Q41817833
The FliP and FliR proteins of Salmonella typhimurium, putative components of the type III flagellar export apparatus, are located in the flagellar basal bodyQ42449241
Roles of the extreme N-terminal region of FliH for efficient localization of the FliH-FliI complex to the bacterial flagellar type III export apparatus.Q42462440
Interactions among components of the Salmonella flagellar export apparatus and its substratesQ42484827
ATP-induced FliI hexamerization facilitates bacterial flagellar protein exportQ43295990
Energy source of flagellar type III secretionQ46793602
Distinct roles of the FliI ATPase and proton motive force in bacterial flagellar protein exportQ46793605
Oligomerization of the bacterial flagellar ATPase FliI is controlled by its extreme N-terminal regionQ50079660
Structural and functional analysis of the C-terminal cytoplasmic domain of FlhA, an integral membrane component of the type III flagellar protein export apparatus in SalmonellaQ50096485
FliH, a soluble component of the type III flagellar export apparatus of Salmonella, forms a complex with FliI and inhibits its ATPase activityQ50119364
Enzymatic characterization of FliI. An ATPase involved in flagellar assembly in Salmonella typhimuriumQ50136458
Refined genetic analysis of the region II che mutants in Salmonella typhimuriumQ50206780
Genetic Analysis of H2, the Structural Gene for Phase-2 Flagellin in SalmonellaQ50209142
P433issue7
P407language of work or nameEnglishQ1860
P304page(s)1929–1936
P577publication date2010-04-01
P1433published inJournal of BacteriologyQ478419
P1476titleRole of the C-terminal cytoplasmic domain of FlhA in bacterial flagellar type III protein export
P478volume192

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cites work (P2860)
Q35367067An energy transduction mechanism used in bacterial flagellar type III protein export
Q44474595Assembly and stability of flagellar motor in Escherichia coli
Q42452873Assembly and stoichiometry of FliF and FlhA in Salmonella flagellar basal body
Q40108405Assembly and stoichiometry of the core structure of the bacterial flagellar type III export gate complex.
Q30588899Assembly dynamics and the roles of FliI ATPase of the bacterial flagellar export apparatus.
Q27028058Bacterial type III secretion systems: specialized nanomachines for protein delivery into target cells
Q33627041Control of type III secretion activity and substrate specificity by the cytoplasmic regulator PcrG.
Q30463935Cross-complementation study of the flagellar type III export apparatus membrane protein FlhB
Q38689905CsrA-FliW interaction governs flagellin homeostasis and a checkpoint on flagellar morphogenesis in Bacillus subtilis
Q55120336Energetic evolution of cellular Transportomes.
Q38257520Extracellular secretion of a recombinant therapeutic peptide by Bacillus halodurans utilizing a modified flagellin type III secretion system
Q33743275FlgN is required for flagellum-based motility by Bacillus subtilis
Q27662152FlhA provides the adaptor for coordinated delivery of late flagella building blocks to the type III secretion system
Q36999741FliH and FliI ensure efficient energy coupling of flagellar type III protein export in Salmonella.
Q33717044FliO Regulation of FliP in the Formation of the Salmonella enterica Flagellum
Q33979924Genetic characterization of conserved charged residues in the bacterial flagellar type III export protein FlhA
Q55265058Insight into structural remodeling of the FlhA ring responsible for bacterial flagellar type III protein export.
Q42958279Interaction between FliJ and FlhA, components of the bacterial flagellar type III export apparatus
Q28490035Interaction of the extreme N-terminal region of FliH with FlhA is required for efficient bacterial flagellar protein export
Q28484814Isolation of Salmonella mutants resistant to the inhibitory effect of Salicylidene acylhydrazides on flagella-mediated motility
Q40364421Mechanism of type-III protein secretion: Regulation of FlhA conformation by a functionally critical charged-residue cluster.
Q34459768Molecular architecture of the bacterial flagellar motor in cells
Q36015449MxiA, MxiC and IpaD Regulate Substrate Selection and Secretion Mode in the T3SS of Shigella flexneri
Q27704861Rearrangements of α-helical structures of FlgN chaperone control the binding affinity for its cognate substrates during flagellar type III export
Q37258436Recognition and targeting mechanisms by chaperones in flagellum assembly and operation
Q28555062Structural and Functional Characterization of the Bacterial Type III Secretion Export Apparatus
Q49960688Structural stability of flagellin subunit affects the rate of flagellin export in the absence of FliS chaperone
Q27661313Structure of the Cytoplasmic Domain of the Flagellar Secretion Apparatus Component FlhA from Helicobacter pylori
Q35946328The Bacterial Flagellar Type III Export Gate Complex Is a Dual Fuel Engine That Can Use Both H+ and Na+ for Flagellar Protein Export
Q90474195The Third Transmembrane Domain of EscR Is Critical for Function of the Enteropathogenic Escherichia coli Type III Secretion System
Q34755400The bacterial flagellar protein export apparatus processively transports flagellar proteins even with extremely infrequent ATP hydrolysis
Q92824667The flexible linker of the secreted FliK ruler is required for export switching of the flagellar protein export apparatus
Q48359452The role of intrinsically disordered C-terminal region of FliK in substrate specificity switching of the bacterial flagellar type III export apparatus.
Q28074332Type Three Secretion System in Attaching and Effacing Pathogens

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